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Conserved domains on  [gi|33667109|ref|NP_878912|]
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dehydrogenase/reductase SDR family member 2, mitochondrial isoform 1 [Homo sapiens]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 27-226 5.07e-99

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd08936:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 256  Bit Score: 291.37  E-value: 5.07e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  27 GIDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAK 106
Cdd:cd08936   1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 107 ALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVY 185
Cdd:cd08936  81 AVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRgGGSVVIVSSVAAFHPFPGLGPY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 33667109 186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:cd08936 161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSAL 201
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-226 5.07e-99

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: 291.37  E-value: 5.07e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  27 GIDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAK 106
Cdd:cd08936   1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 107 ALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVY 185
Cdd:cd08936  81 AVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRgGGSVVIVSSVAAFHPFPGLGPY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 33667109 186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:cd08936 161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSAL 201
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 34-222 1.19e-66

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: 208.49  E-value: 1.19e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:COG1028  84 LDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMrERGGGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                       170       180       190
                ....*....|....*....|....*....|
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:COG1028 163 VGLTRSLALELAPRGIRVNAVAPGPIDTPM 192
FabG-like PRK07231
SDR family oxidoreductase;
34-241 3.40e-64

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 202.37  E-value: 3.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK07231  82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMrGEGGGAIVNVASTAGLRPRPGLGWYNASKGAV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvvriGFMGMSLSGRTSR 241
Cdd:PRK07231 162 ITLTKALAAELGPDKIRVNAVAPVVVETGLLE----AFMGEPTPENRAK 206
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 37-227 7.54e-54

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 173.95  E-value: 7.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   117 LVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVnISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 33667109   196 TRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 38-217 5.71e-12

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: 64.56  E-value: 5.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    38 VAVVTGSTSGIGFAIARRLARDGAHVVISSRK-----QQNVDRAMAKLQGEGLSVAGIVCHVGKAEDR-EQLVAKALEHC 111
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRsaaaaSTLAAELNARRPNSAVTCQADLSNSATLFSRcEAIIDACFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   112 GGVDFLVCSAGV---NPLV----GSTLGTSEQI---WDKILSVNVKSPALLLSQLLPYMENRRGA--------VILVSSI 173
Cdd:TIGR02685  83 GRCDVLVNNASAfypTPLLrgdaGEGVGDKKSLevqVAELFGSNAIAPYFLIKAFAQRQAGTRAEqrstnlsiVNLCDAM 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 33667109   174 AAyNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGI 217
Cdd:TIGR02685 163 TD-QPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL 205
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 40-175 4.56e-07

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: 49.02  E-value: 4.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109     40 VVTGSTSGIGFAIARRLARDGA-HVVISSR---KQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    116 FLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYMENRrgAVILVSSIAA 175
Cdd:smart00822  84 GVIHAAGVLDD-GVLASLTPERFAAVLAPKAAG-AWNLHELTADLPLD--FFVLFSSIAG 139
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-226 5.07e-99

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: 291.37  E-value: 5.07e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  27 GIDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAK 106
Cdd:cd08936   1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 107 ALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVY 185
Cdd:cd08936  81 AVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRgGGSVVIVSSVAAFHPFPGLGPY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 33667109 186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:cd08936 161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSAL 201
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 34-222 1.19e-66

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: 208.49  E-value: 1.19e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:COG1028  84 LDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMrERGGGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                       170       180       190
                ....*....|....*....|....*....|
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:COG1028 163 VGLTRSLALELAPRGIRVNAVAPGPIDTPM 192
FabG-like PRK07231
SDR family oxidoreductase;
34-241 3.40e-64

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 202.37  E-value: 3.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK07231  82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMrGEGGGAIVNVASTAGLRPRPGLGWYNASKGAV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvvriGFMGMSLSGRTSR 241
Cdd:PRK07231 162 ITLTKALAAELGPDKIRVNAVAPVVVETGLLE----AFMGEPTPENRAK 206
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 39-239 2.84e-61

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: 194.42  E-value: 2.84e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAmAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLV 118
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAEL-AAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 119 CSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTR 197
Cdd:cd05233  80 NNAGIARPGPLEELTDED-WDRVLDVNLTGVFLLTRAALPHMkKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 33667109 198 TLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSLSGRT 239
Cdd:cd05233 159 SLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAI 200
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
34-236 8.47e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 178.14  E-value: 8.47e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:COG0300  83 IDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMrARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSLS 236
Cdd:COG0300 162 EGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLS 205
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
34-221 5.88e-54

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 175.73  E-value: 5.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK05653  83 LDILVNNAGITR-DALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMiKARYGRIVNISSVSGVTGNPGQTNYSAAKAGV 161

                        170       180
                 ....*....|....*....|....*....
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK05653 162 IGFTKALALELASRGITVNAVAPGFIDTD 190
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 37-227 7.54e-54

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 173.95  E-value: 7.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   117 LVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVnISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 33667109   196 TRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 35-229 9.60e-53

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: 172.67  E-value: 9.60e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEglsVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGR---ALAVPLDVTDEAAVEAAVAAAVAEFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:COG4221  81 DVLVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMrARGSGHIVNISSIAGLRPYPGGAVYAATKAAVR 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 33667109 194 GLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIG 229
Cdd:COG4221 160 GLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDG 195
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 44-221 1.71e-47

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: 158.75  E-value: 1.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    44 STSGIGFAIARRLARDGAHVVIS--SRKQQNVDRAMAKLQGEGLsvagIVCHVGKAEDREQLVAKALEHCGGVDFLVCSA 121
Cdd:pfam13561   4 NESGIGWAIARALAEEGAEVVLTdlNEALAKRVEELAEELGAAV----LPCDVTDEEQVEALVAAAVEKFGRLDILVNNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   122 GV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRTLA 200
Cdd:pfam13561  80 GFaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM-KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLA 158

                         170       180
                  ....*....|....*....|.
gi 33667109   201 LELAPKDIRVNCVVPGIIKTD 221
Cdd:pfam13561 159 VELGPRGIRVNAISPGPIKTL 179
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 36-221 1.09e-46

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: 157.44  E-value: 1.09e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 116 FLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:cd05344  81 ILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159

                       170       180
                ....*....|....*....|....*..
gi 33667109 195 LTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05344 160 LVKTLSRELAPDGVTVNSVLPGYIDTE 186
PRK12826 PRK12826
SDR family oxidoreductase;
34-250 1.40e-44

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 151.99  E-value: 1.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAynPVVA---LGVYNVSK 189
Cdd:PRK12826  84 LDILVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALiRAGGGRIVLTSSVAG--PRVGypgLAHYAASK 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKTDfskvvRIGFMGMSLSGRTSRNIISCRGLG 250
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDTP-----MAGNLGDAQWAEAIAAAIPLGRLG 216
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 34-227 1.84e-44

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 151.50  E-value: 1.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE-GLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGAlGGKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGV---NPLvgstLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK05557  83 GVDILVNNAGItrdNLL----MRMKEEDWDRVIDTNLTGVFNLTKAVARPMmKQRSGRIINISSVVGLMGNPGQANYAAS 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK05557 159 KAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALP 197
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 37-227 7.90e-44

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: 149.62  E-value: 7.90e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGVnplvgsT-----LGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAY--NPVVAlgVYNVS 188
Cdd:cd05333  81 LVNNAGI------TrdnllMRMSEEDWDAVINVNLTGVFNVTQAVIRAMiKRRSGRIINISSVVGLigNPGQA--NYAAS 152

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33667109 189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:cd05333 153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALP 191
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-221 8.88e-44

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 149.61  E-value: 8.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAK-LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEeIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK05565  83 KIDILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVnISSIWGLIGASCEVLYSASKGA 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK05565 162 VNAFTKALAKELAPSGIRVNAVAPGAIDTE 191
PRK07035 PRK07035
SDR family oxidoreductase;
34-223 9.76e-43

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 147.08  E-value: 9.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK07035  86 LDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMkEQGGGSIVNVASVNGVSPGDFQGIYSITKAAV 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PRK07035 166 ISMTKAFAKECAPFGIRVNALLPGLTDTKFA 196
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 31-221 5.81e-42

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 145.01  E-value: 5.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   31 KGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRK-QQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:PRK12825   1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSdEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK12825  81 RFGRIDILVNNAGIFED-KPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSNYAAA 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK12825 160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTD 192
PRK07326 PRK07326
SDR family oxidoreductase;
33-223 1.74e-39

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 138.22  E-value: 1.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   33 VLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK07326  82 GLDVLIANAGVG-HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVATHFN 191
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 37-224 7.16e-39

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: 136.98  E-value: 7.16e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDrAMAKLQGEGLSVagIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLE-SLGELLNDNLEV--LELDVTDEESIKAAVKEVIERFGRIDV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:cd05374  78 LVNNAGYG-LFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMrKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEAL 156

                       170       180
                ....*....|....*....|....*....
gi 33667109 196 TRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:cd05374 157 SESLRLELAPFGIKVTIIEPGPVRTGFAD 185
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 34-220 1.39e-38

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 136.55  E-value: 1.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAG---VNPLVgsTLGTSEqiWDKILSVNVKSPALLLSQLLPYMENRRGAVILvsSIAAYNPVVAL---GVYNV 187
Cdd:PRK12429  82 VDILVNNAGiqhVAPIE--DFPTEK--WKKMIAIMLDGAFLTTKAALPIMKAQGGGRII--NMASVHGLVGSagkAAYVS 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK12429 156 AKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 28-220 2.45e-38

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 135.96  E-value: 2.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   28 IDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqgEGLSVAGIVCHVGKAEDREQLVAKA 107
Cdd:PRK12829   3 IDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFDTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  108 LEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAynPVVALGV-- 184
Cdd:PRK12829  81 VERFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLkASGHGGVIIALSSVA--GRLGYPGrt 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  185 -YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK12829 159 pYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRG 195
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 34-222 3.00e-38

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 135.48  E-value: 3.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTlGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK12939  85 LDGLVNNAGITNSKSAT-ELDIDTWDAVMNVNVRGTFLMLRAALPHLrDSGRGRIVNLASDTALWGAPKLGAYVASKGAV 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK12939 164 IGMTRSLARELGGRGITVNAIAPGLTATEA 193
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 34-215 3.06e-38

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: 135.21  E-value: 3.06e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRkqqNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05345   3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADI---NADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd05345  80 LDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIInIASTAGLRPRPGLTWYNASKGWV 159

                       170       180
                ....*....|....*....|...
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVP 215
Cdd:cd05345 160 VTATKAMAVELAPRNIRVNCLCP 182
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 34-257 3.93e-38

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: 135.23  E-value: 3.93e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVG---KAEDREQLVAKALEH 110
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKILLVVAdltEEEGQDRIISTTLAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 111 CGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:cd05364  81 FGRLDILVNNAGI-LAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVLYYCISKA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33667109 191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVvrigfMGMS--LSGRTSRNIISCRGLGSQRTVQE 257
Cdd:cd05364 160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRR-----MGMPeeQYIKFLSRAKETHPLGRPGTVDE 223
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 34-222 4.95e-38

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: 134.71  E-value: 4.95e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVIS-SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 113 GVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd05362  81 GVDILVNNAGVMLK-KPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL-RDGGRIINISSSLTAAYTPNYGAYAGSKAAV 158

                       170       180       190
                ....*....|....*....|....*....|
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:cd05362 159 EAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 34-239 1.11e-37

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 134.30  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnplvgsTLGTSE-----QIWDKILSVNVKSpALLLSQLLP--YMENRR-GAVILVSSIA--AYNPVVALG 183
Cdd:PRK08213  90 VDILVNNAGA------TWGAPAedhpvEAWDKVMNLNVRG-LFLLSQAVAkrSMIPRGyGRIINVASVAglGGNPPEVMD 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 33667109  184 V--YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVrIGFMGMSLSGRT 239
Cdd:PRK08213 163 TiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGT-LERLGEDLLAHT 219
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
33-215 9.28e-37

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 138.83  E-value: 9.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   33 VLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK08324 419 PLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEAALAFG 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME--NRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK08324 498 GVDIVVSNAGIAI-SGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKaqGLGGSIVFIASKNAVNPGPNFGAYGAAKA 576

                        170       180
                 ....*....|....*....|....*
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVP 215
Cdd:PRK08324 577 AELHLVRQLALELGPDGIRVNGVNP 601
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 37-224 2.18e-36

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: 129.66  E-value: 2.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGA-HVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 116 FLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIAAynpVVALGvYNVSKTALLG 194
Cdd:cd05324  81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGrIVNVSSGLG---SLTSA-YGVSKAALNA 156

                       170       180       190
                ....*....|....*....|....*....|
gi 33667109 195 LTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:cd05324 157 LTRILAKELKETGIKVNACCPGWVKTDMGG 186
PRK06181 PRK06181
SDR family oxidoreductase;
36-224 2.48e-36

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 130.87  E-value: 2.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:PRK06181  81 ILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALHGF 160

                        170       180
                 ....*....|....*....|....*....
gi 33667109  196 TRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:PRK06181 161 FDSLRIELADDGVAVTVVCPGFVATDIRK 189
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 34-237 3.18e-36

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: 129.92  E-value: 3.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAgivCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALR---VDVTDEQQVAALFERAVEEFGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd08944  78 LDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVnLSSIAGQSGDPGYGAYGASKAAI 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSLSG 237
Cdd:cd08944 158 RNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPG 202
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 39-223 4.72e-36

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: 129.16  E-value: 4.72e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAmakLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLV 118
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAA---AAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 119 CSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRT 198
Cdd:cd08929  80 NNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEA 159

                       170       180
                ....*....|....*....|....*
gi 33667109 199 LALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:cd08929 160 AMLDLREANIRVVNVMPGSVDTGFA 184
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 34-220 6.64e-36

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: 129.49  E-value: 6.64e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05329   4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 -VDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSpALLLSQLL-PYME-NRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:cd05329  84 kLNILVNNAGTNIRKEAKDYTEED-YSLIMSTNFEA-AYHLSRLAhPLLKaSGNGNIVFISSVAGVIAVPSGAPYGATKG 161

                       170       180       190
                ....*....|....*....|....*....|
gi 33667109 191 ALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05329 162 ALNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 34-224 7.23e-36

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: 129.43  E-value: 7.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQN----VDRAMAKLQGEGLSVAGivcHVGKAEDREQLVAKALE 109
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDaaeeVVEEIKAVGGKAIAVQA---DVSKEEDVVALFQSAIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 110 HCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:cd05358  78 EFGTLDILVNNAGLQGDASSHEMTLED-WNKVIDVNLTGQFLCAREAIKRFrkSKIKGKIINMSSVHEKIPWPGHVNYAA 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 33667109 188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:cd05358 157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINA 193
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 25-224 2.62e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 127.85  E-value: 2.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   25 STGIDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnVDRAMAKLQGEGLsvAGIVCHVGKAEDREQLV 104
Cdd:PRK06841   4 TKQFDLAFDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSED-VAEVAAQLLGGNA--KGLVCDVSDSQSVEAAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  105 AKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAynpVVALG 183
Cdd:PRK06841  81 AAVISAFGRIDILVNSAGVALL-APAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMiAAGGGKIVNLASQAG---VVALE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 33667109  184 ---VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:PRK06841 157 rhvAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGK 200
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 34-227 2.95e-35

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: 127.47  E-value: 2.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05347   3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd05347  83 IDILVNNAGII-RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMiKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:cd05347 162 AGLTKALATEWARHGIQVNAIAPGYFATEMTEAVV 196
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 34-223 6.47e-35

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: 126.93  E-value: 6.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnvdrAMAKLQGEGLSVAGIVCHV-----GKAEDREQLVAKAL 108
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREE----RLEEVKSECLELGAPSPHVvpldmSDLEDAEQVVEEAL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 109 EHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:cd05332  77 KLFGGLDILINNAGISMR-SLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLiERSQGSIVVVSSIAGKIGVPFRTAYAA 155

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 33667109 188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:cd05332 156 SKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIA 191
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 32-218 8.70e-35

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 126.61  E-value: 8.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK07890   1 MLLKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQL-LPYMENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK07890  81 GRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLG-TLRLTQAfTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKG 159

                        170       180
                 ....*....|....*....|....*...
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGII 218
Cdd:PRK07890 160 ALLAASQSLATELGPQGIRVNSVAPGYI 187
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 39-221 1.17e-34

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: 126.04  E-value: 1.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVissrkqqNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLV 118
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVI-------ALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 119 CSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLTR 197
Cdd:cd05331  74 NCAGV-LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152

                       170       180
                ....*....|....*....|....
gi 33667109 198 TLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05331 153 CLGLELAPYGVRCNVVSPGSTDTA 176
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 34-221 1.98e-34

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 125.38  E-value: 1.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVissrkqqNVDRAMakLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVI-------GFDQAF--LTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK08220  77 LDVLVNAAGILRM-GATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFrRQRSGAIVTVGSNAAHVPRIGMAAYGASKAAL 155

                        170       180
                 ....*....|....*....|....*....
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCNVVSPGSTDTD 184
PRK06500 PRK06500
SDR family oxidoreductase;
34-220 2.33e-34

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 125.07  E-value: 2.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqgeGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAEL---GESALVIRADAGDVAAQKALAQALAEAFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnplvgSTLG----TSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK06500  81 LDAVFINAGV-----AKFApledWDEAMFDRSFNTNVKGPYFLIQALLPLL-ANPASIVLNGSINAHIGMPNSSVYAASK 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06500 155 AALLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
PRK06172 PRK06172
SDR family oxidoreductase;
34-221 3.02e-34

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 125.25  E-value: 3.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK06172  85 LDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMlAQGGGAIVNTASVAGLGAAPKMSIYAASKHAV 164

                        170       180
                 ....*....|....*....|....*....
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06172 165 IGLTKSAAIEYAKKGIRVNAVCPAVIDTD 193
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 36-232 5.23e-34

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: 124.57  E-value: 5.23e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:cd08945   3 SEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPID 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 116 FLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLP---YMENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd08945  83 VLVNNAG-RSGGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGV 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMG 232
Cdd:cd08945 162 VGFTKALGLELARTGITVNAVCPGFVETPMAASVREHYAD 201
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 37-222 8.81e-34

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: 123.57  E-value: 8.81e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRkqqNVDRAMAKLQGEGLSVAGIV---CHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDR---NENPGAAAELQAINPKVKATfvqCDVTSWEQLAAAFKKAIEKFGR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVN-PLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME----NRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:cd05323  78 VDILINNAGILdEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDknkgGKGGVIVNIGSVAGLYPAPQFPVYSAS 157

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33667109 189 KTALLGLTRTLALELAPK-DIRVNCVVPGIIKTDF 222
Cdd:cd05323 158 KHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL 192
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 37-220 1.41e-33

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: 122.75  E-value: 1.41e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE----GLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEanasGQKVSYISADLSDYEEVEQAFAQAVEKGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 113 GVDFLVCSAGVN-PLVGSTLgTSEQIwDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:cd08939  82 PPDLVVNCAGISiPGLFEDL-TAEEF-ERGMDVNYFGSLNVAHAVLPLMkEQRPGHIVFVSSQAALVGIYGYSAYCPSKF 159

                       170       180       190
                ....*....|....*....|....*....|
gi 33667109 191 ALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd08939 160 ALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 34-221 1.43e-33

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: 123.08  E-value: 1.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGL-SVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGgRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 113 GVDFLVCSAGVNPLVGSTlGTSEQIWDKILSVNVKSPALLLSQLLPY-MENRRGAVIL-VSSIAAYNPVVALGVYNVSKT 190
Cdd:cd05369  81 KIDILINNAAGNFLAPAE-SLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILnISATYAYTGSPFQVHSAAAKA 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 33667109 191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05369 160 GVDALTRSLAVEWGPYGIRVNAIAPGPIPTT 190
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 37-227 2.43e-33

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: 121.70  E-value: 2.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRamakLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAA----LSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:cd08932  77 LVHNAGIG-RPTTLREGSDAELEAHFSINVIAPAELTRALLPALrEAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRAL 155

                       170       180       190
                ....*....|....*....|....*....|..
gi 33667109 196 TRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:cd08932 156 AHALRQEGWDHGVRVSAVCPGFVDTPMAQGLT 187
PRK07063 PRK07063
SDR family oxidoreductase;
34-220 2.89e-33

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 122.47  E-value: 2.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQ--GEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIArdVAGARVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK07063  85 GPLDVLVNNAGIN-VFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMvERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07063 164 GLLGLTRALGIEYAARNVRVNAIAPGYIET 193
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-234 8.68e-33

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 121.37  E-value: 8.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQ-QNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRaEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK06077  84 VADILVNNAGLG-LFSPFLNVDDKLIDKHISTDFKS-VIYCSQELAKEMREGGAIVNIASVAGIRPAYGLSIYGAMKAAV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 33667109  193 LGLTRTLALELAPKdIRVNCVVPGIIKTDFSKVVrIGFMGMS 234
Cdd:PRK06077 162 INLTKYLALELAPK-IRVNAIAPGFVKTKLGESL-FKVLGMS 201
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 39-226 8.87e-33

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: 120.92  E-value: 8.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQ----QNVDRAMAKLQGEGLSVAGivcHVGKAEDREQLVAKALEHCGGV 114
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSkdaaAEVAAEIEELGGKAVVVRA---DVSQPQDVEEMFAAVKERFGRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd05359  78 DVLVSNAAAGAFR-PLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAKAALE 156

                       170       180       190
                ....*....|....*....|....*....|...
gi 33667109 194 GLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:cd05359 157 ALVRYLAVELGPRGIRVNAVSPGVIDTDALAHF 189
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 34-223 1.59e-32

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: 120.51  E-value: 1.59e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE-GLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:cd05352   6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 113 GVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSpALLLSQL--LPYMENRRGAVILVSSIAAYNPVVAL--GVYNVS 188
Cdd:cd05352  86 KIDILIANAGITVHKPALDYTYEQ-WNKVIDVNLNG-VFNCAQAaaKIFKKQGKGSLIITASMSGTIVNRPQpqAAYNAS 163

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33667109 189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:cd05352 164 KAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 38-221 2.36e-32

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: 119.98  E-value: 2.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  38 VAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFL 117
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 118 VCSAGVNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQL-LPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:cd05365  81 VNNAGGGGPKPFDMPMTEEDFEWAFKLNLFS-AFRLSQLcAPHMQKAGGGAILnISSMSSENKNVRIAAYGSSKAAVNHM 159

                       170       180
                ....*....|....*....|....*.
gi 33667109 196 TRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05365 160 TRNLAFDLGPKGIRVNAVAPGAVKTD 185
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
33-221 2.53e-32

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 119.82  E-value: 2.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   33 VLANRVAVVTGSTSGIGFAIARRLARDGAHVVIS-SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSA--GVN-PLvgstLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK08063  81 GRLDVFVNNAasGVLrPA----MELEESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSLGSIRYLENYTTVGV 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08063 157 SKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PRK09242 PRK09242
SDR family oxidoreductase;
34-220 2.58e-32

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 120.24  E-value: 2.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKL--QGEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeEFPEREVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSpALLLSQLL-PYMENR-RGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK09242  87 DGLHILVNNAGGN-IRKAAIDYTEDEWRGIFETNLFS-AFELSRYAhPLLKQHaSSAIVNIGSVSGLTHVRSGAPYGMTK 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK09242 165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRT 195
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 34-216 3.76e-32

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 119.73  E-value: 3.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqgeGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK08265   4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:PRK08265  81 VDILVNLACT--YLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASKAAIR 158

                        170       180
                 ....*....|....*....|...
gi 33667109  194 GLTRTLALELAPKDIRVNCVVPG 216
Cdd:PRK08265 159 QLTRSMAMDLAPDGIRVNSVSPG 181
PRK09135 PRK09135
pteridine reductase; Provisional
 35-218 4.12e-32

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 119.26  E-value: 4.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAK---LQGEGlSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAelnALRPG-SAAALQADLLDPDALPELVAACVAAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGV---NPLvGSTlgtSEQIWDKILSVNVKSPaLLLSQ-LLPYMENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK09135  84 GRLDALVNNASSfypTPL-GSI---TEAQWDDLFASNLKAP-FFLSQaAAPQLRKQRGAIVNITDIHAERPLKGYPVYCA 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  188 SKTALLGLTRTLALELAPkDIRVNCVVPGII 218
Cdd:PRK09135 159 AKAALEMLTRSLALELAP-EVRVNAVAPGAI 188
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-227 4.85e-32

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 119.30  E-value: 4.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISS-RKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVNPLV-GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRG-------AVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK12745  83 CLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphrSIVFVSSVNAIMVSPNRGEYCI 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK12745 163 SKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVT 202
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 36-221 1.41e-31

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: 118.32  E-value: 1.41e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAM--AKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVraGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVIlvsSIAAYNPVVAL---GVYNVSK 189
Cdd:cd08940  82 VDILVNNAGIQ-HVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRII---NIASVHGLVASankSAYVAAK 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 33667109 190 TALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd08940 158 HGVVGLTKVVALETAGTGVTCNAICPGWVLTP 189
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 31-221 1.98e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 117.80  E-value: 1.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   31 KGVLANRVAVVTGSTSGIGFAIARRLARDGA-HVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR--GAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK06198  81 AFGRLDALVNAAGL-TDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaeGTIVNIGSMSAHGGQPFLAAYCA 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06198 160 SKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PRK06138 PRK06138
SDR family oxidoreductase;
34-220 3.62e-31

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 116.79  E-value: 3.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVcHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAFARQG-DVGSAEAVEALVDFVAARWGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILvsSIAAYNPVVAL---GVYNVSKT 190
Cdd:PRK06138  82 LDVLVNNAGFGCG-GTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIV--NTASQLALAGGrgrAAYVASKG 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06138 159 AIASLTRAMALDHATDGIRVNAVAPGTIDT 188
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 36-220 3.96e-31

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: 117.09  E-value: 3.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKL--QGEGLSVAgIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEisEAGYNAVA-VGADVTDKDDVEALIDQAVEKFGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:cd05366  81 FDVMVNNAGIAP-ITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFkkLGHGGKIINASSIAGVQGFPNLGAYSASKFA 159

                       170       180
                ....*....|....*....|....*....
gi 33667109 192 LLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05366 160 VRGLTQTAAQELAPKGITVNAYAPGIVKT 188
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-224 4.19e-31

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 116.33  E-value: 4.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK07666  85 IDILINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMiERQSGDIINISSTAGQKGAAVTSAYSASKFGV 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:PRK07666 164 LGLTESLMQEVRKHNIRVTALTPSTVATDMAV 195
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 33-249 4.24e-31

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 116.38  E-value: 4.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   33 VLANRVAVVTGSTSGIGFAIARRLARDGAHVVIS-SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK12937   2 TLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENrRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK12937  82 GRIDVLVNNAGVMPL-GTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQ-GGRIINLSTSVIALPLPGYGPYAASKAA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDfskvvrigfmgMSLSGRTSRNIISCRGL 249
Cdd:PRK12937 160 VEGLVHVLANELRGRGITVNAVAPGPVATE-----------LFFNGKSAEQIDQLAGL 206
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 34-226 4.82e-31

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 116.87  E-value: 4.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIWdkILSVNVKSPaLLLSQL-LPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK06113  89 VDILVNNAGGGGPKPFDMPMADFRR--AYELNVFSF-FHLSQLvAPEMEKNGGGVILtITSMAAENKNINMTSYASSKAA 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:PRK06113 166 ASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSV 200
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 34-220 5.41e-31

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 116.92  E-value: 5.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAG---VNPLVgstlGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK13394  85 VDILVSNAGiqiVNPIE----NYSFADWKKMQAIHVDGAFLTTKAALKHMykDDRGGVVIYMGSVHSHEASPLKSAYVTA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 34-222 7.24e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 116.18  E-value: 7.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYN---PVVAlgVYNVSK 189
Cdd:PRK07478  84 LDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGgGSLIFTSTFVGHTagfPGMA--AYAASK 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK07478 162 AGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPM 194
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 37-221 7.82e-31

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: 116.02  E-value: 7.82e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQ-QNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:cd05337   2 PVAIVTGASRGIGRAIATELAARGFDIAINDLPDdDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 116 FLVCSAGVNPLV-GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-------ENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:cd05337  82 CLVNNAGIAVRPrGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMveqpdrfDGPHRSIIFVTSINAYLVSPNRGEYCI 161

                       170       180       190
                ....*....|....*....|....*....|....
gi 33667109 188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05337 162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTD 195
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 34-220 1.43e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 114.89  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIvcHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNRQFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK12828  83 LDALVNIAGAFVWGTIADGDADT-WDRMYGVNVKTTLNASKAALPALtASGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161

                        170       180
                 ....*....|....*....|....*...
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVLPSIIDT 189
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 34-221 2.57e-30

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 114.95  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEG-LSVAGIVCHVGKAEDREQLVaKALEHCG 112
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESnVDVSYIVADLTKREDLERTV-KELKNIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK08339  85 EPDIFFFSTG-GPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGfGRIIYSTSVAIKEPIPNIALSNVVRIS 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08339 164 MAGLVRTLAKELGPKGITVNGIMPGIIRTD 193
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 32-220 2.78e-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: 115.08  E-value: 2.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVIS--SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:cd05355  22 GKLKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVK 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 110 HCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnrRGAVIL-VSSIAAYNPVVALGVYNVS 188
Cdd:cd05355 102 EFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLK--KGSSIInTTSVTAYKGSPHLLDYAAT 179

                       170       180       190
                ....*....|....*....|....*....|..
gi 33667109 189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05355 180 KGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWT 211
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 34-235 3.36e-30

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: 114.10  E-value: 3.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGeglsVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPG----LHTIVLDVADPASIAALAEQVTAEFPD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGV--NPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLLPY-MENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:COG3967  79 LNVLINNAGImrAEDLLDEAEDLADA-EREITTNLLGPIRLTAAFLPHlKAQPEAAIVNVSSGLAFVPLAVTPTYSATKA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 33667109 191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSL 235
Cdd:COG3967 158 ALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRAMPL 202
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
35-227 5.06e-30

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 113.71  E-value: 5.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVC-HVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKElDVTDTEECAEALAEIEEEEGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK12824  81 VDILVNNAGITR-DSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISSVNGLKGQFGQTNYSAAKAGM 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK12824 160 IGFTKALASEGARYGITVNCIAPGYIATPMVEQMG 194
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 37-225 7.80e-30

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: 113.32  E-value: 7.80e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRkqQNVDRA---MAKLQGEGLSVAGivcHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY--RSTESAeavAAEAGERAIAIQA---DVRDRDQVQAMIEEAKNHFGP 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGV----NPLVGSTLGTSE-QIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNV 187
Cdd:cd05349  76 VDTIVNNALIdfpfDPDQRKTFDTIDwEDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGTNLFQNPVVPYHDYTT 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33667109 188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIK-TDFSKV 225
Cdd:cd05349 156 AKAALLGFTRNMAKELGPYGITVNMVSGGLLKvTDASAA 194
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-227 1.03e-29

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 113.29  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQqNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGT-NWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGV---NPLvgstLGTSEQIWDKILSVNVKSpALLLSQLLP--YMENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK06935  92 IDILVNNAGTirrAPL----LEYKDEDWNAVMDINLNS-VYHLSQAVAkvMAKQGSGKIINIASMLSFQGGKFVPAYTAS 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK06935 167 KHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIR 205
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 37-238 1.39e-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: 113.09  E-value: 1.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKL--QGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:cd05327   2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIkkETGNAKVEVIQLDLSSLASVRQFAEEFLARFPRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPlvgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIAA--------------YNPV 179
Cdd:cd05327  82 DILINNAGIMA---PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSrIVNVSSIAHragpidfndldlenNKEY 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33667109 180 VALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSLSGR 238
Cdd:cd05327 159 SPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLRP 217
PRK06398 PRK06398
aldose dehydrogenase; Validated
 34-220 1.75e-29

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 112.62  E-value: 1.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVissrkqqNVDRAMAklqgEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVI-------NFDIKEP----SYNDVDYFKVDVSNKEQVIKGIDYVISKYGR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK06398  73 IDILVNNAGIE-SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMlKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151

                        170       180
                 ....*....|....*....|....*...
gi 33667109  193 LGLTRTLALELAPKdIRVNCVVPGIIKT 220
Cdd:PRK06398 152 LGLTRSIAVDYAPT-IRCVAVCPGSIRT 178
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 34-220 2.57e-29

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: 111.71  E-value: 2.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqGEglsvAGIVCH--VGKAEDREQLVAKALEHC 111
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL-GD----AARFFHldVTDEDGWTAVVDTAREAF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 112 GGVDFLVCSAGVnpLVGSTL--GTSEQiWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:cd05341  78 GRLDVLVNNAGI--LTGGTVetTTLEE-WRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNAS 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 33667109 189 KTALLGLTRTLALELAPKD--IRVNCVVPGIIKT 220
Cdd:cd05341 155 KGAVRGLTKSAALECATQGygIRVNSVHPGYIYT 188
PRK07774 PRK07774
SDR family oxidoreductase;
32-226 2.80e-29

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 111.76  E-value: 2.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK07774   2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVnpLVG----STLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYnpvVALGVYN 186
Cdd:PRK07774  82 GGIDYLVNNAAI--YGGmkldLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVnQSSTAAW---LYSNFYG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 33667109  187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:PRK07774 157 LAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTV 196
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 34-220 3.03e-29

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: 111.78  E-value: 3.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSrKQQNVDRAMAKLQGEGlSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIAD-IDDDAGQAVAAELGDP-DISFVHCDVTVEADVRAAVDTAVARFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:cd05326  80 LDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMiPAKKGSIVSVASVAGVVGGLGPHAYTASKHA 159

                       170       180
                ....*....|....*....|....*....
gi 33667109 192 LLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05326 160 VLGLTRSAATELGEHGIRVNCVSPYGVAT 188
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 37-218 3.69e-29

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: 111.21  E-value: 3.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRK-QQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 116 FLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:cd05357  81 VLVNNASAFY-PTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLaGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEG 159

                       170       180
                ....*....|....*....|....
gi 33667109 195 LTRTLALELAPKdIRVNCVVPGII 218
Cdd:cd05357 160 LTRSAALELAPN-IRVNGIAPGLI 182
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 34-220 4.37e-29

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 111.74  E-value: 4.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQ----QNVDRAMAKLQGEGLSVAGivcHVGKAEDREQLVAKALE 109
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDeeeaNDVAEEIKKAGGEAIAVKG---DVTVESDVVNLIQTAVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK08936  82 EFGTLDVMINNAGIENAVPSHEMSLED-WNKVINTNLTGAFLGSREAIKYFveHDIKGNIINMSSVHEQIPWPLFVHYAA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
PRK07454 PRK07454
SDR family oxidoreductase;
37-220 1.18e-28

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 110.05  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 LVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:PRK07454  87 LINNAGM-AYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMrARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165

                        170       180
                 ....*....|....*....|....*
gi 33667109  196 TRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07454 166 TKCLAEEERSHGIRVCTITLGAVNT 190
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 36-231 1.44e-28

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: 109.62  E-value: 1.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDrAMAKLQGEGLSVAG--IVCHVGKAEDREQLVAKALEHCGg 113
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLD-AVAKEIEEKYGVETktIAADFSAGDDIYERIEKELEGLD- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLVGSTLG-TSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:cd05356  79 IGILVNNVGISHSIPEYFLeTPEDELQDIINVNVMATLKMTRLILPGMVKRkKGAIVNISSFAGLIPTPLLATYSASKAF 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33667109 192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFM 231
Cdd:cd05356 159 LDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSLF 198
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 34-222 1.53e-28

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: 109.91  E-value: 1.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEG-LSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:cd05343   4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGyPTLFPYQCDLSNEEQILSMFSAIRTQHQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 113 GVDFLVCSAGV---NPLVGSTlgTSEqiWDKILSVNVKSPALLLSQLLPYMENR---RGAVILVSSIAAYN--PVVALGV 184
Cdd:cd05343  84 GVDVCINNAGLarpEPLLSGK--TEG--WKEMFDVNVLALSICTREAYQSMKERnvdDGHIININSMSGHRvpPVSVFHF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33667109 185 YNVSKTALLGLTRTLALEL--APKDIRVNCVVPGIIKTDF 222
Cdd:cd05343 160 YAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEF 199
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 34-218 1.67e-28

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: 109.79  E-value: 1.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVD------------RAMAKLQGEGLSVAGIVCHVGKAEDRE 101
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpgtieETAEEIEAAGGQALPIVVDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 102 QLVAKALEHCGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVV 180
Cdd:cd05338  81 ALVEATVDQFGRLDILVNNAGAIWL-SLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILnISPPLSLRPAR 159

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 33667109 181 ALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGII 218
Cdd:cd05338 160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTA 197
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 34-223 1.76e-28

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 110.42  E-value: 1.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISsrkqqNVDRAMAKLQGEGLS-VAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAIG-----DLDEALAKETAAELGlVVGGPLDVTDPASFAAFLDAVEADLG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPaLLLSQL-LPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK07825  78 PIDVLVNNAGVMP-VGPFLDEPDAVTRRILDVNVYGV-ILGSKLaAPRMvPRGRGHVVNVASLAGKIPVPGMATYCASKH 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PRK07825 156 AVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
36-220 2.75e-28

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 109.43  E-value: 2.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAY--NPvvALGVYNVSKTA 191
Cdd:PRK08643  82 VVVNNAGVAPTTPIETITEEQF-DKVYNINVGGVIWGIQAAQEAFkkLGHGGKIINATSQAGVvgNP--ELAVYSSTKFA 158

                        170       180
                 ....*....|....*....|....*....
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08643 159 VRGLTQTAARDLASEGITVNAYAPGIVKT 187
PRK06484 PRK06484
short chain dehydrogenase; Validated
 37-220 4.10e-28

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 113.02  E-value: 4.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLsvaGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHH---ALAMDVSDEAQIREGFEQLHREFGRIDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 LVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALL 193
Cdd:PRK06484  83 LVNNAGVtDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMiEQGHGAAIVnVASGAGLVALPKRTAYSASKAAVI 162

                        170       180
                 ....*....|....*....|....*..
gi 33667109  194 GLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06484 163 SLTRSLACEWAAKGIRVNAVLPGYVRT 189
PRK07074 PRK07074
SDR family oxidoreductase;
35-220 4.59e-28

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 108.70  E-value: 4.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlsVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDAR--FVPVACDLTDAASLAAALANAAAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 DFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIaayNPVVALG--VYNVSKTA 191
Cdd:PRK07074  79 DVLVANAGAARAA-SLHDTTPASWRADNALNLEAAYLCVEAVLEGMlKRSRGAVVNIGSV---NGMAALGhpAYSAAKAG 154

                        170       180
                 ....*....|....*....|....*....
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07074 155 LIHYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
32-220 6.97e-28

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 108.35  E-value: 6.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK08226   2 GKLTGKTALITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAyNPVVALG--VYNVS 188
Cdd:PRK08226  81 GRIDILVNNAGVCRL-GSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMiARKDGRIVMMSSVTG-DMVADPGetAYALT 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08226 159 KAAIVGLTKSLAVEYAQSGIRVNAICPGYVRT 190
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 38-222 9.62e-28

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: 107.71  E-value: 9.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  38 VAVVTGSTSGIGFAIARRLARDGAHVVI-SSRKQQNVDRAmAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVIlDINEKGAEETA-NNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGV---NPLVGStlgTSEQIwDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd05339  80 LINNAGVvsgKKLLEL---PDEEI-EKTFEVNTLAHFWTTKAFLPDMlERNHGHIVTIASVAGLISPAGLADYCASKAAA 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 33667109 193 LGLTRTLALELAP---KDIRVNCVVPGIIKTDF 222
Cdd:cd05339 156 VGFHESLRLELKAygkPGIKTTLVCPYFINTGM 188
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 37-220 1.18e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 107.49  E-value: 1.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVagivcHVGkaedREQLVAKALEHCGGVDF 116
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL-----DVG----DDAAIRAALAAAGAFDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 LVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:PRK07060  81 LVNCAGIASL-ESALDMTAEGFDRVMAVNARGAALVARHVARAMiaAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDA 159

                        170       180
                 ....*....|....*....|....*.
gi 33667109  195 LTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07060 160 ITRVLCVELGPHGIRVNSVNPTVTLT 185
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 34-218 1.27e-27

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 107.79  E-value: 1.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVissrkqqNVDRAMAKLQGEGLSVagIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVV-------NADIHGGDGQHENYQF--VPTDVSSAEEVNHTVAEIIEKFGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVN-P--LV-----GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGV 184
Cdd:PRK06171  78 IDGLVNNAGINiPrlLVdekdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMvKQHDGVIVNMSSEAGLEGSEGQSC 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 33667109  185 YNVSKTALLGLTRTLALELAPKDIRVNCVVPGII 218
Cdd:PRK06171 158 YAATKAALNSFTRSWAKELGKHNIRVVGVAPGIL 191
PRK08589 PRK08589
SDR family oxidoreductase;
32-220 1.46e-27

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 107.94  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVV---ISSRKQQNVDramaKLQGEGLSVAGIVCHVGKAEDREQLVAKAL 108
Cdd:PRK08589   2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLavdIAEAVSETVD----KIKSNGGKAKAYHVDISDEQQVKDFASEIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  109 EHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK08589  78 EQFGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08589 158 KGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 34-226 1.48e-27

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 107.53  E-value: 1.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGV---NPLvgstLGTSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK08085  87 IDVLINNAGIqrrHPF----TEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRqAGKIINICSMQSELGRDTITPYAASK 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:PRK08085 163 GAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKAL 199
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 34-220 1.88e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 107.12  E-value: 1.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISsrkqqNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVG-----DIDPEAGKAAADEVGGLFVPTDVTDEDAVNALFDTAAETYGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLV-GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGV-YNVSKT 190
Cdd:PRK06057  80 VDIAFNNAGISPPEdDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMvRQGKGSIINTASFVAVMGSATSQIsYTASKG 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06057 160 GVLAMSRELGVQFARQGIRVNALCPGPVNT 189
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 36-222 2.78e-27

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 106.20  E-value: 2.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVissrkqqNVDRAMAKLQGEGLsvagivcHVGKAEDREQLvAKALEHCGGVD 115
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVY-------GVDKQDKPDLSGNF-------HFLQLDLSDDL-EPLFDWVPSVD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYnpvVALG---VYNVSKTA 191
Cdd:PRK06550  70 ILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMlERKSGIIINMCSIASF---VAGGggaAYTASKHA 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKT-----DF 222
Cdd:PRK06550 147 LAGFTKQLALDYAKDGIQVFGIAPGAVKTpmtaaDF 182
PRK07856 PRK07856
SDR family oxidoreductase;
34-223 2.93e-27

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 106.56  E-value: 2.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDramaklqgEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETV--------DGRPAEFHAADVRDPDQVAALVDAIVERHGR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK07856  76 LDVLVNNAGGSPYA-LAAEASPRFHEKIVELNLLAPLLVAQAANAVMqqQPGGGSIVNIGSVSGRRPSPGTAAYGAAKAG 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  192 LLGLTRTLALELAPKdIRVNCVVPGIIKTDFS 223
Cdd:PRK07856 155 LLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQS 185
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 32-236 3.09e-27

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 106.58  E-value: 3.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDrAMAKLQGEGlsVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK06200   2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLA-SLRQRFGDH--VLVVEGDVTSYADNQRAVDQTVDAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGV----NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK06200  79 GKLDCFVGNAGIwdynTSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPGGGGPLYTA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 33667109  188 SKTALLGLTRTLALELAPkDIRVNCVVPGIIKTDFSKVVRIGFMGMSLS 236
Cdd:PRK06200 159 SKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLRGPASLGQGETSIS 206
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 34-236 4.17e-27

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: 106.28  E-value: 4.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVdRAMAKLQGEglSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKV-AELRADFGD--AVVGVEGDVRSLADNERAVARCVERFGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLVGSTLGTSEQ----IWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:cd05348  79 LDCFIGNAGIWDYSTSLVDIPEEkldeAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGGGGPLYTASK 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 33667109 190 TALLGLTRTLALELAPKdIRVNCVVPGIIKTDFSKVVRIGFMGMSLS 236
Cdd:cd05348 159 HAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASLGQGETSIS 204
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 34-221 6.34e-27

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 105.47  E-value: 6.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAK-LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNeLGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK12935  84 KVDILVNNAGITR-DRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYItEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAICPGFIDTE 192
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 34-216 8.62e-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: 105.26  E-value: 8.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAgIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIA-IPADLSSEEGIEALVARVAERSDR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNplVGSTLGT-SEQIWDKILSVNVKSPALLLSQLLPYMenRRGA-------VILVSSIAAynpVVALGV- 184
Cdd:cd08942  83 LDVLVNNAGAT--WGAPLEAfPESGWDKVMDINVKSVFFLTQALLPLL--RAAAtaenparVINIGSIAG---IVVSGLe 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33667109 185 ---YNVSKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:cd08942 156 nysYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 34-221 8.96e-27

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: 105.62  E-value: 8.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGT 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVN-------------PLVGSTLGTSEQIWDKILSVNVKSpALLLSQLL--PYMENRRGAVILVSSIAAYNP 178
Cdd:cd08935  83 VDILINGAGGNhpdattdpehyepETEQNFFDLDEEGWEFVFDLNLNG-SFLPSQVFgkDMLEQKGGSIINISSMNAFSP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 33667109 179 VVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd08935 162 LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
34-226 9.48e-27

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 105.11  E-value: 9.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRkqqNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADI---KPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGV---NPLVGSTlgtsEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK07067  81 IDILFNNAALfdmAPILDIS----RDSYDRLFAVNVKGLFFLMQAVARHMveQGRGGKIINMASQAGRRGEALVSHYCAT 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:PRK07067 157 KAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQV 194
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 37-215 1.39e-26

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: 104.78  E-value: 1.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVaGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRAL-GVQCDVTSEAQVQSAFEQAVLEFGGLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:cd08943  81 VVSNAGIAT-SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMksQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAH 159

                       170       180
                ....*....|....*....|.
gi 33667109 195 LTRTLALELAPKDIRVNCVVP 215
Cdd:cd08943 160 LARCLALEGGEDGIRVNTVNP 180
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 37-220 1.42e-26

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: 104.47  E-value: 1.42e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVV---ISSRKQQNVDRamaklqgeGLSVAGIVCHVGKAEDREQLVAKAlehcGG 113
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREGANVIatdINEEKLKELER--------GPGITTRVLDVTDKEQVAALAKEE----GR 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAA-YNPVVALGVYNVSKTA 191
Cdd:cd05368  71 IDVLFNCAGFVH-HGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSIINMSSVASsIKGVPNRFVYSTTKAA 149

                       170       180
                ....*....|....*....|....*....
gi 33667109 192 LLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05368 150 VIGLTKSVAADFAQQGIRCNAICPGTVDT 178
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 34-227 5.07e-26

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: 103.00  E-value: 5.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd08934  81 LDILVNNAGIM-LLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVnISSVAGRVAVRNSAVYNATKFGV 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:cd08934 160 NAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHIT 194
PRK07814 PRK07814
SDR family oxidoreductase;
34-226 6.29e-26

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 103.32  E-value: 6.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAG---VNPLvgstLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR--GAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK07814  88 LDIVVNNVGgtmPNPL----LSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSggGSVINISSTMGRLAGRGFAAYGTA 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 33667109  189 KTALLGLTRTLALELAPKdIRVNCVVPGIIKTDFSKVV 226
Cdd:PRK07814 164 KAALAHYTRLAALDLCPR-IRVNAIAPGSILTSALEVV 200
PRK12743 PRK12743
SDR family oxidoreductase;
35-220 8.75e-26

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 102.80  E-value: 8.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVIS-SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNplVGST-LGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK12743  81 IDVLVNNAGAM--TKAPfLDMDFDEWRKIFTVDVDGAFLCSQIAARHMvkQGQGGRIINITSVHEHTPLPGASAYTAAKH 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK12743 159 ALGGLTKAMALELVEHGILVNAVAPGAIAT 188
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 39-220 1.01e-25

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: 1.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKaEDREQLVAKALE-HCGGVDFL 117
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTD-EERNQLVIAELEaELGGLDLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 118 VCSAGVNplvGSTLGTSEQIWD--KILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:cd05350  80 IINAGVG---KGTSLGDLSFKAfrETIDTNLLGAAAILEAALPQFrAKGRGHLVLISSVAALRGLPGAAAYSASKAALSS 156

                       170       180
                ....*....|....*....|....*.
gi 33667109 195 LTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05350 157 LAESLRYDVKKRGIRVTVINPGFIDT 182
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 35-220 1.31e-25

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: 102.23  E-value: 1.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGL-SVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPgSCKFVPCDVTKEEDIKTLISVTVERFGR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd08933  88 IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAIT 167

                       170       180
                ....*....|....*....|....*..
gi 33667109 194 GLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd08933 168 AMTKALAVDESRYGVRVNCISPGNIWT 194
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 36-220 1.43e-25

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: 101.98  E-value: 1.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAmAKLQGEGLSVAgivCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETV-AKLGDNCRFVP---VDVTSEKDVKAALALAKAKFGRLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 116 FLVCSAGVNPlVGSTLGT------SEQIWDKILSVNV-------KSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVAL 182
Cdd:cd05371  78 IVVNCAGIAV-AAKTYNKkgqqphSLELFQRVINVNLigtfnviRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQ 156

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 33667109 183 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05371 157 AAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 34-226 1.81e-25

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: 101.39  E-value: 1.81e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDramaKLQGEGLSVAGIVCHVGKAEDREqlvaKALEHCGG 113
Cdd:cd05351   5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLD----SLVRECPGIEPVCVDLSDWDATE----EALGSVGP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR--GAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:cd05351  77 VDLLVNNAAV-AILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvpGSIVNVSSQASQRALTNHTVYCSTKAA 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33667109 192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:cd05351 156 LDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDN 190
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 34-220 2.23e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 101.68  E-value: 2.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGV---NPLvgstLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAA---YNPVVAlgvYN 186
Cdd:PRK07097  88 IDILVNNAGIikrIPM----LEMSAEDFRQVIDIDLNAPFIVSKAVIPSMiKKGHGKIINICSMMSelgRETVSA---YA 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 33667109  187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07097 161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
PRK07062 PRK07062
SDR family oxidoreductase;
34-220 2.84e-25

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 101.66  E-value: 2.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE--GLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKfpGARLLAARCDVLDEADVAAFAAAVEARF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNPLvgSTLG-TSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK07062  86 GGVDMLVNNAGQGRV--STFAdTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLALQPEPHMVATSAAR 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07062 164 AGLLNLVKSLATELAPKGVRVNSILLGLVES 194
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-221 2.92e-25

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 104.53  E-value: 2.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQ--NVDRAMAKLQGEGLSvagivCHVGKAEDREQLVAKALEHC 111
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAgeALAAVANRVGGTALA-----LDITAPDAPARIAEHLAERH 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVnpLVGSTLG-TSEQIWDKILSVNVKSP-----ALLLSQLLpymeNRRGAVILVSSIA--AYNpvvaLG 183
Cdd:PRK08261 283 GGLDIVVHNAGI--TRDKTLAnMDEARWDSVLAVNLLAPlriteALLAAGAL----GDGGRIVGVSSISgiAGN----RG 352

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 33667109  184 V--YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08261 353 QtnYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQ 392
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 32-221 5.19e-25

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 100.56  E-value: 5.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVI----SSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKA 107
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  108 LEHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVY 185
Cdd:PRK12827  82 VEEFGRLDILVNNAGIATDAAFAELSIEE-WDDVIDVNLDGFFNVTQAALPPMirARRGGRIVNIASVAGVRGNRGQVNY 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTP 196
PRK06194 PRK06194
hypothetical protein; Provisional
 34-220 5.78e-25

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 101.25  E-value: 5.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-------ENRRGAVILVSSIAAYNPVVALGVYN 186
Cdd:PRK06194  84 VHLLFNNAGVGA-GGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMlaaaekdPAYEGHIVNTASMAGLLAPPAMGIYN 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  187 VSKTALLGLTRTLALELAPKDIRVNCVV--PGIIKT 220
Cdd:PRK06194 163 VSKHAVVSLTETLYQDLSLVTDQVGASVlcPYFVPT 198
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 34-221 6.04e-25

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: 99.69  E-value: 6.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAmaklQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEA----KKELPNIHTIVLDVGDAESVEALAEALLSEYPN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLVGSTLGTSE-QIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:cd05370  79 LDILINNAGIQRPIDLRDPASDlDKADTEIDTNLIGPIRLIKAFLPHLKKQpEATIVNVSSGLAFVPMAANPVYCATKAA 158

                       170       180       190
                ....*....|....*....|....*....|
gi 33667109 192 LLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05370 159 LHSYTLALRHQLKDTGVEVVEIVPPAVDTE 188
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 34-221 7.45e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 100.36  E-value: 7.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQ-QNVDRAMAKLQGEGLSVAGIvchvgkaedrEQLVAKALEHCG 112
Cdd:PRK06523   7 LAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRpDDLPEGVEFVAADLTTAEGC----------AAVARAVLERLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGvnplvGST------LGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPV-VALGV 184
Cdd:PRK06523  77 GVDILVHVLG-----GSSapaggfAALTDEEWQDELNLNLLAAVRLDRALLPGMiARGSGVIIHVTSIQRRLPLpESTTA 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  185 YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06523 152 YAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK08628 PRK08628
SDR family oxidoreductase;
34-215 1.06e-24

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 99.65  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNvDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPD-DEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGstLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:PRK08628  84 IDGLVNNAGVNDGVG--LEAGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQL 161

                        170       180
                 ....*....|....*....|..
gi 33667109  194 GLTRTLALELAPKDIRVNCVVP 215
Cdd:PRK08628 162 ALTREWAVALAKDGVRVNAVIP 183
PRK08219 PRK08219
SDR family oxidoreductase;
37-221 1.08e-24

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 98.85  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDgAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVchvgkaedREQLVAKALEHCGGVDF 116
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELPGATPFPVDLT--------DPEAIAAAVEQLGRLDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 LVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLT 196
Cdd:PRK08219  75 LVHNAGVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALA 153

                        170       180
                 ....*....|....*....|....*
gi 33667109  197 RTLALELAPKdIRVNCVVPGIIKTD 221
Cdd:PRK08219 154 DALREEEPGN-VRVTSVHPGRTDTD 177
PRK05867 PRK05867
SDR family oxidoreductase;
34-222 2.10e-24

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 98.95  E-value: 2.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAG---VNPLVGSTLGTSEQIWDkilsVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAY--NPVVALGVYN 186
Cdd:PRK05867  87 IDIAVCNAGiitVTPMLDMPLEEFQRLQN----TNVTGVFLTAQAAAKAMvkQGQGGVIINTASMSGHiiNVPQQVSHYC 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK05867 163 ASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK06124 PRK06124
SDR family oxidoreductase;
34-221 2.49e-24

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 98.63  E-value: 2.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGV---NPLVGSTLGTSEQiwdkILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAynPVVALG--VYNV 187
Cdd:PRK06124  89 LDILVNNVGArdrRPLAELDDAAIRA----LLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAG--QVARAGdaVYPA 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06124 163 AKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196
PRK05650 PRK05650
SDR family oxidoreductase;
36-220 4.77e-24

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 98.19  E-value: 4.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVaVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:PRK05650   1 NRV-MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGID 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME-NRRGAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:PRK05650  80 VIVNNAGVAS-GGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKrQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVA 158

                        170       180
                 ....*....|....*....|....*.
gi 33667109  195 LTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK05650 159 LSETLLVELADDEIGVHVVCPSFFQT 184
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 39-227 8.47e-24

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: 97.35  E-value: 8.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKqqnVDRaMAKLQGE-----GLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLILTGRR---AER-LQELADElgakfPVKVLPLQLDVSDRESIEAALENLPEEFRD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVnplvgsTLGT------SEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYN 186
Cdd:cd05346  79 IDILVNNAGL------ALGLdpaqeaDLEDWETMIDTNVKGLLNVTRLILPIMIARnQGHIINLGSIAGRYPYAGGNVYC 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 33667109 187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSkVVR 227
Cdd:cd05346 153 ATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFS-LVR 192
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 34-234 9.24e-24

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 97.72  E-value: 9.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK05876  84 VDVVFSNAGI-VVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLleQGTGGHVVFTASFAGLVPNAGLGAYGVAKYG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDF---SKVVRIGFMGMS 234
Cdd:PRK05876 163 VVGLAETLAREVTADGIGVSVLCPMVVETNLvanSERIRGAACAQS 208
PRK07831 PRK07831
SDR family oxidoreductase;
32-225 9.54e-24

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 97.41  E-value: 9.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGST-SGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE-GLS-VAGIVCHVGKAEDREQLVAKAL 108
Cdd:PRK07831  13 GLLAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAElGLGrVEAVVCDVTSEAQVDALIDAAV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  109 EHCGGVDFLVCSAGvnpLVGSTL---GTSEQiWDKILSVNVKSPALLLSQLLPYMENR--RGAVILVSSIAAYNPVVALG 183
Cdd:PRK07831  93 ERLGRLDVLVNNAG---LGGQTPvvdMTDDE-WSRVLDVTLTGTFRATRAALRYMRARghGGVIVNNASVLGWRAQHGQA 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 33667109  184 VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF-SKV 225
Cdd:PRK07831 169 HYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFlAKV 211
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 36-219 1.46e-23

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: 96.63  E-value: 1.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLS-VAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNrVIALELDITSKESIKELIESYLEKFGRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPLVGSTLGT--SEQIWDKILSVNVKSpALLLSQ-LLPYME-NRRGAVILVSSIAA--------------Y 176
Cdd:cd08930  82 DILINNAYPSPKVWGSRFEefPYEQWNEVLNVNLGG-AFLCSQaFIKLFKkQGKGSIINIASIYGviapdfriyentqmY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 33667109 177 NPVValgvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIK 219
Cdd:cd08930 161 SPVE----YSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
PRK06128 PRK06128
SDR family oxidoreductase;
32-220 1.77e-23

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 97.62  E-value: 1.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVIS--SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:PRK06128  51 GRLQGRKALITGADSGIGRATAIAFAREGADIALNylPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENrrGA-VILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK06128 131 ELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPP--GAsIINTGSIQSYQPSPTLLDYAST 208

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06128 209 KAAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 34-221 2.56e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 96.96  E-value: 2.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAEL-GGDDRVLTVVADVTDLAAMQAAAEEAVERFGG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:PRK05872  86 IDVVVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAAYCASKAGVE 164

                        170       180
                 ....*....|....*....|....*...
gi 33667109  194 GLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK05872 165 AFANALRLEVAHHGVTVGSAYLSWIDTD 192
PRK07985 PRK07985
SDR family oxidoreductase;
32-220 2.80e-23

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 96.99  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVIS--SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:PRK07985  45 GRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISylPVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnrRGA-VILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK07985 125 ALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLP--KGAsIITTSSIQAYQPSPHLLDYAAT 202

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07985 203 KAAILNYSRGLAKQVAEKGIRVNIVAPGPIWT 234
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 34-218 4.76e-23

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 95.41  E-value: 4.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNpLVGSTLGTSEQIW------DKILSVNVkspallLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK07576  87 IDVLVSGAAGN-FPAPAAGMSANGFktvvdiDLLGTFNV------LKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCA 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGII 218
Cdd:PRK07576 160 AKAGVDMLTRTLALEWGPEGIRVNSIVPGPI 190
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 33-220 5.20e-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: 94.95  E-value: 5.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  33 VLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVC---HVGKAEDREQLVAKALE 109
Cdd:cd05340   1 LLNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFIldlLTCTSENCQQLAQRIAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 110 HCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:cd05340  81 NYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLlKSDAGSLVFTSSSVGRQGRANWGAYAVS 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 33667109 189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05340 161 KFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 36-220 5.92e-23

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: 94.95  E-value: 5.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISS-RKQQNVDRAmaklQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADiDEERGADFA----EAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGV-NPLVGSTLGTSEqiWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd09761  77 DVLVNNAARgSKGILSSLLLEE--WDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLV 154

                       170       180
                ....*....|....*....|....*..
gi 33667109 194 GLTRTLALELAPkDIRVNCVVPGIIKT 220
Cdd:cd09761 155 ALTHALAMSLGP-DIRVNCISPGWINT 180
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 34-221 6.77e-23

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 95.35  E-value: 6.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVN--------------PLVGSTLGTSEQIWDKILSVNvkspalLLSQLLPY------MENRRGAVIL-VSS 172
Cdd:PRK08277  88 CDILINGAGGNhpkattdnefheliEPTKTFFDLDEEGFEFVFDLN------LLGTLLPTqvfakdMVGRKGGNIInISS 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 33667109  173 IAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08277 162 MNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
PRK07069 PRK07069
short chain dehydrogenase; Validated
 39-220 7.51e-23

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 94.78  E-value: 7.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAK----LQGEGLSVAgIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAeinaAHGEGVAFA-AVQDVTDEAQWQALLAQAADAMGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 DFLVCSAGVnplvgSTLGTSEQI----WDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK07069  81 SVLVNNAGV-----GSFGAIEQIeldeWRRVMAINVESIFLGCKHALPYLrASQPASIVNISSVAAFKAEPDYTAYNASK 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  190 TALLGLTRTLALELAPK--DIRVNCVVPGIIKT 220
Cdd:PRK07069 156 AAVASLTKSIALDCARRglDVRCNSIHPTFIRT 188
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 35-216 1.10e-22

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 94.24  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSEL-VHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 DFLVCSagvnplVGSTLG-------TSEQIWDKILsvnvKS--PALLLSQ-LLPYM-ENRRGAVILVSSIAAYnpvvalG 183
Cdd:PRK12823  86 DVLINN------VGGTIWakpfeeyEEEQIEAEIR----RSlfPTLWCCRaVLPHMlAQGGGAIVNVSSIATR------G 149

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  184 VYNV----SKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:PRK12823 150 INRVpysaAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 32-220 1.14e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 95.10  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISS-RKQQNVDRAMAKLQGEG---LSVAGivcHVGKAEDREQLVAKA 107
Cdd:PRK06701  42 GKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYlDEHEDANETKQRVEKEGvkcLLIPG---DVSDEAFCKDAVEET 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  108 LEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK06701 119 VRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLK-QGSAIINTGSITGYEGNETLIDYSA 197

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06701 198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWT 230
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 32-216 1.19e-22

(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: 93.93  E-value: 1.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVIS----SRKQQNVDRAMAKLQGEGLSVAGivchvGKA-------EDR 100
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNdlggDRKGSGKSSSAADKVVDEIKAAG-----GKAvanydsvEDG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 101 EQLVAKALEHCGGVDFLVCSAGVnpLV-GSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNP 178
Cdd:cd05353  76 EKIVKTAIDAFGRVDILVNNAGI--LRdRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMrKQKFGRIINTSSAAGLYG 153

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 33667109 179 VVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:cd05353 154 NFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK05855 PRK05855
SDR family oxidoreductase;
31-234 1.49e-22

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 97.36  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   31 KGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEH 110
Cdd:PRK05855 310 RGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAE 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  111 CGGVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVN---VKSPALLLSQLLpyMENRRGAVIL-VSSIAAYNPVVALGVYN 186
Cdd:PRK05855 390 HGVPDIVVNNAGIG-MAGGFLDTSAEDWDRVLDVNlwgVIHGCRLFGRQM--VERGTGGHIVnVASAAAYAPSRSLPAYA 466

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 33667109  187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRigFMGMS 234
Cdd:PRK05855 467 TSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTR--FAGAD 512
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-220 1.65e-22

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 93.62  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRkqQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCG- 112
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYH--QSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGV----NPLVGSTLGTSEqiWD---KILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGV 184
Cdd:PRK08642  81 PITTVVNNALAdfsfDGDARKKADDIT--WEdfqQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNLFQNPVVPYHD 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  185 YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08642 159 YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-227 2.64e-22

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 93.43  E-value: 2.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVisSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIV--GVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYM---ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK12481  84 IDILINNAGI-IRRQDLLEFGNKDWDDVININQKT-VFFLSQAVAKQfvkQGNGGKIINIASMLSFQGGIRVPSYTASKS 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK12481 162 AVMGLTRALATELSQYNINVNAIAPGYMATDNTAALR 198
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 36-223 3.79e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 93.44  E-value: 3.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVdRAMAKLQGEglSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:PRK06180   4 MKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAAR-ADFEALHPD--RALARLLDVTDFDAIDAVVADAEATFGPID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVnplvgSTLGTSEQIWD----KILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK06180  81 VLVNNAGY-----GHEGAIEESPLaemrRQFEVNVFGAVAMTKAVLPGMrARRRGHIVNITSMGGLITMPGIGYYCGSKF 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PRK06180 156 ALEGISESLAKEVAPFGIHVTAVEPGSFRTDWA 188
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 34-220 1.24e-21

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 91.13  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqgeGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLL-PYMENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK12936  81 VDILVNNAGITK-DGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGM 159

                        170       180
                 ....*....|....*....|....*...
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIES 187
PRK06182 PRK06182
short chain dehydrogenase; Validated
 37-222 1.85e-21

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 91.17  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKqqnVDRaMAKLQGEGLSVagIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARR---VDK-MEDLASLGVHP--LSLDVTDEASIKAAVDTIIAEEGRIDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 LVCSAGvnplVGStLGTSEQI----WDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAA--YNPVVALgvYNVSK 189
Cdd:PRK06182  78 LVNNAG----YGS-YGAIEDVpideARRQFEVNLFGAARLTQLVLPHMrAQRSGRIINISSMGGkiYTPLGAW--YHATK 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK06182 151 FALEGFSDALRLEVAPFGIDVVVIEPGGIKTEW 183
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 32-255 1.96e-21

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 91.00  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNvdrAMAKLQGEGlsVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---EAKELREKG--VFTIKCDVGNRDQVKKSKEVVEKEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNPLVgSTLGTSEQIWDKILSVNVKSPALLLSQLLPYME-NRRGAVILVSSIAAYNpVVALGV--YNVS 188
Cdd:PRK06463  78 GRVDVLVNNAGIMYLM-PFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKlSKNGAIVNIASNAGIG-TAAEGTtfYAIT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTDfskvvrigfmgMSLSGRTSRNIISCRGLGSQRTV 255
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETD-----------MTLSGKSQEEAEKLRELFRNKTV 211
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 34-221 2.73e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 91.02  E-value: 2.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKL--QGEGLSVAGIVCHVGKAEDREQLVAKALEHC 111
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIeaLKGAGAVRYEPADVTDEDQVARAVDAATAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  112 GGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK05875  85 GRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELvRGGGGSFVGISSIAASNTHRWFGAYGVTKS 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK05875 165 AVDHLMKLAADELGPSWVRVNSIRPGLIRTD 195
PRK05717 PRK05717
SDR family oxidoreductase;
37-220 3.32e-21

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 90.33  E-value: 3.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISsrkqqNVDRA----MAKLQGEglSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLA-----DLDRErgskVAKALGE--NAWFIAMDVADEAQVAAGVAEVLGQFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPLVGSTLGTSE-QIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK05717  84 RLDALVCNAAIADPHNTTLESLSlAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASKGG 163

                        170       180
                 ....*....|....*....|....*....
gi 33667109  192 LLGLTRTLALELAPkDIRVNCVVPGIIKT 220
Cdd:PRK05717 164 LLALTHALAISLGP-EIRVNAVSPGWIDA 191
PRK12746 PRK12746
SDR family oxidoreductase;
34-223 4.12e-21

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 90.09  E-value: 4.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVIS-SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKaLEH-- 110
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQ-LKNel 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  111 -----CGGVDFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEnRRGAVILVSSIAAYNPVVALGVY 185
Cdd:PRK12746  83 qirvgTSEIDILVNNAGIGTQ-GTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSIAY 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 33667109  186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDIN 198
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-221 5.56e-21

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 89.63  E-value: 5.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGV---NPLVGSTLGT-----SEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIA-AYNpvVAL 182
Cdd:PRK08217  83 LNGLINNAGIlrdGLLVKAKDGKvtskmSLEQFQSVIDVNLTGVFLCGREAAAKMieSGSKGVIINISSIArAGN--MGQ 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 33667109  183 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08217 161 TNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETE 199
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 36-222 6.36e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 89.96  E-value: 6.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVdramAKLQGeglsVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARA----APIPG----VELLELDVTDDASVQAAVDEVIARAGRID 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVNpLVGSTLGTS-EQIwDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:PRK06179  76 VLVNNAGVG-LAGAAEESSiAQA-QALFDTNVFGILRMTRAVLPHMrAQGSGRIINISSVLGFLPAPYMALYAASKHAVE 153

                        170       180
                 ....*....|....*....|....*....
gi 33667109  194 GLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK06179 154 GYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 33-223 6.42e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 89.36  E-value: 6.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   33 VLANRVAVVTGSTSGIGFAIARRLARDGAHVVIS-SRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQL---VAKAL 108
Cdd:PRK12747   1 MLKGKVALVTGASRGIGRAIAKRLANDGALVAIHyGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALyssLDNEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  109 EHCGG---VDFLVCSAGVNPlvGSTL-GTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRgaVILVSSIAAYNPVVALG 183
Cdd:PRK12747  81 QNRTGstkFDILINNAGIGP--GAFIeETTEQFFDRMVSVNAKAPFFIIQQALSRLrDNSR--IINISSAATRISLPDFI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 33667109  184 VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PRK12747 157 AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMN 196
PRK09072 PRK09072
SDR family oxidoreductase;
34-222 8.58e-21

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 89.23  E-value: 8.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLsVAGIVCHVGKAEDREQLVAKALEHcGG 113
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGR-HRWVVADLTSEAGREAVLARAREM-GG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAynpvvALG-----VYNV 187
Cdd:PRK09072  81 INVLINNAGVNHFALLEDQDPEAI-ERLLALNLTAPMQLTRALLPLLrAQPSAMVVNVGSTFG-----SIGypgyaSYCA 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK09072 155 SKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 34-221 8.60e-21

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: 89.21  E-value: 8.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSrkqQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIAD---INLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAG---VNPLVGSTlgtsEQIWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:cd05363  78 IDILVNNAAlfdLAPIVDIT----RESYDRLFAINVSGTLFMMQAVARAMiaQGRGGKIINMASQAGRRGEALVGVYCAT 153

                       170       180       190
                ....*....|....*....|....*....|...
gi 33667109 189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05363 154 KAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
PRK06484 PRK06484
short chain dehydrogenase; Validated
 24-220 1.35e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 91.45  E-value: 1.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   24 SSTGIDRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEdreQL 103
Cdd:PRK06484 257 STAQAPSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVE---SA 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  104 VAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMenRRGAVIL-VSSIAAYNPVVAL 182
Cdd:PRK06484 334 FAQIQARWGRLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVnLGSIASLLALPPR 411

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 33667109  183 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06484 412 NAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK07201 PRK07201
SDR family oxidoreductase;
29-208 1.95e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 91.17  E-value: 1.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   29 DRKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKAL 108
Cdd:PRK07201 364 DLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDIL 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  109 EHCGGVDFLVCSAGvNPLVGSTLGTSEQIWD--KILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIA--AYNPvvALG 183
Cdd:PRK07201 444 AEHGHVDYLVNNAG-RSIRRSVENSTDRFHDyeRTMAVNYFGAVRLILGLLPHMrERRFGHVVNVSSIGvqTNAP--RFS 520

                        170       180
                 ....*....|....*....|....*
gi 33667109  184 VYNVSKTALLGLTRTLALELAPKDI 208
Cdd:PRK07201 521 AYVASKAALDAFSDVAASETLSDGI 545
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 38-227 2.24e-20

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: 87.73  E-value: 2.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  38 VAVVTGSTSGIGFAIARRLARDGAH--VVISSRKQQNVDRAMAKLQGeGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIRKLDGERD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 116 FLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR--GAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd05367  80 LLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFKGWGLYCSSKAARD 159

                       170       180       190
                ....*....|....*....|....*....|....
gi 33667109 194 GLTRTLALELapKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:cd05367 160 MFFRVLAAEE--PDVRVLSYAPGVVDTDMQREIR 191
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-216 2.77e-20

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 87.82  E-value: 2.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   33 VLANRVAVVTGST--SGIGFAIARRLARDGAHVVISSrkQQNVDRAM--------AKLQGEGLSVAGIVCH-----VGKA 97
Cdd:PRK12748   2 PLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTY--WSPYDKTMpwgmhdkePVLLKEEIESYGVRCEhmeidLSQP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   98 EDREQLVAKALEHCGGVDFLV---CSAGVNPLvgSTLgTSEQIwDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSI 173
Cdd:PRK12748  80 YAPNRVFYAVSERLGDPSILInnaAYSTHTRL--EEL-TAEQL-DKHYAVNVRATMLLSSAFAKQYDGKAgGRIINLTSG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 33667109  174 AAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:PRK12748 156 QSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 32-220 3.11e-20

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: 87.39  E-value: 3.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  32 GVLANRVAVVTG--STSGIGFAIARRLARDGAHVVISSRKqqnvDRAMAKLQG--EGLSVAGIV-CHVGKAEDREQLVAK 106
Cdd:COG0623   1 GLLKGKRGLITGvaNDRSIAWGIAKALHEEGAELAFTYQG----EALKKRVEPlaEELGSALVLpCDVTDDEQIDALFDE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 107 ALEHCGGVDFLVCS---AGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAynpVVALG 183
Cdd:COG0623  77 IKEKWGKLDFLVHSiafAPKEELGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLM-NEGGSIVTLTYLGA---ERVVP 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33667109 184 VYN---VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:COG0623 153 NYNvmgVAKAALEASVRYLAADLGPKGIRVNAISAGPIKT 192
PRK06949 PRK06949
SDR family oxidoreductase;
34-221 4.67e-20

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 87.12  E-value: 4.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENR---------RGAVILVSSIAAYNPVVALGV 184
Cdd:PRK06949  87 IDILVNNSGVST-TQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARakgagntkpGGRIINIASVAGLRVLPQIGL 165

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  185 YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06949 166 YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTE 202
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 39-220 5.80e-20

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: 85.71  E-value: 5.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQ--QNVDramaklqgeglsvagivchvgkAEDREQlVAKALEHCGGVDF 116
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSgdYQVD----------------------ITDEAS-IKALFEKVGHFDA 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLT 196
Cdd:cd11731  58 IVSTAGDAEFAPLAELTDAD-FQRGLNSKLLGQINLVRHGLPYL-NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFV 135

                       170       180
                ....*....|....*....|....
gi 33667109 197 RTLALELaPKDIRVNCVVPGIIKT 220
Cdd:cd11731 136 RAAAIEL-PRGIRINAVSPGVVEE 158
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 37-237 6.83e-20

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: 86.75  E-value: 6.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGA---HVVISSR---KQQNVDRAMAKLQGEGLSVAGI-VCHvgkaedrEQLVAKALE 109
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSkrfKVYATMRdlkKKGRLWEAAGALAGGTLETLQLdVCD-------SKSVAAAVE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 110 HCGG--VDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYN 186
Cdd:cd09806  74 RVTErhVDVLVCNAGVG-LLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDVYC 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 33667109 187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSLSG 237
Cdd:cd09806 153 ASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVLDRT 203
PRK08264 PRK08264
SDR family oxidoreductase;
34-221 2.12e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 84.94  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARR-LARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAgivchvgkaeDREQlVAKALEHCG 112
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQlLARGAAKVYAAARDPESVTDLGPRVVPLQLDVT----------DPAS-VAAAAEAAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK08264  73 DVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVnVLSVLSWVNFPNLGTYSASKAA 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08264 153 AWSLTQALRAELAPQGTRVLGVHPGPIDTD 182
PRK05993 PRK05993
SDR family oxidoreductase;
35-222 2.52e-19

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 85.46  E-value: 2.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRamakLQGEGLSVagIVCHVGKAEDREQLVAKALEHCGG- 113
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA----LEAEGLEA--FQLDYAEPESIAALVAQVLELSGGr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLV-----CSAG-VNPLvgSTLGTSEQiwdkiLSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAYNPVVALGVYN 186
Cdd:PRK05993  77 LDALFnngayGQPGaVEDL--PTEALRAQ-----FEANFFGWHDLTRRVIPVMRKQgQGRIVQCSSILGLVPMKYRGAYN 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK05993 150 ASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF 185
PRK06114 PRK06114
SDR family oxidoreductase;
34-220 2.57e-19

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 85.22  E-value: 2.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAK-LQGEGLSVAGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEhIEAAGRRAIQIAADVTSKADLRAAVARTEAELG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKspALLLS---QLLPYMENRRGAVILVSSIAAYnpVVALGV----Y 185
Cdd:PRK06114  86 ALTLAVNAAGIANANPAEEMEEEQ-WQTVMDINLT--GVFLScqaEARAMLENGGGSIVNIASMSGI--IVNRGLlqahY 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33667109  186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06114 161 NASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK08278 PRK08278
SDR family oxidoreductase;
34-215 2.58e-19

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 85.34  E-value: 2.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRkqqnVDRAMAKLQG------EGLSVAG-----IVCHVGKAEDREQ 102
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAK----TAEPHPKLPGtihtaaEEIEAAGgqalpLVGDVRDEDQVAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  103 LVAKALEHCGGVDFLVCSAGVNPLVGsTLGTSEQIWDKILSVNVKSpALLLSQL-LPYMENRRGAVILVSS--------- 172
Cdd:PRK08278  80 AVAKAVERFGGIDICVNNASAINLTG-TEDTPMKRFDLMQQINVRG-TFLVSQAcLPHLKKSENPHILTLSpplnldpkw 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 33667109  173 IAAYNPvvalgvYNVSKTALLGLTRTLALELAPKDIRVNCVVP 215
Cdd:PRK08278 158 FAPHTA------YTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 36-221 2.63e-19

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: 84.77  E-value: 2.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGA-HVVISSRKQQNVDRAMAKLQgeglsvAGIVCHVGKAEDREQLVAKAlEHCGGV 114
Cdd:cd05354   3 DKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYG------DKVVPLRLDVTDPESIKAAA-AQAKDV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd05354  76 DVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLkANGGGAIVNLNSVASLKNFPAMGTYSASKSAAY 155

                       170       180
                ....*....|....*....|....*...
gi 33667109 194 GLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd05354 156 SLTQGLRAELAAQGTLVLSVHPGPIDTR 183
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-222 2.77e-19

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 84.81  E-value: 2.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGvnplvGSTLGTSEQI--WDKILSVNVKSPALLLSQLLPYMenRRGA-VILVSSI-AAYNPVVALGVYNVSK 189
Cdd:PRK05786  82 IDGLVVTVG-----GYVEDTVEEFsgLEEMLTNHIKIPLYAVNASLRFL--KEGSsIVLVSSMsGIYKASPDQLSYAVAK 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK05786 155 AGLAKAVEILASELLGRGIRVNGIAPTTISGDF 187
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
34-272 3.16e-19

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 84.68  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVI-----SSRKQQNVDRAMAKlqgeGLSVAGIVCHVGKAEDREQLVAKAL 108
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnSPRRVKWLEDQKAL----GFDFIASEGNVGDWDSTKAAFDKVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  109 EHCGGVDFLVCSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK12938  77 AEVGEIDVLVNNAGITRDVVFRKMTRED-WTAVIDTNLTSLFNVTKQVIDGMVERGwGRIINISSVNGQKGQFGQTNYST 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSLSgrtsrnIISCRGLGSQRTVQESCPSCALQMP 267
Cdd:PRK12938 156 AKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVA------TIPVRRLGSPDEIGSIVAWLASEES 229


                 ....*
gi 33667109  268 ATSTG 272
Cdd:PRK12938 230 GFSTG 234
PRK05866 PRK05866
SDR family oxidoreductase;
19-220 4.33e-19

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 85.18  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   19 LSVRMSSTGIDRKGvlaNRVaVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAE 98
Cdd:PRK05866  27 LINRPPRQPVDLTG---KRI-LLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   99 DREQLVAKALEHCGGVDFLVCSAGVNplVGSTLGTSEQIW---DKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIA 174
Cdd:PRK05866 103 AVDALVADVEKRIGGVDILINNAGRS--IRRPLAESLDRWhdvERTMVLNYYAPLRLIRGLAPGMlERGDGHIINVATWG 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 33667109  175 AYNPVVAL-GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK05866 181 VLSEASPLfSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 36-216 5.76e-19

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 84.32  E-value: 5.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVV---ISSRKQQNVDRAMAKLQGEGLSVaGIVCHVGKAEDREQLVAKALEHCG 112
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAvadINSEKAANVAQEINAEYGEGMAY-GFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGV---NPLVGSTLGTseqiWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAA-----YNpvval 182
Cdd:PRK12384  81 RVDLLVYNAGIakaAFITDFQLGD----FDRSLQVNLVGYFLCAREFSRLMirDGIQGRIIQINSKSGkvgskHN----- 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 33667109  183 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:PRK12384 152 SGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLG 185
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 39-220 8.04e-19

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: 83.79  E-value: 8.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTG--STSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:cd05372   4 ILITGiaNDRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLDG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGVNP---LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd05372  84 LVHSIAFAPkvqLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIM-NPGGSIVTLSYLGSERVVPGYNVMGVAKAALE 162

                       170       180
                ....*....|....*....|....*..
gi 33667109 194 GLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05372 163 SSVRYLAYELGRKGIRVNAISAGPIKT 189
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-227 2.57e-18

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 82.23  E-value: 2.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVV---ISSRKQqnvdrAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEH 110
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVginIVEPTE-----TIEQVTALGRRFLSLTADLRKIDGIPALLERAVAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  111 CGGVDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYM---ENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK08993  83 FGHIDILVNNAGL-IRREDAIEFSEKDWDDVMNLNIKS-VFFMSQAAAKHfiaQGNGGKIINIASMLSFQGGIRVPSYTA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK08993 161 SKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLR 200
PLN02253 PLN02253
xanthoxin dehydrogenase
 34-223 4.19e-18

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 82.18  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRkQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDL-QDDLGQNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKFGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PLN02253  95 LDIMVNNAGLtGPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMiPLKKGSIVSLCSVASAIGGLGPHAYTGSKHA 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PLN02253 175 VLGLTRSVAAELGKHGIRVNCVSPYAVPTALA 206
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 37-222 4.23e-18

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: 81.28  E-value: 4.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDF 116
Cdd:cd05360   1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:cd05360  81 WVNNAGVA-VFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGgGALINVGSLLGYRSAPLQAAYSASKHAVRGF 159

                       170       180
                ....*....|....*....|....*....
gi 33667109 196 TRTLALELAP--KDIRVNCVVPGIIKTDF 222
Cdd:cd05360 160 TESLRAELAHdgAPISVTLVQPTAMNTPF 188
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 34-222 5.48e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 82.66  E-value: 5.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnplvgSTLGTSEQI----WDKILSVNvkspalLLSQL------LPYMENR-RGAVILVSSIAAYNPVVAL 182
Cdd:PRK07109  86 IDTWVNNAMV-----TVFGPFEDVtpeeFRRVTEVT------YLGVVhgtlaaLRHMRPRdRGAIIQVGSALAYRSIPLQ 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 33667109  183 GVYNVSKTALLGLTRTLALEL----APkdIRVNCVVPGIIKTDF 222
Cdd:PRK07109 155 SAYCAAKHAIRGFTDSLRCELlhdgSP--VSVTMVQPPAVNTPQ 196
PRK08340 PRK08340
SDR family oxidoreductase;
40-220 7.35e-18

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 81.39  E-value: 7.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLVC 119
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDALVW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  120 SAG---VNPLVGSTLGTSEqiWDKILSVNVKSPALLLSQLLP-YMENR-RGAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:PRK08340  83 NAGnvrCEPCMLHEAGYSD--WLEAALLHLVAPGYLTTLLIQaWLEKKmKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQ 160

                        170       180
                 ....*....|....*....|....*.
gi 33667109  195 LTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08340 161 LAKGVSRTYGGKGIRAYTVLLGSFDT 186
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 36-220 7.52e-18

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: 81.03  E-value: 7.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQ--GEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd05330   3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLeiAPDAEVLLIKADVSDEAQVEAYVDATVEQFGR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:cd05330  83 IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMrEQGSGMIVNTASVGGIRGVGNQSGYAAAKHGV 162

                       170       180
                ....*....|....*....|....*...
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd05330 163 VGLTRNSAVEYGQYGIRINAIAPGAILT 190
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 39-224 8.14e-18

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: 80.42  E-value: 8.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVI-SSRKQQNVdramAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE---HCGGV 114
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIaTCRDPSAA----TELAALGASHSRLHILELDVTDEIAESAEAVAerlGDAGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEN-RRGAVILVSSIAA------YNPVVAlgvYNV 187
Cdd:cd05325  77 DVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKgARAKIINISSRVGsigdntSGGWYS---YRA 153

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 33667109 188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:cd05325 154 SKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGG 190
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 36-218 1.93e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 79.72  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVNPLVgSTLGTSEQIWDKILSVnVKSPALLLSQLLP--YMENRRGAVILvSSIAAYNPVVALGVYN--VSKTA 191
Cdd:PRK07677  81 ALINNAAGNFIC-PAEDLSVNGWNSVIDI-VLNGTFYCSQAVGkyWIEKGIKGNII-NMVATYAWDAGPGVIHsaAAKAG 157

                        170       180
                 ....*....|....*....|....*...
gi 33667109  192 LLGLTRTLALELAPK-DIRVNCVVPGII 218
Cdd:PRK07677 158 VLAMTRTLAVEWGRKyGIRVNAIAPGPI 185
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 34-224 2.32e-17

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 82.27  E-value: 2.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLsvAGIVCHVGKAEDREQLVAKALEHC-- 111
Cdd:COG3347 423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYG--ADAVDATDVDVTAEAAVAAAFGFAgl 500

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 112 --GGVDFLVCSAGVNPLVGSTLgTSEQIWDKILSVNVKSPALLLSQLLPYMenrRGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:COG3347 501 diGGSDIGVANAGIASSSPEEE-TRLSFWLNNFAHLSTGQFLVARAAFQGT---GGQGLGGSSVFAVSKNAAAAAYGAAA 576

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33667109 190 T-----ALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:COG3347 577 AatakaAAQHLLRALAAEGGANGINANRVNPDAVLDGSAI 616
PRK07577 PRK07577
SDR family oxidoreductase;
36-227 2.95e-17

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 79.00  E-value: 2.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRkqqnvdRAMAKLQGEGLSvagivCHVGKAEDREQLVAKALEHcGGVD 115
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIGIAR------SAIDDFPGELFA-----CDLADIEQTAATLAQINEI-HPVD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGV---NPLVGSTLGTSEQIWDkilsVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNpVVALGVYNVSKTA 191
Cdd:PRK07577  71 AIVNNVGIalpQPLGKIDLAALQDVYD----LNVRAAVQVTQAFLEGMKLREqGRIVNICSRAIFG-ALDRTSYSAAKSA 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK07577 146 LVGCTRTWALELAEYGITVNAVAPGPIETELFRQTR 181
PRK09134 PRK09134
SDR family oxidoreductase;
35-217 3.08e-17

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 79.59  E-value: 3.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVI-SSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK09134   8 APRAALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnpLVGSTLGT-SEQIWDKILSVNVKSPALL---LSQLLPymENRRGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK09134  88 ITLLVNNASL--FEYDSAASfTRASWDRHMATNLRAPFVLaqaFARALP--ADARGLVVNMIDQRVWNLNPDFLSYTLSK 163

                        170       180
                 ....*....|....*....|....*...
gi 33667109  190 TALLGLTRTLALELAPKdIRVNCVVPGI 217
Cdd:PRK09134 164 AALWTATRTLAQALAPR-IRVNAIGPGP 190
PRK07041 PRK07041
SDR family oxidoreductase;
40-220 4.79e-17

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 78.54  E-value: 4.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqGEGLSVAGIVCHVGKAEDREQLVAKAlehcGGVDFLVC 119
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARAL-GGGAPVRTAALDITDEAAVDAFFAEA----GPFDHVVI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  120 SAGVN---PLVGSTLGTSEQIWD-KILSvnvkspALLLS---QLLPymenrRGAVILVSSIAAYNPVVALGVYNVSKTAL 192
Cdd:PRK07041  76 TAADTpggPVRALPLAAAQAAMDsKFWG------AYRVAraaRIAP-----GGSLTFVSGFAAVRPSASGVLQGAINAAL 144

                        170       180
                 ....*....|....*....|....*...
gi 33667109  193 LGLTRTLALELAPkdIRVNCVVPGIIKT 220
Cdd:PRK07041 145 EALARGLALELAP--VRVNTVSPGLVDT 170
PRK07832 PRK07832
SDR family oxidoreductase;
39-228 5.13e-17

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 78.93  E-value: 5.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAgiVCHVGKAEDREQLVAKALE-HC--GGVD 115
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVP--EHRALDISDYDAVAAFAADiHAahGSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVnplvgSTLGTSEQI----WDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAAynpVVAL---GVYN 186
Cdd:PRK07832  81 VVMNIAGI-----SAWGTVDRLtheqWRRMVDVNLMGPIHVIETFVPPMvaAGRGGHLVNVSSAAG---LVALpwhAAYS 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 33667109  187 VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRI 228
Cdd:PRK07832 153 ASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEI 194
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 36-223 6.09e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 78.93  E-value: 6.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVChvgkaeDRE---QLVAKALEHCG 112
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVT------DRAavfAAVETAVEHFG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQ-LLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK08263  77 RLDIVVNNAG-YGLFGMIEEVTESEARAQIDTNFFG-ALWVTQaVLPYLREQRsGHIIQISSIGGISAFPMSGIYHASKW 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTDFS 223
Cdd:PRK08263 155 ALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWA 187
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-216 7.61e-17

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 78.29  E-value: 7.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGST--SGIGFAIARRLARDGAHVVISSrkQQNVDRAM---------AKLQGE----GLSVAGIVCHVGKAE 98
Cdd:PRK12859   4 LKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTY--WTAYDKEMpwgvdqdeqIQLQEEllknGVKVSSMELDLTQND 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   99 DREQLVAKALEHCGGVDFLVCSAGVNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIAAYN 177
Cdd:PRK12859  82 APKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEEL-DKHYMVNVRATTLLSSQFARGFDKKSGGrIINMTSGQFQG 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 33667109  178 PVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:PRK12859 161 PMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
PRK12742 PRK12742
SDR family oxidoreductase;
34-221 9.59e-17

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 77.49  E-value: 9.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAgivchvgKAEDREQLVAkALEHCGG 113
Cdd:PRK12742   4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQETGATAVQT-------DSADRDAVID-VVRKSGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVILVSSIAAYN-PVVALGVYNVSKTAL 192
Cdd:PRK12742  76 LDILVVNAGI-AVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG-GRIIIIGSVNGDRmPVAGMAAYAASKSAL 153

                        170       180
                 ....*....|....*....|....*....
gi 33667109  193 LGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK12742 154 QGMARGLARDFGPRGITINVVQPGPIDTD 182
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 34-227 1.20e-16

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: 77.95  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSEL-VHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 114 VDFLVCSAG----VNPLVGSTLGTSEQIWDKILsvnvkSPALLLSQ-LLPYM-ENRRGAVILVSSIAAYNpvVALGVYNV 187
Cdd:cd08937  81 VDVLINNVGgtiwAKPYEHYEEEQIEAEIRRSL-----FPTLWCCRaVLPHMlERQQGVIVNVSSIATRG--IYRIPYSA 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 33667109 188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:cd08937 154 AKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPR 193
PRK05693 PRK05693
SDR family oxidoreductase;
38-224 2.89e-16

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 77.14  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   38 VAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVdramaklqgEGLSVAGIVC---HVGKAEDREQLVAKALEHCGGV 114
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDV---------EALAAAGFTAvqlDVNDGAALARLAEELEAEHGGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 DFLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:PRK05693  74 DVLINNAGYGAM-GPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHA 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  195 LTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:PRK05693 153 LSDALRLELAPFGVQVMEVQPGAIASQFAS 182
PRK07775 PRK07775
SDR family oxidoreductase;
35-236 3.12e-16

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 76.72  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:PRK07775   9 DRRPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 DFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:PRK07775  89 EVLVSGAG-DTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMiERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLE 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 33667109  194 GLTRTLALELAPKDIRVNCVVPGIIKTDfskvvrigfMGMSLS 236
Cdd:PRK07775 168 AMVTNLQMELEGTGVRASIVHPGPTLTG---------MGWSLP 201
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 34-220 4.66e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 75.96  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVN---PLVgstlGTSEQIWDKILSVNVKSpALLLSQLL--PYMENRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK07523  88 IDILVNNAGMQfrtPLE----DFPADAFERLLRTNISS-VFYVGQAVarHMIARGAGKIINIASVQSALARPGIAPYTAT 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07523 163 KGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK12744 PRK12744
SDR family oxidoreductase;
34-222 6.84e-16

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 75.55  E-value: 6.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVI----SSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSS-IAAYNPVVAlgVYNVS 188
Cdd:PRK12744  86 AFGRPDIAINTVG-KVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDNGKIVTLVTSlLGAFTPFYS--AYAGS 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK12744 163 KAPVEHFTRAASKEFGARGISVTAVGPGPMDTPF 196
PRK09291 PRK09291
SDR family oxidoreductase;
41-222 1.61e-15

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 74.65  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   41 VTGSTSGIGFAIARRLARDGAHVVISSRKQQNVD--RAMAKLQGEGLSVagIVCHVGKAEDReqlvAKALEHcgGVDFLV 118
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTalRAEAARRGLALRV--EKLDLTDAIDR----AQAAEW--DVDVLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  119 CSAGVnplvgstlGTSEQIWD-------KILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK09291  79 NNAGI--------GEAGAVVDipvelvrELFETNVFGPLELTQGFVRKMvARGKGKVVFTSSMAGLITGPFTGAYCASKH 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:PRK09291 151 ALEAIAEAMHAELKPFGIQVATVNPGPYLTGF 182
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 34-221 1.67e-15

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: 74.79  E-value: 1.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMA----KLQGEGLSVagiVCHVGKAEDREQLVAK-AL 108
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAeeieARGGKCIPV---RCDHSDDDEVEALFERvAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 109 EHCGGVDFLVCSA-GVNPLVGSTLG-----TSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAA----YN 177
Cdd:cd09763  78 EQQGRLDILVNNAyAAVQLILVGVAkpfweEPPTIWDDINNVGLRAHYACSVYAAPLMvKAGKGLIVIISSTGGleylFN 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 33667109 178 PvvalgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd09763 158 V-----AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTE 196
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 30-220 2.42e-15

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 73.75  E-value: 2.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   30 RKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIV---CHVGKAEDREQLVAK 106
Cdd:PRK08945   6 KPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIpldLLTATPQNYQQLADT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  107 ALEHCGGVDFLVCSAGVnplvgstLGT-------SEQIWDKILSVNVKSPALLLSQLLPYME-NRRGAVILVSSIAAYNP 178
Cdd:PRK08945  86 IEEQFGRLDGVLHNAGL-------LGElgpmeqqDPEVWQDVMQVNVNATFMLTQALLPLLLkSPAASLVFTSSSVGRQG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 33667109  179 VVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08945 159 RANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT 200
PRK09730 PRK09730
SDR family oxidoreductase;
38-221 6.46e-15

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 72.58  E-value: 6.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   38 VAVVTGSTSGIGFAIARRLARDGAHVVISSrkQQNVDRA---MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNY--QQNLHAAqevVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 DFLVCSAGVnPLVGSTLG--TSEQIwDKILSVNVKSPALLLSQLLPYMENRRG----AVILVSSIAAynpvvALGV---- 184
Cdd:PRK09730  81 AALVNNAGI-LFTQCTVEnlTAERI-NRVLSTNVTGYFLCCREAVKRMALKHGgsggAIVNVSSAAS-----RLGApgey 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 33667109  185 --YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK09730 154 vdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTE 192
PRK06914 PRK06914
SDR family oxidoreductase;
35-221 7.61e-15

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 73.13  E-value: 7.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNvdRAMAKLQGEGLSVAGIVcHVGKAE--DREQLVA--KALEH 110
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEK--QENLLSQATQLNLQQNI-KVQQLDvtDQNSIHNfqLVLKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  111 CGGVDFLVCSAGVnpLVGstlGTSEQI----WDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVY 185
Cdd:PRK06914  79 IGRIDLLVNNAGY--ANG---GFVEEIpveeYRKQFETNVFGAISVTQAVLPYMrKQKSGKIINISSISGRVGFPGLSPY 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06914 154 VSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTN 189
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 38-222 8.51e-15

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: 72.42  E-value: 8.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  38 VAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDramaKLQGEGLSVAG-----IVCHVGKAEDREQLVAKALEHCG 112
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLE----ALLVDIIRDAGgsakaVPTDARDEDEVIALFDLIEEEIG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 113 GVDFLVCSAGVNpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:cd05373  77 PLEVLVYNAGAN-VWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMlARGRGTIIFTGATASLRGRAGFAAFAGAKFA 155

                       170       180       190
                ....*....|....*....|....*....|..
gi 33667109 192 LLGLTRTLALELAPKDIRV-NCVVPGIIKTDF 222
Cdd:cd05373 156 LRALAQSMARELGPKGIHVaHVIIDGGIDTDF 187
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 40-220 1.01e-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: 72.14  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  40 VVTGSTSGIGFAIARRLARDGAHVVISSRKQqnvdramaklqgeglsvAGIVCHVGKAEDREQLVAKALEHCGGV-DFLV 118
Cdd:cd05328   3 VITGAASGIGAATAELLEDAGHTVIGIDLRE-----------------ADVIADLSTPEGRAAAIADVLARCSGVlDGLV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 119 CSAGVNPLVGStlgtseqiwDKILSVNVKSPALLLSQLLPYME-NRRGAVILVSSIAAYNP------------------V 179
Cdd:cd05328  66 NCAGVGGTTVA---------GLVLKVNYFGLRALMEALLPRLRkGHGPAAVVVSSIAGAGWaqdklelakalaagtearA 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 33667109 180 VALG---------VYNVSKTALLGLTRTLALE-LAPKDIRVNCVVPGIIKT 220
Cdd:cd05328 137 VALAehagqpgylAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVET 187
PRK08267 PRK08267
SDR family oxidoreductase;
41-221 8.57e-14

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 69.58  E-value: 8.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   41 VTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVagivcHVGKAEDREQlVAKALEHC-----GGVD 115
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAWT-----GALDVTDRAA-WDAALADFaaatgGRLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:PRK08267  80 VLFNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVInTSSASAIYGQPGLAVYSATKFAVRG 158

                        170       180
                 ....*....|....*....|....*..
gi 33667109  195 LTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08267 159 LTEALDLEWRRHGIRVADVMPLFVDTA 185
PRK08017 PRK08017
SDR family oxidoreductase;
40-226 9.95e-14

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 69.34  E-value: 9.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVdramAKLQGEGLSvaGIVCHVGKAEDREQLVAKALEHCGGVDFLVC 119
Cdd:PRK08017   6 LITGCSSGIGLEAALELKRRGYRVLAACRKPDDV----ARMNSLGFT--GILLDLDDPESVERAADEVIALTDNRLYGLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  120 SAGVNPLVGSTLGTSEQIWDKILSVNV----KSPALLLSQLLPYMENRrgaVILVSSIAAYNPVVALGVYNVSKTALLGL 195
Cdd:PRK08017  80 NNAGFGVYGPLSTISRQQMEQQFSTNFfgthQLTMLLLPAMLPHGEGR---IVMTSSVMGLISTPGRGAYAASKYALEAW 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  196 TRTLALELAPKDIRVNCVVPGIIKTDFSKVV 226
Cdd:PRK08017 157 SDALRMELRHSGIKVSLIEPGPIRTRFTDNV 187
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 41-225 1.19e-13

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 69.02  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   41 VTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLqGEGLSVAGIvchvgKAEDR---EQLVAKALEHCGGVDFL 117
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL-GDNLYIAQL-----DVRNRaaiEEMLASLPAEWRNIDVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  118 VCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNVSKTALLGLT 196
Cdd:PRK10538  79 VNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMvERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFS 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  197 RTLALELAPKDIRVNCVVPGIIK-TDFSKV 225
Cdd:PRK10538 159 LNLRTDLHGTAVRVTDIEPGLVGgTEFSNV 188
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 41-221 1.77e-13

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: 68.25  E-value: 1.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  41 VTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAgiVCHVGKAEDREQLVAKALEHCGG-VDFLVC 119
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVVAG--ALDVTDRAAWAAALADFAAATGGrLDALFN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 120 SAGVnplvgSTLGTSEQI----WDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIAAYNPVVALGVYNVSKTALLG 194
Cdd:cd08931  83 NAGV-----GRGGPFEDVplaaHDRMVDINVKGVLNGAYAALPYLKATPGArVINTASSSAIYGQPDLAVYSATKFAVRG 157

                       170       180
                ....*....|....*....|....*..
gi 33667109 195 LTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:cd08931 158 LTEALDVEWARHGIRVADVWPWFVDTP 184
PRK06123 PRK06123
SDR family oxidoreductase;
35-221 2.01e-13

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 68.65  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRK-QQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGG 113
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLNYLRnRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  114 VDFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR----GAVILVSSIAAYnpvvaLGV----- 184
Cdd:PRK06123  81 LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHggrgGAIVNVSSMAAR-----LGSpgeyi 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 33667109  185 -YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06123 156 dYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE 193
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 32-215 2.11e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 68.93  E-value: 2.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVissrkqqnVDRAMAKLQGEGLS-------VAGIVCHVGKA------- 97
Cdd:PRK07791   2 GLLDGRVVIVTGAGGGIGRAHALAFAAEGARVV--------VNDIGVGLDGSASGgsaaqavVDEIVAAGGEAvangddi 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   98 ---EDREQLVAKALEHCGGVDFLVCSAGVnpLVGSTL-GTSEQIWDKILSVNVKSPALLLSQLLPYM-------ENRRGA 166
Cdd:PRK07791  74 adwDGAANLVDAAVETFGGLDVLVNNAGI--LRDRMIaNMSEEEWDAVIAVHLKGHFATLRHAAAYWraeskagRAVDAR 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 33667109  167 VILVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVP 215
Cdd:PRK07791 152 IINTSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 34-215 2.22e-13

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: 68.24  E-value: 2.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnvdrAMAKLQGEGLSVAGIVCHV-GKA-------EDREQL-- 103
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAE----PHPKLPGTIYTAAEEIEAAgGKAlpcivdiRDEDQVra 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 104 -VAKALEHCGGVDFLVCSAGVNPLVGsTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPV-- 179
Cdd:cd09762  77 aVEKAVEKFGGIDILVNNASAISLTG-TLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILnLSPPLNLNPKwf 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 33667109 180 ---VAlgvYNVSKTALLGLTRTLALELAPKDIRVNCVVP 215
Cdd:cd09762 156 knhTA---YTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 34-221 2.29e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 68.53  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE-GLSVAGIVCHVGKAEDREQLVAKAlehcG 112
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEAREQLAAEA----G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK06125  81 DIDILVNNAGAIP-GGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVnVIGAAGENPDADYICGSAGNAA 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06125 160 LMAFTRALGGKSLDDGVRVVGVNPGPVATD 189
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 39-222 1.41e-12

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: 64.84  E-value: 1.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGA-HVVISSRKqqnvdramaklqgeglsvagivchvgkaedreqlvakalehcggvDFL 117
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSRR---------------------------------------------DVV 35

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 118 VCSAGVnPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRR-GAVILVSSIAAYNPVVALGVYNVSKTALLGLT 196
Cdd:cd02266  36 VHNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                       170       180
                ....*....|....*....|....*.
gi 33667109 197 RTLALELAPKDIRVNCVVPGIIKTDF 222
Cdd:cd02266 115 QQWASEGWGNGLPATAVACGTWAGSG 140
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
37-227 1.53e-12

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 65.86  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVagIVCHVGKAEDREQLVAKAL----EHCG 112
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSNLTF--HSLDLQDVHELETNFNEILssiqEDNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAG-VNPLVGSTLGTSEQIwDKILSVNVKSPALLLSQLLPYMENRRGA--VILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK06924  80 SSIHLINNAGmVAPIKPIEKAESEEL-ITNVHLNLLAPMILTSTFMKHTKDWKVDkrVINISSGAAKNPYFGWSAYCSSK 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVV--PGIIKTDFSKVVR 227
Cdd:PRK06924 159 AGLDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQIR 198
PRK08703 PRK08703
SDR family oxidoreductase;
34-220 1.80e-12

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 65.72  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAM-AKLQGEGLSVAGIVCHVGKAEDRE--QLVAK-ALE 109
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYdAIVEAGHPEPFAIRFDLMSAEEKEfeQFAATiAEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLV-CSAGVNPLVGSTLGTSEQiWDKILSVNVKSPALLLSQLLPYM-ENRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK08703  84 TQGKLDGIVhCAGYFYALSPLDFQTVAE-WVNQYRINTVAPMGLTRALFPLLkQSPDASVIFVGESHGETPKAYWGGFGA 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33667109  188 SKTALLGLTRTLA--LELAPkDIRVNCVVPGIIKT 220
Cdd:PRK08703 163 SKAALNYLCKVAAdeWERFG-NLRANVLVPGPINS 196
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 36-216 2.35e-12

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: 65.56  E-value: 2.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE-GLSVAGIVCHVGKAEDREQLVAKALEHCGGV 114
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIFKRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGV---NPLVGSTLGTseqiWDKILSVNVKSPALLLSQLLPYM--ENRRGAVILVSSIAA-----YNpvvalGV 184
Cdd:cd05322  82 DLLVYSAGIaksAKITDFELGD----FDRSLQVNLVGYFLCAREFSKLMirDGIQGRIIQINSKSGkvgskHN-----SG 152

                       170       180       190
                ....*....|....*....|....*....|..
gi 33667109 185 YNVSKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:cd05322 153 YSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 38-217 5.71e-12

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: 64.56  E-value: 5.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    38 VAVVTGSTSGIGFAIARRLARDGAHVVISSRK-----QQNVDRAMAKLQGEGLSVAGIVCHVGKAEDR-EQLVAKALEHC 111
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRsaaaaSTLAAELNARRPNSAVTCQADLSNSATLFSRcEAIIDACFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   112 GGVDFLVCSAGV---NPLV----GSTLGTSEQI---WDKILSVNVKSPALLLSQLLPYMENRRGA--------VILVSSI 173
Cdd:TIGR02685  83 GRCDVLVNNASAfypTPLLrgdaGEGVGDKKSLevqVAELFGSNAIAPYFLIKAFAQRQAGTRAEqrstnlsiVNLCDAM 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 33667109   174 AAyNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGI 217
Cdd:TIGR02685 163 TD-QPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL 205
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 37-220 1.02e-11

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: 63.11  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVissrkqqNVDRAMAKLQGEGLSVAGIVCHVgkaEDREQLVAKALEHCGGVDF 116
Cdd:cd05334   2 RVVLVYGGRGALGSAVVQAFKSRGWWVA-------SIDLAENEEADASIIVLDSDSFT---EQAKQVVASVARLSGKVDA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 117 LVCSAGvnPLVGSTL--GTSEQIWDKILSVNVKSpALLLSQL-LPYMeNRRGAVILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd05334  72 LICVAG--GWAGGSAksKSFVKNWDLMWKQNLWT-SFIASHLaTKHL-LSGGLLVLTGAKAALEPTPGMIGYGAAKAAVH 147

                       170       180
                ....*....|....*....|....*....
gi 33667109 194 GLTRTLALEL--APKDIRVNCVVPGIIKT 220
Cdd:cd05334 148 QLTQSLAAENsgLPAGSTANAILPVTLDT 176
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 37-218 1.06e-11

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: 63.36  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVI--SSRKQQNVDRAMAKLQGEGLSVAgivchvgkAEDREQLVAKALEHCGGV 114
Cdd:cd05361   2 SIALVTHARHFAGPASAEALTEDGYTVVChdASFADAAERQAFESENPGTKALS--------EQKPEELVDAVLQAGGAI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIAAYNPVVALGVYNVSKTALL 193
Cdd:cd05361  74 DVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGsIIFITSAVPKKPLAYNSLYGPARAAAV 153

                       170       180
                ....*....|....*....|....*
gi 33667109 194 GLTRTLALELAPKDIRVNCVVPGII 218
Cdd:cd05361 154 ALAESLAKELSRDNILVYAIGPNFF 178
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
32-220 1.49e-11

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 63.42  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTG--STSGIGFAIARRLARDGAHVVISS--RKQQNVDRAMAKLQgeglSVAGIV-CHVGKAEDREQLVAK 106
Cdd:PRK07889   3 GLLEGKRILVTGviTDSSIAFHVARVAQEQGAEVVLTGfgRALRLTERIAKRLP----EPAPVLeLDVTNEEHLASLADR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  107 ALEHCGGVDFLVCSAGVNPlvGSTLGTS--EQIWD---KILSVNVKSPALLLSQLLPYMeNRRGAVILVSsiaaYNPVVA 181
Cdd:PRK07889  79 VREHVDGLDGVVHSIGFAP--QSALGGNflDAPWEdvaTALHVSAYSLKSLAKALLPLM-NEGGSIVGLD----FDATVA 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 33667109  182 LGVYN---VSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07889 152 WPAYDwmgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRT 193
PRK07024 PRK07024
SDR family oxidoreductase;
40-220 8.60e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 61.10  E-value: 8.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARDGAHVVISSRKQQnvdrAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKA---LEHCGGVDF 116
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTD----ALQAFAARLPKAARVSVYAADVRDADALAAAAadfIAAHGLPDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 LVCSAGVNplVGSTLGTSEQI--WDKILSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALL 193
Cdd:PRK07024  82 VIANAGIS--VGTLTEEREDLavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVgIASVAGVRGLPGAGAYSASKAAAI 159

                        170       180
                 ....*....|....*....|....*..
gi 33667109  194 GLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07024 160 KYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
92-227 1.09e-10

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 60.91  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   92 CHVGKAEDREQLVAKALEHCGGVDFLVCSAGVNP---LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVI 168
Cdd:PRK08415  62 LDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFAPkeaLEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL-NDGASVL 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33667109  169 LVSSIAAYNPVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVVR 227
Cdd:PRK08415 141 TLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKTlaasgigDFRMILK 206
PRK07023 PRK07023
SDR family oxidoreductase;
39-227 1.18e-10

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 60.41  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   39 AVVTGSTSGIGFAIARRLARDGAHVVISSRkqqNVDRAMAKLQGEglSVAGIVCHVGKAEDREQLVAKALEHCGGVDF-- 116
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVAR---SRHPSLAAAAGE--RLAEVELDLSDAAAAAAWLAGDLLAAFVDGAsr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 --LVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMEN---RRgaVILVSSIAAYNPVVALGVYNVSKTA 191
Cdd:PRK07023  79 vlLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaaeRR--ILHISSGAARNAYAGWSVYCATKAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  192 LLGLTRTLALElAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:PRK07023 157 LDHHARAVALD-ANRALRIVSLAPGVVDTGMQATIR 191
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 37-237 1.62e-10

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: 60.56  E-value: 1.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDR--EQLVAKALEHCGGV 114
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKsiRAFAAEFLAEEDRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 115 DFLVCSAGVNPLVGStlgTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIA---------------AYNP 178
Cdd:cd09807  82 DVLINNAGVMRCPYS---KTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSrIVNVSSLAhkagkinfddlnsekSYNT 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33667109 179 VVAlgvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKvvRIGFMGMSLSG 237
Cdd:cd09807 159 GFA---YCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGR--HTGIHHLFLST 212
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-215 2.06e-10

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 60.57  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVI----SSRKQQNVDRAMAKLQGEGLSVAGivcHVGKAEDREQLVAKALE 109
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVndvaSALDASDVLDEIRAAGAKAVAVAG---DISQRATADELVATAVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 hCGGVDFLVCSAGV--NPLVGStlgTSEQIWDKILSVNVKSPALLLSQLLPYMENRR--------GAVILVSSIAAYNPV 179
Cdd:PRK07792  87 -LGGLDIVVNNAGItrDRMLFN---MSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAkaaggpvyGRIVNTSSEAGLVGP 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  180 VALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVP 215
Cdd:PRK07792 163 VGQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK06947 PRK06947
SDR family oxidoreductase;
37-221 3.18e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 59.43  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQ----QNVDRAMAKLQGEGLSVAGIVCHvgkAEDREQLVAKALEHCG 112
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDaaaaEETADAVRAAGGRACVVAGDVAN---EADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 GVDFLVCSAGV----NPLVGSTLGTSEQIWDkilsVNVKSPALLLSQLLPYMENRRG----AVILVSSIAAynpvvALGV 184
Cdd:PRK06947  80 RLDALVNNAGIvapsMPLADMDAARLRRMFD----TNVLGAYLCAREAARRLSTDRGgrggAIVNVSSIAS-----RLGS 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 33667109  185 ------YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK06947 151 pneyvdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE 193
PRK06139 PRK06139
SDR family oxidoreductase;
30-220 3.33e-10

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 60.12  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   30 RKGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGVNPlVGSTLGTSEQIWDKILSVNvkspalLLSQL------LPY-MENRRGavILVSSIA----AYNP 178
Cdd:PRK06139  81 FGGRIDVWVNNVGVGA-VGRFEETPIEAHEQVIQTN------LIGYMrdahaaLPIfKKQGHG--IFINMISlggfAAQP 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 33667109  179 VVAlgVYNVSKTALLGLTRTLALELAPK-DIRVNCVVPGIIKT 220
Cdd:PRK06139 152 YAA--AYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
PRK07806 PRK07806
SDR family oxidoreductase;
32-121 3.44e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 59.35  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSR-KQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEH 110
Cdd:PRK07806   2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREE 81

                         90
                 ....*....|.
gi 33667109  111 CGGVDFLVCSA 121
Cdd:PRK07806  82 FGGLDALVLNA 92
PRK06482 PRK06482
SDR family oxidoreductase;
41-229 3.50e-10

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 59.36  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   41 VTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKlQGEGLSVAgiVCHVGKAEDREQLVAKALEHCGGVDFLVCS 120
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKAR-YGDRLWVL--QLDVTDSAAVRAVVDRAFAALGRIDVVVSN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  121 AGVNpLVGSTLG-TSEQIWDKIlSVNVKSPALLLSQLLPYMENRRGAVIL-VSSIAAYNPVVALGVYNVSKTALLGLTRT 198
Cdd:PRK06482  84 AGYG-LFGAAEElSDAQIRRQI-DTNLIGSIQVIRAALPHLRRQGGGRIVqVSSEGGQIAYPGFSLYHATKWGIEGFVEA 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 33667109  199 LALELAPKDIRVNCVVPGIIKTDFSKVVRIG 229
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPARTNFGAGLDRG 192
PRK06196 PRK06196
oxidoreductase; Provisional
 27-228 4.57e-10

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 59.31  E-value: 4.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   27 GIDRKGvlanRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKqqnVDRAMAKLQG-EGLSVAGIvcHVGKAEDREQLVA 105
Cdd:PRK06196  21 GHDLSG----KTAIVTGGYSGLGLETTRALAQAGAHVIVPARR---PDVAREALAGiDGVEVVML--DLADLESVRAFAE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  106 KALEHCGGVDFLVCSAGV--NPLVGSTLGtseqiWDKILSVNVKSPALLLSQLLPYMENRRGA-VILVSSIA-------- 174
Cdd:PRK06196  92 RFLDSGRRIDILINNAGVmaCPETRVGDG-----WEAQFATNHLGHFALVNLLWPALAAGAGArVVALSSAGhrrspirw 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33667109  175 -------AYNPVVAlgvYNVSKTA----LLGLTRTlaleLAPKDIRVNCVVPGIIKTDFSKVVRI 228
Cdd:PRK06196 167 ddphftrGYDKWLA---YGQSKTAnalfAVHLDKL----GKDQGVRAFSVHPGGILTPLQRHLPR 224
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 31-220 1.35e-09

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: 57.67  E-value: 1.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  31 KGVLanrvavVTGSTSGIGFAIARRLARDGAHVvISSRKQQNVDRAmAKLQG---EGLSVagIVCHVGKAEDREQLVAKA 107
Cdd:cd09805   1 KAVL------ITGCDSGFGNLLAKKLDSLGFTV-LAGCLTKNGPGA-KELRRvcsDRLRT--LQLDVTKPEQIKRAAQWV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 108 LEHCGGVDF--LVCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALGVY 185
Cdd:cd09805  71 KEHVGEKGLwgLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAY 150

                       170       180       190
                ....*....|....*....|....*....|....*
gi 33667109 186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd09805 151 CASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKT 185
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
32-227 1.53e-09

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 57.29  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTG--STSGIGFAIARRLARDGAHVVIS--SRKQQNVDRAMAKLQGEGLSVAgivCHVGKAEDREQLVAKA 107
Cdd:PRK08690   2 GFLQGKKILITGmiSERSIAYGIAKACREQGAELAFTyvVDKLEERVRKMAAELDSELVFR---CDVASDDEINQVFADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  108 LEHCGGVDFLVCSAGVNP---LVGSTLGT-SEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSSIAAYNPVVALG 183
Cdd:PRK08690  79 GKHWDGLDGLVHSIGFAPkeaLSGDFLDSiSREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNYN 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 33667109  184 VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVVR 227
Cdd:PRK08690 159 VMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTlaasgiaDFGKLLG 209
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 39-237 1.56e-09

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 57.95  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   39 AVVTGSTSGIGFAIARRLARDGAHVVISSR---KQQNVDRAMAKLQGEgLSVAGIVchVGKAEDREQLVAKALEHCGGVD 115
Cdd:PLN02780  56 ALVTGPTDGIGKGFAFQLARKGLNLVLVARnpdKLKDVSDSIQSKYSK-TQIKTVV--VDFSGDIDEGVKRIKETIEGLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 --FLVCSAGVN-PLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENR-RGAVILVSSIAAY----NPVVAlgVYNV 187
Cdd:PLN02780 133 vgVLINNVGVSyPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRkKGAIINIGSGAAIvipsDPLYA--VYAA 210

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 33667109  188 SKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVRIGFMGMSLSG 237
Cdd:PLN02780 211 TKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSFLVPSSDG 260
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 38-227 3.68e-09

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: 56.46  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    38 VAVVTGSTSGIGFAIARRLAR----DGAHVVISSRKQQNVDRAMAKLQGE--GLSVAGIVCHVGKAEDREQLVaKALEHC 111
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLL-KALREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   112 GGVD-----FLVCSAGVnplVGST------LGTSEQIwDKILSVNVKSPALLLSQLLPYMENRRGAVILV---SSIAAYN 177
Cdd:TIGR01500  81 PRPKglqrlLLINNAGT---LGDVskgfvdLSDSTQV-QNYWALNLTSMLCLTSSVLKAFKDSPGLNRTVvniSSLCAIQ 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 33667109   178 PVVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSKVVR 227
Cdd:TIGR01500 157 PFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVR 206
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 39-222 9.08e-09

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: 54.45  E-value: 9.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnvdrAMAKLqGEGLSVAGIVCHVGKaedrEQLVAKALEHCGGVDFLV 118
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAG----ALAGL-AAEVGALARPADVAA----ELEVWALAQELGPLDLLV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 119 CSAGvNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENrRGAVILVSSIAAYNPVVALGVYNVSKTALLGLTRT 198
Cdd:cd11730  72 YAAG-AILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAA-GARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEV 149

                       170       180
                ....*....|....*....|....
gi 33667109 199 LALELapKDIRVNCVVPGIIKTDF 222
Cdd:cd11730 150 ARKEV--RGLRLTLVRPPAVDTGL 171
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
32-227 9.30e-09

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 55.21  E-value: 9.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTG--STSGIGFAIARRLARDGAHVVISSRKQQNVDRaMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALE 109
Cdd:PRK06997   2 GFLAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVGDRFKDR-ITEFAAEFGSDLVFPCDVASDEQIDALFASLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAGVNP---LVGSTL-GTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVALGVY 185
Cdd:PRK06997  81 HWDGLDGLVHSIGFAPreaIAGDFLdGLSRENFRIAHDISAYSFPALAKAALPML-SDDASLLTLSYLGAERVVPNYNTM 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 33667109  186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVVR 227
Cdd:PRK06997 160 GLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaasgikDFGKILD 208
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 35-220 2.05e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 54.26  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGStSGIGFAIARRLARdGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHcGGV 114
Cdd:PRK06940   1 MKEVVVVIGA-GGIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQTL-GPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 DFLVCSAGVNPLVGSTlgtseqiwDKILSVNVKSPALLLSQLLPYMEnRRGAVILVSSIAAYNP---------------- 178
Cdd:PRK06940  78 TGLVHTAGVSPSQASP--------EAILKVDLYGTALVLEEFGKVIA-PGGAGVVIASQSGHRLpaltaeqeralattpt 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 33667109  179 --------------VVALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06940 149 eellslpflqpdaiEDSLHAYQIAKRANALRVMAEAVKWGERGARINSISPGIIST 204
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 39-200 2.65e-08

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: 54.06  E-value: 2.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGA-HVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFL 117
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDAL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 118 VCSAGVNPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGA---VILVSSIaAYNPVVALGvyNVSKTALLG 194
Cdd:cd09810  84 VCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENAsprIVIVGSI-THNPNTLAG--NVPPRATLG 160


                ....*.
gi 33667109 195 LTRTLA 200
Cdd:cd09810 161 DLEGLA 166
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 40-218 2.84e-08

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 53.40  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARDGAHVVISSRKQQ-NVDramaklqgeGLSVAGIVCHVG---KAEDREQLVAKALEHCGGVD 115
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYpAID---------GLRQAGAQCIQAdfsTNAGIMAFIDELKQHTDGLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  116 FLVCSAgvNPLVGSTLGTS-EQIWDKILSVNVKSPALL---LSQLLpymenrRGAVILVSSIAAY-NPVVALG-----VY 185
Cdd:PRK06483  77 AIIHNA--SDWLAEKPGAPlADVLARMMQIHVNAPYLLnlaLEDLL------RGHGHAASDIIHItDYVVEKGsdkhiAY 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  186 NVSKTALLGLTRTLALELAPKdIRVNCVVPGII 218
Cdd:PRK06483 149 AASKAALDNMTLSFAAKLAPE-VKVNSIAPALI 180
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
34-220 2.97e-08

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 53.56  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTG--STSGIGFAIARRLARDGAHVVIS------SRKQQNVDRAMAKLQGEGLsvagIVCHVGKAEDREQLVA 105
Cdd:PRK07370   4 LTGKKALVTGiaNNRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVRELTEPLNPSLF----LPCDVQDDAQIEETFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  106 KALEHCGGVDFLV-CSAGVNP--LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMeNRRGAVILVSSIAAYNPVVAL 182
Cdd:PRK07370  80 TIKQKWGKLDILVhCLAFAGKeeLIGDFSATSREGFARALEISAYSLAPLCKAAKPLM-SEGGSIVTLTYLGGVRAIPNY 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 33667109  183 GVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07370 159 NVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRT 196
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 41-220 3.75e-08

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: 53.27  E-value: 3.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  41 VTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDreqlVAKALEHCGGVDFLVCS 120
Cdd:cd08951  12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRK----LADQVNAIGRFDAVIHN 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 121 AGVnpLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLP-----YMEN--RRGAVILVSSIAAYN-PVVALGVYNVSKtaL 192
Cdd:cd08951  88 AGI--LSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRpkrliYLSSgmHRGGNASLDDIDWFNrGENDSPAYSDSK--L 163

                       170       180
                ....*....|....*....|....*...
gi 33667109 193 LGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:cd08951 164 HVLTLAAAVARRWKDVSSNAVHPGWVPT 191
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
40-191 3.78e-08

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 53.44  E-value: 3.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  40 VVTGSTSGIGFAIARRLARDGAHVVISSRKqqnvDRAMAKLQGeglsVAGIVCHVGKAEDREQLvakaLEHCGGVDFLVC 119
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGHEVVGLDRS----PPGAANLAA----LPGVEFVRGDLRDPEAL----AAALAGVDAVVH 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 120 SAGVnplvgstLGTSEQIWDKILSVNVKSPALLLSQLLpymENRRGAVILVSSIAAY----------NPVVALGVYNVSK 189
Cdd:COG0451  71 LAAP-------AGVGEEDPDETLEVNVEGTLNLLEAAR---AAGVKRFVYASSSSVYgdgegpidedTPLRPVSPYGASK 140


                ..
gi 33667109 190 TA 191
Cdd:COG0451 141 LA 142
PRK09186 PRK09186
flagellin modification protein A; Provisional
 34-219 5.62e-08

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 52.68  E-value: 5.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVI----SSRKQQNVDRAMAKLQGEGLSVagIVCHVGKAEDREQLVAKALE 109
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAadidKEALNELLESLGKEFKSKKLSL--VELDITDQESLEEFLSKSAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  110 HCGGVDFLVCSAgvNPLvGSTLGTS--EQIWDKI---LSVNVKSPALLLSQLLPYMENRR-GAVILVSSI---------- 173
Cdd:PRK09186  80 KYGKIDGAVNCA--YPR-NKDYGKKffDVSLDDFnenLSLHLGSSFLFSQQFAKYFKKQGgGNLVNISSIygvvapkfei 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 33667109  174 ----AAYNPVValgvYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIK 219
Cdd:PRK09186 157 yegtSMTSPVE----YAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIL 202
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 25-176 5.72e-08

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: 53.53  E-value: 5.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  25 STGIDRKGVLanrvaVVTGSTSGIGFAIARRLARD-GAHVVISSR-----KQQNVDRAMAKLQGEGLSVAGIVCHVGKAE 98
Cdd:cd08953 199 SAPLKPGGVY-----LVTGGAGGIGRALARALARRyGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTDAA 273

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33667109  99 DREQLVAKALEHCGGVDFLVCSAGVNPlvGSTLGT-SEQIWDKILSVNVKSpALLLSQLLPYMENRRgaVILVSSIAAY 176
Cdd:cd08953 274 AVRRLLEKVRERYGAIDGVIHAAGVLR--DALLAQkTAEDFEAVLAPKVDG-LLNLAQALADEPLDF--FVLFSSVSAF 347
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 40-175 7.72e-08

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: 51.41  E-value: 7.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    40 VVTGSTSGIGFAIARRLARDGA-HVVISSRKQQNVDRA---MAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAqalIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33667109   116 FLVCSAGV---NPLVGSTLGTseqiWDKILSVNVKSpALLLSQLLPYMENRrgAVILVSSIAA 175
Cdd:pfam08659  84 GVIHAAGVlrdALLENMTDED----WRRVLAPKVTG-TWNLHEATPDEPLD--FFVLFSSIAG 139
PRK06101 PRK06101
SDR family oxidoreductase;
36-220 9.13e-08

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 51.79  E-value: 9.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   36 NRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQnvdrAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKA-------L 108
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIACGRNQS----VLDELHTQSANIFTLAFDVTDHPGTKAALSQLpfipelwI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  109 EHCGGVDFLvcSAGVnplvgstlgTSEQIWDKILSVNVKSPALLLSQLLPYMEnRRGAVILVSSIAAYNPVVALGVYNVS 188
Cdd:PRK06101  77 FNAGDCEYM--DDGK---------VDATLMARVFNVNVLGVANCIEGIQPHLS-CGHRVVIVGSIASELALPRAEAYGAS 144

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06101 145 KAAVAYFARTLQLDLRPKGIEVVTVFPGFVAT 176
PRK08177 PRK08177
SDR family oxidoreductase;
37-221 9.43e-08

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 51.57  E-value: 9.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVD--RAMAKLQGEGLSVagivchvgkaEDREQLVAKALEHCGGV 114
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTalQALPGVHIEKLDM----------NDPASLDQLLQRLQGQR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  115 -DFLVCSAGV-NPLVGSTLG-TSEQIWDKILSvNVKSPALLLSQLLPYMENRRGAVILVSSI---AAYNPVVALGVYNVS 188
Cdd:PRK08177  72 fDLLFVNAGIsGPAHQSAADaTAAEIGQLFLT-NAIAPIRLARRLLGQVRPGQGVLAFMSSQlgsVELPDGGEMPLYKAS 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 33667109  189 KTALLGLTRTLALELAPKDIRVNCVVPGIIKTD 221
Cdd:PRK08177 151 KAALNSMTRSFVAELGEPTLTVLSMHPGWVKTD 183
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 37-80 1.52e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 51.95  E-value: 1.52e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKL 80
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARI 60
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
34-220 1.90e-07

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 51.09  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTG--STSGIGFAIARRLARDGAHVVISsrkQQNvDRAMAKLQ--GEGLSvAGIV--CHVGKAEDREQLVAKA 107
Cdd:PRK07533   8 LAGKRGLVVGiaNEQSIAWGCARAFRALGAELAVT---YLN-DKARPYVEplAEELD-APIFlpLDVREPGQLEAVFARI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  108 LEHCGGVDFLVCSAGVNP---LVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVILVSSIAAYNPVVALGV 184
Cdd:PRK07533  83 AEEWGRLDFLLHSIAFAPkedLHGRVVDCSREGFALAMDVSCHSFIRMARLAEPLMTNG-GSLLTMSYYGAEKVVENYNL 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 33667109  185 YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07533 162 MGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKT 197
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
34-227 2.19e-07

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 50.88  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTG--STSGIGFAIARRLARDGAHVVISSRKQ---QNVDRAMAKLQGEGLSVagIVCHVGKAEDREQLVAKAL 108
Cdd:PRK08594   5 LEGKTYVVMGvaNKRSIAWGIARSLHNAGAKLVFTYAGErleKEVRELADTLEGQESLL--LPCDVTSDEEITACFETIK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  109 EHCGGVDFLVCS---AGVNPLVGSTLGTSEQIWdkILSVNVKSPAL-LLSQLLPYMENRRGAVILVSSIAAYNPVVALGV 184
Cdd:PRK08594  83 EEVGVIHGVAHCiafANKEDLRGEFLETSRDGF--LLAQNISAYSLtAVAREAKKLMTEGGSIVTLTYLGGERVVQNYNV 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 33667109  185 YNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVVR 227
Cdd:PRK08594 161 MGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTlsakgvgGFNSILK 210
PRK05854 PRK05854
SDR family oxidoreductase;
34-80 2.80e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 51.22  E-value: 2.80e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKL 80
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAI 58
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
32-220 4.30e-07

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 50.11  E-value: 4.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTG--STSGIGFAIARRLARDGAHVVISsrkQQN--VDRAMAKLQGEglSVAGIVCHVGKAEDREQLVAKA 107
Cdd:PRK06079   3 GILSGKKIVVMGvaNKRSIAWGCAQAIKDQGATVIYT---YQNdrMKKSLQKLVDE--EDLLVECDVASDESIERAFATI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  108 LEHCGGVDFLVCS---AGVNPLVGSTLGTSEQIWDkiLSVNVKSPALLLSQLL--PYMENRRGAVIL-----VSSIAAYN 177
Cdd:PRK06079  78 KERVGKIDGIVHAiayAKKEELGGNVTDTSRDGYA--LAQDISAYSLIAVAKYarPLLNPGASIVTLtyfgsERAIPNYN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 33667109  178 pvvalgVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK06079 156 ------VMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKT 192
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 40-175 4.56e-07

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: 49.02  E-value: 4.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109     40 VVTGSTSGIGFAIARRLARDGA-HVVISSR---KQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVD 115
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109    116 FLVCSAGVNPLvGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYMENRrgAVILVSSIAA 175
Cdd:smart00822  84 GVIHAAGVLDD-GVLASLTPERFAAVLAPKAAG-AWNLHELTADLPLD--FFVLFSSIAG 139
PRK08251 PRK08251
SDR family oxidoreductase;
40-231 1.04e-06

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 48.78  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGE--GLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFL 117
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELGGLDRV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  118 VCSAGVNPlvGSTLGTSE-QIWDKILSVNVKSpalLLSQLLPYME----NRRGAVILVSSIAAYNPVV-ALGVYNVSKTA 191
Cdd:PRK08251  86 IVNAGIGK--GARLGTGKfWANKATAETNFVA---ALAQCEAAMEifreQGSGHLVLISSVSAVRGLPgVKAAYAASKAG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 33667109  192 LLGLTRTLALELAPKDIRVNCVVPGIIKTDFS-KVVRIGFM 231
Cdd:PRK08251 161 VASLGEGLRAELAKTPIKVSTIEPGYIRSEMNaKAKSTPFM 201
PRK06953 PRK06953
SDR family oxidoreductase;
37-221 1.30e-06

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 48.53  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAkLQGEGLSV----AGIVCHVGKAEDREQLvakalehcg 112
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQA-LGAEALALdvadPASVAGLAWKLDGEAL--------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  113 gvDFLVCSAGV-NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRRGAVILVSS----IAAYnPVVALGVYNV 187
Cdd:PRK06953  72 --DAAVYVAGVyGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSrmgsIGDA-TGTTGWLYRA 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  188 SKTALlgltrTLALELAPKDIR-VNCVV--PGIIKTD 221
Cdd:PRK06953 149 SKAAL-----NDALRAASLQARhATCIAlhPGWVRTD 180
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
43-224 1.39e-06

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 48.55  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   43 GSTSGIGFAIARR-LARDGAHVVISSRKQQ-NVDRAMAKLQGEGL-SVAGIVCHVGKAEDREQLVAKALEHcGGVDFLVC 119
Cdd:PRK07904  15 GGTSEIGLAICERyLKNAPARVVLAALPDDpRRDAAVAQMKAAGAsSVEVIDFDALDTDSHPKVIDAAFAG-GDVDVAIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  120 SAGvnplvgsTLGTSEQIWD------KILSVNVKSP---ALLLSQllpYMENR-RGAVILVSSIAAYNPVVALGVYNVSK 189
Cdd:PRK07904  94 AFG-------LLGDAEELWQnqrkavQIAEINYTAAvsvGVLLGE---KMRAQgFGQIIAMSSVAGERVRRSNFVYGSTK 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33667109  190 TALLGLTRTLALELAPKDIRVNCVVPGIIKTDFSK 224
Cdd:PRK07904 164 AGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSA 198
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
32-220 1.63e-06

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 48.59  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTG--STSGIGFAIARRLARDGAHVVISSRK---QQNVDRAMAKLQGEglsVAGiVCHVGKAEDREQLVAK 106
Cdd:PRK08159   6 GLMAGKRGLILGvaNNRSIAWGIAKACRAAGAELAFTYQGdalKKRVEPLAAELGAF---VAG-HCDVTDEASIDAVFET 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  107 ALEHCGGVDFLVCSAGV---NPLVGSTLGTSEQIWDKILSVNVKSPALLLSQLLPYMENRrGAVILVSSIAAYNPVVALG 183
Cdd:PRK08159  82 LEKKWGKLDFVVHAIGFsdkDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLMTDG-GSILTLTYYGAEKVMPHYN 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 33667109  184 VYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK08159 161 VMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKT 197
PRK07102 PRK07102
SDR family oxidoreductase;
41-220 1.91e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 48.00  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   41 VTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGlsVAGIVCHVGKAEDREQLVAkALEHCGGV-DFLVC 119
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARG--AVAVSTHELDILDTASHAA-FLDSLPALpDIVLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  120 SAGvnplvgsTLGT---SEQIWD---KILSVNVKSPALLLSQLLPYMENRRGAVILV-SSIAA-------YnpvvalgVY 185
Cdd:PRK07102  83 AVG-------TLGDqaaCEADPAlalREFRTNFEGPIALLTLLANRFEARGSGTIVGiSSVAGdrgrasnY-------VY 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 33667109  186 NVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT 220
Cdd:PRK07102 149 GSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRT 183
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 37-224 4.50e-06

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: 47.21  E-value: 4.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDR------EQLVAKALEh 110
Cdd:cd09809   2 KVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRsvqrfaEAFKAKNSP- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109 111 cggVDFLVCSAGVNPL--------VGSTLGTSE-------QIWDKILSVNVKSPALLLSQllpymENRRGAVILVSS--- 172
Cdd:cd09809  81 ---LHVLVCNAAVFALpwtltedgLETTFQVNHlghfylvQLLEDVLRRSAPARVIVVSS-----ESHRFTDLPDSCgnl 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33667109 173 -IAAYNPVV----ALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPG-IIKTDFSK 224
Cdd:cd09809 153 dFSLLSPPKkkywSMLAYNRAKLCNILFSNELHRRLSPRGITSNSLHPGnMMYSSIHR 210
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 31-216 1.24e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 46.15  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   31 KGVLANRVAVVTGSTSGIGFAIARRLARDGAHVVISSR----KQQNVDRA---------MAKLQGEGLSVAgiVCHVgKA 97
Cdd:PRK08303   3 MKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRstraRRSEYDRPetieetaelVTAAGGRGIAVQ--VDHL-VP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   98 EDREQLVAKALEHCGGVDFLvcsagVNPLVGSTLGT--SEQIWD-------KILSVNVKSPALLLSQLLPYMENRRGAVI 168
Cdd:PRK08303  80 EQVRALVERIDREQGRLDIL-----VNDIWGGEKLFewGKPVWEhsldkglRMLRLAIDTHLITSHFALPLLIRRPGGLV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 33667109  169 L--VSSIAAYNPV-VALGV-YNVSKTALLGLTRTLALELAPKDIRVNCVVPG 216
Cdd:PRK08303 155 VeiTDGTAEYNAThYRLSVfYDLAKTSVNRLAFSLAHELAPHGATAVALTPG 206
PRK06720 PRK06720
hypothetical protein; Provisional
 34-123 8.10e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 42.27  E-value: 8.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQ---QNVDRAMAKLQGEGLSVAgivCHVGKAEDREQLVAKALEH 110
Cdd:PRK06720  14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQesgQATVEEITNLGGEALFVS---YDMEKQGDWQRVISITLNA 90

                         90
                 ....*....|...
gi 33667109  111 CGGVDFLVCSAGV 123
Cdd:PRK06720  91 FSRIDMLFQNAGL 103
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 34-86 1.03e-04

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: 42.38  E-value: 1.03e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33667109  34 LANRVAVVTGSTSGIGFAIARRLARDGAHVVISSR---KQQNVDRAMAKLQGEGLS 86
Cdd:cd01078  26 LKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRdleRAQKAADSLRARFGEGVG 81
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 40-125 1.16e-04

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: 42.53  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  40 VVTGSTSGIGFAIARRLARDGAHVVISSRkqqNVDRAmaklqgEGLSVAGIVCHVGKAEDREQLvAKALEhcgGVDFLVC 119
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARGHPVRALVR---DPEKA------AALAAAGVEVVQGDLDDPESL-AAALA---GVDAVFL 69


                ....*.
gi 33667109 120 SAGVNP 125
Cdd:COG0702  70 LVPSGP 75
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 38-80 4.48e-04

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: 41.22  E-value: 4.48e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 33667109  38 VAVVTGSTSGIGFAIARRL-----ARDGAHVVISSRKQQNVDRAMAKL 80
Cdd:cd08941   3 VVLVTGANSGLGLAICERLlaeddENPELTLILACRNLQRAEAACRAL 50
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
32-227 7.21e-04

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 40.38  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   32 GVLANRVAVVTG--STSGIGFAIARRLARDGAHVVISSRKQQnVDRAMAKLQGEglsvagIVCH------VGKAEDREQL 103
Cdd:PRK06603   4 GLLQGKKGLITGiaNNMSISWAIAQLAKKHGAELWFTYQSEV-LEKRVKPLAEE------IGCNfvseldVTNPKSISNL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  104 VAKALEHCGGVDFLV---CSAGVNPLVGSTLGTSEQIWDKILSVNVKSpALLLSQLLPYMENRRGAVILVSSIAAYNPVV 180
Cdd:PRK06603  77 FDDIKEKWGSFDFLLhgmAFADKNELKGRYVDTSLENFHNSLHISCYS-LLELSRSAEALMHDGGSIVTLTYYGAEKVIP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 33667109  181 ALGVYNVSKTALLGLTRTLALELAPKDIRVNCVVPGIIKT-------DFSKVVR 227
Cdd:PRK06603 156 NYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTlassaigDFSTMLK 209
PRK05599 PRK05599
SDR family oxidoreductase;
40-218 1.35e-03

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 39.48  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARdGAHVVISSRKQQNVDRAMAKLQGEG-LSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLV 118
Cdd:PRK05599   4 LILGGTSDIAGEIATLLCH-GEDVVLAARRPEAAQGLASDLRQRGaTSVHVLSFDAQDLDTHRELVKQTQELAGEISLAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  119 CSAGVnplvgstLG------TSEQIWDKILSVNVKSPALLLSQLLPYMENR--RGAVILVSSIAAYNPVVALGVYNVSKT 190
Cdd:PRK05599  83 VAFGI-------LGdqeraeTDEAHAVEIATVDYTAQVSMLTVLADELRAQtaPAAIVAFSSIAGWRARRANYVYGSTKA 155

                        170       180
                 ....*....|....*....|....*...
gi 33667109  191 ALLGLTRTLALELAPKDIRVNCVVPGII 218
Cdd:PRK05599 156 GLDAFCQGLADSLHGSHVRLIIARPGFV 183
PLN00015 PLN00015
protochlorophyllide reductase
 40-123 1.37e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 39.69  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLARDGA-HVVISSRKQQNVDRAMAKLQGEGLSVAGIVCHVGKAEDREQLVAKALEHCGGVDFLV 118
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKwHVVMACRDFLKAERAAKSAGMPKDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDVLV 80


                 ....*
gi 33667109  119 CSAGV 123
Cdd:PLN00015  81 CNAAV 85
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 36-175 1.44e-03

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: 39.67  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  36 NRVAVVTGSTSGIGFAIARRLARDGA-HVVISSRKQQN--VDRAMAKLQGEGLSVAGIVCHVGkaeDREQL--VAKALEH 110
Cdd:cd05274 150 DGTYLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAprAAARAALLRAGGARVSVVRCDVT---DPAALaaLLAELAA 226

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33667109 111 CGGVDFLVCSAGV-NPLVGSTLGTSEqiWDKILSVNVKsPALLLSQLLPymeNRRGAVILV-SSIAA 175
Cdd:cd05274 227 GGPLAGVIHAAGVlRDALLAELTPAA--FAAVLAAKVA-GALNLHELTP---DLPLDFFVLfSSVAA 287
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
152-220 1.74e-03

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 39.21  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  152 LLSQLLPYMeNRRGAVILVSSIAAY---------------------------NPVVALGVYNVSKTALLGLTRTLALE-L 203
Cdd:PRK12428  78 LTEALLPRM-APGGAIVNVASLAGAewpqrlelhkalaatasfdegaawlaaHPVALATGYQLSKEALILWTMRQAQPwF 156

                         90
                 ....*....|....*..
gi 33667109  204 APKDIRVNCVVPGIIKT 220
Cdd:PRK12428 157 GARGIRVNCVAPGPVFT 173
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
 41-112 2.53e-03

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 38.87  E-value: 2.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33667109  41 VTGSTSGIGFAIARRLARDGAHVVISSRKqqnvDRAMAKLQGEGLSVagivcHVGKAEDREQLVAKALE-----HCG 112
Cdd:cd05262   5 VTGATGFIGSAVVRELVAAGHEVVGLARS----DAGAAKLEAAGAQV-----HRGDLEDLDILRKAAAEadaviHLA 72
PLN02686 PLN02686
cinnamoyl-CoA reductase
 35-114 4.71e-03

cinnamoyl-CoA reductase


Pssm-ID: 215370  Cd Length: 367  Bit Score: 38.22  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   35 ANRVAVVTGSTSGIGFAIARRLARDGAHVVISSRKQQNVD--RAMAKLQGEGLSVAGIVCHVGKAEDREQLVaKALEHCG 112
Cdd:PLN02686  52 EARLVCVTGGVSFLGLAIVDRLLRHGYSVRIAVDTQEDKEklREMEMFGEMGRSNDGIWTVMANLTEPESLH-EAFDGCA 130


                 ..
gi 33667109  113 GV 114
Cdd:PLN02686 131 GV 132
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 40-219 5.20e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 37.49  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109   40 VVTGSTSGIGFAIARRLArdGAHVVIS---SRKQQNVDramaklqgeglsvagivchVGKAEDREQLVAKAlehcGGVDF 116
Cdd:PRK07578   4 LVIGASGTIGRAVVAELS--KRHEVITagrSSGDVQVD-------------------ITDPASIRALFEKV----GKVDA 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  117 LVCSAGV---NPLVGSTlgtSEQIWdkiLSVNVKspalLLSQL------LPYMeNRRGAVILVSSIAAYNPVVALGVYNV 187
Cdd:PRK07578  59 VVSAAGKvhfAPLAEMT---DEDFN---VGLQSK----LMGQVnlvligQHYL-NDGGSFTLTSGILSDEPIPGGASAAT 127

                        170       180       190
                 ....*....|....*....|....*....|..
gi 33667109  188 SKTALLGLTRTLALELaPKDIRVNCVVPGIIK 219
Cdd:PRK07578 128 VNGALEGFVKAAALEL-PRGIRINVVSPTVLT 158
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 37-122 6.63e-03

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 37.22  E-value: 6.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33667109  37 RVAVVtGSTSGIGFAIARRLARDGAHVVISSRKQQNVdramAKLQGEGLSVAgivchVGKAEDREQLVAKalehCGGVDF 116
Cdd:cd05243   1 KVLVV-GATGKVGRHVVRELLDRGYQVRALVRDPSQA----EKLEAAGAEVV-----VGDLTDAESLAAA----LEGIDA 66


                ....*.
gi 33667109 117 LVCSAG 122
Cdd:cd05243  67 VISAAG 72
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 39-68 7.05e-03

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: 37.92  E-value: 7.05e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 33667109  39 AVVTGSTSGIGFAIARRLARDGA-HVVISSR 68
Cdd:cd08952 233 VLVTGGTGALGAHVARWLARRGAeHLVLTSR 263
 
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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