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Conserved domains on  [gi|4504503|ref|NP_002144|]
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17-beta-hydroxysteroid dehydrogenase type 2 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176849)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; 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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0051287|GO:0016491
PubMed:  12604210|19011748|19027726|20423462|19011750

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 83-362 1.84e-169

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: 474.46  E-value: 1.84e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLW 162
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMF 242
Cdd:cd09805  81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  243 SSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYILAQRNFLLLINSLASKDFSPVL 322
Cdd:cd09805 161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4504503  323 RDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYF 362
Cdd:cd09805 241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFL 280
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 83-362 1.84e-169

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: 474.46  E-value: 1.84e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLW 162
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMF 242
Cdd:cd09805  81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  243 SSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYILAQRNFLLLINSLASKDFSPVL 322
Cdd:cd09805 161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4504503  323 RDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYF 362
Cdd:cd09805 241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFL 280
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 83-277 5.69e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 192.44  E-value: 5.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503     83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGP--GAEELRRtCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrG 160
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLeaVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    161 LWAVINNAGVLGFPTDGELLLMtDYKQCMAVNFFGTVEVTKTFLPLL-RKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:pfam00106  78 LDILVNNAGITGLGPFSELSDE-DWERVIDVNLTGVFNLTRAVLPAMiKGSGGRIVNISSVAGLVPYPGGSAYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 4504503    240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWE 277
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 81-290 3.76e-43

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: 150.33  E-value: 3.76e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrG 160
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAER--LEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--R 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:COG4221  80 LDVLVNNAGVALL---GPLEELDpeDWDRMIDVNVKGVLYVTRAALPAMRARGsGHIVNISSIAGLRPYPGGAVYAATKA 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4504503  238 AVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTS----DKWEKLEKDILDHLPAE 290
Cdd:COG4221 157 AVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVfdgdAEAAAAVYEGLEPLTPE 213
PRK06914 PRK06914
SDR family oxidoreductase;
82-367 1.63e-35

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 131.30  E-value: 1.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELR-----RTCSPRLSVLQMDITKPVQIKDAYSKVAAML 156
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEK--QENLLsqatqLNLQQNIKVQQLDVTDQNSIHNFQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDRGLwavINNAG--VLGFPTDgelLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYG 233
Cdd:PRK06914  81 RIDLL---VNNAGyaNGGFVEE---IPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSPYV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   234 SSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIagtsdkWEKLEKDildhlpAEVQEDYGQDYILAQRNFLLLINSL 313
Cdd:PRK06914 155 SSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNI------WEVGKQL------AENQSETTSPYKEYMKKIQKHINSG 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504503   314 ASKDFSP--VLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYFAKRHF 367
Cdd:PRK06914 223 SDTFGNPidVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRLWEYLVLKSL 278
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 164-263 1.67e-06

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: 48.76  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    164 VINNAGVLGFPTDGELLLmTDYKQCM---AVNFFGTVEVTKTFLPLLRKSKG---RLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:TIGR01500  91 LINNAGTLGDVSKGFVDL-SDSTQVQnywALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSLCAIQPFKGWALYCAGKA 169

                          90       100
                  ....*....|....*....|....*.
gi 4504503    238 AVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:TIGR01500 170 ARDMLFQVLALEEKNPNVRVLNYAPG 195
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 83-362 1.84e-169

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: 474.46  E-value: 1.84e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLW 162
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMF 242
Cdd:cd09805  81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  243 SSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYILAQRNFLLLINSLASKDFSPVL 322
Cdd:cd09805 161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKKLWERLPPEVKKDYGEDYIDELKNKMLKYCSRASPDLSPVI 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4504503  323 RDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYF 362
Cdd:cd09805 241 DSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFL 280
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 83-277 5.69e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 192.44  E-value: 5.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503     83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGP--GAEELRRtCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrG 160
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLeaVAKELGA-LGGKALFIQGDVTDRAQVKALVEQAVERLG--R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    161 LWAVINNAGVLGFPTDGELLLMtDYKQCMAVNFFGTVEVTKTFLPLL-RKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:pfam00106  78 LDILVNNAGITGLGPFSELSDE-DWERVIDVNLTGVFNLTRAVLPAMiKGSGGRIVNISSVAGLVPYPGGSAYSASKAAV 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 4504503    240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWE 277
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 83-345 2.44e-52

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: 174.73  E-value: 2.44e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNengPGA-EELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAmlQDRGL 161
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATARN---PDKlESLGELLNDNLEVLELDVTDEESIKAAVKEVIE--RFGRI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVLGF-PTdgELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:cd05374  76 DVLVNNAGYGLFgPL--EETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFLGPYCASKAAL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWeklekdildHLPAEVQEDYGQDYILAQRNFLLLINSLASKDfs 319
Cdd:cd05374 154 EALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGS---------ALEDPEISPYAPERKEIKENAAGVGSNPGDPE-- 222

                       250       260
                ....*....|....*....|....*.
gi 4504503  320 PVLRDIQHAILAKSPFAYYTPGKGAY 345
Cdd:cd05374 223 KVADVIVKALTSESPPLRYFLGSDAL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 81-290 3.76e-43

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: 150.33  E-value: 3.76e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrG 160
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAER--LEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--R 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:COG4221  80 LDVLVNNAGVALL---GPLEELDpeDWDRMIDVNVKGVLYVTRAALPAMRARGsGHIVNISSIAGLRPYPGGAVYAATKA 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4504503  238 AVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTS----DKWEKLEKDILDHLPAE 290
Cdd:COG4221 157 AVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVfdgdAEAAAAVYEGLEPLTPE 213
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
81-274 4.62e-43

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 150.40  E-value: 4.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngPGAEELRRTCS---PRLSVLQMDITKPVQIKDAYSKVAAmlQ 157
Cdd:COG0300   4 TGKTVLITGASSGIGRALARALAARGARVVLVARDA--ERLEALAAELRaagARVEVVALDVTDPDAVAALAEAVLA--R 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 DRGLWAVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGS 234
Cdd:COG0300  80 FGPIDVLVNNAGVGGG---GPFEELDleDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAA 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4504503  235 SKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSD 274
Cdd:COG0300 157 SKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAG 196
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 85-289 8.98e-38

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: 135.87  E-value: 8.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrGLWAV 164
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  165 INNAGVLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKAAVTMFS 243
Cdd:cd05233  79 VNNAGIARPGPLEELTD-EDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGQAAYAASKAALEGLT 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4504503  244 SVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKlEKDILDHLPA 289
Cdd:cd05233 158 RSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEA-EKELAAAIPL 202
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 81-289 1.91e-36

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: 132.99  E-value: 1.91e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngPGAEELRRTCS---PRLSVLQMDITKPVQIKDAYSKVAAMLq 157
Cdd:COG1028   5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDA--EALEAAAAELRaagGRALAVAADVTDEAAVEALVAAAVAAF- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 dRGLWAVINNAGVLGfptDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGS 234
Cdd:COG1028  82 -GRLDILVNNAGITP---PGPLEELTeeDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAA 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504503  235 SKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPA 289
Cdd:COG1028 158 SKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPL 212
PRK06914 PRK06914
SDR family oxidoreductase;
82-367 1.63e-35

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 131.30  E-value: 1.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELR-----RTCSPRLSVLQMDITKPVQIKDAYSKVAAML 156
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEK--QENLLsqatqLNLQQNIKVQQLDVTDQNSIHNFQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDRGLwavINNAG--VLGFPTDgelLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYG 233
Cdd:PRK06914  81 RIDLL---VNNAGyaNGGFVEE---IPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSPYV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   234 SSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIagtsdkWEKLEKDildhlpAEVQEDYGQDYILAQRNFLLLINSL 313
Cdd:PRK06914 155 SSKYALEGFSESLRLELKPFGIDVALIEPGSYNTNI------WEVGKQL------AENQSETTSPYKEYMKKIQKHINSG 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504503   314 ASKDFSP--VLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYFAKRHF 367
Cdd:PRK06914 223 SDTFGNPidVANLIVEIAESKRPKLRYPIGKGVKLMILAKKILPWRLWEYLVLKSL 278
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 83-263 4.71e-35

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: 128.51  E-value: 4.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGF-TVFAGVLNEN-GPGA-EELRRT-CSPRlsVLQMDITKPVQIKDAYSKVAAmlQD 158
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVErGQAAvEKLRAEgLSVR--FHQLDVTDDASIEAAADFVEE--KY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 RGLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGgapmeRLAS-YGSSK 236
Cdd:cd05324  77 GGLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLG-----SLTSaYGVSK 151

                       170       180
                ....*....|....*....|....*..
gi 4504503  237 AAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05324 152 AALNALTRILAKELKETGIKVNACCPG 178
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 85-263 6.64e-31

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: 117.78  E-value: 6.64e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELG-FTVFAGVLNENGpgAEELR--RTCSPRLSVLQMDITKPvqIKDAYSKVAAMLQDRGL 161
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSA--ATELAalGASHSRLHILELDVTDE--IAESAEAVAERLGDAGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSS-MGGGAPMER--LASYGSSKA 237
Cdd:cd05325  77 DVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGArAKIINISSrVGSIGDNTSggWYSYRASKA 156

                       170       180
                ....*....|....*....|....*.
gi 4504503  238 AVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05325 157 ALNMLTKSLAVELKRDGITVVSLHPG 182
PRK06182 PRK06182
short chain dehydrogenase; Validated
 82-368 5.22e-29

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 113.52  E-value: 5.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNengpgAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRGL 161
Cdd:PRK06182   3 KKVALVTGASSGIGKATARRLAAQGYTVYGAARR-----VDKMEDLASLGVHPLSLDVTDEASIKAA---VDTIIAEEGR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 WAV-INNAGvlgFPTDG--ELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGG--APMErlASYGSS 235
Cdd:PRK06182  75 IDVlVNNAG---YGSYGaiEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKiyTPLG--AWYHAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDkweklekdilDHLpAEVQED--YGQdyiLAQRNFLLLINSL 313
Cdd:PRK06182 150 KFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAA----------DHL-LKTSGNgaYAE---QAQAVAASMRSTY 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504503   314 ASKDFSP---VLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYFAKRHFG 368
Cdd:PRK06182 216 GSGRLSDpsvIADAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLIMSATR 273
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 83-280 2.09e-28

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: 111.24  E-value: 2.09e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRT-CSPRLSVLQMDITKPVQIKDAYSKVaamLQDRG- 160
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAInPKVKATFVQCDVTSWEQLAAAFKKA---IEKFGr 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVLGFPTDGEL-LLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK----GRLVNVSSMGGGAPMERLASYGSS 235
Cdd:cd05323  78 VDILINNAGILDEKSYLFAgKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQFPVYSAS 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4504503  236 KAAVTMFSSVMRLEL-SKWGIKVASIQPGGFLTNIAGTSDKWEKLE 280
Cdd:cd05323 158 KHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEM 203
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 81-273 2.23e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 106.54  E-value: 2.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG 160
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAA--RADFEALHPDRALARLLDVTDFDAIDAV---VADAEATFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 -LWAVINNAGV--LGFPTDGELLLMTdyKQcMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK06180  78 pIDVLVNNAGYghEGAIEESPLAEMR--RQ-FEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGIGYYCGSK 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTS 273
Cdd:PRK06180 155 FALEGISESLAKEVAPFGIHVTAVEPGSFRTDWAGRS 191
PRK08264 PRK08264
SDR family oxidoreductase;
83-263 6.83e-26

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 104.20  E-value: 6.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELG-FTVFAGVLNengPGAEELRrtcSPRLSVLQMDITKPVQIKDAyskvAAMLQDRGL 161
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLARGaAKVYAAARD---PESVTDL---GPRVVPLQLDVTDPASVAAA----AEAASDVTI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 waVINNAGVLgfpTDGELLL---MTDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:PRK08264  77 --LVNNAGIF---RTGSLLLegdEDALRAEMETNYFGPLAMARAFAPVLAANgGGAIVNVLSVLSWVNFPNLGTYSASKA 151

                        170       180
                 ....*....|....*....|....*.
gi 4504503   238 AVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK08264 152 AAWSLTQALRAELAPQGTRVLGVHPG 177
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 85-263 1.70e-25

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: 103.48  E-value: 1.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRTC---SPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGL 161
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKVV--ILDINEKGAEETANNVrkaGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 waVINNAGVlgfPTDGELLLMTD--YKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:cd05339  80 --LINNAGV---VSGKKLLELPDeeIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLADYCASKAA 154

                       170       180
                ....*....|....*....|....*...
gi 4504503  239 VTMFSSVMRLEL---SKWGIKVASIQPG 263
Cdd:cd05339 155 AVGFHESLRLELkayGKPGIKTTLVCPY 182
PRK05650 PRK05650
SDR family oxidoreductase;
85-305 6.65e-25

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 102.43  E-value: 6.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    85 VLVTGGDCGLGHALCKYLDELGFTV-FAGVLNENGPGAEELRRTCSPRLSVLQMDITKpvqikdaYSKVAAMLQD----- 158
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLaLADVNEEGGEETLKLLREAGGDGFYQRCDVRD-------YSQLTALAQAceekw 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RGLWAVINNAGVL--GFPTDGELLlmtDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSS 235
Cdd:PRK05650  76 GGIDVIVNNAGVAsgGFFEELSLE---DWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIA----GTSDKWEK-----LEK------DILDHLPAEVQEdyGQDYI 300
Cdd:PRK05650 153 KAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLdsfrGPNPAMKAqvgklLEKspitaaDIADYIYQQVAK--GEFLI 230


                 ....*
gi 4504503   301 LAQRN 305
Cdd:PRK05650 231 LPHEQ 235
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 80-274 7.33e-25

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: 101.33  E-value: 7.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   80 VDQKAVLVTGGDCGLGHALCKYLDELGFT-VFAGVLNENGpgAEELRRTCSPRLSVLQMDITKPVQIKDAyskvAAMLQD 158
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGS--AAHLVAKYGDKVVPLRLDVTDPESIKAA----AAQAKD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 rgLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:cd05354  75 --VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANgGGAIVNLNSVASLKNFPAMGTYSASKS 152

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4504503  238 AVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSD 274
Cdd:cd05354 153 AAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAG 189
PRK05993 PRK05993
SDR family oxidoreductase;
81-360 9.21e-25

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 102.03  E-value: 9.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngpgaEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRg 160
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKE-----EDVAALEAEGLEAFQLDYAEPESIAALVAQVLELSGGR- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNaGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:PRK05993  77 LDALFNN-GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGqGRIVQCSSILGLVPMKYRGAYNASKFAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWekLEKDI-LDHLPAevQEDYgqdyiLAQRNFLLLINSLASKDF 318
Cdd:PRK05993 156 EGLSLTLRMELQGSGIHVSLIEPGPIETRFRANALAA--FKRWIdIENSVH--RAAY-----QQQMARLEGGGSKSRFKL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 4504503   319 SP--VLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYD 360
Cdd:PRK05993 227 GPeaVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLY 270
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
83-295 1.30e-24

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 101.00  E-value: 1.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELR---RTCSPRLSVLQMDITKPVQIKDAYSKVAAmlQDR 159
Cdd:PRK05653   6 KTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEA--AEALAaelRAAGGEARVLVFDVSDEAAVRALIEAAVE--AFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGVLGfptDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK05653  82 ALDILVNNAGITR---DALLPRMSeeDWDRVIDVNLTGTFNVVRAALPPMIKArYGRIVNISSVSGVTGNPGQTNYSAAK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPGgfltNIagtsdkweklEKDILDHLPAEVQEDY 295
Cdd:PRK05653 159 AGVIGFTKALALELASRGITVNAVAPG----FI----------DTDMTEGLPEEVKAEI 203
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 83-289 7.99e-24

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: 98.97  E-value: 7.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVF-AGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG- 160
Cdd:cd05347   6 KVALVTGASRGIGFGIASGLAEAGANIViNSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAA---VEAIEEDFGk 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGvLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:cd05347  83 IDILVNNAG-IIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGhGKIINICSLLSELGGPPVPAYAASKGGV 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4504503  240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPA 289
Cdd:cd05347 162 AGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRIPA 211
PRK05693 PRK05693
SDR family oxidoreductase;
82-373 2.97e-23

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 97.94  E-value: 2.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNengpgAEELRRTCSPRLSVLQMDITKPvqikDAYSKVAAMLQDR-- 159
Cdd:PRK05693   1 MPVVLITGCSSGIGRALADAFKAAGYEVWATARK-----AEDVEALAAAGFTAVQLDVNDG----AALARLAEELEAEhg 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAG--VLGFPTDGELLLMtdyKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:PRK05693  72 GLDVLINNAGygAMGPLLDGGVEAM---RRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   238 AVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGT-SDKWEKLekdildhLPAEVQEDYGQDYILAQrnflllinSLASK 316
Cdd:PRK05693 149 AVHALSDALRLELAPFGVQVMEVQPGAIASQFASNaSREAEQL-------LAEQSPWWPLREHIQAR--------ARASQ 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504503   317 D----FSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYFAKRHFGQDKPM 373
Cdd:PRK05693 214 DnptpAAEFARQLLAAVQQSPRPRLVRLGNGSRALPLLARLLPRGLLDRVLRKRFGLLRPL 274
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 82-295 7.77e-23

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 96.03  E-value: 7.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTV-FAGVLNEngPGAEELRRTCSP---RLSVLQMDITKPVQIKDAYSKVAAMLQ 157
Cdd:PRK05557   5 GKVALVTGASRGIGRAIAERLAAQGANVvINYASSE--AGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 drGLWAVINNAGVLgfpTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGS 234
Cdd:PRK05557  83 --GVDILVNNAGIT---RDNLLMRMKeeDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQANYAA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504503   235 SKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTniagtsdkweklekDILDHLPAEVQEDY 295
Cdd:PRK05557 158 SKAGVIGFTKSLARELASRGITVNAVAPGFIET--------------DMTDALPEDVKEAI 204
PRK09291 PRK09291
SDR family oxidoreductase;
82-286 1.25e-22

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 95.84  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVlnENGPGAEELRR---TCSPRLSVLQMDITKPVQIKDAYSkvaamlqd 158
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAGV--QIAPQVTALRAeaaRRGLALRVEKLDLTDAIDRAQAAE-------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 rglWAV---INNAGVlgfptdGELLLMTD-----YKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERL 229
Cdd:PRK09291  72 ---WDVdvlLNNAGI------GEAGAVVDipvelVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSMAGLITGPFT 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504503   230 ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT----NIAGTSDKWEKLEKDILDH 286
Cdd:PRK09291 143 GAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTgfndTMAETPKRWYDPARNFTDP 203
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 80-267 1.38e-22

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: 95.53  E-value: 1.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   80 VDQKAVLVTGGDCGLGHALCKYL-DELGFTVFAGVLNENGPG-AEELRRtcspRLSVLQMDITKPVQIKDAyskVAAMLQ 157
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLvAEGAKVVLSDILDEEGQAaAAELGD----AARFFHLDVTDEDGWTAV---VDTARE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 DRG-LWAVINNAGVL--GFPTDGELllmTDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYG 233
Cdd:cd05341  76 AFGrLDVLVNNAGILtgGTVETTTL---EEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYN 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4504503  234 SSKAAVTMFSSVMRLELSK--WGIKVASIQPGGFLT 267
Cdd:cd05341 153 ASKGAVRGLTKSAALECATqgYGIRVNSVHPGYIYT 188
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 85-257 1.67e-22

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: 95.23  E-value: 1.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGvlnenGPGAEELRRTCS--PRLSVLQMDITKPVQIKDAYSKVAAMLQDrgLW 162
Cdd:COG3967   8 ILITGGTSGIGLALAKRLHARGNTVIIT-----GRREEKLEEAAAanPGLHTIVLDVADPASIAALAEQVTAEFPD--LN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLGFP--TDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLR-KSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:COG3967  81 VLINNAGIMRAEdlLDEAEDL-ADAEREITTNLLGPIRLTAAFLPHLKaQPEAAIVNVSSGLAFVPLAVTPTYSATKAAL 159

                       170
                ....*....|....*...
gi 4504503  240 TMFSSVMRLELSKWGIKV 257
Cdd:COG3967 160 HSYTQSLRHQLKDTSVKV 177
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 85-273 3.90e-22

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: 94.07  E-value: 3.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEelrrtcSPRLSVLQMDITKPVQIKDAYSKVAAmlQDRGLWAV 164
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEY------GDPLRLTPLDVADAAAVREVCSRLLA--EHGPIDAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  165 INNAGVLGF-PTDGelLLMTDYKQCMAVNFFGTVEVTKTFLPLLR-KSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMF 242
Cdd:cd05331  73 VNCAGVLRPgATDP--LSTEDWEQTFAVNVTGVFNLLQAVAPHMKdRRTGAIVTVASNAAHVPRISMAAYGASKAALASL 150

                       170       180       190
                ....*....|....*....|....*....|.
gi 4504503  243 SSVMRLELSKWGIKVASIQPGGFLTNIAGTS 273
Cdd:cd05331 151 SKCLGLELAPYGVRCNVVSPGSTDTAMQRTL 181
PRK12826 PRK12826
SDR family oxidoreductase;
79-271 5.87e-22

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 93.83  E-value: 5.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVFA-GVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQ 157
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVvDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAA---VAAGVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 DRG-LWAVINNAGVlgFPtDGELLLMTD--YKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGG-GAPMERLASY 232
Cdd:PRK12826  80 DFGrLDILVANAGI--FP-LTPFAEMDDeqWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGpRVGYPGLAHY 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAG 271
Cdd:PRK12826 157 AASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAG 195
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 83-290 5.88e-22

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: 93.80  E-value: 5.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVL---NENGpgAEELRRTC----SPRLSVLQMDITKPVQIKDAYSKVAAM 155
Cdd:cd05332   4 KVVIITGASSGIGEELAYHLARLGARL---VLsarREER--LEEVKSEClelgAPSPHVVPLDMSDLEDAEQVVEEALKL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  156 LqdRGLWAVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGG--GAPMErlASY 232
Cdd:cd05332  79 F--GGLDILINNAGI-SMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPhLIERSQGSIVVVSSIAGkiGVPFR--TAY 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504503  233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIA-----GTSDKWEKLEKDILDHLPAE 290
Cdd:cd05332 154 AASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAmnalsGDGSMSAKMDDTTANGMSPE 216
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 83-263 1.06e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 93.11  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngPGAEELRRTCSP---RLSVLQMDITKPVQIKDAYSKVAAMLQdr 159
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLA--AEARELAAALEAaggRAHAIAADLADPASVQRFFDAAAAALG-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGVLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:PRK12939  84 GLDGLVNNAGITNSKSATELDI-DTWDAVMNVNVRGTFLMLRAALPHLRDSGrGRIVNLASDTALWGAPKLGAYVASKGA 162

                        170       180
                 ....*....|....*....|....*
gi 4504503   239 VTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12939 163 VIGMTRSLARELGGRGITVNAIAPG 187
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 83-274 2.50e-21

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: 92.09  E-value: 2.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAgvlneNGPGAEELRRTcspRLSVLQM------------DITKPVQIKDAYS 150
Cdd:cd05364   4 KVAIITGSSSGIGAGTAILFARLGARLAL-----TGRDAERLEET---RQSCLQAgvsekkillvvaDLTEEEGQDRIIS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  151 KVAAMLQDrgLWAVINNAGVLGfPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLA 230
Cdd:cd05364  76 TTLAKFGR--LDILVNNAGILA-KGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4504503  231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI---AGTSD 274
Cdd:cd05364 153 YYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFhrrMGMPE 199
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 83-287 3.54e-21

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: 91.46  E-value: 3.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAE-ELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrGL 161
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETvEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVlgfpT-DGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGG--GAPMErlASYGSS 235
Cdd:cd05333  79 DILVNNAGI----TrDNLLMRMSeeDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGliGNPGQ--ANYAAS 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 4504503  236 KAAVTMFSSVMRLELSKWGIKVASIQPgGFLtniagTSDKWEKLEKDILDHL 287
Cdd:cd05333 153 KAGVIGFTKSLAKELASRGITVNAVAP-GFI-----DTDMTDALPEKVKEKI 198
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 83-263 9.21e-21

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: 90.42  E-value: 9.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVF-----AGVLNENgpgAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQ 157
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLIltgrrAERLQEL---ADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 DrgLWAVINNAG-VLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSS 235
Cdd:cd05346  78 D--IDILVNNAGlALGLDPAQEADL-EDWETMIDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNVYCAT 154

                       170       180
                ....*....|....*....|....*...
gi 4504503  236 KAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05346 155 KAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 79-263 1.69e-20

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 89.54  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVfAGVLNENGPGAEELRRT---CSPRLSVLQMDITKPVQIKDAyskVAAM 155
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADV-VVHYRSDEEAAEELVEAveaLGRRAQAVQADVTDKAALEAA---VAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQDRG-LWAVINNAGVLGfptDGELLLMTD--YKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLAS 231
Cdd:PRK12825  79 VERFGrIDILVNNAGIFE---DKPLADMSDdeWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSN 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504503   232 YGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12825 156 YAAAKAGLVGLTKALARELAEYGITVNMVAPG 187
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 83-277 2.66e-20

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 88.99  E-value: 2.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENG----PGAEELRrtcsPRLSVLQMDITKPVQIKDAYSKVAamLQD 158
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIaekvAEAAQGG----PRALGVQCDVTSEAQVQSAFEQAV--LEF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 RGLWAVINNAGVLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:cd08943  76 GGLDIVVSNAGIATSSPIAETSL-EDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAK 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4504503  237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWE 277
Cdd:cd08943 155 AAEAHLARCLALEGGEDGIRVNTVNPDAVFRGSKIWEGVWR 195
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 93-288 4.04e-20

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: 88.26  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503     93 GLGHALCKYLDELGFTV-FAGVLNENGPGAEELRRTCSPRlsVLQMDITKPVQIKDAYSKVAAmlQDRGLWAVINNAGVL 171
Cdd:pfam13561   7 GIGWAIARALAEEGAEVvLTDLNEALAKRVEELAEELGAA--VLPCDVTDEEQVEALVAAAVE--KFGRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    172 GfPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKsKGRLVNVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLE 249
Cdd:pfam13561  83 P-KLKGPFLDTSreDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 4504503    250 LSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLP 288
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAP 199
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 85-263 6.75e-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: 6.75e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSV--LQMDITKPVQIKdaySKVAAMLQDRG-L 161
Cdd:cd05367   2 IILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPGLRVttVKADLSDAAGVE---QLLEAIRKLDGeR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKS--KGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:cd05367  79 DLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRglKKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158

                       170       180
                ....*....|....*....|....
gi 4504503  240 TMFSSVMRLELSkwGIKVASIQPG 263
Cdd:cd05367 159 DMFFRVLAAEEP--DVRVLSYAPG 180
FabG-like PRK07231
SDR family oxidoreductase;
83-263 1.20e-19

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 87.19  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENG--PGAEELRRtcSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG 160
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAaeRVAAEILA--GGRAIAVAADVSDEADVEAA---VAAALERFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 -LWAVINNAGVlgFPTDGELLLMT--DYKQCMAVN----FFGTVEVTKTFLpllRKSKGRLVNVSSMGGGAPMERLASYG 233
Cdd:PRK07231  81 sVDILVNNAGT--THRNGPLLDVDeaEFDRIFAVNvkspYLWTQAAVPAMR---GEGGGAIVNVASTAGLRPRPGLGWYN 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 4504503   234 SSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK07231 156 ASKGAVITLTKALAAELGPDKIRVNAVAPV 185
PRK06181 PRK06181
SDR family oxidoreductase;
83-269 1.65e-19

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 87.34  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPG--AEELRRTCSPRLsVLQMDITKPVQIKDAyskVAAMLQDRG 160
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLAslAQELADHGGEAL-VVPTDVSDAEACERL---IEAAVARFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 -LWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:PRK06181  78 gIDILVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHAL 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 4504503   240 TMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATDI 187
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 83-262 1.66e-19

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: 86.21  E-value: 1.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGvlnenGPGAEELRRTCS--PRLSVLQMDITKPVQIKDAYSKVaaMLQDRG 160
Cdd:cd05370   6 NTVLITGGTSGIGLALARKFLEAGNTVIIT-----GRREERLAEAKKelPNIHTIVLDVGDAESVEALAEAL--LSEYPN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVlGFP---TDGELLLmTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:cd05370  79 LDILINNAGI-QRPidlRDPASDL-DKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLAFVPMAANPVYCATK 156

                       170       180
                ....*....|....*....|....*.
gi 4504503  237 AAVTMFSSVMRLELSKWGIKVASIQP 262
Cdd:cd05370 157 AALHSYTLALRHQLKDTGVEVVEIVP 182
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 81-288 2.69e-19

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: 86.28  E-value: 2.69e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENG--PGAEELR---RTCSPRLSVLQMDITKPVQIKDAYSKVAAM 155
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGANV---VVNYRSkeDAAEEVVeeiKAVGGKAIAVQADVSKEEDVVALFQSAIKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  156 LQdrGLWAVINNAGVLGFPTDGELLLmTDYKQCMAVN----FFGTVEVTKTFLPllRKSKGRLVNVSSMGGGAPMERLAS 231
Cdd:cd05358  79 FG--TLDILVNNAGLQGDASSHEMTL-EDWNKVIDVNltgqFLCAREAIKRFRK--SKIKGKIINMSSVHEKIPWPGHVN 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504503  232 YGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIagTSDKWEKLE--KDILDHLP 288
Cdd:cd05358 154 YAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPI--NAEAWDDPEqrADLLSLIP 210
PRK08017 PRK08017
SDR family oxidoreductase;
82-275 2.76e-19

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 86.29  E-value: 2.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNengpgAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRgL 161
Cdd:PRK08017   2 QKSVLITGCSSGIGLEAALELKRRGYRVLAACRK-----PDDVARMNSLGFTGILLDLDDPESVERAADEVIALTDNR-L 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 WAVINNAGvlgFPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:PRK08017  76 YGLFNNAG---FGVYGPLSTISrqQMEQQFSTNFFGTHQLTMLLLPAMLPHgEGRIVMTSSVMGLISTPGRGAYAASKYA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4504503   239 VTMFSSVMRLELSKWGIKVASIQPG----GFLTNIAGT-SDK 275
Cdd:PRK08017 153 LEAWSDALRMELRHSGIKVSLIEPGpirtRFTDNVNQTqSDK 194
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 164-298 2.94e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 86.63  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   164 VINNAG--VLGFPtdgELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGSSKAAVT 240
Cdd:PRK08263  81 VVNNAGygLFGMI---EEVTESEARAQIDTNFFGALWVTQAVLPYLREQrSGHIIQISSIGGISAFPMSGIYHASKWALE 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504503   241 MFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKlEKDILDHLPAEVQEDYGQD 298
Cdd:PRK08263 158 GMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSAKRAT-PLDAYDTLREELAEQWSER 214
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 85-263 2.96e-19

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: 86.12  E-value: 2.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNEN--GPGAEELRRTCSPRLSVLQMDITKpvqIKDAYSKVAAMLQDRGLW 162
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEklDAVAKEIEEKYGVETKTIAADFSA---GDDIYERIEKELEGLDIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVlgFPTDGELLLMTD---YKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:cd05356  81 ILVNNVGI--SHSIPEYFLETPedeLQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIPTPLLATYSASKAF 158

                       170       180
                ....*....|....*....|....*
gi 4504503  239 VTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05356 159 LDFFSRALYEEYKSQGIDVQSLLPY 183
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 83-277 3.14e-19

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: 86.23  E-value: 3.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTV--FAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAamlQDRG 160
Cdd:cd05352   9 KVAIVTGGSRGIGLAIARALAEAGADVaiIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQ---KDFG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 -LWAVINNAGVlgfPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGG---GAPMERlASYG 233
Cdd:cd05352  86 kIDILIANAGI---TVHKPALDYTyeQWNKVIDVNLNGVFNCAQAAAKIFKKQgKGSLIITASMSGtivNRPQPQ-AAYN 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 4504503  234 SSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAG-----TSDKWE 277
Cdd:cd05352 162 ASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDfvdkeLRKKWE 210
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 83-283 3.59e-19

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: 85.25  E-value: 3.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSVLQMDITkpvQIKDAYSKVAAMLQDRG-L 161
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRV--GICARDEARLAAAAAQELEGVLGLAGDVR---DEADVRRAVDAMEEAFGgL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTM 241
Cdd:cd08929  76 DALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLG 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4504503  242 FSSVMRLELSKWGIKVASIQPGGFLTNIAGTS--DKWEKLEKDI 283
Cdd:cd08929 156 LSEAAMLDLREANIRVVNVMPGSVDTGFAGSPegQAWKLAPEDV 199
PRK07326 PRK07326
SDR family oxidoreductase;
83-283 4.67e-19

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 85.45  E-value: 4.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSV--LQMDITKPVQIKDAyskVAAMLQDRG 160
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLAEGYKV--AITARDQKELEEAAAELNNKGNVlgLAADVRDEADVQRA---VDAIVAAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 -LWAVINNAGVLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:PRK07326  82 gLDVLIANAGVGHFAPVEELTP-EEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4504503   240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTS----DKWEKLEKDI 283
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTpsekDAWKIQPEDI 208
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-282 5.34e-19

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 85.61  E-value: 5.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAgVLNENGPGAEELRRTCSprlSVLQMDITKPVQIKDAYSKVAAMLqdRGLW 162
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLREGAKVAV-LYNSAENEAKELREKGV---FTIKCDVGNRDQVKKSKEVVEKEF--GRVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 AVINNAGVLgfptdgelLLM-------TDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGG-GAPMERLASYG 233
Cdd:PRK06463  82 VLVNNAGIM--------YLMpfeefdeEKYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNAGiGTAAEGTTFYA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4504503   234 SSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN--IAG-TSDKWEKLEKD 282
Cdd:PRK06463 154 ITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDmtLSGkSQEEAEKLREL 205
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 83-283 1.43e-18

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: 84.25  E-value: 1.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVLNenGPGAEELRRTCS----PRLSVL--QMDITKPVQIKDAYSKVAAML 156
Cdd:cd05344   2 KVALVTAASSGIGLAIARALAREGARV---AIC--ARNRENLERAASelraGGAGVLavVADLTDPEDIDRLVEKAGDAF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  157 QdrGLWAVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSS 235
Cdd:cd05344  77 G--RVDILVNNAGG-PPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNVA 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 4504503  236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTniagtsDKWEKLEKDI 283
Cdd:cd05344 154 RAGLIGLVKTLSRELAPDGVTVNSVLPGYIDT------ERVRRLLEAR 195
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 83-263 1.66e-18

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: 83.57  E-value: 1.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRtcsPRLSVLQMDITKPVQikdaYSKVAAMLQDR--G 160
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASG---GDVEAVPYDARDPED----ARALVDALRDRfgR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVLGfPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:cd08932  74 IDVLVHNAGIGR-PTTLREGSDAELEAHFSINVIAPAELTRALLPALREAgSGRVVFLNSLSGKRVLAGNAGYSASKFAL 152

                       170       180
                ....*....|....*....|....
gi 4504503  240 TMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd08932 153 RALAHALRQEGWDHGVRVSAVCPG 176
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 83-263 4.24e-18

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 83.01  E-value: 4.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEelrrtcspRLSVLQMDITKPVQIKDAyskVAAMLQDRGLW 162
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDY--------PFATFVLDVSDAAAVAQV---CQRLLAETGPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 AV-INNAGVLGF-PTDGelLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:PRK08220  78 DVlVNAAGILRMgATDS--LSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRsGAIVTVGSNAAHVPRIGMAAYGASKAAL 155

                        170       180
                 ....*....|....*....|....
gi 4504503   240 TMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCNVVSPG 179
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 83-267 5.39e-18

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: 82.30  E-value: 5.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngpgaEELRRTC----------SPRLSVLQMDITKPVQIKDAYSKV 152
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSE-----SKLEEAVeeieaeanasGQKVSYISADLSDYEEVEQAFAQA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  153 AAMLQDRGLwaVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERL 229
Cdd:cd08939  77 VEKGGPPDL--VVNCAGISIP---GLFEDLTaeEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGY 151

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4504503  230 ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:cd08939 152 SAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
PRK06484 PRK06484
short chain dehydrogenase; Validated
 83-269 5.80e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 85.29  E-value: 5.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG-L 161
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVV--VADRNVERARERADSLGPDHHALAMDVSDEAQIREG---FEQLHREFGrI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 WAVINNAGVLGfPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:PRK06484  81 DVLVNNAGVTD-PTMTATLDTTleEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKRTAYSASKA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504503   238 AVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK06484 160 AVISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 83-267 8.09e-18

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: 81.94  E-value: 8.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVLN--ENGPGAEELRRTCS---PRLSVLQMDITKPVQIKDAYSKVAAMLQ 157
Cdd:cd05362   4 KVALVTGASRGIGRAIAKRLARDGASV---VVNyaSSKAAAEEVVAEIEaagGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 drGLWAVINNAGVLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLRkSKGRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:cd05362  81 --GVDILVNNAGVMLKKPIAETSE-EEFDRMFTVNTKGAFFVLQEAAKRLR-DGGRIINISSSLTAAYTPNYGAYAGSKA 156

                       170       180       190
                ....*....|....*....|....*....|
gi 4504503  238 AVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:cd05362 157 AVEAFTRVLAKELGGRGITVNAVAPGPVDT 186
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 83-290 1.26e-17

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: 80.96  E-value: 1.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFtvFAGVLNENGPGAEELRRTCSP-RLSVLQMDITKPVQIKDAYSKVAAMLQDRgL 161
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGW--FVGLYDIDEDGLAALAAELGAeNVVAGALDVTDRAAWAAALADFAAATGGR-L 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVLGFP-----TDGELLLMTDykqcmaVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMGGGAPMERLASYGSS 235
Cdd:cd08931  78 DALFNNAGVGRGGpfedvPLAAHDRMVD------INVKGVLNGAYAALPYLKATPGaRVINTASSSAIYGQPDLAVYSAT 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504503  236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAE 290
Cdd:cd08931 152 KFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRVLPVS 206
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
83-291 1.52e-17

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 81.35  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVL--NENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG 160
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFsgNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEA---LAEIEEEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 -LWAVINNAGVlgfPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLR-KSKGRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK12824  80 pVDILVNNAGI---TRDSVFKRMShqEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQTNYSAAK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAgtsdkwEKLEKDILDHLPAEV 291
Cdd:PRK12824 157 AGMIGFTKALASEGARYGITVNCIAPGYIATPMV------EQMGPEVLQSIVNQI 205
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 82-263 2.28e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 81.10  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAeelrrtcSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG- 160
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAP-------IPGVELLELDVTDDASVQAA---VDEVIARAGr 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRK-SKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:PRK06179  74 IDVLVNNAGV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAqGSGRIINISSVLGFLPAPYMALYAASKHAV 152

                        170       180
                 ....*....|....*....|....
gi 4504503   240 TMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06179 153 EGYSESLDHEVRQFGIRVSLVEPA 176
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 75-263 2.57e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 80.87  E-value: 2.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    75 QELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGPGAEELRRTCSPRLSVL--QMDITKPVQIKDAYSKV 152
Cdd:PRK12829   4 DLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARV---HVCDVSEAALAATAARLPGAKVTatVADVADPAQVERVFDTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   153 AAMLQdrGLWAVINNAGVlgFPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGG--GAPM 226
Cdd:PRK12829  81 VERFG--GLDVLVNNAGI--AGPTGGIDEITpeQWEQTLAVNLNGQFYFARAAVPLLKASGhgGVIIALSSVAGrlGYPG 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504503   227 erLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12829 157 --RTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPG 191
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 85-263 2.61e-17

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: 80.45  E-value: 2.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNEN---GPGAEELRRTCSPRLSVLqmDITKPVQIKDAYSKVAAMLQdrGL 161
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDrldELKAELLNPNPSVEVEIL--DVTDEERNQLVIAELEAELG--GL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLR-KSKGRLVNVSSMGGGAPMERLASYGSSKAAVT 240
Cdd:cd05350  77 DLVIINAGV-GKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRaKGRGHLVLISSVAALRGLPGAAAYSASKAALS 155

                       170       180
                ....*....|....*....|...
gi 4504503  241 MFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05350 156 SLAESLRYDVKKRGIRVTVINPG 178
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 83-285 2.65e-17

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: 81.04  E-value: 2.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGF-TVFAGVLNENGPGAE-ELRRTCSPRLSVLQMDITKPVQIKDAYSKVaamLQDRG 160
Cdd:cd08933  10 KVVIVTGGSRGIGRGIVRAFVENGAkVVFCARGEAAGQALEsELNRAGPGSCKFVPCDVTKEEDIKTLISVT---VERFG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 -LWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:cd08933  87 rIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAI 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4504503  240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIagtsdkWEKLEKDILD 285
Cdd:cd08933 167 TAMTKALAVDESRYGVRVNCISPGNIWTPL------WEELAAQTPD 206
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 83-293 2.95e-17

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: 80.59  E-value: 2.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAgvLNENGPGAEELRRTCsPRLSVLQMDITKPVQIKDAYSKVAAMlqdRGLw 162
Cdd:cd05351   8 KRALVTGAGKGIGRATVKALAKAGARVVA--VSRTQADLDSLVREC-PGIEPVCVDLSDWDATEEALGSVGPV---DLL- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 avINNAGVLGFPTDGELLlMTDYKQCMAVNFFGTVEVTKTFLPLL--RKSKGRLVNVSSMGGGAPMERLASYGSSKAAVT 240
Cdd:cd05351  81 --VNNAAVAILQPFLEVT-KEAFDRSFDVNVRAVIHVSQIVARGMiaRGVPGSIVNVSSQASQRALTNHTVYCSTKAALD 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504503  241 MFSSVMRLELSKWGIKVASIQPGGFLTNIAgtSDKWEKLEKD--ILDHLP----AEVQE 293
Cdd:cd05351 158 MLTKVMALELGPHKIRVNSVNPTVVMTDMG--RDNWSDPEKAkkMLNRIPlgkfAEVED 214
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 83-270 3.74e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 80.14  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAgvLNENGPGAEELRRTCSPRlsVLQMDITKPVQIKDAYSKVAAmlqdrgLW 162
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVA--AARNAAALDRLAGETGCE--PLRLDVGDDAAIRAALAAAGA------FD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 AVINNAGVlgfpTDGELLL-MTD--YKQCMAVNFFGTVEVTKTFLPLlRKSKGR---LVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK07060  80 GLVNCAGI----ASLESALdMTAegFDRVMAVNARGAALVARHVARA-MIAAGRggsIVNVSSQAALVGLPDHLAYCASK 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIA 270
Cdd:PRK07060 155 AALDAITRVLCVELGPHGIRVNSVNPTVTLTPMA 188
PRK06484 PRK06484
short chain dehydrogenase; Validated
 81-267 4.13e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 82.59  E-value: 4.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDrg 160
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLL--IIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGR-- 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSkGRLVNVSSMGGGAPMERLASYGSSKAAVT 240
Cdd:PRK06484 344 LDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPRNAYCASKAAVT 422

                        170       180
                 ....*....|....*....|....*..
gi 4504503   241 MFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK06484 423 MLSRSLACEWAPAGIRVNTVAPGYIET 449
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 83-267 5.04e-17

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: 80.20  E-value: 5.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYL--DELG-FTVFAGV--LNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVaamlQ 157
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLasDPSKrFKVYATMrdLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERV----T 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 DRGLWAVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGG--GAPMErlASYGS 234
Cdd:cd09806  77 ERHVDVLVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGlqGLPFN--DVYCA 153

                       170       180       190
                ....*....|....*....|....*....|...
gi 4504503  235 SKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:cd09806 154 SKFALEGLCESLAVQLLPFNVHLSLIECGPVHT 186
PRK07069 PRK07069
short chain dehydrogenase; Validated
 86-262 8.56e-17

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 79.37  E-value: 8.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    86 LVTGGDCGLGHALCKYLDELGFTVFAGVLNEnGPGAE----ELRRTCSPRLS-VLQMDITKPVQIKDAYSK-VAAMlqdR 159
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDIND-AAGLDafaaEINAAHGEGVAfAAVQDVTDEAQWQALLAQaADAM---G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGV--LGFPTDGELllmTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK07069  79 GLSVLVNNAGVgsFGAIEQIEL---DEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASK 155

                        170       180
                 ....*....|....*....|....*...
gi 4504503   237 AAVTMFSSVMRLELSK--WGIKVASIQP 262
Cdd:PRK07069 156 AAVASLTKSIALDCARrgLDVRCNSIHP 183
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 83-263 9.01e-17

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: 79.07  E-value: 9.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSkvAAMLQDRGLW 162
Cdd:cd08944   4 KVAIVTGAGAGIGAACAARLAREGARVV--VADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFE--RAVEEFGGLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMGGGAPMERLASYGSSKAAVTM 241
Cdd:cd08944  80 LLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGgSIVNLSSIAGQSGDPGYGAYGASKAAIRN 159

                       170       180
                ....*....|....*....|..
gi 4504503  242 FSSVMRLELSKWGIKVASIQPG 263
Cdd:cd08944 160 LTRTLAAELRHAGIRCNALAPG 181
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
83-262 1.13e-16

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 81.82  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRTCSPRLSVL--QMDITKPVQIKDAYSKVAamLQDRG 160
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVV--LADLDEEAAEAAAAELGGPDRALgvACDVTDEAAVQAAFEEAA--LAFGG 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:PRK08324 499 VDIVVSNAGIAISGPIEETSD-EDWRRSFDVNATGHFLVAREAVRIMKAQGlgGSIVFIASKNAVNPGPNFGAYGAAKAA 577

                        170       180
                 ....*....|....*....|....
gi 4504503   239 VTMFSSVMRLELSKWGIKVASIQP 262
Cdd:PRK08324 578 ELHLVRQLALELGPDGIRVNGVNP 601
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 80-267 1.22e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 78.68  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    80 VDQKAVLVTGGDCGLGHALCKYLDELGFTVfAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAmlQDR 159
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARV-ALIGRGAAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNR--QFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGVLGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGG---GAPMerlASYGSS 235
Cdd:PRK12828  82 RLDALVNIAGAFVWGTIADGDA-DTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAAlkaGPGM---GAYAAA 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504503   236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK12828 158 KAGVARLTEALAAELLDRGITVNAVLPSIIDT 189
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 85-289 1.37e-16

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: 78.55  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVfagVLN--ENGPGAEELRRTCSP---RLSVLQMDITKPVQIKdaySKVAAMLQDR 159
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADV---VINyrKSKDAAAEVAAEIEElggKAVVVRADVSQPQDVE---EMFAAVKERF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  160 G-LWAVINNAGVLGF-PTDGelLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:cd05359  75 GrLDVLVSNAAAGAFrPLSE--LTPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAK 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 4504503  237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPA 289
Cdd:cd05359 153 AALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAAAANTPA 205
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 80-271 2.45e-16

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: 77.96  E-value: 2.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   80 VDQKAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSP---RLSVLQMDITKPVQIKDAYSKVAAML 156
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAV--AIAARRVDRLEALADELEAeggKALVLELDVTDEQQVDAAVERTVEAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  157 QdrGLWAVINNAGV--LGFPTDGElllMTDYKQCMAVNFFGTVEVTKTFLPLLR-KSKGRLVNVSSMGGGAPMERLASYG 233
Cdd:cd08934  79 G--RLDILVNNAGImlLGPVEDAD---TTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNSAVYN 153

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4504503  234 SSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAG 271
Cdd:cd08934 154 ATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRD 191
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 68-267 3.07e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 77.78  E-value: 3.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    68 MYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKD 147
Cdd:PRK06841   1 MTDTKQFDLAFDLSGKVAVVTGGASGIGHAIAELFAAKGARV--ALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   148 AYSKVAAMLQdrGLWAVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPM 226
Cdd:PRK06841  79 AVAAVISAFG--RIDILVNSAGV-ALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhMIAAGGGKIVNLASQAGVVAL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4504503   227 ERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK06841 156 ERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLT 196
PRK08267 PRK08267
SDR family oxidoreductase;
83-263 3.63e-16

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 77.67  E-value: 3.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTC-SPRLSVLQMDITKPVQIKDAYSKVAAmLQDRGL 161
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRV--GAYDINEAGLAALAAELgAGNAWTGALDVTDRAAWDAALADFAA-ATGGRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 WAVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMGG--GAPmeRLASYGSSK 236
Cdd:PRK08267  79 DVLFNNAGILRG---GPFEDIPleAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSASAiyGQP--GLAVYSATK 153

                        170       180
                 ....*....|....*....|....*..
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK08267 154 FAVRGLTEALDLEWRRHGIRVADVMPL 180
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 82-263 5.84e-16

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 76.70  E-value: 5.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTV---FAGvlneNGPGAEELRRT---CSPRLSVLQMDITKPVQIKDAYSKVAAM 155
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVavnYAG----SAAAADELVAEieaAGGRAIAVQADVADAAAVTRLFDAAETA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQdrGLWAVINNAGVLGFPT--DGELllmTDYKQCMAVNFFGTVEVTKTFLPLLRKSkGRLVNVSSMGGGAPMERLASYG 233
Cdd:PRK12937  81 FG--RIDVLVNNAGVMPLGTiaDFDL---EDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYGPYA 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 4504503   234 SSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12937 155 ASKAAVEGLVHVLANELRGRGITVNAVAPG 184
PRK07577 PRK07577
SDR family oxidoreductase;
83-289 7.26e-16

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 76.30  E-value: 7.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTV--FAGVLNENGPGaeELrrtcsprlsvLQMDITKPVQIKDAyskVAAMLQDRG 160
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVigIARSAIDDFPG--EL----------FACDLADIEQTAAT---LAQINEIHP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVLGFPTDGELLLMTDYkQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERlASYGSSKAAV 239
Cdd:PRK07577  69 VDAIVNNVGIALPQPLGKIDLAALQ-DVYDLNVRAAVQVTQAFLEgMKLREQGRIVNICSRAIFGALDR-TSYSAAKSAL 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4504503   240 TMFSSVMRLELSKWGIKVASIQPGGFLTNI-AGTSDKWEKLEKDILDHLPA 289
Cdd:PRK07577 147 VGCTRTWALELAEYGITVNAVAPGPIETELfRQTRPVGSEEEKRVLASIPM 197
PRK08589 PRK08589
SDR family oxidoreductase;
80-274 1.06e-15

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 76.36  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    80 VDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNE-----------NGPGAEELRRTCSPRLSVLQMditkPVQIKDA 148
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEavsetvdkiksNGGKAKAYHVDISDEQQVKDF----ASEIKEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   149 YSKVAAMLQDRGlwaVINNAG-VLGFPTDgelllmtDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPME 227
Cdd:PRK08589  80 FGRVDVLFNNAG---VDNAAGrIHEYPVD-------VFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADL 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4504503   228 RLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT----NIAGTSD 274
Cdd:PRK08589 150 YRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETplvdKLTGTSE 200
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 85-263 1.07e-15

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: 75.88  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNENG-PGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWa 163
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVVLAARSAEAlHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTW- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  164 vINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVT 240
Cdd:cd05360  82 -VNNAGVAVF---GRFEDVTpeEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVR 157

                       170       180
                ....*....|....*....|....*
gi 4504503  241 MFSSVMRLELSKWG--IKVASIQPG 263
Cdd:cd05360 158 GFTESLRAELAHDGapISVTLVQPT 182
PRK07201 PRK07201
SDR family oxidoreductase;
79-260 1.25e-15

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 78.45  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNengpgAEELRRTCSP------RLSVLQMDITKPVQIKDAyskV 152
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARN-----GEALDELVAEirakggTAHAYTCDLTDSAAVDHT---V 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   153 AAMLQDRGlwAV---INNAG-----VLGFPTDgellLMTDYKQCMAVNFFGTVEVTKTFLPLLR-KSKGRLVNVSSMG-- 221
Cdd:PRK07201 440 KDILAEHG--HVdylVNNAGrsirrSVENSTD----RFHDYERTMAVNYFGAVRLILGLLPHMReRRFGHVVNVSSIGvq 513

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4504503   222 GGAPmeRLASYGSSKAAVTMFSSVMRLELSKWGIKVASI 260
Cdd:PRK07201 514 TNAP--RFSAYVASKAALDAFSDVAASETLSDGITFTTI 550
PRK05855 PRK05855
SDR family oxidoreductase;
164-272 1.37e-15

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 78.10  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   164 VINNAGV------LGFPTDgelllmtDYKQCMAVNFFGTVEVTKTFLPLL--RKSKGRLVNVSSMGGGAPMERLASYGSS 235
Cdd:PRK05855 396 VVNNAGIgmaggfLDTSAE-------DWDRVLDVNLWGVIHGCRLFGRQMveRGTGGHIVNVASAAAYAPSRSLPAYATS 468

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 4504503   236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGT 272
Cdd:PRK05855 469 KAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVAT 505
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 72-288 1.47e-15

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 75.65  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    72 LSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPG--AEELRRTCSPRLSVlQMDITKPVQIKDAY 149
Cdd:PRK06113   1 MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANhvVDEIQQLGGQAFAC-RCDITSEQELSALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   150 SkvAAMLQDRGLWAVINNAGVLG-FPTDgelLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMGGGAPME 227
Cdd:PRK06113  80 D--FALSKLGKVDILVNNAGGGGpKPFD---MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGgVILTITSMAAENKNI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504503   228 RLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEkLEKDILDHLP 288
Cdd:PRK06113 155 NMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPE-IEQKMLQHTP 214
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 83-268 1.48e-15

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: 75.83  E-value: 1.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENG--PGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAmlQDRG 160
Cdd:cd08930   3 KIILITGAAGLIGKAFCKALLSAGARLILADINAPAleQLKEELTNLYKNRVIALELDITSKESIKELIESYLE--KFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVLGFPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSM-GGGAPMERL------- 229
Cdd:cd08930  81 IDILINNAYPSPKVWGSRFEEFPyeQWNEVLNVNLGGAFLCSQAFIKLFKKQgKGSIINIASIyGVIAPDFRIyentqmy 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4504503  230 --ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN 268
Cdd:cd08930 161 spVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNN 201
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 81-291 2.93e-15

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: 74.88  E-value: 2.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGA--EELRRTcSPRLSVLQMDITKPVQIKDAyskVAAMLQD 158
Cdd:cd08945   2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATtvKELREA-GVEADGRTCDVRSVPEIEAL---VAAAVAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 RGLWAV-INNAGVLGfptDGELLLMTD--YKQCMAVNFFGTVEVTKTFLP---LLRKSKGRLVNVSSMGGGAPMERLASY 232
Cdd:cd08945  78 YGPIDVlVNNAGRSG---GGATAELADelWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAAPY 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504503  233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIA-----GTSDKWEKLEKDILDHLPAEV 291
Cdd:cd08945 155 SASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAasvreHYADIWEVSTEEAFDRITARV 218
PRK08628 PRK08628
SDR family oxidoreductase;
83-290 3.64e-15

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 74.61  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYL-DELGFTVfagVLNENGPG---AEELRRTcSPRLSVLQMDITKPVQIKDAyskVAAMLQD 158
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLaEEGAIPV---IFGRSAPDdefAEELRAL-QPRAEFVQVDLTDDAQCRDA---VEQTVAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RG-LWAVINNAGVlgfpTDGeLLLMTDYKQCMA---VNFFGTVEVTKTFLPLLRKSKGRLVNVSS----MGGGapmeRLA 230
Cdd:PRK08628  81 FGrIDGLVNNAGV----NDG-VGLEAGREAFVAsleRNLIHYYVMAHYCLPHLKASRGAIVNISSktalTGQG----GTS 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504503   231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN-----IAGTSDKWEKLEKdILDHLPAE 290
Cdd:PRK08628 152 GYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPlyenwIATFDDPEAKLAA-ITAKIPLG 215
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 77-267 6.84e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 74.96  E-value: 6.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    77 LLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPG----AEELRRTCSPRLSVlQMDITKPVQIKDAYSKV 152
Cdd:PRK07109   3 LKPIGRQVVVITGASAGVGRATARAFARRGAKV--VLLARGEEGlealAAEIRAAGGEALAV-VADVADAEAVQAAADRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   153 AAMLQDRGLWavINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERL 229
Cdd:PRK07109  80 EEELGPIDTW--VNNAMVTVF---GPFEDVTpeEFRRVTEVTYLGVVHGTLAALRhMRPRDRGAIIQVGSALAYRSIPLQ 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504503   230 ASYGSSKAAVTMFSSVMRLEL--SKWGIKVASIQPGGFLT 267
Cdd:PRK07109 155 SAYCAAKHAIRGFTDSLRCELlhDGSPVSVTMVQPPAVNT 194
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 83-281 9.11e-15

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: 73.19  E-value: 9.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSkvAAMLQDRGLW 162
Cdd:cd05345   6 KVAIVTGAGSGFGEGIARRFAQEGARVV--IADINADGAERVAADIGEAAIAIQADVTKRADVEAMVE--AALSKFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTM 241
Cdd:cd05345  82 ILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPhMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVT 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4504503  242 FSSVMRLELSKWGIKVASIQP----GGFLTNIAGtSDKWEKLEK 281
Cdd:cd05345 162 ATKAMAVELAPRNIRVNCLCPvageTPLLSMFMG-EDTPENRAK 204
PRK07454 PRK07454
SDR family oxidoreductase;
82-263 1.73e-14

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 72.30  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRTCSP---RLSVLQMDITKPVQIKdaySKVAAMLQD 158
Cdd:PRK07454   6 MPRALITGASSGIGKATALAFAKAGWDLA--LVARSQDALEALAAELRStgvKAAAYSIDLSNPEAIA---PGIAELLEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RGLWAV-INNAGVlGFptDGELLLM--TDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLV-NVSSMGGGAPMERLASYGS 234
Cdd:PRK07454  81 FGCPDVlINNAGM-AY--TGPLLEMplSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIiNVSSIAARNAFPQWGAYCV 157

                        170       180
                 ....*....|....*....|....*....
gi 4504503   235 SKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK07454 158 SKAALAAFTKCLAEEERSHGIRVCTITLG 186
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-270 1.91e-14

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 72.41  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGftVFAGVLNENGPG----AEELRRTcSPRLSVLQMDITKPVQIKDAYSKVAAMLQD 158
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEG--VNVGLLARTEENlkavAEEVEAY-GVKVVIATADVSDYEEVTAAIEQLKNELGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RGLwaVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGG--GAPMerLASYG 233
Cdd:PRK07666  85 IDI--LINNAGISKF---GKFLELDpaEWEKIIQVNLMGVYYATRAVLPsMIERQSGDIINISSTAGqkGAAV--TSAYS 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504503   234 SSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIA 270
Cdd:PRK07666 158 ASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMA 194
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-284 2.05e-14

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 72.18  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVF-AGVLNENGpgAEELR---RTCSPRLSVLQMDITKPVQIKDAYSKVaamLQD 158
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKEGAKVViAYDINEEA--AQELLeeiKEEGGDAIAVKADVSSEEDVENLVEQI---VEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RG-LWAVINNAGVLGFPTDGElllMTD--YKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGG--GAPMErlASY 232
Cdd:PRK05565  81 FGkIDILVNNAGISNFGLVTD---MTDeeWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVNISSIWGliGASCE--VLY 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEK--LEKDIL 284
Cdd:PRK05565 156 SASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKegLAEEIP 209
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-263 2.47e-14

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 71.92  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENgPGAeelrrtcSPRLSVLQMDITKPV-QIKDAYSKVAAMLqdrgl 161
Cdd:PRK06550   6 KTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDK-PDL-------SGNFHFLQLDLSDDLePLFDWVPSVDILC----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 waviNNAGVL-GFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSM-----GGGApmerlASYGS 234
Cdd:PRK06550  73 ----NTAGILdDYKPLLDTSL-EEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIINMCSIasfvaGGGG-----AAYTA 142

                        170       180
                 ....*....|....*....|....*....
gi 4504503   235 SKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06550 143 SKHALAGFTKQLALDYAKDGIQVFGIAPG 171
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 79-276 2.64e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 72.28  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngpgaEELRRTCS--PRLSVLQMDITKPVQIKDAYSKVAAml 156
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDE-----ALAKETAAelGLVVGGPLDVTDPASFAAFLDAVEA-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 qDRGLWAV-INNAGV--LGfPTDGELLLMTDykQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASY 232
Cdd:PRK07825  75 -DLGPIDVlVNNAGVmpVG-PFLDEPDAVTR--RILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGMATY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGgfLTN---IAGTSDKW 276
Cdd:PRK07825 151 CASKHAVVGFTDAARLELRGTGVHVSVVLPS--FVNtelIAGTGGAK 195
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 83-269 3.00e-14

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: 72.26  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELR---RTCSP--RLSVLQMDITKPVQIKdaysKVAAMLQ 157
Cdd:cd05327   2 KVVVITGANSGIGKETARELAKRGAHVI--IACRNEEKGEEAAaeiKKETGnaKVEVIQLDLSSLASVR----QFAEEFL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 DRG--LWAVINNAGVLGFPT----DG-ELLlmtdykqcMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMG-------- 221
Cdd:cd05327  76 ARFprLDILINNAGIMAPPRrltkDGfELQ--------FAVNYLGHFLLTNLLLPVLKASaPSRIVNVSSIAhragpidf 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4504503  222 ------GGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:cd05327 148 ndldleNNKEYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 78-263 3.84e-14

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 71.97  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    78 LPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEelrrtcspRLSVLQMDITKPVQIKDAyskVAAMLQ 157
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQHE--------NYQFVPTDVSSAEEVNHT---VAEIIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 DRG-LWAVINNAGVlGFPTdgellLMTDYK--------------QCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMG 221
Cdd:PRK06171  74 KFGrIDGLVNNAGI-NIPR-----LLVDEKdpagkyelneaafdKMFNINQKGVFLMSQAVARqMVKQHDGVIVNMSSEA 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4504503   222 GGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06171 148 GLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPG 189
PRK09072 PRK09072
SDR family oxidoreductase;
82-262 4.35e-14

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 71.51  E-value: 4.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAgvlneNGPGAEELRRTC-----SPRLSVLQMDITKPvqikDAYSKV-AAM 155
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAAAGARLLL-----VGRNAEKLEALAarlpyPGRHRWVVADLTSE----AGREAVlARA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQDRGLWAVINNAGVLGFptdGEL--LLMTDYKQCMAVNFFGTVEVTKTFLPLLRK-SKGRLVNVSSMGG--GAPmeRLA 230
Cdd:PRK09072  76 REMGGINVLINNAGVNHF---ALLedQDPEAIERLLALNLTAPMQLTRALLPLLRAqPSAMVVNVGSTFGsiGYP--GYA 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504503   231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQP 262
Cdd:PRK09072 151 SYCASKFALRGFSEALRRELADTGVRVLYLAP 182
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 78-290 8.40e-14

(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: 70.43  E-value: 8.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   78 LPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGPGAEELRRTCSPRLSVLQmditkpvQIKDAYSKVAA--- 154
Cdd:cd05353   1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKV---VVNDLGGDRKGSGKSSSAADKVVD-------EIKAAGGKAVAnyd 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  155 -------MLQDR-----GLWAVINNAGVLgfpTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSS 219
Cdd:cd05353  71 svedgekIVKTAidafgRVDILVNNAGIL---RDRSFAKMSeeDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSS 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504503  220 MGG-----GApmerlASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPggfltnIAGTSDKWEKLEKDILDHLPAE 290
Cdd:cd05353 148 AAGlygnfGQ-----ANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP------AAGSRMTETVMPEDLFDALKPE 212
PRK07832 PRK07832
SDR family oxidoreductase;
83-274 8.47e-14

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 70.84  E-value: 8.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgaeeLRRTCSP-RLSVLQMDITKPVQIKDaYSKVAAMLQD--- 158
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADG-----LAQTVADaRALGGTVPEHRALDISD-YDAVAAFAADiha 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 --RGLWAVINNAGVLGFPTDgELLLMTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGR-LVNVSSMGGGAPMERLASYGS 234
Cdd:PRK07832  75 ahGSMDVVMNIAGISAWGTV-DRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGGhLVNVSSAAGLVALPWHAAYSA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504503   235 SKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSD 274
Cdd:PRK07832 154 SKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVE 193
PRK07024 PRK07024
SDR family oxidoreductase;
85-263 1.30e-13

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 69.96  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    85 VLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRT--CSPRLSVLQMDITKPVQIKDAyskVAAMLQDRGLW 162
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATL--GLVARRTDALQAFAARlpKAARVSVYAADVRDADALAAA---AADFIAAHGLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 A-VINNAGV-----LGFPTDgelllMTDYKQCMAVNFFGTVevtKTFLPLL----RKSKGRLVNVSSMGG-----GApme 227
Cdd:PRK07024  80 DvVIANAGIsvgtlTEERED-----LAVFREVMDTNYFGMV---ATFQPFIapmrAARRGTLVGIASVAGvrglpGA--- 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4504503   228 rlASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK07024 149 --GAYSASKAAAIKYLESLRVELRPAGVRVVTIAPG 182
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
82-263 1.46e-13

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 70.14  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSP---RLSVLQMDITKPVQIKDAYSKVAAMLQD 158
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKV--AIVDYNEETAQAAADKLSKdggKAIAVKADVSDRDQVFAAVRQVVDTFGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 rgLWAVINNAGVlGFPTDGELLLMTDYKQCMAVN----FFGTVEVTKTFLPLlrKSKGRLVNVSSMGG--GAPmeRLASY 232
Cdd:PRK08643  80 --LNVVVNNAGV-APTTPIETITEEQFDKVYNINvggvIWGIQAAQEAFKKL--GHGGKIINATSQAGvvGNP--ELAVY 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK08643 153 SSTKFAVRGLTQTAARDLASEGITVNAYAPG 183
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 83-263 1.73e-13

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: 69.71  E-value: 1.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENgPGAEELRRTCSP---RLSVLQMDITKPVQIKDAYSKVAAMLQDr 159
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLNLE-EAAKSTIQEISEagyNAVAVGADVTDKDDVEALIDQAVEKFGS- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  160 gLWAVINNAGVLgfPTDgELLLMT--DYKQCMAVN----FFGTVEVTKTFLPLlrKSKGRLVNVSSMGGGAPMERLASYG 233
Cdd:cd05366  81 -FDVMVNNAGIA--PIT-PLLTITeeDLKKVYAVNvfgvLFGIQAAARQFKKL--GHGGKIINASSIAGVQGFPNLGAYS 154

                       170       180       190
                ....*....|....*....|....*....|
gi 4504503  234 SSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05366 155 ASKFAVRGLTQTAAQELAPKGITVNAYAPG 184
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 83-268 1.76e-13

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 69.93  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNEN-GPG---AEELR----RTCSPRLSVLQMDITKPV--QIKDAYSKV 152
Cdd:PRK08277  11 KVAVITGGGGVLGGAMAKELARAGAKV--AILDRNqEKAeavVAEIKaaggEALAVKADVLDKESLEQArqQILEDFGPC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   153 AAMlqdrglwavINNAG--VLGFPTDGELLL------------MTDYKQCMAVNFFGTVEVTKTFL-PLLRKSKGRLVNV 217
Cdd:PRK08277  89 DIL---------INGAGgnHPKATTDNEFHElieptktffdldEEGFEFVFDLNLLGTLLPTQVFAkDMVGRKGGNIINI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4504503   218 SSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN 268
Cdd:PRK08277 160 SSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
PRK12743 PRK12743
SDR family oxidoreductase;
80-274 1.97e-13

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 69.68  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    80 VDQKAVlVTGGDCGLGHALCKYLDELGFTVfaGVL-NENGPGAE---ELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAM 155
Cdd:PRK12743   1 MAQVAI-VTASDSGIGKACALLLAQQGFDI--GITwHSDEEGAKetaEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQdrGLWAVINNAGVLgfptDGELLLMTDYKQCMAVNffgTVEVTKTFLPLLRKSK--------GRLVNVSSMGGGAPME 227
Cdd:PRK12743  78 LG--RIDVLVNNAGAM----TKAPFLDMDFDEWRKIF---TVDVDGAFLCSQIAARhmvkqgqgGRIINITSVHEHTPLP 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4504503   228 RLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSD 274
Cdd:PRK12743 149 GASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDD 195
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 79-288 2.30e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 70.00  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSVLQM--DITKPvqikDAYSKVAAML 156
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKL--ALVDLEEAELAALAAELGGDDRVLTVvaDVTDL----AAMQAAAEEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDR--GLWAVINNAGVlgfpTDGELLLMTD---YKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMG--GGAPMerL 229
Cdd:PRK05872  80 VERfgGIDVVVANAGI----ASGGSVAQVDpdaFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAafAAAPG--M 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   230 ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN-IAGTSDKWEKLEKdILDHLP 288
Cdd:PRK05872 154 AAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDlVRDADADLPAFRE-LRARLP 212
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 81-271 2.64e-13

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: 69.02  E-value: 2.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELG-FTVFAGVLNENGPG-AEELRRtcsPRLSVLQMDITKPVQIKDAyskVAAMLQD 158
Cdd:cd05326   3 DGKVAIITGGASGIGEATARLFAKHGaRVVIADIDDDAGQAvAAELGD---PDISFVHCDVTVEADVRAA---VDTAVAR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 RG-LWAVINNAGVLGFPTdGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSS----MGGGAPMerla 230
Cdd:cd05326  77 FGrLDIMFNNAGVLGAPC-YSILETSleEFERVLDVNVYGAFLGTKHAARVMIPAKkGSIVSVASvagvVGGLGPH---- 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4504503  231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAG 271
Cdd:cd05326 152 AYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLT 192
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
81-290 2.81e-13

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 68.99  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG 160
Cdd:PRK06935  14 DGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKV---VKEALEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 -LWAVINNAGVLgfpTDGELLLMT--DYKQCMAVN----FFGTVEVTKTFlplLRKSKGRLVNVSSM----GGgapmERL 229
Cdd:PRK06935  91 kIDILVNNAGTI---RRAPLLEYKdeDWNAVMDINlnsvYHLSQAVAKVM---AKQGSGKIINIASMlsfqGG----KFV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504503   230 ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT-NIAGTSDKwEKLEKDILDHLPAE 290
Cdd:PRK06935 161 PAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTaNTAPIRAD-KNRNDEILKRIPAG 221
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 68-269 5.22e-13

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 68.60  E-value: 5.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    68 MYTYLSGqellpvdqKAVLVTGGDCGLGHALCKYLDELGFTVFAGVL-NENGP--GAEELRRTCSPRLSVlQMDITKPVQ 144
Cdd:PRK08936   1 MYSDLEG--------KVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEAndVAEEIKKAGGEAIAV-KGDVTVESD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   145 IKDAYSKVAAMLQDRGLWavINNAGVLGfPTDGELLLMTDYKQCMAVN----FFGTVEVTKTFLPllRKSKGRLVNVSSM 220
Cdd:PRK08936  72 VVNLIQTAVKEFGTLDVM--INNAGIEN-AVPSHEMSLEDWNKVINTNltgaFLGSREAIKYFVE--HDIKGNIINMSSV 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 4504503   221 GGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK08936 147 HEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPI 195
PRK08219 PRK08219
SDR family oxidoreductase;
81-263 6.95e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 67.27  E-value: 6.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDElGFTVFAGvlnenGPGAEELRRTCS--PRLSVLQMDITKPVQIKDAYSKVaamlqD 158
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAP-THTLLLG-----GRPAERLDELAAelPGATPFPVDLTDPEAIAAAVEQL-----G 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RgLWAVINNAGVLGFPTDGELLlMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:PRK08219  71 R-LDVLVHNAGVADLGPVAEST-VDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFA 148

                        170       180
                 ....*....|....*....|....*
gi 4504503   239 VTMFSSVMRLELSKwGIKVASIQPG 263
Cdd:PRK08219 149 LRALADALREEEPG-NVRVTSVHPG 172
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 83-288 9.14e-13

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: 67.55  E-value: 9.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEE---LRRTCSPRLSVLQMDITKPVQIKdAYskVAAMLQDR 159
Cdd:cd05330   4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKaalLEIAPDAEVLLIKADVSDEAQVE-AY--VDATVEQF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  160 G-LWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:cd05330  81 GrIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQSGYAAAKH 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4504503  238 AVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDK------WEKLEKDILDHLP 288
Cdd:cd05330 161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKqlgpenPEEAGEEFVSVNP 217
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 82-289 1.22e-12

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: 67.23  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   82 QKAVLVTGGDCGLGHALCKYLDELGFTV-FAG----VLNEngpGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAML 156
Cdd:cd05369   3 GKVAFITGGGTGIGKAIAKAFAELGASVaIAGrkpeVLEA---AAEEISSATGGRAHPIQCDVRDPEAVEAA---VDETL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  157 QDRG-LWAVINNAGvlG-FPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGG--GAPMErlA 230
Cdd:cd05369  77 KEFGkIDILINNAA--GnFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhgGSILNISATYAytGSPFQ--V 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504503  231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGfltnIAGTS-----DKWEKLEKDILDHLPA 289
Cdd:cd05369 153 HSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGP----IPTTEgmerlAPSGKSEKKMIERVPL 212
PRK06101 PRK06101
SDR family oxidoreductase;
84-263 1.23e-12

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 66.82  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    84 AVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELRRTcSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrgLWa 163
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSV--LDELHTQ-SANIFTLAFDVTDHPGTKAALSQLPFIPE---LW- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   164 vINNAGVLGFPTDG--ELLLMTdykQCMAVNFFGTVEVTKTFLPLLRKSKgRLVNVSSMGGGAPMERLASYGSSKAAVTM 241
Cdd:PRK06101  76 -IFNAGDCEYMDDGkvDATLMA---RVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPRAEAYGASKAAVAY 150

                        170       180
                 ....*....|....*....|..
gi 4504503   242 FSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06101 151 FARTLQLDLRPKGIEVVTVFPG 172
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 77-265 1.50e-12

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: 66.74  E-value: 1.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   77 LLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRRtcspRLSVLQMDITKPVQI--KDAYSKVAA 154
Cdd:cd08942   1 LFSVAGKIVLVTGGSRGIGRMIAQGFLEAGARVI--ISARKAEACADAAE----ELSAYGECIAIPADLssEEGIEALVA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  155 MLQDRG--LWAVINNAG------VLGFPTDGelllmtdYKQCMAVNFFGTVEVTKTFLPLLRKSK-----GRLVNVSSMG 221
Cdd:cd08942  75 RVAERSdrLDVLVNNAGatwgapLEAFPESG-------WDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIA 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4504503  222 G-GAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGF 265
Cdd:cd08942 148 GiVVSGLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRF 192
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 83-268 1.85e-12

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: 67.10  E-value: 1.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEEL--------RRTCSPRLSVLQMDITKPV--QIKDAYSKV 152
Cdd:cd08935   6 KVAVITGGTGVLGGAMARALAQAGAKV--AALGRNQEKGDKVakeitalgGRAIALAADVLDRASLERAreEIVAQFGTV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  153 AAMLQDRG--LWAVINNAGVLGFPTDGELLLMTD--YKQCMAVNFFGTVEVTKTFL-PLLRKSKGRLVNVSSMGGGAPME 227
Cdd:cd08935  84 DILINGAGgnHPDATTDPEHYEPETEQNFFDLDEegWEFVFDLNLNGSFLPSQVFGkDMLEQKGGSIINISSMNAFSPLT 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4504503  228 RLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN 268
Cdd:cd08935 164 KVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 83-263 2.03e-12

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: 66.45  E-value: 2.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTV-FAGVLNENGPGAEELRRtcsPRLSVLQMDITKPVQIKDAYSKVAAMLQdrGL 161
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGDKVvFADIDEERGADFAEAEG---PNLFFVHGDVADETLVKFVVYAMLEKLG--RI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTM 241
Cdd:cd09761  77 DVLVNNAAR-GSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVA 155

                       170       180
                ....*....|....*....|..
gi 4504503  242 FSSVMRLELSKWgIKVASIQPG 263
Cdd:cd09761 156 LTHALAMSLGPD-IRVNCISPG 176
PRK06482 PRK06482
SDR family oxidoreductase;
86-289 2.07e-12

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 67.06  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    86 LVTGGDCGLGHALCKYLDELGFTVFAGVlneNGPGA-EELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG-LWA 163
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATV---RRPDAlDDLKARYGDRLWVLQLDVTDSAAVRAV---VDRAFAALGrIDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   164 VINNAGvLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMGGGAPMERLASYGSSKAAVTMF 242
Cdd:PRK06482  80 VVSNAG-YGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGgRIVQVSSEGGQIAYPGFSLYHATKWGIEGF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4504503   243 SSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLekDILDHLPA 289
Cdd:PRK06482 159 VEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPL--DAYDDTPV 203
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 85-288 2.22e-12

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: 66.44  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGP--GAEELRRTCSPRLSvLQMDITKPVQIKDAYSkvAAMLQDRGLW 162
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAeaVAAAIQQAGGQAIG-LECNVTSEQDLEAVVK--ATVSQFGGIT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLG---FPTDgelLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:cd05365  79 ILVNNAGGGGpkpFDMP---MTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNVRIAAYGSSKAA 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4504503  239 VTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEkLEKDILDHLP 288
Cdd:cd05365 156 VNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPE-IERAMLKHTP 204
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 83-283 2.47e-12

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: 66.32  E-value: 2.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGA--EELRRTcSPRLSVLQMDITKPVQIKDAYSKVAAMLqDRG 160
Cdd:cd05329   7 KTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDEclTEWREK-GFKVEGSVCDVSSRSERQELMDTVASHF-GGK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVLgFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:cd05329  85 LNILVNNAGTN-IRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASgNGNIVFISSVAGVIAVPSGAPYGATKGAL 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 4504503  240 TMFSSVMRLELSKWGIKVASIQPGGFLTNIA-GTSDKWEKLEKDI 283
Cdd:cd05329 164 NQLTRSLACEWAKDNIRVNAVAPWVIATPLVePVIQQKENLDKVI 208
PRK06138 PRK06138
SDR family oxidoreductase;
82-263 2.94e-12

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 65.94  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGftVFAGVLNENGPGAEELRR--TCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdr 159
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREG--ARVVVADRDAEAAERVAAaiAAGGRAFARQGDVGSAEAVEALVDFVAARWG-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGvlgFPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK06138  81 RLDVLVNNAG---FGCGGTVVTTDeaDWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGRAAYVASK 157

                        170       180
                 ....*....|....*....|....*..
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06138 158 GAIASLTRAMALDHATDGIRVNAVAPG 184
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 79-263 3.27e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 65.90  E-value: 3.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGF--TVFAGVLNENGPGAEELRRTCSP---RLSVLQMDITKPVQIKDAyskVA 153
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGAdvIVLDIHPMRGRAEADAVAAGIEAaggKALGLAFDVRDFAATRAA---LD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   154 AMLQDRG-LWAVINNAGVLgfpTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGGGAPMER 228
Cdd:PRK12827  80 AGVEEFGrLDILVNNAGIA---TDAAFAELSieEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRG 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 4504503   229 LASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12827 157 QVNYAASKAGLIGLTKTLANELAPRGITVNAVAPG 191
PRK06949 PRK06949
SDR family oxidoreductase;
83-288 5.07e-12

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 65.55  E-value: 5.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGF-TVFAGVLNENgpgAEELRRTCSPR---LSVLQMDITKPVQIKDAyskVAAMLQD 158
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAkVVLASRRVER---LKELRAEIEAEggaAHVVSLDVTDYQSIKAA---VAHAETE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RG-LWAVINNAGVlgfPTDGELLLMT--DYKQCMAVN----FFGTVEVTKTFLPLLR-----KSKGRLVNVSSMGGGAPM 226
Cdd:PRK06949  84 AGtIDILVNNSGV---STTQKLVDVTpaDFDFVFDTNtrgaFFVAQEVAKRMIARAKgagntKPGGRIINIASVAGLRVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504503   227 ERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIagTSDKWEKLE-KDILDHLP 288
Cdd:PRK06949 161 PQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI--NHHHWETEQgQKLVSMLP 221
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 78-266 8.03e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 64.73  E-value: 8.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    78 LPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLN--ENGPGAEELRRTCSPRLSVLQMDITKPVQikdayskVAAM 155
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARV---VVNyhQSEDAAEALADELGDRAIALQADVTDREQ-------VQAM 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQD------RGLWAVINNAgVLGFPTDG------ELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGG 222
Cdd:PRK08642  71 FATatehfgKPITTVVNNA-LADFSFDGdarkkaDDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNLF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4504503   223 GAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQpGGFL 266
Cdd:PRK08642 150 QNPVVPYHDYTTAKAALLGLTRNLAAELGPYGITVNMVS-GGLL 192
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 81-281 9.03e-12

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 64.60  E-value: 9.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngpgaEELRRTCSP--RLSV----LQMDITKPVQIKDAYSKVAa 154
Cdd:PRK08217   4 KDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQ-----EKLEEAVAEcgALGTevrgYAANVTDEEDVEATFAQIA- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   155 mlQDRG-LWAVINNAGVLgfpTDGELLLMTDYK--QCMAVNFFGTV---EVTKTFL--------PLLRKSKGRLVNVSSM 220
Cdd:PRK08217  78 --EDFGqLNGLINNAGIL---RDGLLVKAKDGKvtSKMSLEQFQSVidvNLTGVFLcgreaaakMIESGSKGVIINISSI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504503   221 GGGAPMERlASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGtSDKWEKLEK 281
Cdd:PRK08217 153 ARAGNMGQ-TNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA-AMKPEALER 211
PRK05866 PRK05866
SDR family oxidoreductase;
79-261 9.60e-12

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 65.15  E-value: 9.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGA---EELRRTCSPRlsVLQMDITKPvqikDAYSKVAAM 155
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAvadRITRAGGDAM--AVPCDLSDL----DAVDALVAD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQDR--GLWAVINNAG-VLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMG---GGAPMer 228
Cdd:PRK05866 111 VEKRigGVDILINNAGrSIRRPLAESLDRWHDVERTMVLNYYAPLRLIRGLAPgMLERGDGHIINVATWGvlsEASPL-- 188

                        170       180       190
                 ....*....|....*....|....*....|...
gi 4504503   229 LASYGSSKAAVTMFSSVMRLELSKWGIKVASIQ 261
Cdd:PRK05866 189 FSVYNASKAALSAVSRVIETEWGDRGVHSTTLY 221
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 86-275 1.14e-11

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: 64.23  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   86 LVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRrTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrGLWAVI 165
Cdd:cd05371   6 VVTGGASGLGLATVERLLAQGAKVV--ILDLPNSPGETVA-KLGDNCRFVPVDVTSEKDVKAALALAKAKFG--RLDIVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  166 NNAGV------LGFPTDGELLLmTDYKQCMAVNFFGTVEVTKTFLPLLRKS-------KGRLVNVSSMGG--GAPMErlA 230
Cdd:cd05371  81 NCAGIavaaktYNKKGQQPHSL-ELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggeRGVIINTASVAAfeGQIGQ--A 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 4504503  231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN-IAGTSDK 275
Cdd:cd05371 158 AYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPlLAGLPEK 203
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 83-263 1.19e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 64.21  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGV-----LNEngpGAEELRRTCSPRLSVlQMDITKPVQIKdaySKVAAMLQ 157
Cdd:PRK07890   6 KVVVVSGVGPGLGRTLAVRAARAGADVVLAArtaerLDE---VAAEIDDLGRRALAV-PTDITDEDQCA---NLVALALE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 DRG-LWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK07890  79 RFGrVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKMAK 158

                        170       180
                 ....*....|....*....|....*..
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK07890 159 GALLAASQSLATELGPQGIRVNSVAPG 185
PRK09730 PRK09730
SDR family oxidoreductase;
83-269 1.22e-11

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 64.10  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfAGVLNENGPGAEELRRTCSP---RLSVLQMDITKPVQIKDAYSKVAAmlQDR 159
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTV-AVNYQQNLHAAQEVVNLITQaggKAFVLQADISDENQVVAMFTAIDQ--HDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNffgtveVTKTFLPLLRKSK----------GRLVNVSSMGG--GAPME 227
Cdd:PRK09730  79 PLAALVNNAGILFTQCTVENLTAERINRVLSTN------VTGYFLCCREAVKrmalkhggsgGAIVNVSSAASrlGAPGE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4504503   228 RLaSYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK09730 153 YV-DYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM 193
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 75-288 1.28e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 64.20  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    75 QELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVF-----AGVLNEngpGAEELrrtcsPRLSV----LQMDITKPVQI 145
Cdd:PRK08213   5 LELFDLSGKTALVTGGSRGLGLQIAEALGEAGARVVlsarkAEELEE---AAAHL-----EALGIdalwIAADVADEADI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   146 KDAyskVAAMLQDRG-LWAVINNAGVL-GFPTdgELLLMTDYKQCMAVNffgtveVTKTFL--------PLLRKSKGRLV 215
Cdd:PRK08213  77 ERL---AEETLERFGhVDILVNNAGATwGAPA--EDHPVEAWDKVMNLN------VRGLFLlsqavakrSMIPRGYGRII 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504503   216 NVSSMGG--GAPMERLAS--YGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSdkWEKLEKDILDHLP 288
Cdd:PRK08213 146 NVASVAGlgGNPPEVMDTiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGT--LERLGEDLLAHTP 220
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
82-291 1.61e-11

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 63.88  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVlNENGPGAE---ELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQD 158
Cdd:PRK12938   3 QRIAYVTGGMGGIGTSICQRLHKDGFKVVAGC-GPNSPRRVkwlEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RGLwaVINNAGVlgfPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSS 235
Cdd:PRK12938  82 IDV--LVNNAGI---TRDVVFRKMTreDWTAVIDTNLTSLFNVTKQVIDgMVERGWGRIINISSVNGQKGQFGQTNYSTA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504503   236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAgtsdkwEKLEKDILDHLPAEV 291
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMV------KAIRPDVLEKIVATI 206
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 85-291 3.34e-11

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: 62.90  E-value: 3.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVLNEngpgaeelrrtcsprlSVLQMDITKPVQIKDAYSKVAAmLQDRGLWAV 164
Cdd:cd05328   2 IVITGAASGIGAATAELLEDAGHTVIGIDLRE----------------ADVIADLSTPEGRAAAIADVLA-RCSGVLDGL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  165 INNAGVLGfPTDGELLLmtdykqcmAVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMGG---------------GAPMER 228
Cdd:cd05328  65 VNCAGVGG-TTVAGLVL--------KVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAGagwaqdklelakalaAGTEAR 135

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504503  229 LAS------------YGSSKAAVTMFssVMRLE---LSKWGIKVASIQPGGFLTNIAGTSdKWEKLEKDILDHLPAEV 291
Cdd:cd05328 136 AVAlaehagqpgylaYAGSKEALTVW--TRRRAatwLYGAGVRVNTVAPGPVETPILQAF-LQDPRGGESVDAFVTPM 210
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-279 3.67e-11

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 63.06  E-value: 3.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELR--RTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrG 160
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQelRALGVEVIFFPADVADLSAHEAMLDAAQAAWG--R 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVlGFPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSKGR-------LVNVSSMGGG-APMERLa 230
Cdd:PRK12745  81 IDCLVNNAGV-GVKVRGDLLDLTpeSFDRVLAINLRGPFFLTQAVAKRMLAQPEPeelphrsIVFVSSVNAImVSPNRG- 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 4504503   231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI-AGTSDKWEKL 279
Cdd:PRK12745 159 EYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMtAPVTAKYDAL 208
PRK07063 PRK07063
SDR family oxidoreductase;
83-277 5.64e-11

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 62.38  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENG--PGAEELRRTCSP-RLSVLQMDITKPVQIKDAYSKVAAMLQdr 159
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALaeRAAAAIARDVAGaRVLAVPADVTDAASVAAAVAAAEEAFG-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK07063  86 PLDVLVNNAGINVF---ADPLAMTdeDWRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVNIASTHAFKIIPGCFPYPVAK 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIagTSDKWE 277
Cdd:PRK07063 163 HGLLGLTRALGIEYAARNVRVNAIAPGYIETQL--TEDWWN 201
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 76-267 6.95e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 62.08  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    76 ELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFA-GVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAa 154
Cdd:PRK08085   3 DLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIInDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIE- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   155 mlQDRGLWAV-INNAGV------LGFPTDgelllmtDYKQCMAVN----FFGTVEVTKTflpLLRKSKGRLVNVSSMGGG 223
Cdd:PRK08085  82 --KDIGPIDVlINNAGIqrrhpfTEFPEQ-------EWNDVIAVNqtavFLVSQAVARY---MVKRQAGKIINICSMQSE 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4504503   224 APMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK08085 150 LGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKT 193
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 79-263 8.59e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 61.95  E-value: 8.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVF-AGVLNENGPG-AEELrrtcSPRLSVLQMDITKPVQIKDAyskVAAML 156
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAiVDIDADNGAAvAASL----GERARFIATDITDDAAIERA---VATVV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDRG-LWAVINNAGVL---GFPTDGElllmtDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASY 232
Cdd:PRK08265  76 ARFGrVDILVNLACTYlddGLASSRA-----DWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLY 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK08265 151 PASKAAIRQLTRSMAMDLAPDGIRVNSVSPG 181
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 85-263 1.14e-10

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 61.31  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    85 VLVTGGDCGLGHALCKYLDELGFTVFA-GVLNENgpgAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLwa 163
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIAtGRRQER---LQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   164 VINNAGV-LGF-------PTDGELLLMTDYKqcmavnffGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGS 234
Cdd:PRK10538  78 LVNNAGLaLGLepahkasVEDWETMIDTNNK--------GLVYMTRAVLPgMVERNHGHIINIGSTAGSWPYAGGNVYGA 149

                        170       180
                 ....*....|....*....|....*....
gi 4504503   235 SKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK10538 150 TKAFVRQFSLNLRTDLHGTAVRVTDIEPG 178
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
80-274 1.16e-10

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 61.35  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    80 VDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGPGAEEL-RRTCSP--RLSVLQMDITKPVQIKDAySKVAAML 156
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANL---ILLDISPEIEKLaDELCGRghRCTAVVADVRDPASVAAA-IKRAKEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDRgLWAVINNAGV------LGFPTDgelllMTDYKqcMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGG---GAPM 226
Cdd:PRK08226  80 EGR-IDILVNNAGVcrlgsfLDMSDE-----DRDFH--IDINIKGVWNVTKAVLPeMIARKDGRIVMMSSVTGdmvADPG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4504503   227 ErlASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT----NIAGTSD 274
Cdd:PRK08226 152 E--TAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTpmaeSIARQSN 201
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-288 1.67e-10

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 60.96  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGD--CGLGHALCKYLDELGFTVFAGVL-------------NENGPGAEELRrTCSPRLSVLQMDITKPVQIKD 147
Cdd:PRK12859   7 KVAVVTGVSrlDGIGAAICKELAEAGADIFFTYWtaydkempwgvdqDEQIQLQEELL-KNGVKVSSMELDLTQNDAPKE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   148 AYSKVAAMLQDRGLwaVINNAGV---LGFPTDGELLLMTDYkqcmAVNFFGTVEVTKTFLPLL-RKSKGRLVNVSSMGGG 223
Cdd:PRK12859  86 LLNKVTEQLGYPHI--LVNNAAYstnNDFSNLTAEELDKHY----MVNVRATTLLSSQFARGFdKKSGGRIINMTSGQFQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504503   224 APMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGgfltniaGTSDKW--EKLEKDILDHLP 288
Cdd:PRK12859 160 GPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG-------PTDTGWmtEEIKQGLLPMFP 219
PRK09135 PRK09135
pteridine reductase; Provisional
 83-288 1.72e-10

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 60.71  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGPGAE------ELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAML 156
Cdd:PRK09135   7 KVALITGGARRIGAAIARTLHAAGYRV---AIHYHRSAAEadalaaELNALRPGSAAALQADLLDPDALPELVAACVAAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QdrGLWAVINNAGVLgFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK09135  84 G--RLDALVNNASSF-YPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAERPLKGYPVYCAAK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4504503   237 AAVTMFSSVMRLELSKwGIKVASIQPGgflTNIAGTSDKW--EKLEKDILDHLP 288
Cdd:PRK09135 161 AALEMLTRSLALELAP-EVRVNAVAPG---AILWPEDGNSfdEEARQAILARTP 210
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 71-268 2.18e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 60.27  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    71 YLSGQELLpvDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLnengpgaeeLRRTCSpRLSVLQMDITK--------- 141
Cdd:PRK08945   3 YQPKPDLL--KDRIILVTGAGDGIGREAALTYARHGATV---IL---------LGRTEE-KLEAVYDEIEAaggpqpaii 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   142 PVQIKDA----YSKVAAMLQDR--GLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRL 214
Cdd:PRK08945  68 PLDLLTAtpqnYQQLADTIEEQfgRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASL 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4504503   215 VNVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN 268
Cdd:PRK08945 148 VFTSSSVGRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTA 201
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
83-290 2.19e-10

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 60.66  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSvLQMDITKPVQIKDAYSKVAAMLQDRGLw 162
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVTALGRRFLS-LTADLRKIDGIPALLERAVAEFGHIDI- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 aVINNAGVLGfPTDGELLLMTDYKQCMAVN----FFGTVEVTKTFLPllRKSKGRLVNVSSM---GGGApmeRLASYGSS 235
Cdd:PRK08993  89 -LVNNAGLIR-REDAIEFSEKDWDDVMNLNiksvFFMSQAAAKHFIA--QGNGGKIINIASMlsfQGGI---RVPSYTAS 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4504503   236 KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAE 290
Cdd:PRK08993 162 KSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAG 216
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 83-263 2.20e-10

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 60.31  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrGLW 162
Cdd:PRK12936   7 RKALVTGASGGIGEEIARLLHAQGAIV--GLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLE--GVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 AVINNAGVlgfPTDGELLLMTD--YKQCMAVNFFGTVEVTKTFL-PLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:PRK12936  83 ILVNNAGI---TKDGLFVRMSDedWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGM 159

                        170       180
                 ....*....|....*....|....
gi 4504503   240 TMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPG 183
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 83-281 2.91e-10

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: 60.38  E-value: 2.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRR---TCSPRLSVLQMDITKPVQIKDAYSKVaaMLQDR 159
Cdd:cd05355  27 KKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEETKKlieEEGRKCLLIPGDLGDESFCRDLVKEV--VKEFG 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  160 GLWAVINNAG-------VLGFPTdgELLLMTdykqcMAVNFFGTVEVTKTFLPLLrKSKGRLVNVSSMGGGAPMERLASY 232
Cdd:cd05355 105 KLDILVNNAAyqhpqesIEDITT--EQLEKT-----FRTNIFSMFYLTKAALPHL-KKGSSIINTTSVTAYKGSPHLLDY 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 4504503  233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEK 281
Cdd:cd05355 177 AATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSE 225
PRK07774 PRK07774
SDR family oxidoreductase;
81-288 2.93e-10

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 60.14  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEelrRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDR- 159
Cdd:PRK07774   5 DDKVAIVTGAAGGIGQAYAEALAREGASVV--VADINAEGAE---RVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVs 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 ---GLWAVINNAGVLGfPTDGELLLMTD---YKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGapmerLAS- 231
Cdd:PRK07774  80 afgGIDYLVNNAAIYG-GMKLDLLITVPwdyYKKFMSVNLDGALVCTRAVYKHMAKRGgGAIVNQSSTAAW-----LYSn 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504503   232 -YGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKwEKLEKDILDHLP 288
Cdd:PRK07774 154 fYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTP-KEFVADMVKGIP 210
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
81-263 3.00e-10

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 60.04  E-value: 3.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCK-YLDELGFTVFAGVlneNGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdr 159
Cdd:PRK07067   5 QGKVALLTGAASGIGEAVAErYLAEGARVVIADI---KPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGVLgfptDGELLL---MTDYKQCMAVNFFGTVEVTKTFLPLL--RKSKGRLVNVSSMGG--GAPMerLASY 232
Cdd:PRK07067  80 GIDILFNNAALF----DMAPILdisRDSYDRLFAVNVKGLFFLMQAVARHMveQGRGGKIINMASQAGrrGEAL--VSHY 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK07067 154 CATKAAVISYTQSAALALIRHGINVNAIAPG 184
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 83-263 4.24e-10

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: 59.78  E-value: 4.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVLN--ENGPGAEELRRTCSPRLSVLQMDITKPvqikdaySKVAAMLQDRG 160
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARV---VVNyyRSTESAEAVAAEAGERAIAIQADVRDR-------DQVQAMIEEAK 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LW-----AVINNAgVLGFPTDG------ELLLMTDYKQcmAVNFF--GTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPM 226
Cdd:cd05349  71 NHfgpvdTIVNNA-LIDFPFDPdqrktfDTIDWEDYQQ--QLEGAvkGALNLLQAVLPDFKERGsGRVINIGTNLFQNPV 147

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4504503  227 ERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05349 148 VPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGG 184
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 81-288 4.29e-10

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: 59.41  E-value: 4.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELRRTcsPRLSVLQMDITKPVQikdayskVAAMLQDRG 160
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEK--LKELERG--PGITTRVLDVTDKEQ-------VAALAKEEG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGvlGFPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGG---GAPMErlASYGS 234
Cdd:cd05368  70 RIDVLFNCA--GFVHHGSILDCEddDWDFAMNLNVRSMYLMIKAVLPkMLARKDGSIINMSSVASsikGVPNR--FVYST 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504503  235 SKAAVTMFSSVMRLELSKWGIKVASIQPGGF----LTNIAGTSDKWEKLEKDILDHLP 288
Cdd:cd05368 146 TKAAVIGLTKSVAADFAQQGIRCNAICPGTVdtpsLEERIQAQPDPEEALKAFAARQP 203
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 86-283 4.78e-10

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: 59.40  E-value: 4.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   86 LVTGGDCGLGHALCKYLDELGF--TVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPvqiKDAYSKVAAMLQDRG-LW 162
Cdd:cd05337   5 IVTGASRGIGRAIATELAARGFdiAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGEL---SDHEALLDQAWEDFGrLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVlGFPTDGELLLMTD--YKQCMAVNFFGTVEVTKTF-LPLLRKSK------GRLVNVSSMGGG-APMERlASY 232
Cdd:cd05337  82 CLVNNAGI-AVRPRGDLLDLTEdsFDRLIAINLRGPFFLTQAVaRRMVEQPDrfdgphRSIIFVTSINAYlVSPNR-GEY 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4504503  233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIagTSDKWEKLEKDI 283
Cdd:cd05337 160 CISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDM--TAPVKEKYDELI 208
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
79-289 5.12e-10

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 59.35  E-value: 5.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLN--ENGPGAEELR---RTCSPRLSVLQMDITKPVQIKDAYSKVA 153
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDI---AVNyaRSRKAAEETAeeiEALGRKALAVKANVGDVEKIKEMFAQID 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   154 AMLQdrGLWAVINNA--GVLGFPTDGElllMTDYKQCMAVN----FFGTVEVTKTflpLLRKSKGRLVNVSSMGGGAPME 227
Cdd:PRK08063  78 EEFG--RLDVFVNNAasGVLRPAMELE---ESHWDWTMNINakalLFCAQEAAKL---MEKVGGGKIISLSSLGSIRYLE 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504503   228 RLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPA 289
Cdd:PRK08063 150 NYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELLEDARAKTPA 211
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 83-267 5.57e-10

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: 59.13  E-value: 5.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVLNenGPGAEELRRTC---------SPRLSVLQMDITKPVQIKDAYSKVA 153
Cdd:cd05340   5 RIILVTGASDGIGREAALTYARYGATV---ILL--GRNEEKLRQVAdhineeggrQPQWFILDLLTCTSENCQQLAQRIA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  154 AMLQDrgLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASY 232
Cdd:cd05340  80 VNYPR--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAY 157

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4504503  233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:cd05340 158 AVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
PRK07074 PRK07074
SDR family oxidoreductase;
82-263 5.99e-10

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 59.40  E-value: 5.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAgvLNENGPGAEELRRTCS-PRLSVLQMDITKPVQIKDAYSKVAAmlqDRG 160
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLA--LDIDAAALAAFADALGdARFVPVACDLTDAASLAAALANAAA---ERG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAV-INNAGVlgfpTDGELLLMTD---YKQCMAVNFFGTVEVTKTFL-PLLRKSKGRLVNVSSMGG----GAPmerlaS 231
Cdd:PRK07074  77 PVDVlVANAGA----ARAASLHDTTpasWRADNALNLEAAYLCVEAVLeGMLKRSRGAVVNIGSVNGmaalGHP-----A 147

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504503   232 YGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK07074 148 YSAAKAGLIHYTKLLAVEYGRFGIRANAVAPG 179
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
83-272 6.69e-10

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 58.93  E-value: 6.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAE--ELRRtcsPRLSVLQMDITKPVQIKDAYSKVAAMLQDRG 160
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKlaEQYN---SNLTFHSLDLQDVHELETNFNEILSSIQEDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAV--INNAGVLGfPTD----GEL-LLMTDYKqcmaVNFFGTVEVTKTFLPLL--RKSKGRLVNVSSMGGGAPMERLAS 231
Cdd:PRK06924  79 VSSIhlINNAGMVA-PIKpiekAESeELITNVH----LNLLAPMILTSTFMKHTkdWKVDKRVINISSGAAKNPYFGWSA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4504503   232 YGSSKAAVTMFSSVMRLE--LSKWGIKVASIQPGGFLTNIAGT 272
Cdd:PRK06924 154 YCSSKAGLDMFTQTVATEqeEEEYPVKIVAFSPGVMDTNMQAQ 196
PLN02253 PLN02253
xanthoxin dehydrogenase
 69-330 7.64e-10

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 59.45  E-value: 7.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    69 YTYLSGQELLpvdQKAVLVTGGDCGLGHALCKYLDELGFTV-FAGVLNENGpgaEELRRTC--SPRLSVLQMDITKPVQI 145
Cdd:PLN02253   8 ASSLPSQRLL---GKVALVTGGATGIGESIVRLFHKHGAKVcIVDLQDDLG---QNVCDSLggEPNVCFFHCDVTVEDDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   146 KDAyskVAAMLQDRG-LWAVINNAGVLGFP-TDGELLLMTDYKQCMAVN----FFGTVEVTKTFLPLLRKSKGRLVNVSS 219
Cdd:PLN02253  82 SRA---VDFTVDKFGtLDIMVNNAGLTGPPcPDIRNVELSEFEKVFDVNvkgvFLGMKHAARIMIPLKKGSIVSLCSVAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   220 -MGGGAPMerlaSYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAgtsdkweklekdiLDHLPaevQEDYGQD 298
Cdd:PLN02253 159 aIGGLGPH----AYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA-------------LAHLP---EDERTED 218

                        250       260       270
                 ....*....|....*....|....*....|..
gi 4504503   299 YILAQRNFLLLINSLASKDFSPvlRDIQHAIL 330
Cdd:PLN02253 219 ALAGFRAFAGKNANLKGVELTV--DDVANAVL 248
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 83-263 8.97e-10

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 58.86  E-value: 8.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGP--GAE----ELRRTCSPRLSVlQMDITKpvqIKDAYSKVAAML 156
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKV---VINYNSSkeAAEnlvnELGKEGHDVYAV-QADVSK---VEDANRLVEEAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDRG-LWAVINNAGVL---GFPTDGElllmTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLAS 231
Cdd:PRK12935  80 NHFGkVDILVNNAGITrdrTFKKLNR----EDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGQTN 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4504503   232 YGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12935 156 YSAAKAGMLGFTKSLALELAKTNVTVNAICPG 187
PRK06114 PRK06114
SDR family oxidoreductase;
75-263 9.34e-10

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 58.64  E-value: 9.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    75 QELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRR--TCSPRLSVLQMDITKPVQIKDAYSKV 152
Cdd:PRK06114   1 PQLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHieAAGRRAIQIAADVTSKADLRAAVART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   153 AAMLQdrGLWAVINNAGVLGfPTDGELLLMTDYKQCMAVNffgtveVTKTFLP-------LLRKSKGRLVNVSSMGGGAP 225
Cdd:PRK06114  81 EAELG--ALTLAVNAAGIAN-ANPAEEMEEEQWQTVMDIN------LTGVFLScqaearaMLENGGGSIVNIASMSGIIV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504503   226 MERL--ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06114 152 NRGLlqAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPG 191
PRK05854 PRK05854
SDR family oxidoreductase;
82-269 9.44e-10

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 59.31  E-value: 9.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVlVTGGDCGLGHALCKYLDELGFTVFAGVLNE-NGPGAEELRRTCSP--RLSVLQMDITkpvqikdAYSKVAA---- 154
Cdd:PRK05854  15 KRAV-VTGASDGLGLGLARRLAAAGAEVILPVRNRaKGEAAVAAIRTAVPdaKLSLRALDLS-------SLASVAAlgeq 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   155 MLQD-RGLWAVINNAGVLGFPT-----DG-ELLLMTdykqcmavNFFGTVEVTKTFLPLLRKSKGRLVNVSSMG------ 221
Cdd:PRK05854  87 LRAEgRPIHLLINNAGVMTPPErqttaDGfELQFGT--------NHLGHFALTAHLLPLLRAGRARVTSQSSIAarrgai 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504503   222 ---------GGAPMErlaSYGSSKAAVTMFSsvmrLELSK------WGIKVASIQPGGFLTNI 269
Cdd:PRK05854 159 nwddlnwerSYAGMR---AYSQSKIAVGLFA----LELDRrsraagWGITSNLAHPGVAPTNL 214
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
76-289 1.09e-09

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 58.38  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    76 ELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfAGVLNENGPGAEELRRTCSPRLSVLQMDItkpVQIKDAYSKVAAM 155
Cdd:PRK12481   2 QLFDLNGKVAIITGCNTGLGQGMAIGLAKAGADI-VGVGVAEAPETQAQVEALGRKFHFITADL---IQQKDIDSIVSQA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQDRG-LWAVINNAGVLgfpTDGELLLMT--DYKQCMAVN----FFGTVEVTKTFLPllRKSKGRLVNVSSM---GGGAp 225
Cdd:PRK12481  78 VEVMGhIDILINNAGII---RRQDLLEFGnkDWDDVININqktvFFLSQAVAKQFVK--QGNGGKIINIASMlsfQGGI- 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504503   226 meRLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPA 289
Cdd:PRK12481 152 --RVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAILERIPA 213
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 83-267 1.11e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 58.38  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRrtcsprlsVLQMDITKPvqikDAYSKVAAMLQDR--G 160
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVE--------FVAADLTTA----EGCAAVARAVLERlgG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVLGFPTDGELLLM-TDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPM-ERLASYGSSKA 237
Cdd:PRK06523  78 VDILVHVLGGSSAPAGGFAALTdEEWQDELNLNLLAAVRLDRALLPGMIARgSGVIIHVTSIQRRLPLpESTTAYAAAKA 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 4504503   238 AVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK06523 158 ALSTYSKSLSKEVAPKGVRVNTVSPGWIET 187
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 83-267 2.34e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 57.76  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFT-VFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRGL 161
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATiVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAM---VSQIEKEVGV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 WAV-INNAGVLG-FPtdgeLLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSK 236
Cdd:PRK07097  88 IDIlVNNAGIIKrIP----MLEMSaeDFRQVIDIDLNAPFIVSKAVIPsMIKKGHGKIINICSMMSELGRETVSAYAAAK 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK07097 164 GGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
PRK07062 PRK07062
SDR family oxidoreductase;
78-260 2.65e-09

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 57.36  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    78 LPVDQKAVLVTGGDCGLGHALCKYLDELGFTV-FAG-----------VLNENGPGAEELRRTCsprlsvlqmDITKPvqi 145
Cdd:PRK07062   4 IQLEGRVAVVTGGSSGIGLATVELLLEAGASVaICGrdeerlasaeaRLREKFPGARLLAARC---------DVLDE--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   146 kDAYSKVAAMLQDR--GLWAVINNAG---VLGF--PTDGELLLMTDYKqcmavnFFGTVEVTKTFLPLLRKS-KGRLVNV 217
Cdd:PRK07062  72 -ADVAAFAAAVEARfgGVDMLVNNAGqgrVSTFadTTDDAWRDELELK------YFSVINPTRAFLPLLRASaAASIVCV 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4504503   218 SSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASI 260
Cdd:PRK07062 145 NSLLALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSI 187
PRK08177 PRK08177
SDR family oxidoreductase;
83-271 2.68e-09

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 56.96  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLN-ENGPGAEELrrtcsPRLSVLQMDITKPVQIKdaysKVAAMLQDRGL 161
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGpQQDTALQAL-----PGVHIEKLDMNDPASLD----QLLQRLQGQRF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 WAVINNAGVLGfPTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSS------MGGGAPMerlASYG 233
Cdd:PRK08177  73 DLLFVNAGISG-PAHQSAADATaaEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSqlgsveLPDGGEM---PLYK 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4504503   234 SSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAG 271
Cdd:PRK08177 149 ASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGG 186
PRK06947 PRK06947
SDR family oxidoreductase;
81-279 3.00e-09

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 57.12  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTV---FAGvlneNGPGAEE---LRRTCSPRLSVLQMDITKPVQIKDAYSKVAA 154
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVginYAR----DAAAAEEtadAVRAAGGRACVVAGDVANEADVIAMFDAVQS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   155 MLQdrGLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK----GRLVNVSSMGG--GAPMER 228
Cdd:PRK06947  77 AFG--RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASrlGSPNEY 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4504503   229 LaSYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI---AGTSDKWEKL 279
Cdd:PRK06947 155 V-DYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIhasGGQPGRAARL 207
PRK09242 PRK09242
SDR family oxidoreductase;
75-262 3.44e-09

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 57.06  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    75 QELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGA--EELRRTCSPR-LSVLQMDITKPV---QIKDA 148
Cdd:PRK09242   2 QHRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQarDELAEEFPEReVHGLAADVSDDEdrrAILDW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   149 YSKVAAmlqdrGLWAVINNAG------VLGFPTDgelllmtDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMG 221
Cdd:PRK09242  82 VEDHWD-----GLHILVNNAGgnirkaAIDYTED-------EWRGIFETNLFSAFELSRYAHPLLKQHAsSAIVNIGSVS 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4504503   222 GGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQP 262
Cdd:PRK09242 150 GLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAP 190
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 81-281 4.83e-09

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 56.31  E-value: 4.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpgAEELRRTCSpRLSVLQM---DITKPVQIKDAYSKVAAMLQ 157
Cdd:PRK05786   4 KGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENK--LKRMKKTLS-KYGNIHYvvgDVSSTESARNVIEKAAKVLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 drGLWAVINNAGvlGFPTDG-----ELLLMtdykqcMAVNFFGTVEVTKTFLPLLRKSKGrLVNVSSMGG-GAPMERLAS 231
Cdd:PRK05786  81 --AIDGLVVTVG--GYVEDTveefsGLEEM------LTNHIKIPLYAVNASLRFLKEGSS-IVLVSSMSGiYKASPDQLS 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504503   232 YGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGfltnIAGT---SDKWEKLEK 281
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPTT----ISGDfepERNWKKLRK 198
PRK06398 PRK06398
aldose dehydrogenase; Validated
 83-239 5.45e-09

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 56.38  E-value: 5.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELrrtcsprlsvLQMDITKPVQIKDAYSKVAAmlQDRGLW 162
Cdd:PRK06398   7 KVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDY----------FKVDVSNKEQVIKGIDYVIS--KYGRID 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4504503   163 AVINNAGVLGFPTDgELLLMTDYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:PRK06398  75 ILVNNAGIESYGAI-HAVEEDEWDRIINVNVNGIFLMSKYTIPyMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 83-267 5.55e-09

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 56.44  E-value: 5.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGA--EELRRTCSPRLSVlQMDITKPVQIKDAYSKVAAMLQDRG 160
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAvaDEINKAGGKAIGV-AMDVTNEDAVNAGIDKVAERFGSVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LwaVINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGG--GAPMErlASYGSSK 236
Cdd:PRK13394  87 I--LVSNAGI-QIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSheASPLK--SAYVTAK 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK13394 162 HGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 83-286 5.68e-09

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: 56.30  E-value: 5.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVF-AGVLNENG-PG-AEELRRTCSPRLSVlQMDITKPVQIKDAYSKVAAMLQDR 159
Cdd:cd09763   4 KIALVTGASRGIGRGIALQLGEAGATVYiTGRTILPQlPGtAEEIEARGGKCIPV-RCDHSDDDEVEALFERVAREQQGR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  160 gLWAVINNA--GV-LGFPTDG-----ELLLMTDykqCM---------AVNFFGTvevtktflPLLRKS-KGRLVNVSSMG 221
Cdd:cd09763  83 -LDILVNNAyaAVqLILVGVAkpfweEPPTIWD---DInnvglrahyACSVYAA--------PLMVKAgKGLIVIISSTG 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  222 GGAPMERLAsYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN-----IAGTSDKWEKLEKDILDH 286
Cdd:cd09763 151 GLEYLFNVA-YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTElvlemPEDDEGSWHAKERDAFLN 219
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 81-238 5.96e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 56.17  E-value: 5.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFT--VFAGVLNENGPG-AEELRRTCSPRLSVlQMDITKPVQIKDAyskVAAMLQ 157
Cdd:PRK06198   5 DGKVALVTGGTQGLGAAIARAFAERGAAglVICGRNAEKGEAqAAELEALGAKAVFV-QADLSDVEDCRRV---VAAADE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 DRG-LWAVINNAGVlgfpTDGELLLMTD---YKQCMAVN----FFGTVEVTKTFLPllRKSKGRLVNVSSMG--GGAPMe 227
Cdd:PRK06198  81 AFGrLDALVNAAGL----TDRGTILDTSpelFDRHFAVNvrapFFLMQEAIKLMRR--RKAEGTIVNIGSMSahGGQPF- 153

                        170
                 ....*....|.
gi 4504503   228 rLASYGSSKAA 238
Cdd:PRK06198 154 -LAAYCASKGA 163
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 83-272 6.24e-09

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: 56.25  E-value: 6.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFA-----------------GVLNENGPGAEELRRTCSPrlsvLQMDITKPVQI 145
Cdd:cd05338   4 KVAFVTGASRGIGRAIALRLAKAGATVVVaaktasegdngsakslpGTIEETAEEIEAAGGQALP----IVVDVRDEDQV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  146 KDAYSKVAAmlQDRGLWAVINNAG------VLGFPTDgELLLMTDykqcmaVNFFGTVEVTKTFLPLLRKS-KGRLVNVS 218
Cdd:cd05338  80 RALVEATVD--QFGRLDILVNNAGaiwlslVEDTPAK-RFDLMQR------VNLRGTYLLSQAALPHMVKAgQGHILNIS 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 4504503  219 SMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGT 272
Cdd:cd05338 151 PPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAAT 204
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 83-263 6.49e-09

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: 55.98  E-value: 6.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAgvLNENGPGAEELRRTC----SPRLSVLQMDITKPVQIKDAYSKVAAMLQd 158
Cdd:cd05343   7 RVALVTGASVGIGAAVARALVQHGMKVVG--CARRVDKIEALAAECqsagYPTLFPYQCDLSNEEQILSMFSAIRTQHQ- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 rGLWAVINNAGvLGFPtdgELLL---MTDYKQCMAVNFFGTVEVTKTFLPLLRKSK---GRLVNVSSMGGG--APMERLA 230
Cdd:cd05343  84 -GVDVCINNAG-LARP---EPLLsgkTEGWKEMFDVNVLALSICTREAYQSMKERNvddGHIININSMSGHrvPPVSVFH 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4504503  231 SYGSSKAAVTMFSSVMRLEL--SKWGIKVASIQPG 263
Cdd:cd05343 159 FYAATKHAVTALTEGLRQELreAKTHIRATSISPG 193
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 78-262 7.64e-09

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 56.33  E-value: 7.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    78 LPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGPG------AEELRRTCSPRLSVLQmDITkpvQIKDAYSK 151
Cdd:PRK07792   8 TDLSGKVAVVTGAAAGLGRAEALGLARLGATV---VVNDVASAldasdvLDEIRAAGAKAVAVAG-DIS---QRATADEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   152 VAAMLQDRGLWAVINNAGVLgfpTDGELLLMTD--YKQCMAVNFFGTVEVTKTFLPLLR-KSK-------GRLVNVSSMG 221
Cdd:PRK07792  81 VATAVGLGGLDIVVNNAGIT---RDRMLFNMSDeeWDAVIAVHLRGHFLLTRNAAAYWRaKAKaaggpvyGRIVNTSSEA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 4504503   222 GGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQP 262
Cdd:PRK07792 158 GLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK09009 PRK09009
SDR family oxidoreductase;
83-263 7.83e-09

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 55.84  E-value: 7.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDE--LGFTVFAgVLNENGPGAEElrrtcsPRLSVLQMDITKPVQIKdAYSKVAAMLQdrg 160
Cdd:PRK09009   1 MNILIVGGSGGIGKAMVKQLLEryPDATVHA-TYRHHKPDFQH------DNVQWHALDVTDEAEIK-QLSEQFTQLD--- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 lWaVINNAGVLGFPTDG--ELLLMTD---YKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLA---S 231
Cdd:PRK09009  70 -W-LINCVGMLHTQDKGpeKSLQALDadfFLQNITLNTLPSLLLAKHFTPKLKQSeSAKFAVISAKVGSISDNRLGgwyS 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 4504503   232 YGSSKAAVTMFSSVMRLELS---KWGIkVASIQPG 263
Cdd:PRK09009 148 YRASKAALNMFLKTLSIEWQrslKHGV-VLALHPG 181
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 81-274 9.00e-09

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 55.73  E-value: 9.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCK-YLDElGFTVfaGVLNENGPGAEELRRTCSPRLSVLQMDITKpvqiKDAYSKVAAMLQDR 159
Cdd:PRK06200   5 HGQVALITGGGSGIGRALVErFLAE-GARV--AVLERSAEKLASLRQRFGDHVLVVEGDVTS----YADNQRAVDQTVDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 --GLWAVINNAGVLGFPT-----DGElLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLV---NVSSM--GGGAPMe 227
Cdd:PRK06200  78 fgKLDCFVGNAGIWDYNTslvdiPAE-TLDTAFDEIFNVNVKGYLLGAKAALPALKASGGSMIftlSNSSFypGGGGPL- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4504503   228 rlasYGSSKAAVTMFSSVMRLELSKwGIKVASIQPGGFLTNIAGTSD 274
Cdd:PRK06200 156 ----YTASKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLRGPAS 197
PRK06172 PRK06172
SDR family oxidoreductase;
83-263 9.67e-09

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 55.53  E-value: 9.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNE-NGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDrgL 161
Cdd:PRK06172   8 KVALVTGGAAGIGRATALAFAREGAKVVVADRDAaGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGR--L 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   162 WAVINNAGVLGFPtdGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGG--GAPmeRLASYGSSK 236
Cdd:PRK06172  86 DYAFNNAGIEIEQ--GRLAEGSeaEFDAIMGVNVKGVWLCMKYQIPlMLAQGGGAIVNTASVAGlgAAP--KMSIYAASK 161

                        170       180
                 ....*....|....*....|....*..
gi 4504503   237 AAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06172 162 HAVIGLTKSAAIEYAKKGIRVNAVCPA 188
PRK07985 PRK07985
SDR family oxidoreductase;
81-267 1.03e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 56.16  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAvLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRR---TCSPRLSVLQMDITKPVQIKDAYSKVAAMLQ 157
Cdd:PRK07985  49 DRKA-LVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAQDVKKiieECGRKAVLLPGDLSDEKFARSLVHEAHKALG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 DRGLWAVInnAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSkGRLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:PRK07985 128 GLDIMALV--AGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAYQPSPHLLDYAATKA 204

                        170       180       190
                 ....*....|....*....|....*....|
gi 4504503   238 AVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK07985 205 AILNYSRGLAKQVAEKGIRVNIVAPGPIWT 234
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 83-263 1.24e-08

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: 55.55  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGV--LNENGPGAEELRR-TCSPRLSVLQMDITKPVQIKdAYSKVAAMLQDR 159
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGARVIMACrdMAKCEEAAAEIRRdTLNHEVIVRHLDLASLKSIR-AFAAEFLAEEDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  160 gLWAVINNAGVLGFP----TDGelllmtdYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMG--GG--------- 223
Cdd:cd09807  81 -LDVLINNAGVMRCPysktEDG-------FEMQFGVNHLGHFLLTNLLLDLLKKSApSRIVNVSSLAhkAGkinfddlns 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4504503  224 -APMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd09807 153 eKSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPG 193
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 82-263 1.40e-08

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: 54.64  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEelrrtcsprlSVLQMDITKPV-QIKDAYSKVAAMLQdrG 160
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADA----------SIIVLDSDSFTeQAKQVVASVARLSG--K 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 LWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSkGRLVNVSSMGGGAPMERLASYGSSKAAVT 240
Cdd:cd05334  69 VDALICVAGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSG-GLLVLTGAKAALEPTPGMIGYGAAKAAVH 147

                       170       180
                ....*....|....*....|....*
gi 4504503  241 MFSSVMRLELS--KWGIKVASIQPG 263
Cdd:cd05334 148 QLTQSLAAENSglPAGSTANAILPV 172
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 78-263 1.81e-08

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 54.70  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    78 LPVDQKAVLVTGGD--CGLGHALCKYLDELGFTVFA------GVLNENGPG-------AEELRRTcSPRLSVLQMDITKP 142
Cdd:PRK12748   1 LPLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspyDKTMPWGMHdkepvllKEEIESY-GVRCEHMEIDLSQP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   143 vqikDAYSKVAAMLQDR--GLWAVINNAGVLGFPTDGELLL-MTD--YKQCMAVNFFGTVEVTKTFLPllrKSKGRLVNV 217
Cdd:PRK12748  80 ----YAPNRVFYAVSERlgDPSILINNAAYSTHTRLEELTAeQLDkhYAVNVRATMLLSSAFAKQYDG---KAGGRIINL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 4504503   218 SSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12748 153 TSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 81-271 2.34e-08

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: 54.67  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   81 DQKAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSVLQMDITKpvqIKDAYSKVAAMLQDRG 160
Cdd:cd05348   3 KGEVALITGGGSGLGRALVERFVAEGAKV--AVLDRSAEKVAELRADFGDAVVGVEGDVRS---LADNERAVARCVERFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  161 -LWAVINNAGVLGFPTD----GELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSM-----GGGAPMerla 230
Cdd:cd05348  78 kLDCFIGNAGIWDYSTSlvdiPEEKLDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNagfypGGGGPL---- 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4504503  231 sYGSSKAAVTMFSSVMRLELSKWgIKVASIQPGGFLTNIAG 271
Cdd:cd05348 154 -YTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRG 192
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 83-263 2.77e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 54.65  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGpGAEELRRTCSP---RLSVLQMDITKPVQIKDAyskVAAMLQDR 159
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHE-DANETKQRVEKegvKCLLIPGDVSDEAFCKDA---VEETVREL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 G-LWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLrKSKGRLVNVSSMGGGAPMERLASYGSSKAA 238
Cdd:PRK06701 123 GrLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQGSAIINTGSITGYEGNETLIDYSATKGA 201

                        170       180
                 ....*....|....*....|....*
gi 4504503   239 VTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06701 202 IHAFTRSLAQSLVQKGIRVNAVAPG 226
PRK06124 PRK06124
SDR family oxidoreductase;
83-275 3.61e-08

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 53.95  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGftvfAGVLnENGPGAEELRRTCSP------RLSVLQMDITKPVQIKDAYskVAAML 156
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAG----AHVL-VNGRNAATLEAAVAAlraaggAAEALAFDIADEEAVAAAF--ARIDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDRGLWAVINNAGV-----LGFPTDGELLLMTDykqcmaVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLA 230
Cdd:PRK06124  85 EHGRLDILVNNVGArdrrpLAELDDAAIRALLE------TDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVARAGDA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4504503   231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT--NIAGTSDK 275
Cdd:PRK06124 159 VYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATetNAAMAADP 205
PRK08251 PRK08251
SDR family oxidoreductase;
83-263 4.37e-08

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 53.79  E-value: 4.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGH-------------ALC----KYLDELGftvfagvlnengpgAEELRRTCSPRLSVLQMDITKpvqi 145
Cdd:PRK08251   3 QKILITGASSGLGAgmarefaakgrdlALCarrtDRLEELK--------------AELLARYPGIKVAVAALDVND---- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   146 KDAYSKVAAMLQDR--GLWAVINNAGV-LGFPtdgellLMTDY----KQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNV 217
Cdd:PRK08251  65 HDQVFEVFAEFRDElgGLDRVIVNAGIgKGAR------LGTGKfwanKATAETNFVAALAQCEAAMEIFREQgSGHLVLI 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 4504503   218 SSMGGGAPMER-LASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK08251 139 SSVSAVRGLPGvKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPG 185
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 83-293 4.93e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 53.51  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENG--PGAEELRRTCSPRLSVLQMDITKPvqikDAYSKVAAMLQDRG 160
Cdd:PRK06125   8 KRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADAleALAADLRAAHGVDVAVHALDLSSP----EAREQLAAEAGDID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LwaVINNAGvlGFPTdGELLLMTD--YKQCMAVNFFGTVEVTKTFLPLLR-KSKGRLVNVSSMGGGAPMerlASY--GSS 235
Cdd:PRK06125  84 I--LVNNAG--AIPG-GGLDDVDDaaWRAGWELKVFGYIDLTRLAYPRMKaRGSGVIVNVIGAAGENPD---ADYicGSA 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504503   236 -KAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN------------IAGTSDKWEKLekdiLDHLP----AEVQE 293
Cdd:PRK06125 156 gNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDrmltllkgraraELGDESRWQEL----LAGLPlgrpATPEE 226
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 43-257 4.95e-08

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 54.10  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    43 GLCAVCLLILSPFWGLILFSVSCF---------LMYTYLS----GQELLPVDQKAvLVTGGDCGLGHALCKYLDELGFTV 109
Cdd:PLN02780   2 ELCFVDKLKSQPLWLLVLFVLGSLsilkffftiLNWVYVYflrpAKNLKKYGSWA-LVTGPTDGIGKGFAFQLARKGLNL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   110 FagVLNENGPGAEELRRTCSPRLSVLQM---------DITKPVQ-IKDAYSKVaamlqDRGLwaVINNAGVlGFP----- 174
Cdd:PLN02780  81 V--LVARNPDKLKDVSDSIQSKYSKTQIktvvvdfsgDIDEGVKrIKETIEGL-----DVGV--LINNVGV-SYPyarff 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   175 --TDGELLlmtdyKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNvssMGGGA----PMERL-ASYGSSKAAVTMFSSVM 246
Cdd:PLN02780 151 heVDEELL-----KNLIKVNVEGTTKVTQAVLPgMLKRKKGAIIN---IGSGAaiviPSDPLyAVYAATKAYIDQFSRCL 222

                        250
                 ....*....|.
gi 4504503   247 RLELSKWGIKV 257
Cdd:PLN02780 223 YVEYKKSGIDV 233
PRK06953 PRK06953
SDR family oxidoreductase;
83-241 6.87e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 52.77  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVlnENGPGAEELRRTCSprlSVLQMDITKPVQIkdaySKVAAMLQDRGLW 162
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATA--RDAAALAALQALGA---EALALDVADPASV----AGLAWKLDGEALD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 AVINNAGVLGFPTDG-ELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSS-MG--GGAPMERLASYGSSKAA 238
Cdd:PRK06953  73 AAVYVAGVYGPRTEGvEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSrMGsiGDATGTTGWLYRASKAA 152


                 ...
gi 4504503   239 VTM 241
Cdd:PRK06953 153 LND 155
PRK09186 PRK09186
flagellin modification protein A; Provisional
 81-268 7.98e-08

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 53.07  E-value: 7.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGdCGL-GHALCKYLDELGFTVFAGVLNEngPGAEELRRTC-----SPRLSVLQMDITKPVQIKDAYSKVaa 154
Cdd:PRK09186   3 KGKTILITGA-GGLiGSALVKAILEAGGIVIAADIDK--EALNELLESLgkefkSKKLSLVELDITDQESLEEFLSKS-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   155 mlqdRGLWAVINNAGVLGFPTD---GELLLMTDYKQ-CMAVN------FFGTVEVTKTFLpllRKSKGRLVNVSSMGG-- 222
Cdd:PRK09186  78 ----AEKYGKIDGAVNCAYPRNkdyGKKFFDVSLDDfNENLSlhlgssFLFSQQFAKYFK---KQGGGNLVNISSIYGvv 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4504503   223 --------GAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTN 268
Cdd:PRK09186 151 apkfeiyeGTSMTSPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDN 204
PRK07775 PRK07775
SDR family oxidoreductase;
81-314 1.35e-07

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.45  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVLVTGGDCGLGHALCKYLDELGFTVFAGV-----LNENgpgAEELRRTCSPRLSVlQMDITKPVQIKDAYSKVAAM 155
Cdd:PRK07775   9 DRRPALVAGASSGIGAATAIELAAAGFPVALGArrvekCEEL---VDKIRADGGEAVAF-PLDVTDPDSVKSFVAQAEEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQDrgLWAVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMGGGAPMERLASY 232
Cdd:PRK07775  85 LGE--IEVLVSGAGDTYF---GKLHEISteQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSDVALRQRPHMGAY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTsdkweklekdildhLPAEVQEDYGQDYI---LAQRNFLLL 309
Cdd:PRK07775 160 GAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWS--------------LPAEVIGPMLEDWAkwgQARHDYFLR 225


                 ....*
gi 4504503   310 INSLA 314
Cdd:PRK07775 226 ASDLA 230
PRK06128 PRK06128
SDR family oxidoreductase;
86-267 1.56e-07

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 52.55  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    86 LVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEE---LRRTCSPRLSVLQMDITKPVQIKDAYSKvaAMLQDRGLW 162
Cdd:PRK06128  59 LITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEvvqLIQAEGRKAVALPGDLKDEAFCRQLVER--AVKELGGLD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   163 AVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLrKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMF 242
Cdd:PRK06128 137 ILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSIQSYQPSPTLLDYASTKAAIVAF 215

                        170       180
                 ....*....|....*....|....*
gi 4504503   243 SSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK06128 216 TKALAKQVAEKGIRVNAVAPGPVWT 240
PRK06123 PRK06123
SDR family oxidoreductase;
82-269 2.13e-07

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 51.70  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    82 QKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLnENGPGAEELR---RTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQD 158
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYL-RNRDAAEAVVqaiRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 rgLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTV----EVTKTFLPLLRKSKGRLVNVSSMGG--GAPMERLaSY 232
Cdd:PRK06123  81 --LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFlcarEAVKRMSTRHGGRGGAIVNVSSMAArlGSPGEYI-DY 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK06123 158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI 194
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 83-263 2.54e-07

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 51.26  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENgPGAEELRRTcsprlsvLQMditkpvqIKDAYSKVAAMLQD---- 158
Cdd:PRK06077   7 KVVVVTGSGRGIGRAIAVRLAKEGSLV---VVNAK-KRAEEMNET-------LKM-------VKENGGEGIGVLADvstr 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 --------------RGLWAVINNAGV-LGFP---TDGELLlmtdyKQCMAVNFFGTVEVTKTFLPLLRKSkGRLVNVSSM 220
Cdd:PRK06077  69 egcetlakatidryGVADILVNNAGLgLFSPflnVDDKLI-----DKHISTDFKSVIYCSQELAKEMREG-GAIVNIASV 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4504503   221 GGGAPMERLASYGSSKAAVTMFSSVMRLELSKwGIKVASIQPG 263
Cdd:PRK06077 143 AGIRPAYGLSIYGAMKAAVINLTKYLALELAP-KIRVNAIAPG 184
PRK12746 PRK12746
SDR family oxidoreductase;
80-269 2.99e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 51.19  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    80 VDQKAVLVTGGDCGLGHALCKYLDELGFTVfAGVLNENGPGAEELRRTCSP---RLSVLQMDITKPVQIKDAYSKVAAML 156
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALV-AIHYGRNKQAADETIREIESnggKAFLIEADLNSIDGVKKLVEQLKNEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   157 QDR----GLWAVINNAGVlgfPTDGELLLMTD--YKQCMAVNFFGTVEVTKTFLPLLRkSKGRLVNVSSMGGGAPMERLA 230
Cdd:PRK12746  83 QIRvgtsEIDILVNNAGI---GTQGTIENTTEeiFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSI 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4504503   231 SYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 83-277 3.27e-07

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: 50.95  E-value: 3.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENgpGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQdrgLW 162
Cdd:cd08951   8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQK--RAADAKAACPGAAGVLIGDLSSLAETRKLADQVNAIGR---FD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVLGfpTDGELLLMTDYKQCMAVNFFGTVEVTKtflpLLRKSKgRLVNVSS---MGGGAPMERL---------- 229
Cdd:cd08951  83 AVIHNAGILS--GPNRKTPDTGIPAMVAVNVLAPYVLTA----LIRRPK-RLIYLSSgmhRGGNASLDDIdwfnrgends 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4504503  230 ASYGSSKAAVTMFSSVMRLELSKwgIKVASIQPGGFLTNI--AGTSDKWE 277
Cdd:cd08951 156 PAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKMggAGAPDDLE 203
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 173-272 3.50e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 51.11  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   173 FPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSK 252
Cdd:PRK07576  98 FPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGP 177

                         90       100
                 ....*....|....*....|
gi 4504503   253 WGIKVASIQPGgfltNIAGT 272
Cdd:PRK07576 178 EGIRVNSIVPG----PIAGT 193
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 76-267 4.24e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 50.54  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    76 ELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGP----GAEELRRTCSPRLSVLQMDITKPVQIKDAysk 151
Cdd:PRK07523   4 NLFDLTGRRALVTGSSQGIGYALAEGLAQAGAEV---ILNGRDPaklaAAAESLKGQGLSAHALAFDVTDHDAVRAA--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   152 VAAMLQDRG-LWAVINNAGVL------GFPTDG-ELLLMTDykqcMAVNFFGTVEVTKtflPLLRKSKGRLVNVSSMGGG 223
Cdd:PRK07523  78 IDAFEAEIGpIDILVNNAGMQfrtpleDFPADAfERLLRTN----ISSVFYVGQAVAR---HMIARGAGKIINIASVQSA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 4504503   224 APMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLT 267
Cdd:PRK07523 151 LARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK07814 PRK07814
SDR family oxidoreductase;
81-281 5.71e-07

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 50.55  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQKAVlVTGGDCGLGHALCKYLDELGFTVF--AGVLNENGPGAEELRRTCSpRLSVLQMDITKPvqiKDAYSKVAAMLQD 158
Cdd:PRK07814  10 DQVAV-VTGAGRGLGAAIALAFAEAGADVLiaARTESQLDEVAEQIRAAGR-RAHVVAADLAHP---EATAGLAGQAVEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RG-LWAVINNAGvlgfPTDGELLLMT---DYKQCMAVNFFGTVEVTKTFLPLLRKSK--GRLVNVSSMGGGAPMERLASY 232
Cdd:PRK07814  85 FGrLDIVVNNVG----GTMPNPLLSTstkDLADAFTFNVATAHALTVAAVPLMLEHSggGSVINISSTMGRLAGRGFAAY 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504503   233 GSSKAAVTMFSSVMRLELSKwGIKVASIQPGGFLTN----IAGTSDKWEKLEK 281
Cdd:PRK07814 161 GTAKAALAHYTRLAALDLCP-RIRVNAIAPGSILTSalevVAANDELRAPMEK 212
PRK07035 PRK07035
SDR family oxidoreductase;
77-288 6.00e-07

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 50.40  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    77 LLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVF------------AGVLNENGPGAEELrrTCSprlsVLQMDitkpvQ 144
Cdd:PRK07035   3 LFDLTGKIALVTGASRGIGEAIAKLLAQQGAHVIvssrkldgcqavADAIVAAGGKAEAL--ACH----IGEME-----Q 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   145 IKDAYSKVAAmlqDRG-LWAVINNAGVlgFPTDGELLlMTD---YKQCMAVN----FFGTVEVTKtflpLLRKS-KGRLV 215
Cdd:PRK07035  72 IDALFAHIRE---RHGrLDILVNNAAA--NPYFGHIL-DTDlgaFQKTVDVNirgyFFMSVEAGK----LMKEQgGGSIV 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504503   216 NVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLP 288
Cdd:PRK07035 142 NVASVNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQALAHIP 214
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 79-264 7.40e-07

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: 49.83  E-value: 7.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITkpvQIKDAYSKVAAMLQD 158
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDAAHVHTADLE---TYAGAQGVVRAAVER 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 RG-LWAVINNAG--VLGFP---TDGELLlmtdyKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSSMG--GGapmeRL 229
Cdd:cd08937  78 FGrVDVLINNVGgtIWAKPyehYEEEQI-----EAEIRRSLFPTLWCCRAVLPhMLERQQGVIVNVSSIAtrGI----YR 148

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4504503  230 ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGG 264
Cdd:cd08937 149 IPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGG 183
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 80-263 1.24e-06

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: 49.15  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   80 VDQKAVLVTGGDCGLGHALCK-YLDELGFTVFAGV-LNENGPGAEELrrtcSPRLSVLQMDITKPVQIKDAYSkvAAMLQ 157
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQaYVREGARVAIADInLEAARATAAEI----GPAACAISLDVTDQASIDRCVA--ALVDR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  158 DRGLWAVINNAGVLGFptdGELLLMT--DYKQCMAVNFFGTV----EVTKTFLPLLRKskGRLVNVSSMGGGAPMERLAS 231
Cdd:cd05363  75 WGSIDILVNNAALFDL---APIVDITreSYDRLFAINVSGTLfmmqAVARAMIAQGRG--GKIINMASQAGRRGEALVGV 149

                       170       180       190
                ....*....|....*....|....*....|..
gi 4504503  232 YGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd05363 150 YCATKAAVISLTQSAGLNLIRHGINVNAIAPG 181
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 84-263 1.57e-06

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: 49.69  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   84 AVLVTGGDCGLGHALCKYLDELGFTVFAgVLNENGPGAEE-----LRRTCSPRLSVLQMDITKPVQIKDAYSKVAAmlqD 158
Cdd:cd05274 152 TYLITGGLGGLGLLVARWLAARGARHLV-LLSRRGPAPRAaaraaLLRAGGARVSVVRCDVTDPAALAALLAELAA---G 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  159 RGLWAVINNAGVLgfpTDGELLLMT--DYKQCMAVNffgtVEVTKTFLPLLRKSKG-RLVNVSSMGG--GAPmeRLASYG 233
Cdd:cd05274 228 GPLAGVIHAAGVL---RDALLAELTpaAFAAVLAAK----VAGALNLHELTPDLPLdFFVLFSSVAAllGGA--GQAAYA 298

                       170       180       190
                ....*....|....*....|....*....|
gi 4504503  234 SSKAAVTMFSSVMRLElskwGIKVASIQPG 263
Cdd:cd05274 299 AANAFLDALAAQRRRR----GLPATSVQWG 324
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 164-263 1.67e-06

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: 48.76  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    164 VINNAGVLGFPTDGELLLmTDYKQCM---AVNFFGTVEVTKTFLPLLRKSKG---RLVNVSSMGGGAPMERLASYGSSKA 237
Cdd:TIGR01500  91 LINNAGTLGDVSKGFVDL-SDSTQVQnywALNLTSMLCLTSSVLKAFKDSPGlnrTVVNISSLCAIQPFKGWALYCAGKA 169

                          90       100
                  ....*....|....*....|....*.
gi 4504503    238 AVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:TIGR01500 170 ARDMLFQVLALEEKNPNVRVLNYAPG 195
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 83-263 2.25e-06

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: 48.43  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVF------AGVLNENGPGAEELRRTCsprlSVLQMDITKPvqikDAYSKV--AA 154
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVvhynrsEAEAQRLKDELNALRNSA----VLVQADLSDF----AACADLvaAA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  155 MLQDRGLWAVINNAGVLgFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKS-KGRLVNVSSMGGGAPMERLASYG 233
Cdd:cd05357  73 FRAFGRCDVLVNNASAF-YPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSrNGSIINIIDAMTDRPLTGYFAYC 151

                       170       180       190
                ....*....|....*....|....*....|
gi 4504503  234 SSKAAVTMFSSVMRLELSKwGIKVASIQPG 263
Cdd:cd05357 152 MSKAALEGLTRSAALELAP-NIRVNGIAPG 180
PRK06196 PRK06196
oxidoreductase; Provisional
 72-297 2.57e-06

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 48.91  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    72 LSGQELlpvDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENgPGAEELRRTcsPRLSVLQMDITKPVQIKDAYSK 151
Cdd:PRK06196  19 LAGHDL---SGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPD-VAREALAGI--DGVEVVMLDLADLESVRAFAER 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   152 VAAMlqDRGLWAVINNAGVLGFPtdgELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMGGG------- 223
Cdd:PRK06196  93 FLDS--GRRIDILINNAGVMACP---ETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGaRVVALSSAGHRrspirwd 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   224 -----APMERLASYGSSKAAVTMFSsvmrLELSK----WGIKVASIQPGGFLTNiagtsdkwekLEKdildHLPAEVQED 294
Cdd:PRK06196 168 dphftRGYDKWLAYGQSKTANALFA----VHLDKlgkdQGVRAFSVHPGGILTP----------LQR----HLPREEQVA 229


                 ...
gi 4504503   295 YGQ 297
Cdd:PRK06196 230 LGW 232
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 83-279 2.72e-06

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 48.49  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSV-----LQMDITKPVQIK-------DAYS 150
Cdd:PRK12384   3 QVAVVIGGGQTLGAFLCHGLAEEGYRV--AVADINSEKAANVAQEINAEYGEgmaygFGADATSEQSVLalsrgvdEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   151 KVAAMlqdrglwavINNAGVL--GFPTDGELllmTDYKQCMAVNFFGTVEVTKTFLPLL--RKSKGRLVNVSSMGGGAPM 226
Cdd:PRK12384  81 RVDLL---------VYNAGIAkaAFITDFQL---GDFDRSLQVNLVGYFLCAREFSRLMirDGIQGRIIQINSKSGKVGS 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4504503   227 ERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLtniagTSDKWEKL 279
Cdd:PRK12384 149 KHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLL-----KSPMFQSL 196
PRK07102 PRK07102
SDR family oxidoreductase;
83-263 3.51e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 48.00  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVF-----AGVLNENgpgAEELRRTCSPRLSVLQMDITkpvqikdAYSKVAAMLQ 157
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLYlaardVERLERL---ADDLRARGAVAVSTHELDIL-------DTASHAAFLD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   158 DrgLWA----VINNAGVLG----FPTDGELLLMTdykqcMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGG--GAPM 226
Cdd:PRK07102  72 S--LPAlpdiVLIAVGTLGdqaaCEADPALALRE-----FRTNFEGPIALLTLLANRFEARGsGTIVGISSVAGdrGRAS 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504503   227 ERLasYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK07102 145 NYV--YGSAKAALTAFLSGLRNRLFKSGVHVLTVKPG 179
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 82-266 3.96e-06

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: 47.84  E-value: 3.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   82 QKAVLVTGGDCGLGHALCKYLDELGFTVfaGVLNENGPGAEELRRTCSPRLSV----LQMDITKPVQ-------IKDAYS 150
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAEAGYDV--AVADINSENAEKVADEINAEYGEkaygFGADATNEQSvialskgVDEIFK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  151 KVAAMLQDRGlWAVINnagvlgFPTDGELllmTDYKQCMAVNFFGTVEVTKTFLPLLRK--SKGRLVNVSSMGGGAPMER 228
Cdd:cd05322  80 RVDLLVYSAG-IAKSA------KITDFEL---GDFDRSLQVNLVGYFLCAREFSKLMIRdgIQGRIIQINSKSGKVGSKH 149

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4504503  229 LASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFL 266
Cdd:cd05322 150 NSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNLL 187
PRK06139 PRK06139
SDR family oxidoreductase;
79-263 4.39e-06

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 48.18  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    79 PVDQKAVLVTGGDCGLGHALCKYLDELGFTVfagVLNENGPGA-EELRRTCSPR---LSVLQMDITKPVQIKDAYSKVAA 154
Cdd:PRK06139   4 PLHGAVVVITGASSGIGQATAEAFARRGARL---VLAARDEEAlQAVAEECRALgaeVLVVPTDVTDADQVKALATQAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   155 MLQDRGLWavINNAGVlGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYG 233
Cdd:PRK06139  81 FGGRIDVW--VNNVGV-GAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGhGIFINMISLGGFAAQPYAAAYS 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   234 SSKAAVTMFSSVMRLELSKW-GIKVASIQPG 263
Cdd:PRK06139 158 ASKFGLRGFSEALRGELADHpDIHVCDVYPA 188
PRK05867 PRK05867
SDR family oxidoreductase;
76-269 8.76e-06

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 46.57  E-value: 8.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    76 ELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNengpgAEELRRTCSPRLSV------LQMDITKPVQIKDAY 149
Cdd:PRK05867   3 DLFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARH-----LDALEKLADEIGTSggkvvpVCCDVSQHQQVTSML 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   150 SKVAAMLQdrGLWAVINNAGVLGFPTDGELLLmTDYKQCMAVNffgtveVTKTFL-------PLLRKSKG-RLVNVSSMG 221
Cdd:PRK05867  78 DQVTAELG--GIDIAVCNAGIITVTPMLDMPL-EEFQRLQNTN------VTGVFLtaqaaakAMVKQGQGgVIINTASMS 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4504503   222 G---GAPmERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK05867 149 GhiiNVP-QQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 83-263 2.70e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 45.11  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENG--PGAEELRRTcsprlsVLQMDITKPVQIKDAYSkvAAMLQDRG 160
Cdd:PRK06057   8 RVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAgkAAADEVGGL------FVPTDVTDEDAVNALFD--TAAETYGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVlgFPTDGELLLMTD---YKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLVNVSS----MGGGAPMerlASY 232
Cdd:PRK06057  80 VDIAFNNAGI--SPPEDDSILNTGldaWQRVQDVNLTSVYLCCKAALPhMVRQGKGSIINTASfvavMGSATSQ---ISY 154

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06057 155 TASKGGVLAMSRELGVQFARQGIRVNALCPG 185
PRK06500 PRK06500
SDR family oxidoreductase;
83-263 4.46e-05

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 44.56  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCK-YLDELGFTVFAGVlneNGPGAEELRRTCSPRLSVLQMDITKPVQIKDayskVAAMLQDRG- 160
Cdd:PRK06500   7 KTALITGGTSGIGLETARqFLAEGARVAITGR---DPASLEAARAELGESALVIRADAGDVAAQKA----LAQALAEAFg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 -LWAVINNAGVLGF-PTdgELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNvSSMGGGAPMERLASYGSSKAA 238
Cdd:PRK06500  80 rLDAVFINAGVAKFaPL--EDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLN-GSINAHIGMPNSSVYAASKAA 156

                        170       180
                 ....*....|....*....|....*
gi 4504503   239 VTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK06500 157 LLSLAKTLSGELLPRGIRVNAVSPG 181
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 84-297 4.54e-05

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: 44.30  E-value: 4.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   84 AVLVTGGDCGLGHALCKYLDELGFTV--FAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDrgL 161
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSValAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGP--L 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  162 WAVINNAGvlGFpTDGELLLMT--DYKQCMAVNFFGTVEVTKTFLP-LLRKSKGRLV---NVSSMGGGAPmerLASYGSS 235
Cdd:cd05373  79 EVLVYNAG--AN-VWFPILETTprVFEKVWEMAAFGGFLAAREAAKrMLARGRGTIIftgATASLRGRAG---FAAFAGA 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504503  236 KAAVTMFSSVMRLELSKWGIKVAS-IQPGGFLTNIAGTS--DKWEKLEKD-ILDhlPAEVQEDYGQ 297
Cdd:cd05373 153 KFALRALAQSMARELGPKGIHVAHvIIDGGIDTDFIRERfpKRDERKEEDgILD--PDAIAEAYWQ 216
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 77-263 4.80e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 44.79  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    77 LLPVDQKAVLVTGGDCGLGHALCKYLDELGFTV-FAGVLNENGPGAEELRRTCSPRLSVL--QMDITKPVQIKDAyskVA 153
Cdd:PRK05875   2 QLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVmIVGRNPDKLAAAAEEIEALKGAGAVRyePADVTDEDQVARA---VD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   154 AMLQDRG-LWAVINNAGvlGFPTDGELLLMTD--YKQCMAVNFFGTVEVTK-TFLPLLRKSKGRLVNVSSMGGGAPMERL 229
Cdd:PRK05875  79 AATAWHGrLHGVVHCAG--GSETIGPITQIDSdaWRRTVDLNVNGTMYVLKhAARELVRGGGGSFVGISSIAASNTHRWF 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 4504503   230 ASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK05875 157 GAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPG 190
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 81-270 6.50e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 44.25  E-value: 6.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    81 DQ--KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLN-ENGPGAEELRRTCSPR--LSVLQMDITKPVQIKDAyskvAAM 155
Cdd:PRK06197  13 DQsgRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNlDKGKAAAARITAATPGadVTLQELDLTSLASVRAA----ADA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   156 LQDR--GLWAVINNAGVLGFP----TDG-ELLLMTdykqcmavNFFGTVEVTKTFLPLLRKSKG-RLVNVSSMG---GGA 224
Cdd:PRK06197  89 LRAAypRIDLLINNAGVMYTPkqttADGfELQFGT--------NHLGHFALTGLLLDRLLPVPGsRVVTVSSGGhriRAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504503   225 ----------PMERLASYGSSKAAVTMFSSVMRLELSKWG---IKVASiQPGGFLTNIA 270
Cdd:PRK06197 161 ihfddlqwerRYNRVAAYGQSKLANLLFTYELQRRLAAAGattIAVAA-HPGVSNTELA 218
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 163-272 6.84e-05

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: 43.27  E-value: 6.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  163 AVINNAGVlgfPTDGELLLMTDYKQCMA--VNFFGTVEVTKTFLPLL-RKSKGRLVNVSSMGGGAPMERLASYGSSKAAV 239
Cdd:cd02266  34 VVVHNAAI---LDDGRLIDLTGSRIERAirANVVGTRRLLEAARELMkAKRLGRFILISSVAGLFGAPGLGGYAASKAAL 110

                        90       100       110
                ....*....|....*....|....*....|...
gi 4504503  240 TMFSSVMRLELSKWGIKVASIQPGgfltNIAGT 272
Cdd:cd02266 111 DGLAQQWASEGWGNGLPATAVACG----TWAGS 139
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 83-288 7.07e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 43.90  E-value: 7.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELG-FTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAyskVAAMLQDRG- 160
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGaNVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKM---VEQIDEKFGr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGvlG-FPTDGELLLMTDYKQCMAV----NFFGTVEVTKTFLPllRKSKGRLVNVSSM---GGGAPMERLAsy 232
Cdd:PRK07677  79 IDALINNAA--GnFICPAEDLSVNGWNSVIDIvlngTFYCSQAVGKYWIE--KGIKGNIINMVATyawDAGPGVIHSA-- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504503   233 gSSKAAVTMFSSVMRLEL-SKWGIKVASIQPGGfLTNIAGTSDKW--EKLEKDILDHLP 288
Cdd:PRK07677 153 -AAKAGVLAMTRTLAVEWgRKYGIRVNAIAPGP-IERTGGADKLWesEEAAKRTIQSVP 209
PRK06194 PRK06194
hypothetical protein; Provisional
 83-239 1.31e-04

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 43.47  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFT-VFAGVLNEN-GPGAEELRRTCSPRLSVlQMDITKPVQIkDAYSKvAAMLQDRG 160
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKlVLADVQQDAlDRAVAELRAQGAEVLGV-RTDVSDAAQV-EALAD-AALERFGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   161 LWAVINNAGVLGfptdGELLL---MTDYKQCMAVNFFGTVEVTKTFLPLL-------RKSKGRLVNVSSMGGGAPMERLA 230
Cdd:PRK06194  84 VHLLFNNAGVGA----GGLVWensLADWEWVLGVNLWGVIHGVRAFTPLMlaaaekdPAYEGHIVNTASMAGLLAPPAMG 159


                 ....*....
gi 4504503   231 SYGSSKAAV 239
Cdd:PRK06194 160 IYNVSKHAV 168
PRK12742 PRK12742
SDR family oxidoreductase;
83-263 1.58e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 42.82  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTV---FAGvlneNGPGAEEL-RRTCSprlSVLQMDITKpvqiKDAyskVAAMLQD 158
Cdd:PRK12742   7 KKVLVLGGSRGIGAAIVRRFVTDGANVrftYAG----SKDAAERLaQETGA---TAVQTDSAD----RDA---VIDVVRK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   159 RG-LWAVINNAGVLGFpTDGELLLMTDYKQCMAVN----FFGTVEVTKTFlpllrKSKGRLVNVSSMGGG-APMERLASY 232
Cdd:PRK12742  73 SGaLDILVVNAGIAVF-GDALELDADDIDRLFKINihapYHASVEAARQM-----PEGGRIIIIGSVNGDrMPVAGMAAY 146

                        170       180       190
                 ....*....|....*....|....*....|.
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:PRK12742 147 AASKSALQGMARGLARDFGPRGITINVVQPG 177
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 83-269 2.70e-04

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 42.37  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    83 KAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAE---ELRRTCSPRLSVlQMDITKPVQIKDAYSKVAAMLQDR 159
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEEtvyEIQSNGGSAFSI-GANLESLHGVEALYSSLDNELQNR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 G----LWAVINNAGVlgfpTDGELLLMTD---YKQCMAVNFFGTVEVTKTFLPLLRKSKgRLVNVSSMGGGAPMERLASY 232
Cdd:PRK12747  84 TgstkFDILINNAGI----GPGAFIEETTeqfFDRMVSVNAKAPFFIIQQALSRLRDNS-RIINISSAATRISLPDFIAY 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4504503   233 GSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNI 269
Cdd:PRK12747 159 SMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
PRK07023 PRK07023
SDR family oxidoreductase;
86-272 3.23e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 41.92  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    86 LVTGGDCGLGHALCKYLDELGFTVFaGVLNENGPgaeELRRTCSPRLSVLQMDITKPVQIKD--AYSKVAAMLQDRGLWA 163
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAVL-GVARSRHP---SLAAAAGERLAEVELDLSDAAAAAAwlAGDLLAAFVDGASRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   164 VINNAGVLGfPT------DGELLLmtdykQCMAVNFFGTVEVTKTFL-----PLLRkskgRLVNVSSMGGGAPMERLASY 232
Cdd:PRK07023  81 LINNAGTVE-PIgplatlDAAAIA-----RAVGLNVAAPLMLTAALAqaasdAAER----RILHISSGAARNAYAGWSVY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4504503   233 GSSKAAVTMFSSVMRLELSKwGIKVASIQPGGFLTNIAGT 272
Cdd:PRK07023 151 CATKAALDHHARAVALDANR-ALRIVSLAPGVVDTGMQAT 189
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 151-263 7.26e-04

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: 40.99  E-value: 7.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  151 KVAAMLQDRGLwAVINNAGVLGFPTDGELLLMTDYKQC---------MAVN-FFGTV-----EV---------------T 200
Cdd:cd08936  49 RAVATLQGEGL-SVTGTVCHVGKAEDRERLVATAVNLHggvdilvsnAAVNpFFGNIldsteEVwdkildvnvkatalmT 127

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4504503  201 KTFLPLLRK-SKGRLVNVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPG 263
Cdd:cd08936 128 KAVVPEMEKrGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPG 191
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 160-270 7.69e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 40.68  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   160 GLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNffgtveVTKTFL-------PLLRKSKGRLVNVSS-MGGGAPMERLAS 231
Cdd:PRK07478  83 GLDIAFNNAGTLGEMGPVAEMSLEGWRETLATN------LTSAFLgakhqipAMLARGGGSLIFTSTfVGHTAGFPGMAA 156

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 4504503   232 YGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIA 270
Cdd:PRK07478 157 YAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMG 195
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 83-229 1.43e-03

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 39.89  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   83 KAVLVTGGDCGLGHALCKYLDELGFTVFagVLNENGPGAEELRR-----TCSPRLSVLQMDITKPVQIKDAYSKVAAmlQ 157
Cdd:cd09808   2 RSFLITGANSGIGKAAALAIAKRGGTVH--MVCRNQTRAEEARKeieteSGNQNIFLHIVDMSDPKQVWEFVEEFKE--E 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504503  158 DRGLWAVINNAGVLgfpTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKG-RLVNVSSmgGGAPMERL 229
Cdd:cd09808  78 GKKLHVLINNAGCM---VNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDpRVITVSS--GGMLVQKL 145
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 86-197 1.48e-03

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: 40.43  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   86 LVTGGDCGLGHALCKYLDE--------LGFTVFAGVLNENGPGAEELRRTcSPRLSVLQMDITKPVQIKDAYSKVAAMLQ 157
Cdd:cd08953 209 LVTGGAGGIGRALARALARrygarlvlLGRSPLPPEEEWKAQTLAALEAL-GARVLYISADVTDAAAVRRLLEKVRERYG 287

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4504503  158 DrgLWAVINNAGVLgfpTDGELLLMT--DYKQCMAVNFFGTV 197
Cdd:cd08953 288 A--IDGVIHAAGVL---RDALLAQKTaeDFEAVLAPKVDGLL 324
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
136-231 2.07e-03

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 39.21  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   136 QMDITKPVQIKDAyskVAAMlqDRGLWAVINNAGVLGFpTDGELLLmtdykqcmAVNFFGTVEVTKTFLPLLRKSkGRLV 215
Cdd:PRK12428  29 QADLGDPASIDAA---VAAL--PGRIDALFNIAGVPGT-APVELVA--------RVNFLGLRHLTEALLPRMAPG-GAIV 93

                         90
                 ....*....|....*.
gi 4504503   216 NVSSMGGGAPMERLAS 231
Cdd:PRK12428  94 NVASLAGAEWPQRLEL 109
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 84-305 2.26e-03

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: 39.53  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503     84 AVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPG---AEELRRTCSPRLSVLQMDITKPVQIKDAYSK-VAAMLQDR 159
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAstlAAELNARRPNSAVTCQADLSNSATLFSRCEAiIDACFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    160 GLWAV-INNAGVLgFPT------DGELLLMTDYKQCMAVNFFGTVEVTKTFL------------PLLRKSKGRLVNVSSM 220
Cdd:TIGR02685  83 GRCDVlVNNASAF-YPTpllrgdAGEGVGDKKSLEVQVAELFGSNAIAPYFLikafaqrqagtrAEQRSTNLSIVNLCDA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503    221 GGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLtniagtsdkweklekdILDHLPAEVQEDYGQDYI 300
Cdd:TIGR02685 162 MTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSL----------------LPDAMPFEVQEDYRRKVP 225


                  ....*
gi 4504503    301 LAQRN 305
Cdd:TIGR02685 226 LGQRE 230
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 85-272 3.07e-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: 38.37  E-value: 3.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503   85 VLVTGGDCGLGHALCKYLDELGFTVFAGVlnENGPGAEELRRtcsPRLSVLQMDITKPVQIKDAyskvaamlqDRGLWAV 164
Cdd:cd05243   2 VLVVGATGKVGRHVVRELLDRGYQVRALV--RDPSQAEKLEA---AGAEVVVGDLTDAESLAAA---------LEGIDAV 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504503  165 INNAGvlGFPTDGELLLMTDYkqcmavnffgtvEVTKTFLPLLRKSK-GRLVNVSSMGGGAPMERLASYGSS----KAAV 239
Cdd:cd05243  68 ISAAG--SGGKGGPRTEAVDY------------DGNINLIDAAKKAGvKRFVLVSSIGADKPSHPLEALGPYldakRKAE 133

                       170       180       190
                ....*....|....*....|....*....|...
gi 4504503  240 tmfssvmrLELSKWGIKVASIQPGGFLTNIAGT 272
Cdd:cd05243 134 --------DYLRASGLDYTIVRPGGLTDDPAGT 158
 
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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