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Conserved domains on  [gi|1498198613|gb|RMG53609|]
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SDR family oxidoreductase [Chloroflexi bacterium]

Protein Classification

SDR family NAD(P)-dependent oxidoreductase( domain architecture ID 11437015)

SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to Bacillus subtilis NADPH-dependent reductase BacG, which is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0070403|GO:0016491
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-248 1.27e-69

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 215.03  E-value: 1.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:COG1028    82 GRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAI-KQLPrvLRIFGtTAEETAELALRIVRE---GK 241
Cdd:COG1028   161 AVVGLTRSLALELAPRG-IRVNAVAPGPIDTPMTRALLGAEEVREALaARIP--LGRLG-TPEEVAAAVLFLASDaasYI 236

                  ....*..
gi 1498198613 242 NGQVFEV 248
Cdd:COG1028   237 TGQVLAV 243
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-248 1.27e-69

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 215.03  E-value: 1.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:COG1028    82 GRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAI-KQLPrvLRIFGtTAEETAELALRIVRE---GK 241
Cdd:COG1028   161 AVVGLTRSLALELAPRG-IRVNAVAPGPIDTPMTRALLGAEEVREALaARIP--LGRLG-TPEEVAAAVLFLASDaasYI 236

                  ....*..
gi 1498198613 242 NGQVFEV 248
Cdd:COG1028   237 TGQVLAV 243
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
13-248 9.22e-66

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 204.83  E-value: 9.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAErALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd05233    80 NNAGIARPGPL-EELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIKQLPrvLRIFGtTAEETAELALRIVREGK---NGQVFEV 248
Cdd:cd05233   159 SLALELAPYG-IRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIP--LGRLG-TPEEVAEAVVFLASDEAsyiTGQVIPV 233
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
13-198 2.14e-60

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 189.75  E-value: 2.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:pfam00106  83 NNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTR 161
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:pfam00106 162 SLALELAPHG-IRVNAVAPGGVDTDM 186
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
13-234 5.44e-60

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 190.37  E-value: 5.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK05653    8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK05653   88 NNAGITR-DALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTK 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHFETVgPGGEAIKQLPrvLRIFGtTAEETAELAL 234
Cdd:PRK05653  167 ALALELASRG-ITVNAVAPGFIDTDMTEGLPEE-VKAEILKEIP--LGRLG-QPEEVANAVA 223
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
13-198 3.15e-47

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 157.37  E-value: 3.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITyRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG-----GGAKRAQrflsaYSTSKAA 166
Cdd:TIGR01830  81 VNNAGITRD-NLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSvvglmGNAGQAN-----YAASKAG 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:TIGR01830 155 VIGFTKSLAKELASRN-ITVNAVAPGFIDTDM 185
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
14-123 4.76e-14

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 68.66  E-value: 4.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   14 VVTGGSRGIGRAIAEALARAGAQVII----SSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVllsrSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1498198613   90 LWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGT 123
Cdd:smart00822  84 GVIHAAGVLDD-GVLASLTPERFAAVLAPKAAGA 116
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-248 1.27e-69

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 215.03  E-value: 1.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:COG1028    82 GRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAI-KQLPrvLRIFGtTAEETAELALRIVRE---GK 241
Cdd:COG1028   161 AVVGLTRSLALELAPRG-IRVNAVAPGPIDTPMTRALLGAEEVREALaARIP--LGRLG-TPEEVAAAVLFLASDaasYI 236

                  ....*..
gi 1498198613 242 NGQVFEV 248
Cdd:COG1028   237 TGQVLAV 243
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
13-248 9.22e-66

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 204.83  E-value: 9.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAErALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd05233    80 NNAGIARPGPL-EELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIKQLPrvLRIFGtTAEETAELALRIVREGK---NGQVFEV 248
Cdd:cd05233   159 SLALELAPYG-IRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIP--LGRLG-TPEEVAEAVVFLASDEAsyiTGQVIPV 233
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
8-262 1.97e-64

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 202.02  E-value: 1.97e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:COG0300    83 IDVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 168 VRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFetvgpggeaikqlPRVLRIFGTTAEETAELALRIVREGKNgqVFE 247
Cdd:COG0300   162 EGFSESLRAELAPTG-VRVTAVCPGPVDTPFTARA-------------GAPAGRPLLSPEEVARAILRALERGRA--EVY 225
                         250
                  ....*....|....*
gi 1498198613 248 VMPRHRTIWRLLKAA 262
Cdd:COG0300   226 VGWDARLLARLLRLL 240
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
13-251 9.87e-63

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 197.33  E-value: 9.87e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:COG4221     8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:COG4221    85 NNAGV-ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHFetvgPGGEAIKQLPRVLRIFGTTAEETAELALRIVREGKNGQVFE--VMP 250
Cdd:COG4221   164 SLRAELRPTG-IRVTVIEPGAVDTEFLDSV----FDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPAHVNVNElvLRP 238

                  .
gi 1498198613 251 R 251
Cdd:COG4221   239 T 239
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
13-198 2.14e-60

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 189.75  E-value: 2.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:pfam00106  83 NNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTR 161
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:pfam00106 162 SLALELAPHG-IRVNAVAPGGVDTDM 186
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
13-234 5.44e-60

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 190.37  E-value: 5.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK05653    8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK05653   88 NNAGITR-DALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTK 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHFETVgPGGEAIKQLPrvLRIFGtTAEETAELAL 234
Cdd:PRK05653  167 ALALELASRG-ITVNAVAPGFIDTDMTEGLPEE-VKAEILKEIP--LGRLG-QPEEVANAVA 223
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-198 1.09e-52

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 171.41  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK07666    4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK07666   84 SIDILINNAGISK-FGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFG 162
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK07666  163 VLGLTESLMQEVRKHN-IRVTALTPSTVATDM 193
PRK12826 PRK12826
SDR family oxidoreductase;
7-234 2.19e-52

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 171.25  E-value: 2.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK12826    3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG-GGAKRAQRFLSAYSTSKA 165
Cdd:PRK12826   83 RLDILVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSvAGPRVGYPGLAHYAASKA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI-NHFETVGPggEAIKQLPRVLRIfgTTAEETAELAL 234
Cdd:PRK12826  162 GLVGFTRALALELAARN-ITVNSVHPGGVDTPMAgNLGDAQWA--EAIAAAIPLGRL--GEPEDIAAAVL 226
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
13-248 6.60e-51

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 167.35  E-value: 6.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISS-TNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK12825    9 ALVTGAARGLGRAIALRLARAGADVVVHYrSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRIDIL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK12825   89 VNNAGIFED-KPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLVGLT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDMINhfETVGPggEAIKQLPRV-LRIFGtTAEETAELALRIVREGK---NGQVFE 247
Cdd:PRK12825  168 KALARELAEYG-ITVNMVAPGDIDTDMKE--ATIEE--AREAKDAETpLGRSG-TPEDIARAVAFLCSDASdyiTGQVIE 241

                  .
gi 1498198613 248 V 248
Cdd:PRK12825  242 V 242
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
12-248 1.06e-49

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 163.87  E-value: 1.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:cd05333    82 VNNAGITRD-NLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVgPGGEAIKQLPrvLRIFGtTAEETAELALRIVREGKN---GQVFEV 248
Cdd:cd05333   161 KSLAKELASRG-ITVNAVAPGFIDTDMTDALPEK-VKEKILKQIP--LGRLG-TPEEVANAVAFLASDDASyitGQVLHV 235
FabG-like PRK07231
SDR family oxidoreductase;
7-211 1.96e-49

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 163.46  E-value: 1.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK07231    2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK07231   81 SVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1498198613 167 IVRLTEAFARDYQdhPY-LRFNVLTPGMVPTDMINHF-ETVGPGGEA 211
Cdd:PRK07231  161 VITLTKALAAELG--PDkIRVNAVAPVVVETGLLEAFmGEPTPENRA 205
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
7-198 3.50e-49

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 162.91  E-value: 3.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd05347     2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPFGyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:cd05347    82 KIDILVNNAGIIRRHP-AEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGG 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:cd05347   161 VAGLTKALATEWARHG-IQVNAIAPGYFATEM 191
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
13-248 1.08e-48

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 161.55  E-value: 1.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK05565    8 AIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK05565   88 VNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVNAFT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 172 EAFARDYQdhPY-LRFNVLTPGMVPTDMINHFETVG-PGGEAIKQLPRVlrifgTTAEETAELALRIVREGK---NGQVF 246
Cdd:PRK05565  167 KALAKELA--PSgIRVNAVAPGAIDTEMWSSFSEEDkEGLAEEIPLGRL-----GKPEEIAKVVLFLASDDAsyiTGQII 239

                  ..
gi 1498198613 247 EV 248
Cdd:PRK05565  240 TV 241
PRK12829 PRK12829
short chain dehydrogenase; Provisional
6-248 1.37e-47

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 159.07  E-value: 1.37e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK12829    7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFDTAVERF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK12829   85 GGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASgHGGVIIALSSVAGRLGYPGRTPYAASK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT-----DMINHFETVGPGGEAIKQ--LPRVLRIFGTTAEETAELALRIV 237
Cdd:PRK12829  165 WAVVGLVKSLAIELGPLG-IRVNAILPGIVRGprmrrVIEARAQQLGIGLDEMEQeyLEKISLGRMVEPEDIAATALFLA 243
                         250
                  ....*....|....
gi 1498198613 238 -REGKN--GQVFEV 248
Cdd:PRK12829  244 sPAARYitGQAISV 257
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
13-198 3.15e-47

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 157.37  E-value: 3.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITyRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG-----GGAKRAQrflsaYSTSKAA 166
Cdd:TIGR01830  81 VNNAGITRD-NLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSvvglmGNAGQAN-----YAASKAG 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:TIGR01830 155 VIGFTKSLAKELASRN-ITVNAVAPGFIDTDM 185
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
13-198 4.45e-45

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 152.27  E-value: 4.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEA-ERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK05557    8 ALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEAlVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGIS--GPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:PRK05557   88 VNNAGITrdNLL---MRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVIG 164
                         170       180
                  ....*....|....*....|....*....
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK05557  165 FTKSLARELASRG-ITVNAVAPGFIETDM 192
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
2-198 5.65e-44

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 149.71  E-value: 5.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   2 ARTPSDLRDLK---AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALA 78
Cdd:PRK08213    1 MMTVLELFDLSgktALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  79 SAAVERMGRIDLWVNNAGIS--GPfgyALDIPPDAWEQVIRVNLLGTYYGCRAALP-YMIKQRNGQIINLSG----GGAK 151
Cdd:PRK08213   81 EETLERFGHVDILVNNAGATwgAP---AEDHPVEAWDKVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASvaglGGNP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1498198613 152 RAQRFLSAYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK08213  158 PEVMDTIAYNTSKGAVINFTRALAAEWGPHG-IRVNAIAPGFFPTKM 203
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
20-234 1.18e-43

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 147.96  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  20 RGIGRAIAEALARAGAQVIISSTNPTNLTEAERAlqAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVNNAGISG 99
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEEL--AEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFAP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 100 PF-GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEAFARDY 178
Cdd:pfam13561  84 KLkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVEL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 179 QDHPyLRFNVLTPGMVPTDM---INHFETVGPggEAIKQLPrvLRIFGTTaEETAELAL 234
Cdd:pfam13561 162 GPRG-IRVNAISPGPIKTLAasgIPGFDELLA--AAEARAP--LGRLGTP-EEVANAAA 214
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
12-234 1.36e-43

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 148.58  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05344     3 VALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:cd05344    83 VNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLV 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTD-MINHFETVGPGG---------EAIKQLPrvLRIFGtTAEETAELAL 234
Cdd:cd05344   162 KTLSRELAPDG-VTVNSVLPGYIDTErVRRLLEARAEKEgisveeaekEVASQIP--LGRVG-KPEELAALIA 230
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
13-237 2.48e-43

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 147.76  E-value: 2.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05374     3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELL---NDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd05374    80 NNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSE 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 173 AFARDYQdhpylRFNV----LTPGMVPTDMINHFETVGPGG----------EAIKQLPRVLRIFGTTAEETAELALRIV 237
Cdd:cd05374   159 SLRLELA-----PFGIkvtiIEPGPVRTGFADNAAGSALEDpeispyaperKEIKENAAGVGSNPGDPEKVADVIVKAL 232
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
7-201 2.80e-43

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 147.48  E-value: 2.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLK---AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAV 82
Cdd:cd05352     2 DLFSLKgkvAIVTGGSRGIGLAIARALAEAGADVAIIyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  83 ERMGRIDLWVNNAGISGPFGyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQII---NLSGGGAKRAQRfLSA 159
Cdd:cd05352    82 KDFGKIDILIANAGITVHKP-ALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIitaSMSGTIVNRPQP-QAA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1498198613 160 YSTSKAAIVRLTEAFARDYQDHpYLRFNVLTPGMVPTDMINH 201
Cdd:cd05352   160 YNASKAAVIHLAKSLAVEWAKY-FIRVNSISPGYIDTDLTDF 200
PRK12939 PRK12939
short chain dehydrogenase; Provisional
4-198 6.28e-42

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 143.96  E-value: 6.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   4 TPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVE 83
Cdd:PRK12939    1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  84 RMGRIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS----GGGAKRaqrfLSA 159
Cdd:PRK12939   81 ALGGLDGLVNNAGIT-NSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLAsdtaLWGAPK----LGA 155
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1498198613 160 YSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK12939  156 YVASKGAVIGMTRSLARELGGRG-ITVNAIAPGLTATEA 193
PRK06398 PRK06398
aldose dehydrogenase; Validated
6-199 2.01e-41

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 143.05  E-value: 2.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVI-ISSTNPTNLteaeralqaaglNVTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK06398    2 LGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVInFDIKEPSYN------------DVDYFKVDVSNKEQVIKGIDYVISK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK06398   70 YGRIDILVNNAGIES-YGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSK 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 165 AAIVRLTEAFARDYQdhPYLRFNVLTPGMVPTDMI 199
Cdd:PRK06398  149 HAVLGLTRSIAVDYA--PTIRCVAVCPGSIRTPLL 181
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
12-234 3.36e-41

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 142.14  E-value: 3.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:cd05358     5 VALVTGASSGIGKAIAIRLATAGANVVVNyRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQR-NGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:cd05358    85 LVNNAGLQGDASSH-EMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIPWPGHVNYAASKGGVKM 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPTDmINHFETVGPggEAIKQLPRV--LRIFGTTaEETAELAL 234
Cdd:cd05358   164 MTKTLAQEYAPKG-IRVNAIAPGAINTP-INAEAWDDP--EQRADLLSLipMGRIGEP-EEIAAAAA 225
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
14-173 6.81e-41

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 140.98  E-value: 6.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:cd05360     4 VITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEA 173
Cdd:cd05360    84 NAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTES 162
PRK06138 PRK06138
SDR family oxidoreductase;
7-234 1.42e-40

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 140.67  E-value: 1.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLtEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK06138    2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAA-ERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK06138   81 RLDVLVNNAGF-GCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIKQLPR---VLRIFGtTAEETAELAL 234
Cdd:PRK06138  160 IASLTRAMALDHATDG-IRVNAVAPGTIDTPYFRRIFARHADPEALREALRarhPMNRFG-TAEEVAQAAL 228
PRK07109 PRK07109
short chain dehydrogenase; Provisional
13-173 1.80e-40

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 142.75  E-value: 1.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK07109   11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPIDTWV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK07109   91 NNAMVT-VFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTD 169

                  .
gi 1498198613 173 A 173
Cdd:PRK07109  170 S 170
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
13-198 8.48e-40

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 138.66  E-value: 8.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTN-LTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05366     5 AIITGAAQGIGRAIAERLAADGFNIVLADLNLEEaAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSFDVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:cd05366    85 VNNAGI-APITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLgHGGKIINASSIAGVQGFPNLGAYSASKFAVRGL 163
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 171 TEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:cd05366   164 TQTAAQELAPKG-ITVNAYAPGIVKTEM 190
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
13-196 9.26e-40

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 138.87  E-value: 9.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK12429    7 ALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDILV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIS--GPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:PRK12429   87 NNAGIQhvAPIE---DFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGL 163
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 171 TEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK12429  164 TKVVALEGATHG-VTVNAICPGYVDT 188
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
13-252 1.09e-39

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 138.20  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTnlTEAERALQAA--GLNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:cd05323     3 AIITGGASGIGLATAKLLLKKGAKVAILDRNEN--PGAAAELQAInpKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISGPFGYALDIPPDA-WEQVIRVNLLGTYYGCRAALPYMIK---QRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:cd05323    81 LINNAGILDEKSYLFAGKLPPpWEKTIDVNLTGVINTTYLALHYMDKnkgGKGGVIVNIGSVAGLYPAPQFPVYSASKHG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 167 IVRLTEAFArDYQDHPY-LRFNVLTPGMVPTDMINHFETVGPggEAIKQLPRvlrifgTTAEETAELALRIV-REGKNGQ 244
Cdd:cd05323   161 VVGFTRSLA-DLLEYKTgVRVNAICPGFTNTPLLPDLVAKEA--EMLPSAPT------QSPEVVAKAIVYLIeDDEKNGA 231

                  ....*...
gi 1498198613 245 VFEVMPRH 252
Cdd:cd05323   232 IWIVDGGK 239
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
8-234 3.36e-39

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 136.95  E-value: 3.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLN-VTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGrAHPIQCDVRDPEAVEAAVDETLKEFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGisGPF-GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRN-GQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:cd05369    81 KIDILINNAA--GNFlAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAAAK 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDmiNHFETVGPGG-EAIKQLPRV-LRIFGTTaEETAELAL 234
Cdd:cd05369   159 AGVDALTRSLAVEWGPYG-IRVNAIAPGPIPTT--EGMERLAPSGkSEKKMIERVpLGRLGTP-EEIANLAL 226
PRK07326 PRK07326
SDR family oxidoreductase;
13-201 8.78e-39

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 135.52  E-value: 8.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK07326    9 ALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAFGGLDVLI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK07326   88 ANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNASKFGLVGFSE 165
                         170       180
                  ....*....|....*....|....*....
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINH 201
Cdd:PRK07326  166 AAMLDLRQYG-IKVSTIMPGSVATHFNGH 193
PRK06841 PRK06841
short chain dehydrogenase; Provisional
7-234 2.57e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 134.79  E-value: 2.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNlteAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK06841   12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDV---AEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK06841   89 RIDILVNSAGV-ALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAG 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMiNHFETVGPGGEAIKQLPRVLRiFGtTAEETAELAL 234
Cdd:PRK06841  168 VVGMTKVLALEWGPYG-ITVNAISPTVVLTEL-GKKAWAGEKGERAKKLIPAGR-FA-YPEEIAAAAL 231
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
13-248 9.30e-38

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 133.25  E-value: 9.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVII---SSTNPTNLTEAEraLQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVInyrKSKDAAAEVAAE--IEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:cd05359    79 VLVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIKQ---LPRVLrifgtTAEETAELALRIVREGK---NG 243
Cdd:cd05359   158 LVRYLAVELGPRG-IRVNAVSPGVIDTDALAHFPNREDLLEAAAAntpAGRVG-----TPQDVADAVGFLCSDAArmiTG 231

                  ....*
gi 1498198613 244 QVFEV 248
Cdd:cd05359   232 QTLVV 236
PRK05650 PRK05650
SDR family oxidoreductase;
14-258 7.50e-37

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 131.32  E-value: 7.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGI-SGpfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK05650   84 NAGVaSG--GFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 173 AFA---RDYQDHpylrFNVLTPGMVPTDMINHFETVGPGGEAikQLPRVLRIFGTTAEETAELALRIVREGKngqvFEVM 249
Cdd:PRK05650  162 TLLvelADDEIG----VHVVCPSFFQTNLLDSFRGPNPAMKA--QVGKLLEKSPITAADIADYIYQQVAKGE----FLIL 231
                         250
                  ....*....|.
gi 1498198613 250 PRH--RTIWRL 258
Cdd:PRK05650  232 PHEqgRRAWQL 242
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
13-215 8.18e-37

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 130.05  E-value: 8.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGA-QVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05324     3 ALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAqrflSAYSTSKAAIVRLT 171
Cdd:cd05324    83 VNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLT----SAYGVSKAALNALT 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1498198613 172 EAFARDYQDhPYLRFNVLTPGMVPTDMINHFE--TVGPGGEAIKQL 215
Cdd:cd05324   159 RILAKELKE-TGIKVNACCPGWVKTDMGGGKApkTPEEGAETPVYL 203
PRK07774 PRK07774
SDR family oxidoreductase;
7-248 8.87e-37

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 130.63  E-value: 8.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK07774    3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISG--PFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFlsaYSTSK 164
Cdd:PRK07774   83 GIDYLVNNAAIYGgmKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYSNF---YGLAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMInhfETVGPG---GEAIKQLPrvLRIFGTTAEETAELALRIVREGK 241
Cdd:PRK07774  160 VGLNGLTQQLARELGGMN-IRVNAIAPGPIDTEAT---RTVTPKefvADMVKGIP--LSRMGTPEDLVGMCLFLLSDEAS 233

                  ....*....
gi 1498198613 242 --NGQVFEV 248
Cdd:PRK07774  234 wiTGQIFNV 242
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
13-204 1.15e-36

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 130.05  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05339     2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGI-SGPFGyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:cd05339    82 NNAGVvSGKKL--LELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 172 EAFARDY--QDHPYLRFNVLTPGMVPTDMINHFET 204
Cdd:cd05339   160 ESLRLELkaYGKPGIKTTLVCPYFINTGMFQGVKT 194
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
12-243 1.80e-36

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 129.68  E-value: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA----GLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:cd08939     3 HVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEanasGQKVSYISADLSDYEEVEQAFAQAVEKGGP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAkraqrFL-----SAYST 162
Cdd:cd08939    83 PDLVVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAA-----LVgiygySAYCP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 163 SKAAIVRLTEAFARDYQDHPYlRFNVLTPGmvptdminhfETVGPGGEA-IKQLPRVLR-IFGTTAEETAELALRIVREG 240
Cdd:cd08939   157 SKFALRGLAESLRQELKPYNI-RVSVVYPP----------DTDTPGFEEeNKTKPEETKaIEGSSGPITPEEAARIIVKG 225

                  ....
gi 1498198613 241 -KNG 243
Cdd:cd08939   226 lDRG 229
PRK06139 PRK06139
SDR family oxidoreductase;
8-201 2.08e-36

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 131.77  E-value: 2.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK06139    5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:PRK06139   85 IDVWVNNVGV-GAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGL 163
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 168 VRLTEAFARDYQDHPYLRFNVLTPGMVPTDMINH 201
Cdd:PRK06139  164 RGFSEALRGELADHPDIHVCDVYPAFMDTPGFRH 197
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
13-181 2.13e-36

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 129.82  E-value: 2.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVII------SSTNPTNLT------EAERALQAAGLNVTGIRCDVANRNEVEALASA 80
Cdd:cd05338     6 AFVTGASRGIGRAIALRLAKAGATVVVaaktasEGDNGSAKSlpgtieETAEEIEAAGGQALPIVVDVRDEDQVRALVEA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  81 AVERMGRIDLWVNNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAY 160
Cdd:cd05338    86 TVDQFGRLDILVNNAG-AIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDVAY 164
                         170       180
                  ....*....|....*....|.
gi 1498198613 161 STSKAAIVRLTEAFARDYQDH 181
Cdd:cd05338   165 AAGKAGMSRLTLGLAAELRRH 185
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
13-220 9.10e-36

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 127.48  E-value: 9.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnltEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08932     3 ALVTGASRGIGIEIARALARDGYRVSLGLRNP----EDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd08932    79 HNAGIGRP-TTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAH 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMIN-HFETVGPGGEAIKQlPRVLR 220
Cdd:cd08932   158 ALRQEGWDHG-VRVSAVCPGFVDTPMAQgLTLVGAFPPEEMIQ-PKDIA 204
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
12-234 1.04e-35

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 127.59  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERalqaaGLNVTGIRCDVANRNEVEALASaaveRMGRIDLW 91
Cdd:cd05368     4 VALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER-----GPGITTRVLDVTDKEQVAALAK----EEGRIDVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS---GGGAKRAQRFlsAYSTSKAAIV 168
Cdd:cd05368    75 FNCAGFV-HHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSsvaSSIKGVPNRF--VYSTTKAAVI 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498198613 169 RLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIKQ--LPRVLRIFGTTAEETAELAL 234
Cdd:cd05368   152 GLTKSVAADFAQQG-IRCNAICPGTVDTPSLEERIQAQPDPEEALKafAARQPLGRLATPEEVAALAV 218
PRK05855 PRK05855
SDR family oxidoreductase;
1-263 2.47e-35

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 133.18  E-value: 2.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   1 MARTPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASA 80
Cdd:PRK05855  306 VGRPRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEW 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  81 AVERMGRIDLWVNNAGI--SGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFL 157
Cdd:PRK05855  386 VRAEHGVPDIVVNNAGIgmAGGF---LDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSL 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 158 SAYSTSKAAIVRLTEAFARDYQDHpylRFNVLT--PGMVPTDMINHFETVGPGGEAI----KQLPRVLRIFGTTAEETAE 231
Cdd:PRK05855  463 PAYATSKAAVLMLSECLRAELAAA---GIGVTAicPGFVDTNIVATTRFAGADAEDEarrrGRADKLYQRRGYGPEKVAK 539
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1498198613 232 LALRIVRegKNGQVFEVMPRHRT---IWRLLKAAL 263
Cdd:PRK05855  540 AIVDAVK--RNKAVVPVTPEAHAgygVSRFAPWLL 572
PRK06194 PRK06194
hypothetical protein; Provisional
13-251 2.48e-35

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 127.82  E-value: 2.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06194    9 AVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHLLF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ------RNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK06194   89 NNAGV-GAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAMGIYNVSKHA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 167 IVRLTEAFardYQD----HPYLRFNVLTPGMVPT-----------DMINHFETVGPGGEAIKQLPRVLRIFGTTAEETAE 231
Cdd:PRK06194  168 VVSLTETL---YQDlslvTDQVGASVLCPYFVPTgiwqsernrpaDLANTAPPTRSQLIAQAMSQKAVGSGKVTAEEVAQ 244
                         250       260
                  ....*....|....*....|
gi 1498198613 232 LALRIVREGKngqvFEVMPR 251
Cdd:PRK06194  245 LVFDAIRAGR----FYIYSH 260
PRK06181 PRK06181
SDR family oxidoreductase;
13-235 2.66e-35

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 127.40  E-value: 2.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06181    4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDILV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIS--GPFGYALDipPDAWEQVIRVNLLGTYYGCRAALPYMiKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:PRK06181   84 NNAGITmwSRFDELTD--LSVFERVMRVNYLGAVYCTHAALPHL-KASRGQIVVVSSLAGLTGVPTRSGYAASKHALHGF 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1498198613 171 TEAFARDYQDHPyLRFNVLTPGMVPTDMinHFETVGPGGEAIKQLPrvLRIFGT-TAEETAELALR 235
Cdd:PRK06181  161 FDSLRIELADDG-VAVTVVCPGFVATDI--RKRALDGDGKPLGKSP--MQESKImSAEECAEAILP 221
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
13-251 3.82e-35

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 126.50  E-value: 3.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08934     6 ALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDILV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd08934    86 NNAGI-MLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSE 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHFeTVGPGGEAIKQlpRVLRIFGTTAEETAELALRIVREGKNGQVFEVMPR 251
Cdd:cd08934   165 GLRQEVTERG-VRVVVIEPGTVDTELRDHI-THTITKEAYEE--RISTIRKLQAEDIAAAVRYAVTAPHHVTVNEILIR 239
PRK06172 PRK06172
SDR family oxidoreductase;
13-240 4.55e-35

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 126.40  E-value: 4.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06172   10 ALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLDYAF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK06172   90 NNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGLTK 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGP-GGEAIKQLPRVLRIfgTTAEETAELALRIVREG 240
Cdd:PRK06172  170 SAAIEYAKKG-IRVNAVCPAVIDTDMFRRAYEADPrKAEFAAAMHPVGRI--GKVEEVASAVLYLCSDG 235
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
13-199 4.58e-35

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 126.84  E-value: 4.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERaLQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK08226    9 ALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADE-LCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDILV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIS--GPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG-GGAKRAQRFLSAYSTSKAAIVR 169
Cdd:PRK08226   88 NNAGVCrlGSF---LDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSvTGDMVADPGETAYALTKAAIVG 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 170 LTEAFARDYQDHpYLRFNVLTPGMVPTDMI 199
Cdd:PRK08226  165 LTKSLAVEYAQS-GIRVNAICPGYVRTPMA 193
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
12-235 6.69e-35

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 126.02  E-value: 6.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA--GLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:cd08940     4 VALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAkhGVKVLYHGADLSKPAAIEDMVAYAQRQFGGVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGIS--GPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:cd08940    84 ILVNNAGIQhvAPIE---DFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498198613 168 VRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINhfetvgpggeaiKQLPRVLRIFGTTAEETAELALR 235
Cdd:cd08940   161 VGLTKVVALETAGTG-VTCNAICPGWVLTPLVE------------KQISALAQKNGVPQEQAARELLL 215
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
13-196 1.12e-34

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 125.62  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISsTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06935   18 AIVTGGNTGLGQGYAVALAKAGADIIIT-THGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDILV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGI--SGPfgyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIIN----LSGGGAKraqrFLSAYSTSKAA 166
Cdd:PRK06935   97 NNAGTirRAP---LLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINiasmLSFQGGK----FVPAYTASKHG 169
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 167 IVRLTEAFARDYQDHpYLRFNVLTPGMVPT 196
Cdd:PRK06935  170 VAGLTKAFANELAAY-NIQVNAIAPGYIKT 198
PRK07063 PRK07063
SDR family oxidoreductase;
8-196 2.55e-34

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 124.78  E-value: 2.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQA--AGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK07063    5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARdvAGARVLAVPADVTDAASVAAAVAAAEEAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK07063   85 GPLDVLVNNAGIN-VFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK07063  164 GLLGLTRALGIEYAARN-VRVNAIAPGYIET 193
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
14-253 2.73e-34

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 124.24  E-value: 2.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTE-AERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05332     7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEvKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFGGLDILI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIvrltE 172
Cdd:cd05332    87 NNAGISMR-SLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHAL----Q 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 173 AFA---RdyqdHPYLRFNV----LTPGMVPTDMINHFETvgpggEAIKQLPRVLRIF--GTTAEETAELALRIVREGKNg 243
Cdd:cd05332   162 GFFdslR----AELSEPNIsvtvVCPGLIDTNIAMNALS-----GDGSMSAKMDDTTanGMSPEECALEILKAIALRKR- 231
                         250
                  ....*....|.
gi 1498198613 244 qvfEV-MPRHR 253
Cdd:cd05332   232 ---EVfYARQV 239
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
13-198 2.94e-34

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 123.92  E-value: 2.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNptNLTEAER---ALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:cd05362     6 ALVTGASRGIGRAIAKRLARDGASVVVNYAS--SKAAAEEvvaEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:cd05362    84 ILVNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEA 160
                         170       180
                  ....*....|....*....|....*....
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:cd05362   161 FTRVLAKELGGRG-ITVNAVAPGPVDTDM 188
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
6-196 3.10e-34

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 124.40  E-value: 3.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLK---AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAV 82
Cdd:PRK07097    3 ENLFSLKgkiALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  83 ERMGRIDLWVNNAGI--SGPfgyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAY 160
Cdd:PRK07097   83 KEVGVIDILVNNAGIikRIP---MLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAY 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1498198613 161 STSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK07097  160 AAAKGGLKMLTKNIASEYGEAN-IQCNGIGPGYIAT 194
PRK07035 PRK07035
SDR family oxidoreductase;
7-196 3.62e-34

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 123.97  E-value: 3.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLK---AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVE 83
Cdd:PRK07035    2 NLFDLTgkiALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  84 RMGRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:PRK07035   82 RHGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSIT 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK07035  162 KAAVISMTKAFAKECAPFG-IRVNALLPGLTDT 193
PRK07856 PRK07856
SDR family oxidoreductase;
5-197 4.00e-34

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 123.89  E-value: 4.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   5 PSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNlteaeralQAAGLNVTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK07856    1 NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPE--------TVDGRPAEFHAADVRDPDQVAALVDAIVER 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:PRK07856   73 HGRLDVLVNNAGGS-PYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPGTAAYGAA 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 164 KAAIVRLTEAFARDYQdhPYLRFNVLTPGMVPTD 197
Cdd:PRK07856  152 KAGLLNLTRSLAVEWA--PKVRVNAVVVGLVRTE 183
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
13-234 4.13e-34

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 123.75  E-value: 4.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNptnLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08944     6 AIVTGAGAGIGAACAARLAREGARVVVADID---GGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDLLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd08944    83 NNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTR 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHF-----ETVGPGGEAI---KQLPRVLRifgttAEETAELAL 234
Cdd:cd08944   163 TLAAELRHAG-IRCNALAPGLIDTPLLLAKlagfeGALGPGGFHLlihQLQGRLGR-----PEDVAAAVV 226
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
13-197 7.36e-34

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 123.06  E-value: 7.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd05365    82 NNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMTR 161
                         170       180
                  ....*....|....*....|....*
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:cd05365   162 NLAFDLGPKG-IRVNAVAPGAVKTD 185
PRK06484 PRK06484
short chain dehydrogenase; Validated
13-206 9.12e-34

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 128.04  E-value: 9.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNptnLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06484    8 VLVTGAAGGIGRAACQRFARAGDQVVVADRN---VERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYA-LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQ-IINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:PRK06484   85 NNAGVTDPTMTAtLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAVISL 164
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1498198613 171 TEAFARDYQdHPYLRFNVLTPGMVPTDMINHFETVG 206
Cdd:PRK06484  165 TRSLACEWA-AKGIRVNAVLPGYVRTQMVAELERAG 199
PRK06057 PRK06057
short chain dehydrogenase; Provisional
8-196 2.11e-33

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 122.15  E-value: 2.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAeralqAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK06057    5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAA-----ADEVGGLFVPTDVTDEDAVNALFDTAAETYGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGISGPF-GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG----GGAKRAQrflSAYST 162
Cdd:PRK06057   80 VDIAFNNAGISPPEdDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASfvavMGSATSQ---ISYTA 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1498198613 163 SKAAIVRLTE----AFARDyqdhpYLRFNVLTPGMVPT 196
Cdd:PRK06057  157 SKGGVLAMSRelgvQFARQ-----GIRVNALCPGPVNT 189
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-245 2.31e-33

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 121.81  E-value: 2.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIIsstNPTNLTEAERALQAAGlnVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK06463    5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAV---LYNSAENEAKELREKG--VFTIKCDVGNRDQVKKSKEVVEKEFGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGI--SGPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINL-SGGGAKRAQRFLSAYSTSK 164
Cdd:PRK06463   80 VDVLVNNAGImyLMPFE---EFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIaSNAGIGTAAEGTTFYAITK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMinhfeTV-GPGGEAIKQLPR------VLRIFGtTAEETAELALRIV 237
Cdd:PRK06463  157 AGIIILTRRLAFELGKYG-IRVNAVAPGWVETDM-----TLsGKSQEEAEKLRElfrnktVLKTTG-KPEDIANIVLFLA 229
                         250
                  ....*....|.
gi 1498198613 238 REGK---NGQV 245
Cdd:PRK06463  230 SDDAryiTGQV 240
PRK12828 PRK12828
short chain dehydrogenase; Provisional
7-199 3.03e-33

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 121.06  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIrcDVANRNEVEALASAAVERMG 86
Cdd:PRK12828    4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNRQFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK12828   82 RLDALVNIAGAF-VWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAG 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:PRK12828  161 VARLTEALAAELLDRG-ITVNAVLPSIIDTPPN 192
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
8-197 3.83e-33

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 121.49  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK06113    9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGISGPfgYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:PRK06113   89 VDILVNNAGGGGP--KPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAA 166
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 168 VRLTEAFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:PRK06113  167 SHLVRNMAFDLGEKN-IRVNGIAPGAILTD 195
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
8-233 4.83e-33

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 121.02  E-value: 4.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISstnptNLTEAERALQAAGL---NVTGIRCDVANRNEVEALASAAVER 84
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVIA-----DIDDDAGQAVAAELgdpDISFVHCDVTVEADVRAAVDTAVAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISGPFGYA-LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:cd05326    77 FGRLDIMFNNAGVLGAPCYSiLETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTAS 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHfeTVGPGGEAIKQLPRVLRIFGTTAEETAELA 233
Cdd:cd05326   157 KHAVLGLTRSAATELGEHG-IRVNCVSPYGVATPLLTA--GFGVEDEAIEEAVRGAANLKGTALRPEDIA 223
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
4-196 5.10e-33

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 121.11  E-value: 5.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   4 TPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVE 83
Cdd:cd08936     4 RRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  84 RMGRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:cd08936    84 LHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVS 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 164 KAAIVRLTEAFARDYqDHPYLRFNVLTPGMVPT 196
Cdd:cd08936   164 KTALLGLTKNLAPEL-APRNIRVNCLAPGLIKT 195
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
13-202 7.15e-33

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 120.57  E-value: 7.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNptnLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05345     8 AIVTGAGSGFGEGIARRFAQEGARVVIADIN---ADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd05345    85 NNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTATK 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDMINHF 202
Cdd:cd05345   165 AMAVELAPRN-IRVNCLCPVAGETPLLSMF 193
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
8-199 1.30e-32

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 119.86  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM-G 86
Cdd:cd05329     4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:cd05329    84 KLNILVNNAGTNIR-KEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:cd05329   163 LNQLTRSLACEWAKDN-IRVNAVAPWVIATPLV 194
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
8-232 1.46e-32

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 119.93  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQ--AAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:cd05330     1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLeiAPDAEVLLIKADVSDEAQVEAYVDATVEQF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:cd05330    81 GRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI-NHFETVGPGG--EAIKQLPRV--LRIFGtTAEETAEL 232
Cdd:cd05330   161 GVVGLTRNSAVEYGQYG-IRINAIAPGAILTPMVeGSLKQLGPENpeEAGEEFVSVnpMKRFG-EPEEVAAV 230
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
13-203 1.66e-32

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 118.76  E-value: 1.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYRVGICARDE---ARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd08929    80 NNAGV-GVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSE 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 173 AFARDYqdHPY-LRFNVLTPGMVPTDMINHFE 203
Cdd:cd08929   159 AAMLDL--REAnIRVVNVMPGSVDTGFAGSPE 188
PRK07825 PRK07825
short chain dehydrogenase; Provisional
6-199 2.19e-32

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 119.66  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISstnptNLTEAERALQAAGL-NVTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK07825    1 DDLRGKVVAITGGARGIGLATARALAALGARVAIG-----DLDEALAKETAAELgLVVGGPLDVTDPASFAAFLDAVEAD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK07825   76 LGPIDVLVNNAGVM-PVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASK 154
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:PRK07825  155 HAVVGFTDAARLELRGTG-VHVSVVLPSFVNTELI 188
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
8-198 2.46e-32

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 119.36  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKP---ARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGIsgpFGYA--LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK07067   81 IDILFNNAAL---FDMApiLDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATK 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK07067  158 AAVISYTQSAALALIRHG-INVNAIAPGVVDTPM 190
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
13-197 2.97e-32

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 119.05  E-value: 2.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGL---NVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:cd05364     6 AIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVsekKILLVVADLTEEEGQDRIISTTLAKFGRLD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRnGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:cd05364    86 ILVNNAGILAK-GGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCISKAALDQ 163
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:cd05364   164 FTRCTALELAPKG-VRVNSVSPGVIVTG 190
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
6-196 5.32e-32

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 118.68  E-value: 5.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK08936    3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINyRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISGPFGyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:PRK08936   83 FGTLDVMINNAGIENAVP-SHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAAS 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK08936  162 KGGVKLMTETLAMEYAPKG-IRVNNIGPGAINT 193
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
6-228 5.85e-32

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 118.46  E-value: 5.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK13394    3 SNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGIS--GPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRN-GQIINLSGGGAKRAQRFLSAYST 162
Cdd:PRK13394   83 GSVDILVSNAGIQivNPI---ENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRgGVVIYMGSVHSHEASPLKSAYVT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1498198613 163 SKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINhfetvgpggeaiKQLPRVLRIFGTTAEE 228
Cdd:PRK13394  160 AKHGLLGLARVLAKEGAKHN-VRSHVVCPGFVRTPLVD------------KQIPEQAKELGISEEE 212
PRK07454 PRK07454
SDR family oxidoreductase;
13-196 1.55e-31

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 116.60  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK07454    9 ALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGI--SGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:PRK07454   89 NNAGMayTGPL---LEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 171 TEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK07454  166 TKCLAEEERSHG-IRVCTITLGAVNT 190
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
10-202 1.71e-31

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 117.00  E-value: 1.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  10 DLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnltEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPN----SPGETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGIsgpfGYALDI---------PPDAWEQVIRVNLLGTYYGCRAALPYMIK-------QRnGQIINLSGGGAKRA 153
Cdd:cd05371    78 IVVNCAGI----AVAAKTynkkgqqphSLELFQRVINVNLIGTFNVIRLAAGAMGKnepdqggER-GVIINTASVAAFEG 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1498198613 154 QRFLSAYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHF 202
Cdd:cd05371   153 QIGQAAYSASKGGIVGMTLPIARDLAPQG-IRVVTIAPGLFDTPLLAGL 200
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-198 4.13e-31

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 115.83  E-value: 4.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK08217    2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGI--SGPFGYALD------IPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSggGAKRAQRF- 156
Cdd:PRK08217   82 QLNGLINNAGIlrDGLLVKAKDgkvtskMSLEQFQSVIDVNLTGVFLCGREAAAKMIESgSKGVIINIS--SIARAGNMg 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1498198613 157 LSAYSTSKAAIVRLTEAFARDYQdhpylRFNV----LTPGMVPTDM 198
Cdd:PRK08217  160 QTNYSASKAGVAAMTVTWAKELA-----RYGIrvaaIAPGVIETEM 200
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
14-227 4.48e-31

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 116.10  E-value: 4.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTG-IRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08933    13 IVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKfVPCDVTKEEDIKTLISVTVERFGRIDCLV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd08933    93 NNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHL-RKSQGNIINLSSLVGSIGQKQAAPYVATKGAITAMTK 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 173 AFARDyqDHPY-LRFNVLTPGMVPTDMINHFETVGPGGEA-IK--QLPRVLRIFGTTAE 227
Cdd:cd08933   172 ALAVD--ESRYgVRVNCISPGNIWTPLWEELAAQTPDTLAtIKegELAQLLGRMGTEAE 228
PRK05867 PRK05867
SDR family oxidoreductase;
7-199 1.18e-30

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 114.75  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK05867    6 DLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQII---NLSGGGAKRAQRfLSAYST 162
Cdd:PRK05867   86 GIDIAVCNAGIIT-VTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIIntaSMSGHIINVPQQ-VSHYCA 163
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1498198613 163 SKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:PRK05867  164 SKAAVIHLTKAMAVELAPHK-IRVNSVSPGYILTELV 199
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
13-198 1.29e-30

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 114.94  E-value: 1.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08945     6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPY--MIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:cd08945    86 NNAGRSGG-GATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVGF 164
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 171 TEAFARDYQdHPYLRFNVLTPGMVPTDM 198
Cdd:cd08945   165 TKALGLELA-RTGITVNAVCPGFVETPM 191
PRK07814 PRK07814
SDR family oxidoreductase;
8-196 1.58e-30

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 114.88  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGISGPFGYaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQR-NGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK07814   88 LDIVVNNVGGTMPNPL-LSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTAKAA 166
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 167 IVRLTEAFARDYQdhPYLRFNVLTPGMVPT 196
Cdd:PRK07814  167 LAHYTRLAALDLC--PRIRVNAIAPGSILT 194
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
8-199 1.91e-30

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 114.70  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIIS--STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:cd05355    24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEF 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:cd05355   104 GKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKG 181
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:cd05355   182 AIVAFTRGLSLQLAEKG-IRVNAVAPGPIWTPLI 214
PRK05872 PRK05872
short chain dehydrogenase; Provisional
2-266 2.06e-30

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 115.07  E-value: 2.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   2 ARTPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTgIRCDVANRNEVEALASAA 81
Cdd:PRK05872    1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLT-VVADVTDLAAMQAAAEEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  82 VERMGRIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRnGQIINLSGGGAKRAQRFLSAYS 161
Cdd:PRK05872   80 VERFGGIDVVVANAGIA-SGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 162 TSKAAIvrltEAFARDyqdhpyLRFNVLT---------PGMVPTDMINHFETVGPGGEAIKQ-LPRVLRIfGTTAEETAE 231
Cdd:PRK05872  158 ASKAGV----EAFANA------LRLEVAHhgvtvgsayLSWIDTDLVRDADADLPAFRELRArLPWPLRR-TTSVEKCAA 226
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1498198613 232 lalRIVR--EGKNGQVFevMPRHRTIWRLLKAALARR 266
Cdd:PRK05872  227 ---AFVDgiERRARRVY--APRWVRLMQWLRPVLVTR 258
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
14-198 2.13e-30

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 113.92  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQ--VIISSTNPTNLTEAERALQAaGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05367     3 ILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQR-NGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:cd05367    82 INNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAARDMF 161
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 171 TEAFARDYQDhpyLRFNVLTPGMVPTDM 198
Cdd:cd05367   162 FRVLAAEEPD---VRVLSYAPGVVDTDM 186
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
7-199 2.38e-30

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 114.02  E-value: 2.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd05341     2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILD---EEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:cd05341    79 RLDVLVNNAGILTG-GTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGA 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 167 IVRLTEAFARDYQDHPY-LRFNVLTPGMVPTDMI 199
Cdd:cd05341   158 VRGLTKSAALECATQGYgIRVNSVHPGYIYTPMT 191
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
13-249 3.02e-30

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 114.08  E-value: 3.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTE--AERALQAAGLNVTgIRCDVANRNEVEAL-ASAAVERMGRID 89
Cdd:cd09763     6 ALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPgtAEEIEARGGKCIP-VRCDHSDDDEVEALfERVAREQQGRLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNA---------GISGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRaQRFLSAY 160
Cdd:cd09763    85 ILVNNAyaavqlilvGVAKPF---WEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLE-YLFNVAY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 161 STSKAAIVRLTEAFARDYQDHpylrfNV----LTPGMVPTDMI-NHFETvgPGGEAIKQLPRVLRifgttAEETAELALR 235
Cdd:cd09763   161 GVGKAAIDRMAADMAHELKPH-----GVavvsLWPGFVRTELVlEMPED--DEGSWHAKERDAFL-----NGETTEYSGR 228
                         250       260
                  ....*....|....*....|..
gi 1498198613 236 IVRE--------GKNGQVFEVM 249
Cdd:cd09763   229 CVVAlaadpdlmELSGRVLITG 250
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-248 3.83e-30

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 113.28  E-value: 3.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTN-PTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK06077    3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKrAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK06077   83 GVADILVNNAGL-GLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 166 AIVRLTEAFARDYQdhPYLRFNVLTPGMVPTDMINH-FETVG-PGGEAIKQLPRVLRIFgtTAEETAELALRIVR-EGKN 242
Cdd:PRK06077  160 AVINLTKYLALELA--PKIRVNAIAPGFVKTKLGESlFKVLGmSEKEFAEKFTLMGKIL--DPEEVAEFVAAILKiESIT 235

                  ....*.
gi 1498198613 243 GQVFEV 248
Cdd:PRK06077  236 GQVFVL 241
PRK08589 PRK08589
SDR family oxidoreductase;
8-200 5.65e-30

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 113.33  E-value: 5.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNpTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK08589    4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIA-EAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQrNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:PRK08589   83 VDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTSSFSGQAADLYRSGYNAAKGAV 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 168 VRLTEAFARDYQDHPyLRFNVLTPGMVPTDMIN 200
Cdd:PRK08589  162 INFTKSIAIEYGRDG-IRANAIAPGTIETPLVD 193
PRK12827 PRK12827
short chain dehydrogenase; Provisional
13-201 6.45e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 112.89  E-value: 6.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNP-TNLTEAERALQ---AAGLNVTGIRCDVANRNEVEALASAAVERMGRI 88
Cdd:PRK12827    9 VLITGGSGGLGRAIAVRLAADGADVIVLDIHPmRGRAEADAVAAgieAAGGKALGLAFDVRDFAATRAALDAGVEEFGRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  89 DLWVNNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIK-QRNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:PRK12827   89 DILVNNAGIATDAAFA-ELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYAASKAGL 167
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 168 VRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINH 201
Cdd:PRK12827  168 IGLTKTLANELAPRG-ITVNAVAPGAINTPMADN 200
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
7-177 7.56e-30

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 113.18  E-value: 7.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtNLTEAEralqaaglNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK06171    6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHG-GDGQHE--------NYQFVPTDVSSAEEVNHTVAEIIEKFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPF----------GYALDIPpdAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRF 156
Cdd:PRK06171   77 RIDGLVNNAGINIPRllvdekdpagKYELNEA--AFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEG 154
                         170       180
                  ....*....|....*....|.
gi 1498198613 157 LSAYSTSKAAIVRLTEAFARD 177
Cdd:PRK06171  155 QSCYAATKAALNSFTRSWAKE 175
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
15-249 1.04e-29

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 112.18  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaagLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVNN 94
Cdd:COG3967    10 ITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAAN----PGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  95 AGISGPfgYALDIPPDAWEQV---IRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:COG3967    86 AGIMRA--EDLLDEAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 172 EAfardyqdhpyLRF-----NV----LTPGMVPTDMINHFETvGPGG----EAIKQlprVLRIFGTTAEE----TAELAL 234
Cdd:COG3967   164 QS----------LRHqlkdtSVkvieLAPPAVDTDLTGGQGG-DPRAmpldEFADE---VMAGLETGKYEilvgRVKLLR 229
                         250
                  ....*....|....*
gi 1498198613 235 RIVREGKNgQVFEVM 249
Cdd:COG3967   230 FAERLGPY-AAFAIM 243
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
13-200 1.97e-29

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 111.40  E-value: 1.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVI-ISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK12824    5 ALVTGAKRGIGSAIARELLNDGYRVIaTYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK12824   85 VNNAGITRDSVF-KRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGFT 163
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 172 EAFARdyQDHPY-LRFNVLTPGMVPTDMIN 200
Cdd:PRK12824  164 KALAS--EGARYgITVNCIAPGYIATPMVE 191
PRK07478 PRK07478
short chain dehydrogenase; Provisional
8-234 2.05e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 111.56  E-value: 2.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK07478    4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS---GGGAKRAQrfLSAYSTSK 164
Cdd:PRK07478   84 LDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTStfvGHTAGFPG--MAAYAASK 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIKQLPRVLRIfgTTAEETAELAL 234
Cdd:PRK07478  162 AGLIGLTQVLAAEYGAQG-IRVNALLPGGTDTPMGRAMGDTPEALAFVAGLHALKRM--AQPEEIAQAAL 228
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
13-254 2.76e-29

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 111.55  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLN--VTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:cd05327     4 VVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNakVEVIQLDLSSLASVRQFAEEFLARFPRLDI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGI-SGPFGYAldipPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRA----QRFLS------- 158
Cdd:cd05327    84 LINNAGImAPPRRLT----KDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGpidfNDLDLennkeys 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 159 ---AYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVgpggeaiKQLPRVLRIFGT-TAEETAELAL 234
Cdd:cd05327   160 pykAYGQSKLANILFTRELARRLEGTG-VTVNALHPGVVRTELLRRNGSF-------FLLYKLLRPFLKkSPEQGAQTAL 231
                         250       260
                  ....*....|....*....|....*...
gi 1498198613 235 RIV----REGKNGQVF----EVMPRHRT 254
Cdd:cd05327   232 YAAtspeLEGVSGKYFsdckIKMSSSEA 259
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
1-196 3.21e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 111.01  E-value: 3.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   1 MARTPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASA 80
Cdd:PRK07523    1 MSLNLFDLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  81 AVERMGRIDLWVNNAGISgpFGYAL-DIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSA 159
Cdd:PRK07523   81 FEAEIGPIDILVNNAGMQ--FRTPLeDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAP 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1498198613 160 YSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK07523  159 YTATKGAVGNLTKGMATDWAKHG-LQCNAIAPGYFDT 194
PRK08267 PRK08267
SDR family oxidoreductase;
15-241 5.07e-29

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 110.80  E-value: 5.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLnVTGiRCDVANRNEVE-ALASAAVERMGRIDLWVN 93
Cdd:PRK08267    6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNA-WTG-ALDVTDRAAWDaALADFAAATGGRLDVLFN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGI--SGPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK08267   84 NAGIlrGGPFE---DIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDMINHfetvGPGGEAIKQLPRV-LRIfgtTAEETAELALRIVREGK 241
Cdd:PRK08267  161 EALDLEWRRHG-IRVADVMPLFVDTAMLDG----TSNEVDAGSTKRLgVRL---TPEDVAEAVWAAVQHPT 223
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
13-192 6.28e-29

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 110.51  E-value: 6.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNL--TEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:PRK12384    5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAanVAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGRVDL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISgpfgYALDI---PPDAWEQVIRVNLLGTYYGCRAALPYMIKQR-NGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK12384   85 LVYNAGIA----KAAFItdfQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFG 160
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPG 192
Cdd:PRK12384  161 GVGLTQSLALDLAEYG-ITVHSLMLG 185
PRK12937 PRK12937
short chain dehydrogenase; Provisional
13-218 1.02e-28

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 109.45  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK12937    8 AIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRIDVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK12937   88 VNNAGVMPLGTIA-DFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKAAVEGLV 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDMINHfetvGPGGEAIKQLPRV 218
Cdd:PRK12937  165 HVLANELRGRG-ITVNAVAPGPVATELFFN----GKSAEQIDQLAGL 206
PRK06198 PRK06198
short chain dehydrogenase; Provisional
5-197 1.04e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 109.71  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   5 PSDLRDLKAVVTGGSRGIGRAIAEALARAGAQ-VIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVE 83
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  84 RMGRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQR-NGQIINLSGGGAKRAQRFLSAYST 162
Cdd:PRK06198   81 AFGRLDALVNAAGLTDR-GTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHGGQPFLAAYCA 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1498198613 163 SKAAIVRLTE--AFA--RDyqdhpYLRFNVLTPGMVPTD 197
Cdd:PRK06198  160 SKGALATLTRnaAYAllRN-----RIRVNGLNIGWMATE 193
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
13-198 1.34e-28

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 109.10  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAaglnvtgIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRL-------TPLDVADAAAVREVCSRLLAEHGPIDALV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd05331    74 NCAGVLRP-GATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152
                         170       180
                  ....*....|....*....|....*..
gi 1498198613 173 AFARDYQdhPY-LRFNVLTPGMVPTDM 198
Cdd:cd05331   153 CLGLELA--PYgVRCNVVSPGSTDTAM 177
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
13-198 1.73e-28

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 109.28  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPT-NLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK12745    5 ALVTGGRRGIGLGIARALAAAGFDLAINDRPDDeELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPF-GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQ------IINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK12745   85 VNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVSPNRGEYCISK 164
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 165 AAIVRLTEAFARDYQDHPYLRFNVlTPGMVPTDM 198
Cdd:PRK12745  165 AGLSMAAQLFAARLAEEGIGVYEV-RPGLIKTDM 197
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
12-216 2.10e-28

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 108.16  E-value: 2.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAeralQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05370     7 TVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEA----KKELPNIHTIVLDVGDAESVEALAEALLSEYPNLDIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYA-LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAkraqrFLS-----AYSTSKA 165
Cdd:cd05370    83 INNAGIQRPIDLRdPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLA-----FVPmaanpVYCATKA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1498198613 166 AIVRLTEAFaRDYQDHPYLRFNVLTPGMVPTDMinHFETVGPGGEAIKQLP 216
Cdd:cd05370   158 ALHSYTLAL-RHQLKDTGVEVVEIVPPAVDTEL--HEERRNPDGGTPRKMP 205
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
8-198 2.13e-28

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 108.86  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnltEAERAL-QAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINL----EAARATaAEIGPAACAISLDVTDQASIDRCVAALVDRWG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGIsgpFGYA--LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:cd05363    77 SIDILVNNAAL---FDLApiVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCAT 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:cd05363   154 KAAVISLTQSAGLNLIRHG-INVNAIAPGVVDGEH 187
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
13-244 2.20e-28

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 108.15  E-value: 2.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAG-AQVIISSTNPTNLTEAErALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELA-ALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFL---SAYSTSKAAIV 168
Cdd:cd05325    80 INNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDNTSggwYSYRASKAALN 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1498198613 169 RLTEAFARDYQDHPyLRFNVLTPGMVPTDMinhfetvgpGGEAIKQLPRVlrifgtTAEETAELALRIVREGKNGQ 244
Cdd:cd05325   160 MLTKSLAVELKRDG-ITVVSLHPGWVRTDM---------GGPFAKNKGPI------TPEESVAGLLKVIDNLNEED 219
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
13-198 2.89e-28

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 108.66  E-value: 2.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK08643    5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNVVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK08643   85 NNAGV-APTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLgHGGKIINATSQAGVVGNPELAVYSSTKFAVRGLT 163
                         170       180
                  ....*....|....*....|....*..
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK08643  164 QTAARDLASEG-ITVNAYAPGIVKTPM 189
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
13-196 8.34e-28

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 106.89  E-value: 8.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd09761     4 AIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAE---GPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQrNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd09761    81 NNAARGSK-GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKN-KGRIINIASTRAFQSEPDSEAYAASKGGLVALTH 158
                         170       180
                  ....*....|....*....|....
gi 1498198613 173 AFARDYQdhPYLRFNVLTPGMVPT 196
Cdd:cd09761   159 ALAMSLG--PDIRVNCISPGWINT 180
PRK07890 PRK07890
short chain dehydrogenase; Provisional
14-192 1.10e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 106.97  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK07890    9 VVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEA 173
Cdd:PRK07890   89 NAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAKGALLAASQS 167
                         170
                  ....*....|....*....
gi 1498198613 174 FARDYQDHPyLRFNVLTPG 192
Cdd:PRK07890  168 LATELGPQG-IRVNSVAPG 185
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
13-195 1.28e-27

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 106.65  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLN-VTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd08930     5 ILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNrVIALELDITSKESIKELIESYLEKFGRIDIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISgPFGYAL---DIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS---GGGA------KRAQRFLSA 159
Cdd:cd08930    85 INNAYPS-PKVWGSrfeEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIAsiyGVIApdfriyENTQMYSPV 163
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1498198613 160 -YSTSKAAIVRLTEAFARDYQDHpYLRFNVLTPGMVP 195
Cdd:cd08930   164 eYSVIKAGIIHLTKYLAKYYADT-GIRVNAISPGGIL 199
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
7-197 1.55e-27

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 107.29  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK08277    7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPFGYA--------------LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKR 152
Cdd:PRK08277   87 PCDILINGAGGNHPKATTdnefhelieptktfFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFT 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1498198613 153 AQRFLSAYSTSKAAIVRLTEAFARDYQdHPYLRFNVLTPGMVPTD 197
Cdd:PRK08277  167 PLTKVPAYSAAKAAISNFTQWLAVHFA-KVGIRVNAIAPGFFLTE 210
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
13-199 5.30e-27

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 105.24  E-value: 5.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQV-IISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05337     4 AIVTGASRGIGRAIATELAARGFDIaINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISG-PFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRN------GQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:cd05337    84 VNNAGIAVrPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNRGEYCISK 163
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 165 AAIVRLTEAFARDYQDHPYLRFNVlTPGMVPTDMI 199
Cdd:cd05337   164 AGLSMATRLLAYRLADEGIAVHEI-RPGLIHTDMT 197
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
7-234 5.62e-27

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 104.87  E-value: 5.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd08942     3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERSD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISgpFGYALD-IPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQ----IINL---SGGGAKRAQRFls 158
Cdd:cd08942    82 RLDVLVNNAGAT--WGAPLEaFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAEnparVINIgsiAGIVVSGLENY-- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198613 159 AYSTSKAAIVRLTEAFARDYQDHpYLRFNVLTPGMVPTDMINHFETVGPGGEAI-KQLPrvLRIFGtTAEETAELAL 234
Cdd:cd08942   158 SYGASKAAVHQLTRKLAKELAGE-HITVNAIAPGRFPSKMTAFLLNDPAALEAEeKSIP--LGRWG-RPEDMAGLAI 230
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
8-251 1.07e-26

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 104.13  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAG-LNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd05343     4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGyPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRN---GQIINLSGGGAKRA--QRFLSAYS 161
Cdd:cd05343    84 GVDVCINNAGLARP-EPLLSGKTEGWKEMFDVNVLALSICTREAYQSM-KERNvddGHIININSMSGHRVppVSVFHFYA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 162 TSKAAIVRLTEAF---ARDYQDHpyLRFNVLTPGMVPTDMI-NHFETVGPGGEAIKQLPRVLRifgttAEETAELALRIV 237
Cdd:cd05343   162 ATKHAVTALTEGLrqeLREAKTH--IRATSISPGLVETEFAfKLHDNDPEKAAATYESIPCLK-----PEDVANAVLYVL 234
                         250
                  ....*....|....
gi 1498198613 238 REGKNGQVFEVMPR 251
Cdd:cd05343   235 STPPHVQIHDILLR 248
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
13-198 1.09e-26

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 103.84  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERAL-QAAGLNVTGIRCDVANRNEV-EALASAAVERmgRIDL 90
Cdd:cd05356     4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIeEKYGVETKTIAADFSAGDDIyERIEKELEGL--DIGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISGPF-GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:cd05356    82 LVNNVGISHSIpEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDF 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 170 LTEAFARDYQDHpylrfNV----LTPGMVPTDM 198
Cdd:cd05356   162 FSRALYEEYKSQ-----GIdvqsLLPYLVATKM 189
PRK07831 PRK07831
SDR family oxidoreductase;
8-191 1.22e-26

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 104.35  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGS-RGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA-GLN-VTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK07831   15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAElGLGrVEAVVCDVTSEAQVDALIDAAVER 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:PRK07831   95 LGRLDVLVNNAGLGGQ-TPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARgHGGVIVNNASVLGWRAQHGQAHYAAA 173
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTP 191
Cdd:PRK07831  174 KAGVMALTRCSALEAAEYG-VRINAVAP 200
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
7-197 1.98e-26

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 104.08  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd08935     2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPFGYA-------------LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRA 153
Cdd:cd08935    82 TVDILINGAGGNHPDATTdpehyepeteqnfFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1498198613 154 QRFLSAYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:cd08935   162 LTKVPAYSAAKAAVSNFTQWLAVEFATTG-VRVNAIAPGFFVTP 204
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
13-196 2.02e-26

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 103.31  E-value: 2.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNltEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd05349     3 VLVTGASRGLGAAIARSFAREGARVVVNYYRSTE--SAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPF-----GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:cd05349    81 NNALIDFPFdpdqrKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAAL 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 168 VRLTEAFARDYQdhPY-LRFNVLTPGMVPT 196
Cdd:cd05349   161 LGFTRNMAKELG--PYgITVNMVSGGLLKV 188
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
7-198 2.19e-26

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 103.43  E-value: 2.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNptnlteaerALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK08220    5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQA---------FLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK08220   76 PLDVLVNAAGIL-RMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAA 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 167 IVRLTEAFARDYQdhPY-LRFNVLTPGMVPTDM 198
Cdd:PRK08220  155 LTSLAKCVGLELA--PYgVRCNVVSPGSTDTDM 185
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
13-191 2.58e-26

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 107.62  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK08324  425 ALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEAALAFGGVDIVV 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRN-GQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK08324  504 SNAGIAIS-GPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNPGPNFGAYGAAKAAELHLV 582
                         170       180
                  ....*....|....*....|
gi 1498198613 172 EAFARDYQDHPyLRFNVLTP 191
Cdd:PRK08324  583 RQLALELGPDG-IRVNGVNP 601
PRK07060 PRK07060
short chain dehydrogenase; Provisional
14-198 2.71e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 103.26  E-value: 2.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNptnltEAERALQAAGLNVTGIRCDVANrnevEALASAAVERMGRIDLWVN 93
Cdd:PRK07060   13 LVTGASSGIGRACAVALAQRGARVVAAARN-----AAALDRLAGETGCEPLRLDVGD----DAAIRAALAAAGAFDGLVN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGISGPFGyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK07060   84 CAGIASLES-ALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITR 162
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK07060  163 VLCVELGPHG-IRVNSVNPTVTLTPM 187
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
15-206 2.89e-26

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 102.53  E-value: 2.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAglNVTGIRCDVANRNEVE-ALASAAVERMGRIDLWVN 93
Cdd:cd08931     5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAE--NVVAGALDVTDRAAWAaALADFAAATGGRLDALFN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEA 173
Cdd:cd08931    83 NAGV-GRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEA 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 174 FARDYQDHPyLRFNVLTPGMVPTDMINHFETVG 206
Cdd:cd08931   162 LDVEWARHG-IRVADVWPWFVDTPILTKGETGA 193
PRK06114 PRK06114
SDR family oxidoreductase;
7-198 3.30e-26

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 102.94  E-value: 3.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQV-IISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK06114    5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVaLFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFL--SAYSTS 163
Cdd:PRK06114   85 GALTLAVNAAGIANA-NPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGLlqAHYNAS 163
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK06114  164 KAGVIHLSKSLAMEWVGRG-IRVNSISPGYTATPM 197
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
13-198 6.57e-26

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 102.02  E-value: 6.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTE--AERALQAAGlnVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDElkAELLNPNPS--VEVEILDVTDEERNQLVIAELEAELGGLDL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:cd05350    79 VIINAGVGKG-TSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSL 157
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 171 TEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:cd05350   158 AESLRYDVKKRG-IRVTVINPGFIDTPL 184
PRK07069 PRK07069
short chain dehydrogenase; Validated
12-217 7.41e-26

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 102.10  E-value: 7.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnltEAERALQAAGLNVT-------GIRCDVANRNEVEALASAAVER 84
Cdd:PRK07069    1 RAFITGAAGGLGRAIARRMAEQGAKVFLTDIND----AAGLDAFAAEINAAhgegvafAAVQDVTDEAQWQALLAQAADA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK07069   77 MGGLSVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1498198613 165 AAIVRLTEAFARDYQDHPY-LRFNVLTPGMVPTDMINH-FETVGPgGEAIKQLPR 217
Cdd:PRK07069  156 AAVASLTKSIALDCARRGLdVRCNSIHPTFIRTGIVDPiFQRLGE-EEATRKLAR 209
PRK07201 PRK07201
SDR family oxidoreductase;
14-176 1.10e-25

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 105.80  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK07201  375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVN 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAG------ISGPFGYALDippdaWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAK-RAQRFlSAYSTSKAA 166
Cdd:PRK07201  455 NAGrsirrsVENSTDRFHD-----YERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQtNAPRF-SAYVASKAA 528
                         170
                  ....*....|
gi 1498198613 167 IvrltEAFAR 176
Cdd:PRK07201  529 L----DAFSD 534
PRK06914 PRK06914
SDR family oxidoreductase;
13-173 1.11e-25

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 102.41  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNlteAERAL-QAAGLNVTG----IRCDVANRNEVEAlASAAVERMGR 87
Cdd:PRK06914    6 AIVTGASSGFGLLTTLELAKKGYLVIATMRNPEK---QENLLsQATQLNLQQnikvQQLDVTDQNSIHN-FQLVLKEIGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGIS-GpfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK06914   82 IDLLVNNAGYAnG--GFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYA 159

                  ....*..
gi 1498198613 167 IVRLTEA 173
Cdd:PRK06914  160 LEGFSES 166
PRK05876 PRK05876
short chain dehydrogenase; Provisional
13-205 1.20e-25

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 101.96  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK05876    9 AVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGI--SGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRF-LSAYSTSKAAIVR 169
Cdd:PRK05876   89 SNAGIvvGGPI---VEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAgLGAYGVAKYGVVG 165
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETV 205
Cdd:PRK05876  166 LAETLAREVTADG-IGVSVLCPMVVETNLVANSERI 200
PRK06179 PRK06179
short chain dehydrogenase; Provisional
13-188 1.27e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 101.90  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTnlteaeRALQAAGlnVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06179    7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPA------RAAPIPG--VELLELDVTDDASVQAAVDEVIARAGRIDVLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGggakrAQRFLSA-----YSTSKAAI 167
Cdd:PRK06179   79 NNAGV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISS-----VLGFLPApymalYAASKHAV 152
                         170       180
                  ....*....|....*....|.
gi 1498198613 168 VRLTEAFardyqDHPYLRFNV 188
Cdd:PRK06179  153 EGYSESL-----DHEVRQFGI 168
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
13-192 3.51e-25

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 100.40  E-value: 3.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTnLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK12823   11 VVVTGAAQGIGRGVALRAAAEGARVVLVDRSEL-VHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDVLI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIS---GPFG-YAldipPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG---GGAKRAqrflsAYSTSKA 165
Cdd:PRK12823   90 NNVGGTiwaKPFEeYE----EEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSiatRGINRV-----PYSAAKG 160
                         170       180
                  ....*....|....*....|....*..
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPG 192
Cdd:PRK12823  161 GVNALTASLAFEYAEHG-IRVNAVAPG 186
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
13-202 3.85e-25

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 100.18  E-value: 3.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK08063    7 ALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK08063   87 VNNAA-SGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAALEALT 165
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDMINHF 202
Cdd:PRK08063  166 RYLAVELAPKG-IAVNAVSGGAVDTDALKHF 195
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
13-254 4.45e-25

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 100.05  E-value: 4.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA-GLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05346     3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKfPVKVLPLQLDVSDRESIEAALENLPEEFRDIDIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:cd05346    83 VNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDminhFETVGPGGEAIKQLPRVLRIFGTTAEETAELALRIVREGKNGQV--FEVM 249
Cdd:cd05346   163 LNLRKDLIGTG-IRVTNIEPGLVETE----FSLVRFHGDKEKADKVYEGVEPLTPEDIAETILWVASRPAHVNIndIEIM 237

                  ....*
gi 1498198613 250 PRHRT 254
Cdd:cd05346   238 PVNQA 242
PRK08265 PRK08265
short chain dehydrogenase; Provisional
6-192 6.25e-25

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 99.70  E-value: 6.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNlteAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK08265    2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADN---GAAVAASLGERARFIATDITDDAAIERAVATVVARF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRNGQIINLSGGGAKRAQ--RFLsaYSTS 163
Cdd:PRK08265   79 GRVDILVNLACTYLDDG--LASSRADWLAALDVNLVSAAMLAQAAHPHL-ARGGGAIVNFTSISAKFAQtgRWL--YPAS 153
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 164 KAAIVRLTEAFARDY-QDHpyLRFNVLTPG 192
Cdd:PRK08265  154 KAAIRQLTRSMAMDLaPDG--IRVNSVSPG 181
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
13-195 7.33e-25

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 98.89  E-value: 7.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05357     3 ALVTGAAKRIGRAIAEALAAEGYRVVVHyNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:cd05357    83 VNNASAFYP-TPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLT 161
                         170       180
                  ....*....|....*....|....
gi 1498198613 172 EAFARDYQdhPYLRFNVLTPGMVP 195
Cdd:cd05357   162 RSAALELA--PNIRVNGIAPGLIL 183
PRK07677 PRK07677
short chain dehydrogenase; Provisional
14-233 1.03e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 98.98  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK07677    5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALIN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAgiSGPF-GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK07677   85 NA--AGNFiCPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKgIKGNIINMVATYAWDAGPGVIHSAAAKAGVLAMT 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1498198613 172 EAFARDYQDHPYLRFNVLTPGmvPTDMINHFETVGPGGEA----IKQLPrvLRIFGTTaEETAELA 233
Cdd:PRK07677  163 RTLAVEWGRKYGIRVNAIAPG--PIERTGGADKLWESEEAakrtIQSVP--LGRLGTP-EEIAGLA 223
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
8-198 1.42e-24

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 98.67  E-value: 1.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK08085    7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGIS--GPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK08085   87 IDVLINNAGIQrrHPF---TEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKG 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK08085  164 AVKMLTRGMCVELARHN-IQVNGIAPGYFKTEM 195
PRK06523 PRK06523
short chain dehydrogenase; Provisional
5-197 1.61e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 98.82  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   5 PSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISS-TNPTNLTEAeralqaaglnVTGIRCDVANRNEVEALASAAVE 83
Cdd:PRK06523    4 FLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTArSRPDDLPEG----------VEFVAADLTTAEGCAAVARAVLE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  84 RMGRIDLWVNNAGIS-GPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGggakrAQRFL----- 157
Cdd:PRK06523   74 RLGGVDILVHVLGGSsAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTS-----IQRRLplpes 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1498198613 158 -SAYSTSKAAIVRLTEAFARDYQdhPY-LRFNVLTPGMVPTD 197
Cdd:PRK06523  149 tTAYAAAKAALSTYSKSLSKEVA--PKgVRVNTVSPGWIETE 188
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
7-198 1.62e-24

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 98.31  E-value: 1.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLteaeRALQAAGLNVTGIRCDVANRNEVEalasAAVERMG 86
Cdd:cd05351     4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADL----DSLVRECPGIEPVCVDLSDWDATE----EALGSVG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGIS--GPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMI-KQRNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:cd05351    76 PVDLLVNNAAVAilQPF---LEVTKEAFDRSFDVNVRAVIHVSQIVARGMIaRGVPGSIVNVSSQASQRALTNHTVYCST 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:cd05351   153 KAALDMLTKVMALELGPHK-IRVNSVNPTVVMTDM 186
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
13-196 3.33e-24

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 97.98  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERaLQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08937     7 VVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAE-ILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDVLI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAG---ISGPFGYaldIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRflSAYSTSKAAIVR 169
Cdd:cd08937    86 NNVGgtiWAKPYEH---YEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIYR--IPYSAAKGGVNA 160
                         170       180
                  ....*....|....*....|....*..
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:cd08937   161 LTASLAFEHARDG-IRVNAVAPGGTEA 186
PRK06701 PRK06701
short chain dehydrogenase; Provisional
8-199 4.10e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 98.18  E-value: 4.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTN-LTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK06701   44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:PRK06701  124 RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSATKGA 201
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 167 IVRLTEAFARDY-QDHpyLRFNVLTPGMVPTDMI 199
Cdd:PRK06701  202 IHAFTRSLAQSLvQKG--IRVNAVAPGPIWTPLI 233
PRK09242 PRK09242
SDR family oxidoreductase;
8-191 4.17e-24

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 97.51  E-value: 4.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA--GLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK09242    7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEfpEREVHGLAADVSDDEDRRAILDWVEDHW 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK09242   87 DGLHILVNNAGGNIR-KAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKA 165
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTP 191
Cdd:PRK09242  166 ALLQMTRNLAVEWAEDG-IRVNAVAP 190
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
13-240 4.29e-24

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 97.38  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEA-ERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK12935    9 AIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENlVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDIL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK12935   89 VNNAGITRDRTFK-KLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGFT 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 172 EAFARDYQdHPYLRFNVLTPGMVPTDMINHF-ETVgpGGEAIKQLPRvlRIFGtTAEETAELALRIVREG 240
Cdd:PRK12935  168 KSLALELA-KTNVTVNAICPGFIDTEMVAEVpEEV--RQKIVAKIPK--KRFG-QADEIAKGVVYLCRDG 231
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
13-177 6.53e-24

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 97.08  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIsstNPTNLTEAERAL-QAAGLNVTGIRCDVANRNEVEALASAAVERMGR-IDL 90
Cdd:PRK08642    8 VLVTGGSRGLGAAIARAFAREGARVVV---NYHQSEDAAEALaDELGDRAIALQADVTDREQVQAMFATATEHFGKpITT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISGPF-GYALDIPPD-AWE---QVIRVNLLGTYYGCRAALPYMIKQRNGQIINLsggGAKRAQRFLSA---YST 162
Cdd:PRK08642   85 VVNNALADFSFdGDARKKADDiTWEdfqQQLEGSVKGALNTIQAALPGMREQGFGRIINI---GTNLFQNPVVPyhdYTT 161
                         170
                  ....*....|....*
gi 1498198613 163 SKAAIVRLTEAFARD 177
Cdd:PRK08642  162 AKAALLGLTRNLAAE 176
PRK06484 PRK06484
short chain dehydrogenase; Validated
2-206 1.12e-23

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 99.92  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   2 ARTPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTnltEAERALQAAGLNVTGIRCDVANRNEVEALASAA 81
Cdd:PRK06484  261 APSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAE---GAKKLAEALGDEHLSVQADITDEAAVESAFAQI 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  82 VERMGRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKqrNGQIINLSGGGAKRAQRFLSAYS 161
Cdd:PRK06484  338 QARWGRLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQ--GGVIVNLGSIASLLALPPRNAYC 415
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1498198613 162 TSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVG 206
Cdd:PRK06484  416 ASKAAVTMLSRSLACEWAPAG-IRVNTVAPGYIETPAVLALKASG 459
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
6-216 1.22e-23

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 96.56  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK06200    2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF---GDHVLVVEGDVTSYADNQRAVDQTVDAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGYALDIPPD----AWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS------GGGAkraqr 155
Cdd:PRK06200   79 GKLDCFVGNAGIWDYNTSLVDIPAEtldtAFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSnssfypGGGG----- 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498198613 156 flSAYSTSKAAIVRLTEAFArdYQDHPYLRFNVLTPGMVPTDMiNHFETVGPGGEAIKQLP 216
Cdd:PRK06200  154 --PLYTASKHAVVGLVRQLA--YELAPKIRVNGVAPGGTVTDL-RGPASLGQGETSISDSP 209
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
15-198 1.69e-23

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 95.71  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGI-RCDV--ANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK08945   17 VTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIiPLDLltATPQNYQQLADTIEEQFGRLDGV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK08945   97 LHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVSKFATEGMM 176
                         170       180
                  ....*....|....*....|....*..
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK08945  177 QVLADEYQGTN-LRVNCINPGGTRTAM 202
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
8-198 1.71e-23

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 95.34  E-value: 1.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAG---LNVTGIRCDVANRNEVEALASAAVER 84
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGgrqPQWFILDLLTCTSENCQQLAQRIAVN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:cd05340    82 YPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSK 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:cd05340   162 FATEGL*QVLADEYQQRN-LRVNCINPGGTRTAM 194
PRK08263 PRK08263
short chain dehydrogenase; Provisional
15-175 2.17e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 95.88  E-value: 2.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTE-AERAlqaaGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK08263    8 ITGASRGFGRAWTEAALERGDRVVATARDTATLADlAEKY----GDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEA 173
Cdd:PRK08263   84 NAGY-GLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSEA 162

                  ..
gi 1498198613 174 FA 175
Cdd:PRK08263  163 LA 164
PRK07062 PRK07062
SDR family oxidoreductase;
7-196 2.75e-23

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 95.49  E-value: 2.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA--GLNVTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK07062    5 QLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKfpGARLLAARCDVLDEADVAAFAAAVEAR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGIS--GPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYST 162
Cdd:PRK07062   85 FGGVDMLVNNAGQGrvSTFA---DTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSA 161
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 163 SKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK07062  162 ARAGLLNLVKSLATELAPKG-VRVNSILLGLVES 194
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
13-207 2.80e-23

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 95.22  E-value: 2.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNlteAERALQAA----GLNVTGIRCDVANRNEVEALASAAVERMGRI 88
Cdd:cd05322     5 AVVIGGGQTLGEFLCHGLAEAGYDVAVADINSEN---AEKVADEInaeyGEKAYGFGADATNEQSVIALSKGVDEIFKRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  89 DLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRN-GQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:cd05322    82 DLLVYSAGIAKS-AKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFGG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1498198613 168 VRLTEAFARDYQDHPyLRFNVLTPG-MVPTDMinhFETVGP 207
Cdd:cd05322   161 VGLTQSLALDLAEHG-ITVNSLMLGnLLKSPM---FQSLLP 197
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
8-203 2.86e-23

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 94.78  E-value: 2.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGA-QVIISSTNPTNLTEAEralQAAGLNVTGIRCDVANRNEVEALASAAVErmg 86
Cdd:cd05354     1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLV---AKYGDKVVPLRLDVTDPESIKAAAAQAKD--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 rIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAA 166
Cdd:cd05354    75 -VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSA 153
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1498198613 167 IVRLTEAFARDYQDHPYLRFNVlTPGMVPTDMINHFE 203
Cdd:cd05354   154 AYSLTQGLRAELAAQGTLVLSV-HPGPIDTRMAAGAG 189
PRK06949 PRK06949
SDR family oxidoreductase;
1-217 2.88e-23

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 95.21  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   1 MARTpSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASA 80
Cdd:PRK06949    1 MGRS-INLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  81 AVERMGRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNG--------QIINLSGGGAKR 152
Cdd:PRK06949   80 AETEAGTIDILVNNSGVSTT-QKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGagntkpggRIINIASVAGLR 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1498198613 153 AQRFLSAYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIKQLPR 217
Cdd:PRK06949  159 VLPQIGLYCMSKAAVVHMTRAMALEWGRHG-INVNAICPGYIDTEINHHHWETEQGQKLVSMLPR 222
PRK07576 PRK07576
short chain dehydrogenase; Provisional
13-234 3.25e-23

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 95.41  E-value: 3.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK07576   12 VVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIDVLV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 nnAGISGPF-GYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQrNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK07576   92 --SGAAGNFpAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRP-GASIIQISAPQAFVPMPMQAHVCAAKAGVDMLT 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1498198613 172 EAFARDYQDHPyLRFNVLTPGmvPTDMINHFETVGPGGEAIKQLPRV--LRIFGTTaEETAELAL 234
Cdd:PRK07576  169 RTLALEWGPEG-IRVNSIVPG--PIAGTEGMARLAPSPELQAAVAQSvpLKRNGTK-QDIANAAL 229
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-234 4.11e-23

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 94.26  E-value: 4.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVI-ISSTNPTNLTEAERALQAaglnvtgircDVanRNEVEALASAAverm 85
Cdd:PRK06550    2 EFMTKTVLITGAASGIGLAQARAFLAQGAQVYgVDKQDKPDLSGNFHFLQL----------DL--SDDLEPLFDWV---- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS--------GGGAkraqrfl 157
Cdd:PRK06550   66 PSVDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCsiasfvagGGGA------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 158 sAYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMiNH--FEtvgPGGEA---IKQLP--RvlrifGTTAEETA 230
Cdd:PRK06550  139 -AYTASKHALAGFTKQLALDYAKDG-IQVFGIAPGAVKTPM-TAadFE---PGGLAdwvARETPikR-----WAEPEEVA 207

                  ....
gi 1498198613 231 ELAL 234
Cdd:PRK06550  208 ELTL 211
PRK09135 PRK09135
pteridine reductase; Provisional
13-192 6.64e-23

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 94.22  E-value: 6.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNptnlTEAERALQAAGLN------VTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK09135    9 ALITGGARRIGAAIARTLHAAGYRVAIHYHR----SAAEADALAAELNalrpgsAAALQADLLDPDALPELVAACVAAFG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAG--ISGPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK09135   85 RLDALVNNASsfYPTPLG---SITEAQWDDLFASNLKAPFFLSQAAAPQL-RKQRGAIVNITDIHAERPLKGYPVYCAAK 160
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 165 AAIVRLTEAFARDYQdhPYLRFNVLTPG 192
Cdd:PRK09135  161 AALEMLTRSLALELA--PEVRVNAVAPG 186
PRK07832 PRK07832
SDR family oxidoreductase;
12-241 7.33e-23

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 94.34  E-value: 7.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRC-DVANRNEVEALASAAVERMGRIDL 90
Cdd:PRK07832    2 RCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAHGSMDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISGpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:PRK07832   82 VMNIAGISA-WGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAgRGGHLVNVSSAAGLVALPWHAAYSASKFGLRG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1498198613 170 LTEAFARDYQDHpYLRFNVLTPGMVPTDMINHFETVGPGGE--AIKQLPRVLRIFGTTAEETAELALRIVREGK 241
Cdd:PRK07832  161 LSEVLRFDLARH-GIGVSVVVPGAVKTPLVNTVEIAGVDREdpRVQKWVDRFRGHAVTPEKAAEKILAGVEKNR 233
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
7-216 9.72e-23

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 93.96  E-value: 9.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAEralQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:cd05348     1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELR---ADFGDAVVGVEGDVRSLADNERAVARCVERFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPFGYALDIPPD----AWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS-------GGGakraqr 155
Cdd:cd05348    78 KLDCFIGNAGIWDYSTSLVDIPEEkldeAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSnagfypgGGG------ 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498198613 156 flSAYSTSKAAIVRLTEAFArdYQDHPYLRFNVLTPGMVPTDMINhFETVGPGGEAIKQLP 216
Cdd:cd05348   152 --PLYTASKHAVVGLVKQLA--YELAPHIRVNGVAPGGMVTDLRG-PASLGQGETSISTPP 207
PRK06128 PRK06128
SDR family oxidoreductase;
12-196 1.01e-22

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 94.54  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIIS--STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:PRK06128   57 KALITGADSGIGRATAIAFAREGADIALNylPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLD 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:PRK06128  137 ILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTGSIQSYQPSPTLLDYASTKAAIVA 214
                         170       180
                  ....*....|....*....|....*..
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK06128  215 FTKALAKQVAEKG-IRVNAVAPGPVWT 240
PRK06124 PRK06124
SDR family oxidoreductase;
13-197 1.03e-22

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 93.62  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06124   14 ALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLDILV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK06124   94 NNVGARDRRPLA-ELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGLMR 172
                         170       180
                  ....*....|....*....|....*
gi 1498198613 173 AFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:PRK06124  173 ALAAEFGPHG-ITSNAIAPGYFATE 196
PRK08628 PRK08628
SDR family oxidoreductase;
7-234 2.01e-22

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 93.10  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGA-QVIISSTNPTNltEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK08628    4 NLKDKVVIVTGGASGIGAAISLRLAEEGAiPVIFGRSAPDD--EFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGpfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYmIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK08628   82 GRIDGLVNNAGVND--GVGLEAGREAFVASLERNLIHYYVMAHYCLPH-LKASRGAIVNISSKTALTGQGGTSGYAAAKG 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM----INHFETVGPGGEAIKQlprvlRI-FG---TTAEETAELAL 234
Cdd:PRK08628  159 AQLALTREWAVALAKDG-VRVNAVIPAEVMTPLyenwIATFDDPEAKLAAITA-----KIpLGhrmTTAEEIADTAV 229
PRK05875 PRK05875
short chain dehydrogenase; Provisional
8-199 3.21e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 92.94  E-value: 3.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEA--ERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAaeEIEALKGAGAVRYEPADVTDEDQVARAVDAATAWH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK05875   85 GRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKS 164
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 166 AIVRLTeAFARDYQDHPYLRFNVLTPGMVPTDMI 199
Cdd:PRK05875  165 AVDHLM-KLAADELGPSWVRVNSIRPGLIRTDLV 197
PRK06947 PRK06947
SDR family oxidoreductase;
14-198 3.51e-22

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 92.18  E-value: 3.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISST-NPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06947    6 LITGASRGIGRATAVLAAARGWSVGINYArDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLDALV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQ---IINLSGGGAKRAQRF-LSAYSTSKAAIV 168
Cdd:PRK06947   86 NNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGSPNeYVDYAGSKGAVD 165
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498198613 169 RLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK06947  166 TLTLGLAKELGPHG-VRVNAVRPGLIETEI 194
PRK08278 PRK08278
SDR family oxidoreductase;
6-146 9.12e-22

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 91.50  E-value: 9.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTN-------PTNLTEAERALQAAGLNVTGIRCDVANRNEVEALA 78
Cdd:PRK08278    2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTaephpklPGTIHTAAEEIEAAGGQALPLVGDVRDEDQVAAAV 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613  79 SAAVERMGRIDLWVNNAG-ISgpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS 146
Cdd:PRK08278   82 AKAVERFGGIDICVNNASaIN--LTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLS 148
PRK05866 PRK05866
SDR family oxidoreductase;
2-196 1.03e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 91.73  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   2 ARTPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAA 81
Cdd:PRK05866   32 PRQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADV 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  82 VERMGRIDLWVNNAG--ISGPFGYALdippDAWEQVIRVNLLgTYYG----CRAALPYMIKQRNGQIINLSGGGAK-RAQ 154
Cdd:PRK05866  112 EKRIGGVDILINNAGrsIRRPLAESL----DRWHDVERTMVL-NYYAplrlIRGLAPGMLERGDGHIINVATWGVLsEAS 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1498198613 155 RFLSAYSTSKAA---IVRLTEAFARDYQDH-PYLRFN-VLTPGMVPT 196
Cdd:PRK05866  187 PLFSVYNASKAAlsaVSRVIETEWGDRGVHsTTLYYPlVATPMIAPT 233
PRK07074 PRK07074
SDR family oxidoreductase;
13-196 1.22e-21

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 90.98  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAglNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK07074    5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDA--RFVPVACDLTDAASLAAALANAAAERGPVDVLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG--GGAKRAQrflSAYSTSKAAIVRL 170
Cdd:PRK07074   83 ANAGAARAASLH-DTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSvnGMAALGH---PAYSAAKAGLIHY 158
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 171 TEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK07074  159 TKLLAVEYGRFG-IRANAVAPGTVKT 183
PRK09072 PRK09072
SDR family oxidoreductase;
7-182 1.30e-21

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 90.77  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALAsAAVERMG 86
Cdd:PRK09072    2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPG-RHRWVVADLTSEAGREAVL-ARAREMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISgPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINL-SGGGAKRAQRFlSAYSTSKA 165
Cdd:PRK09072   80 GINVLINNAGVN-HFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVgSTFGSIGYPGY-ASYCASKF 157
                         170
                  ....*....|....*..
gi 1498198613 166 AIVRLTEAFARDYQDHP 182
Cdd:PRK09072  158 ALRGFSEALRRELADTG 174
PLN02253 PLN02253
xanthoxin dehydrogenase
13-198 1.71e-21

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 91.04  E-value: 1.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PLN02253   21 ALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEP-NVCFFHCDVTVEDDVSRAVDFTVDKFGTLDIMV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPfgYALDIPPDA---WEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:PLN02253  100 NNAGLTGP--PCPDIRNVElseFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHAVLG 177
                         170       180
                  ....*....|....*....|....*....
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PLN02253  178 LTRSVAAELGKHG-IRVNCVSPYAVPTAL 205
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
15-146 5.00e-21

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 89.04  E-value: 5.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTN-------PTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:cd09762     8 ITGASRGIGKAIALKAARDGANVVIAAKTaephpklPGTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVEKFGG 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNA-GISgpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS 146
Cdd:cd09762    88 IDILVNNAsAIS--LTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLS 145
PRK12742 PRK12742
SDR family oxidoreductase;
6-198 5.94e-21

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 88.66  E-value: 5.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   6 SDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlTEAERALqAAGLNVTGIRCDVANRNEVealaSAAVERM 85
Cdd:PRK12742    2 GAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGS---KDAAERL-AQETGATAVQTDSADRDAV----IDVVRKS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLsggGAKRAQRF----LSAYS 161
Cdd:PRK12742   74 GALDILVVNAGI-AVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIII---GSVNGDRMpvagMAAYA 147
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1498198613 162 TSKAAIVRLTEAFARDYqDHPYLRFNVLTPGMVPTDM 198
Cdd:PRK12742  148 ASKSALQGMARGLARDF-GPRGITINVVQPGPIDTDA 183
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
13-248 1.15e-20

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 88.15  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTnLTEAERALQAAGLNVTGIRCD----VANRNEVE---ALASAAVERM 85
Cdd:cd05353     8 VLVTGAGGGLGRAYALAFAERGAKVVVNDLGGD-RKGSGKSSSAADKVVDEIKAAggkaVANYDSVEdgeKIVKTAIDAF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGI--SGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:cd05353    87 GRVDILVNNAGIlrDRSF---AKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 164 KAAIVRLTEAFARDYQdhpylRFNVLTPGMVPTDMINHFETVGPggeaikqlPRVLRIFGttAEETAELALRIVREG--K 241
Cdd:cd05353   164 KLGLLGLSNTLAIEGA-----KYNITCNTIAPAAGSRMTETVMP--------EDLFDALK--PEYVAPLVLYLCHESceV 228

                  ....*..
gi 1498198613 242 NGQVFEV 248
Cdd:cd05353   229 TGGLFEV 235
PRK12743 PRK12743
SDR family oxidoreductase;
12-198 1.28e-20

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 88.17  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:PRK12743    4 VAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRIDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAG--ISGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:PRK12743   84 LVNNAGamTKAPF---LDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHAL 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1498198613 168 VRLTEAFARDYQDHPYLrFNVLTPGMVPTDM 198
Cdd:PRK12743  161 GGLTKAMALELVEHGIL-VNAVAPGAIATPM 190
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
13-191 2.14e-20

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 87.45  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQaAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:cd08943     4 ALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ-GGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGI--SGPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ-RNGQIINLSGGGAKRAQRFLSAYSTSKAAIVR 169
Cdd:cd08943    83 SNAGIatSSPIA---ETSLEDWNRSMDINLTGHFLVSREAFRIMKSQgIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAH 159
                         170       180
                  ....*....|....*....|..
gi 1498198613 170 LTEAFARDYQDHPyLRFNVLTP 191
Cdd:cd08943   160 LARCLALEGGEDG-IRVNTVNP 180
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
13-198 2.35e-20

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 87.43  E-value: 2.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVI-ISSTNPTNLTEAEralQAAGLNVTGIRCDVANRNEVEA-----LASAAVERMG 86
Cdd:PRK06924    4 VIITGTSQGLGEAIANQLLEKGTHVIsISRTENKELTKLA---EQYNSNLTFHSLDLQDVHELETnfneiLSSIQEDNVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLwVNNAGISGPFGYALDIPPDAWEQVIRVNLLG----TYYGCRAALPYMIKQRngqIINLSGGGAKRAQRFLSAYST 162
Cdd:PRK06924   81 SIHL-INNAGMVAPIKPIEKAESEELITNVHLNLLApmilTSTFMKHTKDWKVDKR---VINISSGAAKNPYFGWSAYCS 156
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1498198613 163 SKAAIVRLTEAFARDYQDHPY-LRFNVLTPGMVPTDM 198
Cdd:PRK06924  157 SKAGLDMFTQTVATEQEEEEYpVKIVAFSPGVMDTNM 193
PRK06180 PRK06180
short chain dehydrogenase; Provisional
15-176 2.87e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 87.66  E-value: 2.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPtnltEAERALQA-AGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK06180    9 ITGVSSGFGRALAQAALAAGHRVVGTVRSE----AARADFEAlHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEA 173
Cdd:PRK06180   85 NAGY-GHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISES 163

                  ...
gi 1498198613 174 FAR 176
Cdd:PRK06180  164 LAK 166
PRK07775 PRK07775
SDR family oxidoreductase;
13-198 5.44e-20

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 86.73  E-value: 5.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIvrltE 172
Cdd:PRK07775   93 SGAG-DTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGL----E 167
                         170       180
                  ....*....|....*....|....*....
gi 1498198613 173 AFARDYQ---DHPYLRFNVLTPGMVPTDM 198
Cdd:PRK07775  168 AMVTNLQmelEGTGVRASIVHPGPTLTGM 196
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-198 1.98e-19

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 87.20  E-value: 1.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIisstnPTNLTEAERALQ--AAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:PRK08261  212 VALVTGAARGIGAAIAEVLARDGAHVV-----CLDVPAAGEALAavANRVGGTALALDITAPDAPARIAEHLAERHGGLD 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS---GGGAKRAQrflSAYSTSKAA 166
Cdd:PRK08261  287 IVVHNAGITRDKTLA-NMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSsisGIAGNRGQ---TNYAASKAG 362
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK08261  363 VIGLVQALAPLLAERG-ITINAVAPGFIETQM 393
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
7-198 2.58e-19

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 84.20  E-value: 2.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNptnlTEAERALQAA-GLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK12936    3 DLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTR----VEKLEALAAElGERVKIFPANLSDRDEVKALGQKAEADL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK12936   79 EGVDILVNNAGITKD-GLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKA 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK12936  158 GMIGFSKSLAQEIATRN-VTVNCVAPGFIESAM 189
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-197 3.49e-19

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 84.19  E-value: 3.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   5 PSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAEraLQAAGLNVTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK12481    3 LFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQ--VEALGRKFHFITADLIQQKDIDSIVSQAVEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISGPFGyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRN-GQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:PRK12481   81 MGHIDILINNAGIIRRQD-LLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVPSYTAS 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:PRK12481  160 KSAVMGLTRALATELSQYN-INVNAIAPGYMATD 192
PRK06500 PRK06500
SDR family oxidoreductase;
1-196 3.88e-19

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 83.85  E-value: 3.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   1 MARtpsdLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASA 80
Cdd:PRK06500    1 MSR----LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAEL---GESALVIRADAGDVAAQKALAQA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  81 AVERMGRIDLWVNNAGIS--GPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMikqRNGQIINLSGG-----GAKRA 153
Cdd:PRK06500   74 LAEAFGRLDAVFINAGVAkfAPLE---DWDEAMFDRSFNTNVKGPYFLIQALLPLL---ANPASIVLNGSinahiGMPNS 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1498198613 154 qrflSAYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK06500  148 ----SVYAASKAALLSLAKTLSGELLPRG-IRVNAVSPGPVQT 185
PRK08264 PRK08264
SDR family oxidoreductase;
7-203 8.40e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 82.63  E-value: 8.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEA-LARAGAQVIISSTNPTNLTEAeralqaaGLNVTGIRCDVANRNEVEALASAAverm 85
Cdd:PRK08264    3 DIKGKVVLVTGANRGIGRAFVEQlLARGAAKVYAAARDPESVTDL-------GPRVVPLQLDVTDPASVAAAAEAA---- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK08264   72 SDVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKA 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1498198613 166 AIVRLTEAfardyqdhpyLRfNVLTP----------GMVPTDMINHFE 203
Cdd:PRK08264  152 AAWSLTQA----------LR-AELAPqgtrvlgvhpGPIDTDMAAGLD 188
PRK08219 PRK08219
SDR family oxidoreductase;
13-198 1.35e-18

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 81.90  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAgAQVIISSTNPTNLTEAERALQaaglNVTGIRCDVANrnevEALASAAVERMGRIDLWV 92
Cdd:PRK08219    6 ALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELP----GATPFPVDLTD----PEAIAAAVEQLGRLDVLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIS--GPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPyMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRL 170
Cdd:PRK08219   77 HNAGVAdlGPVA---ESTVDEWRATLEVNVVAPAELTRLLLP-ALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRAL 152
                         170       180
                  ....*....|....*....|....*...
gi 1498198613 171 TEAFARDyqDHPYLRFNVLTPGMVPTDM 198
Cdd:PRK08219  153 ADALREE--EPGNVRVTSVHPGRTDTDM 178
PRK09730 PRK09730
SDR family oxidoreductase;
13-198 1.72e-18

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 82.21  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK09730    4 ALVTGGSRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQ---IINLSGGGAKraqrfLSA------YST 162
Cdd:PRK09730   84 VNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASR-----LGApgeyvdYAA 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1498198613 163 SKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK09730  159 SKGAIDTLTTGLSLEVAAQG-IRVNCVRPGFIYTEM 193
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-197 3.35e-18

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 81.46  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIisSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK08993    7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIV--GINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGPFGyALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRN-GQIIN----LSGGGAKRaqrfLSAYS 161
Cdd:PRK08993   85 HIDILVNNAGLIRRED-AIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINiasmLSFQGGIR----VPSYT 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1498198613 162 TSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:PRK08993  160 ASKSGVMGVTRLMANEWAKHN-INVNAIAPGYMATN 194
PRK06182 PRK06182
short chain dehydrogenase; Validated
13-174 3.81e-18

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 81.54  E-value: 3.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNptnlTEAERALQAAGlnVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06182    6 ALVTGASSGIGKATARRLAAQGYTVYGAARR----VDKMEDLASLG--VHPLSLDVTDEASIKAAVDTIIAEEGRIDVLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIvrltE 172
Cdd:PRK06182   80 NNAGY-GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFAL----E 154

                  ..
gi 1498198613 173 AF 174
Cdd:PRK06182  155 GF 156
PRK05717 PRK05717
SDR family oxidoreductase;
13-194 6.53e-18

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 80.70  E-value: 6.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK05717   13 ALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKAL---GENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALD-IPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK05717   90 CNAAIADPHNTTLEsLSLAHWNRVLAVNLTGPMLLAKHCAPYL-RAHNGAIVNLASTRARQSEPDTEAYAASKGGLLALT 168
                         170       180
                  ....*....|....*....|...
gi 1498198613 172 EAFARDYQdhPYLRFNVLTPGMV 194
Cdd:PRK05717  169 HALAISLG--PEIRVNAVSPGWI 189
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
13-179 1.29e-17

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 79.73  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTE-AERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd05373     2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAlLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:cd05373    82 VYNAGANVWFPI-LETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALA 160

                  ....*...
gi 1498198613 172 EAFARDYQ 179
Cdd:cd05373   161 QSMARELG 168
PRK08703 PRK08703
SDR family oxidoreductase;
5-194 2.28e-17

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 78.82  E-value: 2.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   5 PSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAG-LNVTGIRCDV--ANRNEVEALA-SA 80
Cdd:PRK08703    1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGhPEPFAIRFDLmsAEEKEFEQFAaTI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  81 AVERMGRIDLWVNNAGisgpFGYAL----DIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRF 156
Cdd:PRK08703   81 AEATQGKLDGIVHCAG----YFYALspldFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAY 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1498198613 157 LSAYSTSKAAIVRLTEAFARDYQDHPYLRFNVLTPGMV 194
Cdd:PRK08703  157 WGGFGASKAALNYLCKVAADEWERFGNLRANVLVPGPI 194
PRK05693 PRK05693
SDR family oxidoreductase;
13-173 2.72e-17

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 79.45  E-value: 2.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLteaeRALQAAGLNvtGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK05693    4 VLITGCSSGIGRALADAFKAAGYEVWATARKAEDV----EALAAAGFT--AVQLDVNDGAALARLAEELEAEHGGLDVLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRnGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:PRK05693   78 NNAGY-GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSR-GLVVNIGSVSGVLVTPFAGAYCASKAAVHALSD 155

                  .
gi 1498198613 173 A 173
Cdd:PRK05693  156 A 156
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-176 5.77e-17

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 79.06  E-value: 5.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   4 TPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtNLTEAERA--LQAAGLNVTGIRCDVANRNEVEALASAA 81
Cdd:PRK07792    6 NTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVAS-ALDASDVLdeIRAAGAKAVAVAGDISQRATADELVATA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  82 VErMGRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMiKQRN--------GQIINLSgggakrA 153
Cdd:PRK07792   85 VG-LGGLDIVVNNAGITRD-RMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYW-RAKAkaaggpvyGRIVNTS------S 155
                         170       180
                  ....*....|....*....|....*....
gi 1498198613 154 QRFLSA------YSTSKAAIVRLTEAFAR 176
Cdd:PRK07792  156 EAGLVGpvgqanYGAAKAGITALTLSAAR 184
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
13-199 1.19e-16

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 76.97  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVII----SSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASAAVERMGRI 88
Cdd:PRK12938    6 AYVTGGMGGIGTSICQRLHKDGFKVVAgcgpNSPRRVKWLEDQKAL---GFDFIASEGNVGDWDSTKAAFDKVKAEVGEI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  89 DLWVNNAGISGPFGYALDIPPDaWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIV 168
Cdd:PRK12938   83 DVLVNNAGITRDVVFRKMTRED-WTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIH 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1498198613 169 RLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:PRK12938  162 GFTMSLAQEVATKG-VTVNTVSPGYIGTDMV 191
PRK06125 PRK06125
short chain dehydrogenase; Provisional
7-199 1.92e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 76.62  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA-GLNVTGIRCDVANRNEVEALASAAverm 85
Cdd:PRK06125    4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEAREQLAAEA---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK06125   80 GDIDILVNNAG-AIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADYICGSAGNA 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:PRK06125  159 ALMAFTRALGGKSLDDG-VRVVGVNPGPVATDRM 191
PRK07985 PRK07985
SDR family oxidoreductase;
8-233 2.56e-16

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 76.96  E-value: 2.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTnPTNLTEAERA---LQAAGLNVTGIRCDVANRNEVEALASAAVER 84
Cdd:PRK07985   47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYL-PVEEEDAQDVkkiIEECGRKAVLLPGDLSDEKFARSLVHEAHKA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKqrNGQIINLSGGGAKRAQRFLSAYSTSK 164
Cdd:PRK07985  126 LGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPK--GASIITTSSIQAYQPSPHLLDYAATK 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1498198613 165 AAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM-INhfetvgpGGEAIKQLPRvlriFGTT-----AEETAELA 233
Cdd:PRK07985  204 AAILNYSRGLAKQVAEKG-IRVNIVAPGPIWTALqIS-------GGQTQDKIPQ----FGQQtpmkrAGQPAELA 266
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
12-175 2.78e-16

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 76.55  E-value: 2.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAV-VTGGSRGIGRAIAEALARAGAQVIISSTNPtNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:cd09805     1 KAVlITGCDSGFGNLLAKKLDSLGFTVLAGCLTK-NGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 W--VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPyMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIv 168
Cdd:cd09805    80 WglVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAV- 157

                  ....*..
gi 1498198613 169 rltEAFA 175
Cdd:cd09805   158 ---EAFS 161
PRK06123 PRK06123
SDR family oxidoreductase;
13-198 5.81e-16

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 75.20  E-value: 5.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAER-ALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:PRK06123    5 MIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVqAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQ---RNGQIINLSgggaKRAQRFLSA-----YSTS 163
Cdd:PRK06123   85 VNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVS----SMAARLGSPgeyidYAAS 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK06123  161 KGAIDTMTIGLAKEVAAEG-IRVNAVRPGVIYTEI 194
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
13-198 6.50e-16

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 74.10  E-value: 6.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVtgircDVANRNEVEALAsaavERMGRIDLWV 92
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPA-----DVAAELEVWALA----QELGPLDLLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQrnGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd11730    72 YAAGAILGKPLA-RTKPAAWRRILDANLTGAALVLKHALALLAAG--ARLVFLGAYPELVMLPGLSAYAAAKAALEAYVE 148
                         170       180
                  ....*....|....*....|....*.
gi 1498198613 173 AFARDYQDhpyLRFNVLTPGMVPTDM 198
Cdd:cd11730   149 VARKEVRG---LRLTLVRPPAVDTGL 171
PRK08339 PRK08339
short chain dehydrogenase; Provisional
7-199 2.08e-15

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 73.74  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEA-ERALQAAGLNVTGIRCDVANRNEVEALASaAVERM 85
Cdd:PRK08339    5 DLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKArEKIKSESNVDVSYIVADLTKREDLERTVK-ELKNI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK08339   84 GEPDIFFFSTGGPKP-GYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRI 162
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1498198613 166 AIVRLTEAFARDYQdhPY-LRFNVLTPGMVPTDMI 199
Cdd:PRK08339  163 SMAGLVRTLAKELG--PKgITVNGIMPGIIRTDRV 195
PRK08340 PRK08340
SDR family oxidoreductase;
11-254 2.29e-15

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 73.69  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  11 LKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:PRK08340    1 MNVLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAG-ISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALP-YMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIV 168
Cdd:PRK08340   80 LVWNAGnVRCEPCMLHEAGYSDWLEAALLHLVAPGYLTTLLIQaWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 169 RLTEAFARDYQDHPYLRFNVLtpgmvptdmINHFETvgPGgeAIKQLPRVLRIFGTTAEETAElalrivREgkngqVFEV 248
Cdd:PRK08340  160 QLAKGVSRTYGGKGIRAYTVL---------LGSFDT--PG--ARENLARIAEERGVSFEETWE------RE-----VLER 215

                  ....*.
gi 1498198613 249 MPRHRT 254
Cdd:PRK08340  216 TPLKRT 221
PRK06482 PRK06482
SDR family oxidoreductase;
15-177 2.86e-15

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 73.61  E-value: 2.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEaeraLQAA-GLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK06482    7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALDD----LKARyGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEA 173
Cdd:PRK06482   83 NAGY-GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEA 161

                  ....
gi 1498198613 174 FARD 177
Cdd:PRK06482  162 VAQE 165
PRK12747 PRK12747
short chain dehydrogenase; Provisional
13-198 1.09e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 71.64  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTN-PTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASA----AVERMG- 86
Cdd:PRK12747    7 ALVTGASRGIGRAIAKRLANDGALVAIHYGNrKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSldneLQNRTGs 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 -RIDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK12747   87 tKFDILINNAGI-GPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAYSMTKG 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK12747  164 AINTMTFTLAKQLGARG-ITVNAILPGFIKTDM 195
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
13-248 1.34e-14

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 70.24  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGaqviisstnptnlteaeralqaaglnvtgircdvanrnevealaSAAVERMGRIDLWV 92
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRG--------------------------------------------SPKVLVVSRRDVVV 36
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTE 172
Cdd:cd02266    37 HNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQ 115
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1498198613 173 AFARDYQDHpYLRFNVLTPGMVPTDMinHFEtvGPGGEAIKQLPRVLRIFGTTAEETAELALRIVREGKNGQVFEV 248
Cdd:cd02266   116 QWASEGWGN-GLPATAVACGTWAGSG--MAK--GPVAPEEILGNRRHGVRTMPPEEVARALLNALDRPKAGVCYII 186
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
15-145 2.12e-14

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 70.94  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALqaaGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWVNN 94
Cdd:PRK10538    5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL---GDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNN 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1498198613  95 AGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINL 145
Cdd:PRK10538   82 AGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINI 132
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
14-231 4.25e-14

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 70.22  E-value: 4.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIisstnPTNLTEAEralqaaglnvtgIRCDVANRNEVEALASAAVERM-GRIDLWV 92
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTVI-----GIDLREAD------------VIADLSTPEGRAAAIADVLARCsGVLDGLV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALdippdaweqVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS-----GGGAKRAQRFLS--------- 158
Cdd:cd05328    66 NCAGVGGTTVAGL---------VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSsiagaGWAQDKLELAKAlaagteara 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 159 -------------AYSTSKAAIVRLTEAFARDYQDHPYLRFNVLTPGMVPTDMINHFETVGPGGEAIKQLP-RVLRIfgT 224
Cdd:cd05328   137 valaehagqpgylAYAGSKEALTVWTRRRAATWLYGAGVRVNTVAPGPVETPILQAFLQDPRGGESVDAFVtPMGRR--A 214

                  ....*..
gi 1498198613 225 TAEETAE 231
Cdd:cd05328   215 EPDEIAP 221
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
14-123 4.76e-14

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 68.66  E-value: 4.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   14 VVTGGSRGIGRAIAEALARAGAQVII----SSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVllsrSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1498198613   90 LWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGT 123
Cdd:smart00822  84 GVIHAAGVLDD-GVLASLTPERFAAVLAPKAAGA 116
PRK09134 PRK09134
SDR family oxidoreductase;
13-196 5.24e-14

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 69.96  E-value: 5.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVII---SSTnptnlTEAE---RALQAAGLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:PRK09134   12 ALVTGAARRIGRAIALDLAAHGFDVAVhynRSR-----DEAEalaAEIRALGRRAVALQADLADEAEVRALVARASAALG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGIsgpFGY--ALDIPPDAWEQVIRVNLLGTYYGCRA---ALPymiKQRNGQIINLSGggakraQR------ 155
Cdd:PRK09134   87 PITLLVNNASL---FEYdsAASFTRASWDRHMATNLRAPFVLAQAfarALP---ADARGLVVNMID------QRvwnlnp 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1498198613 156 -FLSaYSTSKAAIVRLTEAFARDYQdhPYLRFNVLTPGmvPT 196
Cdd:PRK09134  155 dFLS-YTLSKAALWTATRTLAQALA--PRIRVNAIGPG--PT 191
PRK07806 PRK07806
SDR family oxidoreductase;
5-134 6.63e-14

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 69.36  E-value: 6.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   5 PSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNptnltEAERA------LQAAGLNVTGIRCDVANRNEVEALA 78
Cdd:PRK07806    1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQ-----KAPRAnkvvaeIEAAGGRASAVGADLTDEESVAALM 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613  79 SAAVERMGRIDLWVNNAgiSG------PFGYALDIPPDAweqviRVNLLgtyygcRAALPYM 134
Cdd:PRK07806   76 DTAREEFGGLDALVLNA--SGgmesgmDEDYAMRLNRDA-----QRNLA------RAALPLM 124
PRK05993 PRK05993
SDR family oxidoreductase;
14-171 1.15e-13

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 69.29  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTeaerALQAAGLnvTGIRCDVANRNEVEALASAAVERM-GRIDLWV 92
Cdd:PRK05993    8 LITGCSSGIGAYCARALQSDGWRVFATCRKEEDVA----ALEAEGL--EAFQLDYAEPESIAALVAQVLELSgGRLDALF 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613  93 NNaGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK05993   82 NN-GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFAIEGLS 159
PRK07791 PRK07791
short chain dehydrogenase; Provisional
13-171 1.80e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 68.55  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS------STNPTNLTEAERALQ---AAGLNVTGIRCDVANRNEVEALASAAVE 83
Cdd:PRK07791    9 VIVTGAGGGIGRAHALAFAAEGARVVVNdigvglDGSASGGSAAQAVVDeivAAGGEAVANGDDIADWDGAANLVDAAVE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  84 RMGRIDLWVNNAGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMI------KQRNGQIINLSGGGAKRAQRFL 157
Cdd:PRK07791   89 TFGGLDVLVNNAGILRD-RMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRaeskagRAVDARIINTSSGAGLQGSVGQ 167
                         170
                  ....*....|....
gi 1498198613 158 SAYSTSKAAIVRLT 171
Cdd:PRK07791  168 GNYSAAKAGIAALT 181
PLN02780 PLN02780
ketoreductase/ oxidoreductase
13-179 2.65e-13

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 68.74  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PLN02780   56 ALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIEGLDVGV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 --NNAGISGPFG-YALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAK--RAQRFLSAYSTSKAAI 167
Cdd:PLN02780  136 liNNVGVSYPYArFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIviPSDPLYAVYAATKAYI 215
                         170
                  ....*....|..
gi 1498198613 168 VRLTEAFARDYQ 179
Cdd:PLN02780  216 DQFSRCLYVEYK 227
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-197 7.40e-13

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 66.73  E-value: 7.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSR--GIGRAIAEALARAGAQVII--------SSTNPTNLTEA---ERALQAAGLNVTGIRCDVANRNEV 74
Cdd:PRK12859    4 LKNKVAVVTGVSRldGIGAAICKELAEAGADIFFtywtaydkEMPWGVDQDEQiqlQEELLKNGVKVSSMELDLTQNDAP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  75 EALASAAVERMGRIDLWVNNAGISGPFGY-ALDIppDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRA 153
Cdd:PRK12859   84 KELLNKVTEQLGYPHILVNNAAYSTNNDFsNLTA--EELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGP 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1498198613 154 QRFLSAYSTSKAAIVRLTEAFARDYQdHPYLRFNVLTPGmvPTD 197
Cdd:PRK12859  162 MVGELAYAATKGAIDALTSSLAAEVA-HLGITVNAINPG--PTD 202
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
14-175 9.70e-13

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 65.81  E-value: 9.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIIsstnpTNLTEAERAlqAAGLNVTGIRCDVANRNEVealASAAVERMGRIDLWVN 93
Cdd:cd05334     5 LVYGGRGALGSAVVQAFKSRGWWVAS-----IDLAENEEA--DASIIVLDSDSFTEQAKQV---VASVARLSGKVDALIC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGisgpfGYALDIPPD-----AWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIV 168
Cdd:cd05334    75 VAG-----GWAGGSAKSksfvkNWDLMWKQNLWTSFIASHLATKHL--LSGGLLVLTGAKAALEPTPGMIGYGAAKAAVH 147

                  ....*..
gi 1498198613 169 RLTEAFA 175
Cdd:cd05334   148 QLTQSLA 154
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
14-246 1.12e-12

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 66.34  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLN--VTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd09807     5 IITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNheVIVRHLDLASLKSIRAFAAEFLAEEDRLDVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGIsgpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRA----------QRF--LSA 159
Cdd:cd09807    85 INNAGV---MRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGkinfddlnseKSYntGFA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 160 YSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGEAIkqLPRVLRIFGTTAEETAE----LALR 235
Cdd:cd09807   162 YCQSKLANVLFTRELARRLQGTG-VTVNALHPGVVRTELGRHTGIHHLFLSTL--LNPLFWPFVKTPREGAQtsiyLALA 238
                         250
                  ....*....|.
gi 1498198613 236 IVREGKNGQVF 246
Cdd:cd09807   239 EELEGVSGKYF 249
PRK07023 PRK07023
SDR family oxidoreductase;
10-198 1.18e-12

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 65.80  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  10 DLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNptnlTEAERAlQAAGLNVTGIRCDVANRNEVEA-LASAAVERMGR- 87
Cdd:PRK07023    1 AVRAIVTGHSRGLGAALAEQLLQPGIAVLGVARS----RHPSLA-AAAGERLAEVELDLSDAAAAAAwLAGDLLAAFVDg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 --IDLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK07023   76 asRVLLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKA 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 166 AIVRLTEAFARDYQDHpyLRFNVLTPGMVPTDM 198
Cdd:PRK07023  156 ALDHHARAVALDANRA--LRIVSLAPGVVDTGM 186
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
12-220 1.36e-12

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 66.16  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNlteaeRALQAAGLNVTGIRCDVANRNEVEALasaaverMGRIDLW 91
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPG-----AANLAALPGVEFVRGDLRDPEALAAA-------LAGVDAV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPfgyaldiPPDAWEQVIRVNLLGTYYGCRAALpymiKQRNGQIINLSGGGA----------KRAQRFLSAYS 161
Cdd:COG0451    69 VHLAAPAGV-------GEEDPDETLEVNVEGTLNLLEAAR----AAGVKRFVYASSSSVygdgegpideDTPLRPVSPYG 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 162 TSKAAivrlTEAFARDYQDHPYLRFNVLTPGMVptdminhfetVGPGGEAIkqLPRVLR 220
Cdd:COG0451   138 ASKLA----AELLARAYARRYGLPVTILRPGNV----------YGPGDRGV--LPRLIR 180
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
13-248 1.46e-12

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 64.91  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIsstnptnlteaeralqaAGLNVTGIRCDVANRNEVEALAsaavERMGRIDLWV 92
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVIT-----------------AGRSSGDYQVDITDEASIKALF----EKVGHFDAIV 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikqRNGQIINLSGGGAKRAQR-FLSAYSTSKAAIVRLT 171
Cdd:cd11731    60 STAG-DAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL---NDGGSITLTSGILAQRPIpGGAAAATVNGALEGFV 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198613 172 EAFARDYQDHpyLRFNVLTPGMVPTDMINHFETVgPGGEAIkqlprvlrifgtTAEETAELALRIVREGKNGQVFEV 248
Cdd:cd11731   136 RAAAIELPRG--IRINAVSPGVVEESLEAYGDFF-PGFEPV------------PAEDVAKAYVRSVEGAFTGQVLHV 197
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
14-238 1.50e-12

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 65.94  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAG----LNVTGIRCDVANRNEVealaSAAVERM--GR 87
Cdd:cd09806     4 LITGCSSGIGLHLAVRLASDPSKRFKVYATMRDLKKKGRLWEAAGalagGTLETLQLDVCDSKSV----AAAVERVteRH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAI 167
Cdd:cd09806    80 VDVLVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 168 VRLTEAFARDyqdhpYLRFNV----LTPGMVPTDMINHFETVGPGGEAIKQLPRVLRIF---------------GTTAEE 228
Cdd:cd09806   159 EGLCESLAVQ-----LLPFNVhlslIECGPVHTAFMEKVLGSPEEVLDRTADDITTFHFfyqylahskqvfreaAQNPEE 233
                         250
                  ....*....|
gi 1498198613 229 TAELALRIVR 238
Cdd:cd09806   234 VAEVFLTAIR 243
PRK06940 PRK06940
short chain dehydrogenase; Provisional
12-123 2.34e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 65.43  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALArAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAvERMGRIDLW 91
Cdd:PRK06940    3 EVVVVIGAGGIGQAIARRVG-AGKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATA-QTLGPVTGL 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1498198613  92 VNNAGISgpfgyaldiPPDA-WEQVIRVNLLGT 123
Cdd:PRK06940   81 VHTAGVS---------PSQAsPEAILKVDLYGT 104
PRK07577 PRK07577
SDR family oxidoreductase;
13-248 2.40e-12

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 64.75  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERalqaaglnvtgIRCDVANRNEVEALASAAVERmGRIDLWV 92
Cdd:PRK07577    6 VLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDFPGEL-----------FACDLADIEQTAATLAQINEI-HPVDAIV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGIS--GPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSG----GGAKRaqrflSAYSTSKAA 166
Cdd:PRK07577   74 NNVGIAlpQPLG---KIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSraifGALDR-----TSYSAAKSA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 167 IVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMINHFETVGPGGE--AIKQLPrvLRIFGTTAEETAELALRIVREGK--N 242
Cdd:PRK07577  146 LVGCTRTWALELAEYG-ITVNAVAPGPIETELFRQTRPVGSEEEkrVLASIP--MRRLGTPEEVAAAIAFLLSDDAGfiT 222

                  ....*.
gi 1498198613 243 GQVFEV 248
Cdd:PRK07577  223 GQVLGV 228
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
12-200 2.68e-12

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 66.48  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLnvtGIRCDVANRNEVEALASAAVER-----MG 86
Cdd:COG3347   427 VALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYG---ADAVDATDVDVTAEAAVAAAFGfagldIG 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 RIDLWVNNAGISGpfgyaldiPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQ--------IINLSGGGAKRAQRFLS 158
Cdd:COG3347   504 GSDIGVANAGIAS--------SSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTggqglggsSVFAVSKNAAAAAYGAA 575
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1498198613 159 AYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMIN 200
Cdd:COG3347   576 AAATAKAAAQHLLRALAAEGGANG-INANRVNPDAVLDGSAI 616
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
15-198 2.76e-12

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 65.21  E-value: 2.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGircDVANRNEVEALASaAVERMGRIDLWVNN 94
Cdd:cd08951    12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIG---DLSSLAETRKLAD-QVNAIGRFDAVIHN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  95 AGI-SGPFgyaLDIPPDAWEQVIRVNLLGtyygcraalPYMIK---QRNGQIINLS-----GGGA--------KRAQRFL 157
Cdd:cd08951    88 AGIlSGPN---RKTPDTGIPAMVAVNVLA---------PYVLTaliRRPKRLIYLSsgmhrGGNAslddidwfNRGENDS 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1498198613 158 SAYSTSKAAIVRLTEAFARDYQDhpyLRFNVLTPGMVPTDM 198
Cdd:cd08951   156 PAYSDSKLHVLTLAAAVARRWKD---VSSNAVHPGWVPTKM 193
PRK12744 PRK12744
SDR family oxidoreductase;
4-178 2.79e-12

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 65.15  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   4 TPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVI-ISSTNPTNLTEAER---ALQAAGLNVTGIRCDVANRNEVEALAS 79
Cdd:PRK12744    2 ADHSLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVaIHYNSAASKADAEEtvaAVKAAGAKAVAFQADLTTAAAVEKLFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  80 AAVERMGRIDLWVNNAG--ISGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINL--SGGGAKRAqr 155
Cdd:PRK12744   82 DAKAAFGRPDIAINTVGkvLKKPI---VEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTLvtSLLGAFTP-- 154
                         170       180
                  ....*....|....*....|...
gi 1498198613 156 FLSAYSTSKAAIVRLTEAFARDY 178
Cdd:PRK12744  155 FYSAYAGSKAPVEHFTRAASKEF 177
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
14-123 3.72e-12

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 65.85  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALAR-AGAQVIISS-----TNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:cd08953   209 LVTGGAGGIGRALARALARrYGARLVLLGrsplpPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGA 288
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1498198613  88 IDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGT 123
Cdd:cd08953   289 IDGVIHAAGV-LRDALLAQKTAEDFEAVLAPKVDGL 323
PRK12746 PRK12746
SDR family oxidoreductase;
13-198 4.06e-12

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 64.67  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIS-STNPTNLTEAERALQAAGLNVTGIRCDVAN----RNEVEALASAAVERMG- 86
Cdd:PRK12746    9 ALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGGKAFLIEADLNSidgvKKLVEQLKNELQIRVGt 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 -RIDLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKA 165
Cdd:PRK12746   89 sEIDILVNNAGI-GTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAYGLSKG 165
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1498198613 166 AIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK12746  166 ALNTMTLPLAKHLGERG-ITVNTIMPGYTKTDI 197
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-197 5.59e-12

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 64.01  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALASAAVERMGR 87
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLNA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGisgpfGYALDI--PPDAWEQVIRVNLLGTYYGCRAALPYMikqRNGQIINL--SGGGAKRAQRFLSAYSTS 163
Cdd:PRK05786   82 IDGLVVTVG-----GYVEDTveEFSGLEEMLTNHIKIPLYAVNASLRFL---KEGSSIVLvsSMSGIYKASPDQLSYAVA 153
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1498198613 164 KAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTD 197
Cdd:PRK05786  154 KAGLAKAVEILASELLGRG-IRVNGIAPTTISGD 186
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
13-196 1.18e-11

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 63.69  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGA-QVIISSTNPtnlTEAERALQAAGL---NVTGIRCDVANRNEVEALASAAVERMGRI 88
Cdd:cd09810     4 VVITGASSGLGLAAAKALARRGEwHVVMACRDF---LKAEQAAQEVGMpkdSYSVLHCDLASLDSVRQFVDNFRRTGRPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  89 DLWVNNAGISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQ---II---------------------- 143
Cdd:cd09810    81 DALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENASpriVIvgsithnpntlagnvppratlg 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1498198613 144 NLSG--GGAKRAQRFLS--------AYSTSKAAIVRLTEAFARDYQDHPYLRFNVLTPGMVPT 196
Cdd:cd09810   161 DLEGlaGGLKGFNSMIDggefegakAYKDSKVCNMLTTYELHRRLHEETGITFNSLYPGCIAE 223
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
12-234 1.22e-11

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 63.12  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTG--GSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTgIRCDVANRNEVEALASAAVERMGRID 89
Cdd:COG0623     7 RGLITGvaNDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEELGSALV-LPCDVTDDEQIDALFDEIKEKWGKLD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWV------NNAGISGPFgyaLDIPPDAWEQ--------VIRVnllgtyygCRAALPYMikQRNGQIINLSGGGAKRAQR 155
Cdd:COG0623    86 FLVhsiafaPKEELGGRF---LDTSREGFLLamdisaysLVAL--------AKAAEPLM--NEGGSIVTLTYLGAERVVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 156 FLSAYSTSKAAIvrltEAFARdyqdhpYL---------RFNVLTPGMVPT----------DMINHFETVGPGGEAIkqlp 216
Cdd:COG0623   153 NYNVMGVAKAAL----EASVR------YLaadlgpkgiRVNAISAGPIKTlaasgipgfdKLLDYAEERAPLGRNV---- 218
                         250
                  ....*....|....*...
gi 1498198613 217 rvlrifgtTAEETAELAL 234
Cdd:COG0623   219 --------TIEEVGNAAA 228
PRK06196 PRK06196
oxidoreductase; Provisional
7-153 1.42e-11

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 63.55  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlTEAERALqaAGLNVTGI-RCDVANRNEVEALASAAVERM 85
Cdd:PRK06196   23 DLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRP---DVAREAL--AGIDGVEVvMLDLADLESVRAFAERFLDSG 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613  86 GRIDLWVNNAGI-SGPFGYAldipPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRA 153
Cdd:PRK06196   98 RRIDILINNAGVmACPETRV----GDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRS 162
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
14-123 4.26e-11

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 60.27  E-value: 4.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQ--VIISSTNPTN--LTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhlVLLSRSAAPRpdAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1498198613  90 LWVNNAGISGpFGYALDIPPDAWEQVIRVNLLGT 123
Cdd:pfam08659  84 GVIHAAGVLR-DALLENMTDEDWRRVLAPKVTGT 116
PRK08177 PRK08177
SDR family oxidoreductase;
13-198 8.21e-11

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 60.43  E-value: 8.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTeaerALQAAGlNVTGIRCDVANRNEVEALASAAVERmgRIDLWV 92
Cdd:PRK08177    4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDT----ALQALP-GVHIEKLDMNDPASLDQLLQRLQGQ--RFDLLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYAL-DIPPDAWEQV--------IRV--NLLGTYYGCRAALPYMIKQRNGQIINLSGGgakraqrfLSAYS 161
Cdd:PRK08177   77 VNAGISGPAHQSAaDATAAEIGQLfltnaiapIRLarRLLGQVRPGQGVLAFMSSQLGSVELPDGGE--------MPLYK 148
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1498198613 162 TSKAAIVRLTEAFARDYQDHPylrFNVLT--PGMVPTDM 198
Cdd:PRK08177  149 ASKAALNSMTRSFVAELGEPT---LTVLSmhPGWVKTDM 184
PRK09186 PRK09186
flagellin modification protein A; Provisional
8-192 9.59e-11

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 60.39  E-value: 9.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAgLNVTGI---RCDVANRNEVEALASAAVER 84
Cdd:PRK09186    2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKE-FKSKKLslvELDITDQESLEEFLSKSAEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  85 MGRIDLWVNNAgisGPFGYA-----LDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLS- 158
Cdd:PRK09186   81 YGKIDGAVNCA---YPRNKDygkkfFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVAPKFEIy 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1498198613 159 ---------AYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPG 192
Cdd:PRK09186  158 egtsmtspvEYAAIKAGIIHLTKYLAKYFKDSN-IRVNCVSPG 199
PRK08303 PRK08303
short chain dehydrogenase; Provisional
4-202 9.81e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 60.78  E-value: 9.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   4 TPSDLRDLKAVVTGGSRGIGRAIAEALARAGAQVIIS--STN--------PTNLTE-AERALQAAGLNVtGIRCDVANRN 72
Cdd:PRK08303    2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTgrSTRarrseydrPETIEEtAELVTAAGGRGI-AVQVDHLVPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  73 EVEALASAAVERMGRIDLWVNNagISGpfGYAL---DIPpdAWEQ-----------VIRVNLLGTYYgcraALPYMIKQR 138
Cdd:PRK08303   81 QVRALVERIDREQGRLDILVND--IWG--GEKLfewGKP--VWEHsldkglrmlrlAIDTHLITSHF----ALPLLIRRP 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498198613 139 NGQIINLSGGGAK------RAQRFlsaYSTSKAAIVRLTEAFARDYQDHPYLRFNvLTPGMVPTD-MINHF 202
Cdd:PRK08303  151 GGLVVEITDGTAEynathyRLSVF---YDLAKTSVNRLAFSLAHELAPHGATAVA-LTPGWLRSEmMLDAF 217
PRK08251 PRK08251
SDR family oxidoreductase;
12-198 1.38e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 59.95  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA--GLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:PRK08251    4 KILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELGGLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGI-------SGPFgyaldippDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKR-AQRFLSAYS 161
Cdd:PRK08251   84 RVIVNAGIgkgarlgTGKF--------WANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRgLPGVKAAYA 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1498198613 162 TSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDM 198
Cdd:PRK08251  156 ASKAGVASLGEGLRAELAKTP-IKVSTIEPGYIRSEM 191
PRK07024 PRK07024
SDR family oxidoreductase;
11-201 1.64e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 59.94  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  11 LKAVVTGGSRGIGRAIAEALARAGAQVIISSTNptnlTEAERALQAAGLNVTGIRCDVANRNEVEALASAA---VERMGR 87
Cdd:PRK07024    3 LKVFITGASSGIGQALAREYARQGATLGLVARR----TDALQAFAARLPKAARVSVYAADVRDADALAAAAadfIAAHGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGIS-GPF-GYALDIppDAWEQVIRVNLLGTyygCRAALPY---MIKQRNGQIINLSGGGAKRAQRFLSAYST 162
Cdd:PRK07024   79 PDVVIANAGISvGTLtEEREDL--AVFREVMDTNYFGM---VATFQPFiapMRAARRGTLVGIASVAGVRGLPGAGAYSA 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1498198613 163 SKAAIVRLTEAFaRDYQDHPYLRFNVLTPGMVPTDMINH 201
Cdd:PRK07024  154 SKAAAIKYLESL-RVELRPAGVRVVTIAPGYIRTPMTAH 191
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
13-197 1.96e-10

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 59.70  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSR--GIGRAIAEALARAGAQVIISSTNPTNLTEA------ERALQAAGLNVTGIRC-----DVANRNEVEALAS 79
Cdd:PRK12748    8 ALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPwgmhdkEPVLLKEEIESYGVRCehmeiDLSQPYAPNRVFY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  80 AAVERMGRIDLWVNNAGISGPFGYAlDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSA 159
Cdd:PRK12748   88 AVSERLGDPSILINNAAYSTHTRLE-ELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMPDELA 166
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1498198613 160 YSTSKAAIVRLTEAFArDYQDHPYLRFNVLTPGmvPTD 197
Cdd:PRK12748  167 YAATKGAIEAFTKSLA-PELAEKGITVNAVNPG--PTD 201
PRK09291 PRK09291
SDR family oxidoreductase;
15-175 3.18e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 58.86  E-value: 3.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAavermgRIDLWVNN 94
Cdd:PRK09291    7 ITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQAAEW------DVDVLLNN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  95 AGISGPfGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIvrltEAF 174
Cdd:PRK09291   81 AGIGEA-GAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHAL----EAI 155

                  .
gi 1498198613 175 A 175
Cdd:PRK09291  156 A 156
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
12-234 3.48e-10

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 58.75  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTG--GSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRID 89
Cdd:cd05372     3 RILITGiaNDRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWV------NNAGISGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAqrfLSAY--- 160
Cdd:cd05372    83 GLVhsiafaPKVQLKGPF---LDTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYLGSERV---VPGYnvm 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 161 STSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT----------DMINHFETVGPGGEAikqlprvlrifgTTAEETA 230
Cdd:cd05372   155 GVAKAALESSVRYLAYELGRKG-IRVNAISAGPIKTlaasgitgfdKMLEYSEQRAPLGRN------------VTAEEVG 221

                  ....
gi 1498198613 231 ELAL 234
Cdd:cd05372   222 NTAA 225
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
13-198 5.64e-10

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 58.08  E-value: 5.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIIsstnPTNLTEAERALQAAGLNVtgIRCDVANRNEVEALASAAvermgRIDLWV 92
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIG----LDRLTSASNTARLADLRF--VEGDLTDRDALEKLLADV-----RPDAVI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  93 NNAGISGPFGYALDIppdawEQVIRVNLLGTYYGCRAALPYMIKqrngQIINLS-----GGGAKRAQ---------RFLS 158
Cdd:pfam01370  70 HLAAVGGVGASIEDP-----EDFIEANVLGTLNLLEAARKAGVK----RFLFASssevyGDGAEIPQeettltgplAPNS 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1498198613 159 AYSTSKAAIVRLTEAFARDYQDHP-YLR-FNVLTPGMVPTDM 198
Cdd:pfam01370 141 PYAAAKLAGEWLVLAYAAAYGLRAvILRlFNVYGPGDNEGFV 182
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
14-123 1.28e-09

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 58.16  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQ--VIISSTNPT-NLTEAERALQAAGLNVTGIRCDVANRNEVEALAsAAVERMGRIDL 90
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGARhlVLLSRRGPApRAAARAALLRAGGARVSVVRCDVTDPAALAALL-AELAAGGPLAG 232
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1498198613  91 WVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGT 123
Cdd:cd05274   233 VIHAAGV-LRDALLAELTPAAFAAVLAAKVAGA 264
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
14-196 1.52e-09

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 57.22  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQA--AGLNVTGIRCDVANRNEVEALASAAVERMGRIDLW 91
Cdd:cd09808     5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETesGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKKLHVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGIsgpFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLS------------- 158
Cdd:cd09808    85 INNAGC---MVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLVQKLNTNnlqsertafdgtm 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1498198613 159 AYSTSKAAIVRLTEAFArdyQDHPYLRFNVLTPGMVPT 196
Cdd:cd09808   162 VYAQNKRQQVIMTEQWA---KKHPEIHFSVMHPGWADT 196
PRK05854 PRK05854
SDR family oxidoreductase;
7-100 2.09e-09

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 57.00  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlTEAERAL-----QAAGLNVTGIRCDVANRNEVEALASAA 81
Cdd:PRK05854   11 DLSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNR---AKGEAAVaairtAVPDAKLSLRALDLSSLASVAALGEQL 87
                          90
                  ....*....|....*....
gi 1498198613  82 VERMGRIDLWVNNAGISGP 100
Cdd:PRK05854   88 RAEGRPIHLLINNAGVMTP 106
PRK06197 PRK06197
short chain dehydrogenase; Provisional
13-97 3.81e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 56.19  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAA--GLNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:PRK06197   19 AVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAAtpGADVTLQELDLTSLASVRAAADALRAAYPRIDL 98

                  ....*..
gi 1498198613  91 WVNNAGI 97
Cdd:PRK06197   99 LINNAGV 105
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
14-194 7.96e-09

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 54.55  E-value: 7.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlTEAERALQAAGlnVTGIRCDVANRNEVEALASAAVERMGRIDLWVN 93
Cdd:PRK06483    6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTH---YPAIDGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDGLRAIIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAGIsgpfgYALDIPPDAWEQVI----RVNLLGTYYGCRAALPYMIKQRNGQ--IINLSG-----GGAKRAqrflsAYST 162
Cdd:PRK06483   81 NASD-----WLAEKPGAPLADVLarmmQIHVNAPYLLNLALEDLLRGHGHAAsdIIHITDyvvekGSDKHI-----AYAA 150
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 163 SKAAIVRLTEAFARDYQdhPYLRFNVLTPGMV 194
Cdd:PRK06483  151 SKAALDNMTLSFAAKLA--PEVKVNSIAPALI 180
PRK07041 PRK07041
SDR family oxidoreductase;
14-196 1.54e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 53.89  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGlNVTGIRCDVANRNEVEALasaaVERMGRIDLWVN 93
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGA-PVRTAALDITDEAAVDAF----FAEAGPFDHVVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAgISGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAAlpymIKQRNGQIINLSGGGAKRAqrflSAYSTSKAAIVRLTEA 173
Cdd:PRK07041   76 TA-ADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVSGFAAVRP----SASGVLQGAINAALEA 146
                         170       180
                  ....*....|....*....|....
gi 1498198613 174 FARDYQ-DHPYLRFNVLTPGMVPT 196
Cdd:PRK07041  147 LARGLAlELAPVRVNTVSPGLVDT 170
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
13-198 3.10e-08

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 53.38  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARA----GAQVIISSTNPTNLTEAERALQAA--GLNVTGIRCDVANRNEVEALASAAVERMG 86
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLKALRELPR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  87 -----RIdLWVNNAGISGPFGYALDIPPDAwEQVIRVNLLGTYYGCRAALPYMIKQRNGQ-----IINLSGGGAKRAQRF 156
Cdd:TIGR01500  83 pkglqRL-LLINNAGTLGDVSKGFVDLSDS-TQVQNYWALNLTSMLCLTSSVLKAFKDSPglnrtVVNISSLCAIQPFKG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1498198613 157 LSAYSTSKAAIVRLTEAFARDYQDHPYLRFNvLTPGMVPTDM 198
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEKNPNVRVLN-YAPGVLDTDM 201
PRK08416 PRK08416
enoyl-ACP reductase;
14-202 3.14e-08

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 53.24  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQviISSTNPTNLTEAERALQAAGLNVtGIRC-----DVANRNEVEALASAAVERMGRI 88
Cdd:PRK08416   12 VISGGTRGIGKAIVYEFAQSGVN--IAFTYNSNVEEANKIAEDLEQKY-GIKAkayplNILEPETYKELFKKIDEDFDRV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  89 DLWVNNAGISGP-----FGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTS 163
Cdd:PRK08416   89 DFFISNAIISGRavvggYTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNLVYIENYAGHGTS 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1498198613 164 KAAIvrltEAFARdYQDHPY----LRFNVLTPGMVPTDMINHF 202
Cdd:PRK08416  169 KAAV----ETMVK-YAATELgeknIRVNAVSGGPIDTDALKAF 206
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
13-198 1.43e-07

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 51.47  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNptnlTEAERALQAAGLNV----TGIRC--DVANRNEV----EALASAAV 82
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHR----SAAAASTLAAELNArrpnSAVTCqaDLSNSATLfsrcEAIIDACF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  83 ERMGRIDLWVNNAGISGPFGYaldIPPDAWEQVIRVNLLGT----YYGCRAALPYMI---------------KQRNGQII 143
Cdd:TIGR02685  80 RAFGRCDVLVNNASAFYPTPL---LRGDAGEGVGDKKSLEVqvaeLFGSNAIAPYFLikafaqrqagtraeqRSTNLSIV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1498198613 144 NLSGGGAKRAQRFLSAYSTSKAAIVRLTEAFARDYQdhPY-LRFNVLTPG--MVPTDM 198
Cdd:TIGR02685 157 NLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELA--PLqIRVNGVAPGlsLLPDAM 212
PRK06101 PRK06101
SDR family oxidoreductase;
15-214 1.97e-07

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 50.64  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEaeraLQAAGLNVTGIRCDVANRNEV-EALASAAVERmgriDLWVN 93
Cdd:PRK06101    6 ITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDE----LHTQSANIFTLAFDVTDHPGTkAALSQLPFIP----ELWIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAgisGPFGYALDIPPDA--WEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLT 171
Cdd:PRK06101   78 NA---GDCEYMDDGKVDAtlMARVFNVNVLGVANCIEGIQPHL--SCGHRVVIVGSIASELALPRAEAYGASKAAVAYFA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1498198613 172 EAFARDYQDhpyLRFNVLT--PGMVPTDMI--NHFE-----TVGPGGEAIKQ 214
Cdd:PRK06101  153 RTLQLDLRP---KGIEVVTvfPGFVATPLTdkNTFAmpmiiTVEQASQEIRA 201
PRK08017 PRK08017
SDR family oxidoreductase;
12-207 1.26e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 48.54  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAV-VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAEralqaaGLNVTGIRCDVANRNEVEAlASAAVERM--GRI 88
Cdd:PRK08017    3 KSVlITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMN------SLGFTGILLDLDDPESVER-AADEVIALtdNRL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  89 DLWVNNAGIsGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLS---------GGGAKRAQRF-LS 158
Cdd:PRK08017   76 YGLFNNAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSsvmglistpGRGAYAASKYaLE 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613 159 AYSTS----------KAAIV-------RLTEAFARDYQDHPYL------RFNvLTPGMVPTDMINHFETVGP 207
Cdd:PRK08017  155 AWSDAlrmelrhsgiKVSLIepgpirtRFTDNVNQTQSDKPVEnpgiaaRFT-LGPEAVVPKLRHALESPKP 225
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
7-215 3.23e-06

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 47.40  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   7 DLRDLKAVVTG--GSRGIGRAIAEALARAGAQVIISSTnPTNLTEAERALQ--AAGLNVTGIR-CDVANRNEVEALASAA 81
Cdd:PRK07370    3 DLTGKKALVTGiaNNRSIAWGIAQQLHAAGAELGITYL-PDEKGRFEKKVRelTEPLNPSLFLpCDVQDDAQIEETFETI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  82 VERMGRIDLWV------NNAGISGPFGyalDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSGGGAKRAQR 155
Cdd:PRK07370   82 KQKWGKLDILVhclafaGKEELIGDFS---ATSREGFARALEISAYSLAPLCKAAKPLM--SEGGSIVTLTYLGGVRAIP 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613 156 FLSAYSTSKAAIvrltEAFARdyqdhpYL---------RFNVLTPGMVPT----------DMINHFETVGPGGEAIKQL 215
Cdd:PRK07370  157 NYNVMGVAKAAL----EASVR------YLaaelgpkniRVNAISAGPIRTlassavggilDMIHHVEEKAPLRRTVTQT 225
PRK06720 PRK06720
hypothetical protein; Provisional
13-97 5.65e-06

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 45.73  E-value: 5.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDLWV 92
Cdd:PRK06720   19 AIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSRIDMLF 98

                  ....*
gi 1498198613  93 NNAGI 97
Cdd:PRK06720   99 QNAGL 103
PRK06953 PRK06953
SDR family oxidoreductase;
13-198 1.55e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 45.06  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnltEAERALQAAGLNVTGIrcDVANRNEVEALASaaveRMG--RIDL 90
Cdd:PRK06953    4 VLIVGASRGIGREFVRQYRADGWRVIATARDA----AALAALQALGAEALAL--DVADPASVAGLAW----KLDgeALDA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  91 WVNNAGISGPFGYAldIPPDAWEQ---VIRVNLLGTYYGCRAALPyMIKQRNGQIINLSG-----GGAKRAQRFLsaYST 162
Cdd:PRK06953   74 AVYVAGVYGPRTEG--VEPITREDfdaVMHTNVLGPMQLLPILLP-LVEAAGGVLAVLSSrmgsiGDATGTTGWL--YRA 148
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1498198613 163 SKAAivrLTEAFARDYQDHPYLRFNVLTPGMVPTDM 198
Cdd:PRK06953  149 SKAA---LNDALRAASLQARHATCIALHPGWVRTDM 181
PRK08862 PRK08862
SDR family oxidoreductase;
15-201 1.97e-05

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 44.71  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  15 VTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERMGR-IDLWVN 93
Cdd:PRK08862   10 ITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNRaPDVLVN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  94 NAgISGPFGYALDipPDAWEQVIR--VNLLGTYYG-CRAALPYMIK-QRNGQIINLsggGAKRAQRFLSAYSTSKAAIVR 169
Cdd:PRK08862   90 NW-TSSPLPSLFD--EQPSESFIQqlSSLASTLFTyGQVAAERMRKrNKKGVIVNV---ISHDDHQDLTGVESSNALVSG 163
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1498198613 170 LTEAFARDYQDhpylrFNVLTPGMVPTdmINH 201
Cdd:PRK08862  164 FTHSWAKELTP-----FNIRVGGVVPS--IFS 188
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
12-196 2.41e-05

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 44.73  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTG--GSRGIGRAIAEALARAGAQVIIsstnpTNLTEA-ERALQ--AAGLNVTGI-RCDVANRNEVEALASAAVERM 85
Cdd:PRK08415    7 KGLIVGvaNNKSIAYGIAKACFEQGAELAF-----TYLNEAlKKRVEpiAQELGSDYVyELDVSKPEHFKSLAESLKKDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNA------GISGPFgyaLDIPPDAWEQVIRVNLLGTYYGCRAALPYMikQRNGQIINLSG-GGAKraqrFLS 158
Cdd:PRK08415   82 GKIDFIVHSVafapkeALEGSF---LETSKEAFNIAMEISVYSLIELTRALLPLL--NDGASVLTLSYlGGVK----YVP 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1498198613 159 AYS---TSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPT 196
Cdd:PRK08415  153 HYNvmgVAKAALESSVRYLAVDLGKKG-IRVNAISAGPIKT 192
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
50-177 4.40e-05

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 43.72  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  50 AERALQAAGLNVTGIRCDVANRNEVEALAS------------------AAVERMGRIDLWVNNAGISGPFGyALDIPPDA 111
Cdd:cd05361    17 SAEALTEDGYTVVCHDASFADAAERQAFESenpgtkalseqkpeelvdAVLQAGGAIDVLVSNDYIPRPMN-PIDGTSEA 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198613 112 -WEQVIRVNLLGTYYGCRAALPYMIKQRNGQIINLSGGGAKRAQRFLSAYSTSKAAIVRLTEAFARD 177
Cdd:cd05361    96 dIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKE 162
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
13-125 4.48e-05

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 44.13  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEA-ERAL-QAAGLNVTGIRCDVANRNEVEALASAAVERMGRIDL 90
Cdd:cd09809     4 IIITGANSGIGFETARSFALHGAHVILACRNMSRASAAvSRILeEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSPLHV 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1498198613  91 WVNNAGIsgpFGYALDIPPDAWEQVIRVNLLGTYY 125
Cdd:cd09809    84 LVCNAAV---FALPWTLTEDGLETTFQVNHLGHFY 115
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
13-199 5.09e-05

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 43.91  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  13 AVVTGGSRGIGRAIAEAL-----ARAGAQVIISSTNPTNLTEAERALQA----AGLNVTGIRCDVANRNEVEALASAAVE 83
Cdd:cd08941     4 VLVTGANSGLGLAICERLlaeddENPELTLILACRNLQRAEAACRALLAshpdARVVFDYVLVDLSNMVSVFAAAKELKK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  84 RMGRIDLWVNNAGIsGPFG----------------YALDIP-----------------PDAWEQVIRVNLLGTYYGCRAA 130
Cdd:cd08941    84 RYPRLDYLYLNAGI-MPNPgidwigaikevltnplFAVTNPtykiqaegllsqgdkatEDGLGEVFQTNVFGHYYLIREL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 131 LPyMIKQRN--GQIINLSGGGAKRAQRFLS---------AYSTSKAAIVRLTEAFARDYQDHPyLRFNVLTPGMVPTDMI 199
Cdd:cd08941   163 EP-LLCRSDggSQIIWTSSLNASPKYFSLEdiqhlkgpaPYSSSKYLVDLLSLALNRKFNKLG-VYSYVVHPGICTTNLT 240
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
12-170 5.18e-05

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 43.30  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPtnlteaERALQAAGLNVTGIRCDVANRnevEALASAaverMGRIDLW 91
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGHPVRALVRDP------EKAAALAAAGVEVVQGDLDDP---ESLAAA----LAGVDAV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGISGPFGYALDippdaWEQVIRVnllgtyygCRAAlpymikQRNG--QIINLSGGGAKRAQrfLSAYSTSKAAIVR 169
Cdd:COG0702    68 FLLVPSGPGGDFAVD-----VEGARNL--------ADAA------KAAGvkRIVYLSALGADRDS--PSPYLRAKAAVEE 126

                  .
gi 1498198613 170 L 170
Cdd:COG0702   127 A 127
PLN00015 PLN00015
protochlorophyllide reductase
14-122 1.26e-04

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 42.77  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQVIISSTNptNLTEAERALQAAGL---NVTGIRCDVANRNEVEALASaAVERMGR-ID 89
Cdd:PLN00015    1 IITGASSGLGLATAKALAETGKWHVVMACR--DFLKAERAAKSAGMpkdSYTVMHLDLASLDSVRQFVD-NFRRSGRpLD 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1498198613  90 LWVNNAGISGPFGYALDIPPDAWEQVIRVNLLG 122
Cdd:PLN00015   78 VLVCNAAVYLPTAKEPTFTADGFELSVGTNHLG 110
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
12-196 2.52e-04

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 41.82  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVII----SSTNPTNLTEAERalqaaglNVTGIRCDVANRNEVEalasaavERMGR 87
Cdd:cd05256     1 RVLVTGGAGFIGSHLVERLLERGHEVIVldnlSTGKKENLPEVKP-------NVKFIEGDIRDDELVE-------FAFEG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  88 IDLWVNNAGISgpfgyalDIPPDAWEQVI--RVNLLGTYYGCRAALPYMIKqrngQIINLSGGGA-----------KRAQ 154
Cdd:cd05256    67 VDYVFHQAAQA-------SVPRSIEDPIKdhEVNVLGTLNLLEAARKAGVK----RFVYASSSSVygdppylpkdeDHPP 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1498198613 155 RFLSAYSTSKAAIVRLTEAFARDYqDHPY--LR-FNVLTPGMVPT 196
Cdd:cd05256   136 NPLSPYAVSKYAGELYCQVFARLY-GLPTvsLRyFNVYGPRQDPN 179
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
12-80 3.53e-04

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 41.12  E-value: 3.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERalqaaglnVTGIRCDVANRNEVEALASA 80
Cdd:cd05265     2 KILIIGGTRFIGKALVEELLAAGHDVTVFNRGRTKPDLPEG--------VEHIVGDRNDRDALEELLGG 62
PRK05579 PRK05579
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
5-47 4.82e-04

bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated


Pssm-ID: 235513 [Multi-domain]  Cd Length: 399  Bit Score: 40.89  E-value: 4.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   5 PSDLRDLKAVVTGGS--------RGI--------GRAIAEALARAGAQVI-ISStnPTNL 47
Cdd:PRK05579  183 PKDLAGKRVLITAGPtrepidpvRYItnrssgkmGYALARAAARRGADVTlVSG--PVNL 240
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
13-83 4.86e-04

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 41.00  E-value: 4.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1498198613  13 AVVTGGSRGIGRAIAEALARAGAQ--VIISSTNP--TNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVE 83
Cdd:cd08952   233 VLVTGGTGALGAHVARWLARRGAEhlVLTSRRGPdaPGAAELVAELTALGARVTVAACDVADRDALAALLAALPA 307
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
8-173 9.86e-04

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 39.57  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   8 LRDLKAVVTG--GSRGIGRAIAEALARAGAQVIISSTNpTNLTEAERALQAAGLNVTGIRCDVANRNEVEALASAAVERM 85
Cdd:PRK08690    4 LQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVV-DKLEERVRKMAAELDSELVFRCDVASDDEINQVFADLGKHW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  86 GRIDLWVNNAG------ISGPFgyaLD-IPPDAWEQVIRVNLLGTYYGCRAALPyMIKQRNGQIINLSGGGAKRAQRFLS 158
Cdd:PRK08690   83 DGLDGLVHSIGfapkeaLSGDF---LDsISREAFNTAHEISAYSLPALAKAARP-MMRGRNSAIVALSYLGAVRAIPNYN 158
                         170
                  ....*....|....*...
gi 1498198613 159 AYSTSKAAI---VRLTEA 173
Cdd:PRK08690  159 VMGMAKASLeagIRFTAA 176
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
12-214 1.31e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 39.54  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAGAQVIIsstnPTNLTEAERALQAAGLN--VTGIRCDVANRNEVEALasaaverMGRID 89
Cdd:cd05271     2 VVTVFGATGFIGRYVVNRLAKRGSQVIV----PYRCEAYARRLLVMGDLgqVLFVEFDLRDDESIRKA-------LEGSD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  90 LWVNNAGI---SGPFGYAlDIPPDAWEQVIRVnllgtyygCRAAlpymikqRNGQIINLSGGGAKRAQRflSAYSTSKAA 166
Cdd:cd05271    71 VVINLVGRlyeTKNFSFE-DVHVEGPERLAKA--------AKEA-------GVERLIHISALGADANSP--SKYLRSKAE 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613 167 -------------IVRLTEAFAR-DYQDHPYLRFNVLTPgmvptdminhFETVGPGGEAIKQ 214
Cdd:cd05271   133 geeavreafpeatIVRPSVVFGReDRFLNRFAKLLAFLP----------FPPLIGGGQTKFQ 184
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
1-85 1.67e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 39.28  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613   1 MARTPSDLRDlKAVVTGGSRgIGRAIAEALARAGAQVIISSTNPtnlteaERALQAAGLNVTGIRCDVANRnevEALASA 80
Cdd:COG0569    87 MERGIKKLKM-HVIIIGAGR-VGRSLARELEEEGHDVVVIDKDP------ERVERLAEEDVLVIVGDATDE---EVLEEA 155

                  ....*
gi 1498198613  81 AVERM 85
Cdd:COG0569   156 GIEDA 160
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
7-82 1.78e-03

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 38.53  E-value: 1.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198613   7 DLRDLKAVVTGGSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERALQA-AGLNVTGIRCDvANRNEVEALASAAV 82
Cdd:cd01078    25 DLKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRArFGEGVGAVETS-DDAARAAAIKGADV 100
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
14-77 3.12e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 38.42  E-value: 3.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198613  14 VVTGGSRGIGRAIAEALARAGAQ--VIISSTNPTNLTEAE-RALQAAGLNVTGIRCDVANRNEVEAL 77
Cdd:cd08955   153 LITGGLGGLGLLVAEWLVERGARhlVLTGRRAPSAAARQAiAALEEAGAEVVVLAADVSDRDALAAA 219
PRK07578 PRK07578
short chain dehydrogenase; Provisional
12-248 4.19e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 37.49  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  12 KAVVTGGSRGIGRAIAEALARAgAQVIisstnptnlteaeralqAAGLNVTGIRCDVANRNEVEALasaaVERMGRIDLW 91
Cdd:PRK07578    2 KILVIGASGTIGRAVVAELSKR-HEVI-----------------TAGRSSGDVQVDITDPASIRAL----FEKVGKVDAV 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  92 VNNAGiSGPFGYALDIPPDAWEQVIRVNLLGTYYGCRAALPYMikqRNGQIINL-SGGGAKRAQRFLSAYSTSKAAIvrl 170
Cdd:PRK07578   60 VSAAG-KVHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYL---NDGGSFTLtSGILSDEPIPGGASAATVNGAL--- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613 171 tEAFAR----DYQDHpyLRFNVLTPGMVpTDMINHFETVGPGGEAIkqlprvlrifgtTAEETAELALRIVREGKNGQVF 246
Cdd:PRK07578  133 -EGFVKaaalELPRG--IRINVVSPTVL-TESLEKYGPFFPGFEPV------------PAARVALAYVRSVEGAQTGEVY 196

                  ..
gi 1498198613 247 EV 248
Cdd:PRK07578  197 KV 198
CoaBC COG0452
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
4-48 4.93e-03

Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440221 [Multi-domain]  Cd Length: 399  Bit Score: 38.08  E-value: 4.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198613   4 TPSDLRDLKAVVTGGS--------RGI--------GRAIAEALARAGAQVI-ISStnPTNLT 48
Cdd:COG0452   181 PKKDLAGKKVLITAGPtrepidpvRFIsnrssgkmGYALAEAAAARGAEVTlVSG--PVALP 240
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
14-136 6.13e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 37.30  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  14 VVTGGSrGIGRAIAEALARAGAQVIISSTNPTNL------------TEAERALQAAGLNVTGIRCDV----ANRNEVEAL 77
Cdd:cd05188   139 LVLGAG-GVGLLAAQLAKAAGARVIVTDRSDEKLelakelgadhviDYKEEDLEEELRLTGGGGADVvidaVGGPETLAQ 217
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198613  78 ASAAVERMGRIdlwVNNAGISGPfgyalDIPPDAWEQVIR-VNLLGTYYGCRAALPYMIK 136
Cdd:cd05188   218 ALRLLRPGGRI---VVVGGTSGG-----PPLDDLRRLLFKeLTIIGSTGGTREDFEEALD 269
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
80-155 8.58e-03

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 36.90  E-value: 8.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1498198613  80 AAVERM-GRIDLWVNNAGISGPFgyaldiPPDAweqVIRVNLLGTYYGCRAALPYMikQRNGQIINLSG-GGAKRAQR 155
Cdd:PRK12428   40 AAVAALpGRIDALFNIAGVPGTA------PVEL---VARVNFLGLRHLTEALLPRM--APGGAIVNVASlAGAEWPQR 106
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
18-54 8.96e-03

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 36.30  E-value: 8.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1498198613  18 GSRGIGRAIAEALARAGAQVIISSTNPTNLTEAERAL 54
Cdd:COG2085     5 GTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAEL 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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