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Conserved domains on  [gi|511847639|ref|XP_004748198|]
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3-hydroxybutyrate dehydrogenase type 2 [Mustela putorius furo]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143280)

SDR family NAD(P)-dependent oxidoreductase, a classical short-chain dehydrogenase similar to Escherichia coli UcpA or mammalian 3-hydroxybutyrate dehydrogenase type 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-245 3.10e-163

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: 451.15  E-value: 3.10e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVAGF 84
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCAGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  85 VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIGLTKSLAAD 164
Cdd:cd05368   81 VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTKAAVIGLTKSVAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 165 FIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIIDGGWS 244
Cdd:cd05368  161 FAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGGWS 240


                 .
gi 511847639 245 L 245
Cdd:cd05368  241 L 241
 
Name Accession Description Interval E-value
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-245 3.10e-163

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: 451.15  E-value: 3.10e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVAGF 84
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCAGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  85 VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIGLTKSLAAD 164
Cdd:cd05368   81 VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTKAAVIGLTKSVAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 165 FIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIIDGGWS 244
Cdd:cd05368  161 FAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGGWS 240


                 .
gi 511847639 245 L 245
Cdd:cd05368  241 L 241
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-245 7.97e-90

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: 265.50  E-value: 7.97e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPG-IQIRTLDVTKKKQIDQFASEIE-- 73
Cdd:COG1028    1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEaaaaELRAAGGrALAVAADVTDEAAVEALVAAAVaa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 --RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSK 151
Cdd:COG1028   81 fgRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIA-GLRGSPGQAAYAASK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqeRIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:COG1028  160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTP----MTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASY 235

                        250
                 ....*....|....
gi 511847639 232 VTGNPVIIDGGWSL 245
Cdd:COG1028  236 ITGQVLAVDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 13-244 1.44e-74

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: 226.16  E-value: 1.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   13 AAAQGIGRAAALAFAREGAKVIATDINE---SKLQELEECPGIQIRTLDVTKKKQIDQFASEIE----RLDVLFNVAGFV 85
Cdd:pfam13561   3 ANESGIGWAIARALAEEGAEVVLTDLNEalaKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVekfgRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   86 --HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASsIKGVVNRCVYSTSKAAVIGLTKSLAA 163
Cdd:pfam13561  83 pkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGA-ERVVPNYNAYGAAKAALEALTRYLAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  164 DFIQQGIRCNCVCPGTVDTPSLqeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIIDGGW 243
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLAA----SGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235


                  .
gi 511847639  244 S 244
Cdd:pfam13561 236 T 236
PRK06138 PRK06138
SDR family oxidoreductase;
2-244 1.30e-70

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 216.94  E-value: 1.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN----ESKLQELEECPGIQIRTLDVTKKKQ----IDQFASEIE 73
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDaeaaERVAAAIAAGGRAFARQGDVGSAEAvealVDFVAARWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvASSIKGVVNRCVYSTSKAA 153
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTAS-QLALAGGRGRAAYVASKGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK06138 160 IASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFAT 239

                        250
                 ....*....|.
gi 511847639 234 GNPVIIDGGWS 244
Cdd:PRK06138 240 GTTLVVDGGWL 250
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 10-242 1.21e-56

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 180.48  E-value: 1.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   10 VVTAAAQGIGRAAALAFAREGAKVIATDINESKL-----QELEECPG-IQIRTLDVTKKKQIDQFASEIE----RLDVLF 79
Cdd:TIGR01830   2 LVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGaeevvEELKALGVkALGVVLDVSDREDVKAVVEEIEeelgTIDILV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSI--KGVVNrcvYSTSKAAVIGL 157
Cdd:TIGR01830  82 NNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMgnAGQAN---YAASKAGVIGF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  158 TKSLAADFIQQGIRCNCVCPGTVDTP---SLQERIQARpnpkearndFLKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:TIGR01830 159 TKSLAKELASRNITVNAVAPGFIDTDmtdKLSEKVKKK---------ILSQIPLGRFGQPEEVANAVAFLASDEASYITG 229


                  ....*...
gi 511847639  235 NPVIIDGG 242
Cdd:TIGR01830 230 QVIHVDGG 237
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-80 1.31e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 38.26  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639     2 GRLDGKVIVVTAaaqGI-GRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLdvtkKKQIDQFASEIERLDVLFN 80
Cdd:smart01002  17 GVPPAKVVVIGA---GVvGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTL----YSQAELLEEAVKEADLVIG 89
 
Name Accession Description Interval E-value
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-245 3.10e-163

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: 451.15  E-value: 3.10e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVAGF 84
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCAGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  85 VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIGLTKSLAAD 164
Cdd:cd05368   81 VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTKAAVIGLTKSVAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 165 FIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIIDGGWS 244
Cdd:cd05368  161 FAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGGWS 240


                 .
gi 511847639 245 L 245
Cdd:cd05368  241 L 241
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-245 7.97e-90

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: 265.50  E-value: 7.97e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPG-IQIRTLDVTKKKQIDQFASEIE-- 73
Cdd:COG1028    1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEaaaaELRAAGGrALAVAADVTDEAAVEALVAAAVaa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 --RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSK 151
Cdd:COG1028   81 fgRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIA-GLRGSPGQAAYAASK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqeRIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:COG1028  160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTP----MTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASY 235

                        250
                 ....*....|....
gi 511847639 232 VTGNPVIIDGGWSL 245
Cdd:COG1028  236 ITGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 9-240 6.00e-80

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: 239.88  E-value: 6.00e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEC----PGIQIRTLDVTKKKQIDQFASEIE----RLDVLFN 80
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIealgGNAVAVQADVSDEEDVEALVEEALeefgRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  81 VAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAVIGLTKS 160
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVA-GLRPLPGQAAYAASKAALEGLTRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 161 LAADFIQQGIRCNCVCPGTVDTPSLQERIqarpnPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIID 240
Cdd:cd05233  160 LALELAPYGIRVNAVAPGLVDTPMLAKLG-----PEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 13-244 1.44e-74

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: 226.16  E-value: 1.44e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   13 AAAQGIGRAAALAFAREGAKVIATDINE---SKLQELEECPGIQIRTLDVTKKKQIDQFASEIE----RLDVLFNVAGFV 85
Cdd:pfam13561   3 ANESGIGWAIARALAEEGAEVVLTDLNEalaKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVekfgRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   86 --HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASsIKGVVNRCVYSTSKAAVIGLTKSLAA 163
Cdd:pfam13561  83 pkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGA-ERVVPNYNAYGAAKAALEALTRYLAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  164 DFIQQGIRCNCVCPGTVDTPSLqeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIIDGGW 243
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLAA----SGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235


                  .
gi 511847639  244 S 244
Cdd:pfam13561 236 T 236
PRK06138 PRK06138
SDR family oxidoreductase;
2-244 1.30e-70

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 216.94  E-value: 1.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN----ESKLQELEECPGIQIRTLDVTKKKQ----IDQFASEIE 73
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDaeaaERVAAAIAAGGRAFARQGDVGSAEAvealVDFVAARWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvASSIKGVVNRCVYSTSKAA 153
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTAS-QLALAGGRGRAAYVASKGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK06138 160 IASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFAT 239

                        250
                 ....*....|.
gi 511847639 234 GNPVIIDGGWS 244
Cdd:PRK06138 240 GTTLVVDGGWL 250
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3-245 3.95e-68

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 210.02  E-value: 3.95e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE---CPGIQIRTL--DVTKKKQ----IDQFASEIE 73
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAelrAAGGEARVLvfDVSDEAAvralIEAAVEAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVVNRCVYSTSKAA 153
Cdd:PRK05653  82 ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSV-SGVTGNPGQTNYSAAKAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLqeriqaRPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK05653 161 VIGFTKALALELASRGITVNAVAPGFIDTDMT------EGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYIT 234

                        250
                 ....*....|..
gi 511847639 234 GNPVIIDGGWSL 245
Cdd:PRK05653 235 GQVIPVNGGMYM 246
PRK12826 PRK12826
SDR family oxidoreductase;
1-242 4.85e-66

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 205.15  E-value: 4.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-----EECPGIQIRTLDVTKKKQIDQFASEIE-- 73
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATaelveAAGGKARARQVDVRDRAALKAAVAAGVed 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 --RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSK 151
Cdd:PRK12826  81 fgRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPGLAHYAASK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPkearnDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAE-----AIAAAIPLGRLGEPEDIAAAVLFLASDEARY 235

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:PRK12826 236 ITGQTLPVDGG 246
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 7-242 1.31e-64

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: 200.85  E-value: 1.31e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEC---PGIQIRTL--DVTKKKQIDQFASEIE----RLDV 77
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEikaLGGNAAALeaDVSDREAVEALVEKVEaefgPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVVNRCVYSTSKAAVIGL 157
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSV-VGLIGNPGQANYAASKAGVIGF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDTPSLQEriqarpNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPV 237
Cdd:cd05333  160 TKSLAKELASRGITVNAVAPGFIDTDMTDA------LPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVL 233


                 ....*
gi 511847639 238 IIDGG 242
Cdd:cd05333  234 HVNGG 238
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-243 2.09e-64

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 200.84  E-value: 2.09e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKV-IATDINESKLQELEE------CPGIQIRTlDVTKKKQIDQFASEIER 74
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVvIAYDINEEAAQELLEeikeegGDAIAVKA-DVSSEEDVENLVEQIVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 ----LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTS 150
Cdd:PRK05565  80 kfgkIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLI-GASCEVLYSAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 151 KAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriqarpNPKEARNDFLKRQKT-GRFATAEEIALLCVYLASDES 229
Cdd:PRK05565 159 KGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS-------SFSEEDKEGLAEEIPlGRLGKPEEIAKVVLFLASDDA 231

                        250
                 ....*....|....
gi 511847639 230 AYVTGNPVIIDGGW 243
Cdd:PRK05565 232 SYITGQIITVDGGW 245
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 5-227 7.14e-63

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


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 196.56  E-value: 7.14e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRT--LDVTKKKQIDQFASEIE----RLDVL 78
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAvpLDVTDEAAVEAAVAAAVaefgRLDVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAVIGLT 158
Cdd:COG4221   84 VNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIA-GLRPYPGGAVYAATKAAVRGLS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511847639 159 KSLAADFIQQGIRCNCVCPGTVDTPSLQERiqarpnPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:COG4221  163 ESLRAELRPTGIRVTVIEPGAVDTEFLDSV------FDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQ 225
FabG-like PRK07231
SDR family oxidoreductase;
3-245 9.87e-62

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 193.89  E-value: 9.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL----DVTKKKQIDQFASE-IE---R 74
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGRAIavaaDVSDEADVEAAVAAaLErfgS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVH-HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAA 153
Cdd:PRK07231  82 VDILVNNAGTTHrNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTA-GLRPRPGLGWYNASKGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPNPkEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETG-LLEAFMGEPTP-ENRAKFLATIPLGRLGTPEDIANAALFLASDEASWIT 238

                        250
                 ....*....|..
gi 511847639 234 GNPVIIDGGWSL 245
Cdd:PRK07231 239 GVTLVVDGGRCV 250
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-193 3.98e-61

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 190.52  E-value: 3.98e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639    7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEECPG-IQIRTLDVTKKKQIDQFASEIE----RLDV 77
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLeavaKELGALGGkALFIQGDVTDRAQVKALVEQAVerlgRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   78 LFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAVIGL 157
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVA-GLVPYPGGSAYSASKAAVIGF 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 511847639  158 TKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARP 193
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
1-245 2.41e-60

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 190.78  E-value: 2.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE-------CPGIQIRTLDVTKKKQIDQFASEIE 73
Cdd:PRK08226   1 MGKLTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADElcgrghrCTAVVADVRDPASVAAAIKRAKEKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 -RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKA 152
Cdd:PRK08226  81 gRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVADPGETAYALTKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERI--QARP-NPKEARNDFLKRQKTGRFATAEEIALLCVYLASDES 229
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTP-MAESIarQSNPeDPESVLTEMAKAIPLRRLADPLEVGELAAFLASDES 239

                        250
                 ....*....|....*.
gi 511847639 230 AYVTGNPVIIDGGWSL 245
Cdd:PRK08226 240 SYLTGTQNVIDGGSTL 255
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-242 1.30e-59

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 189.11  E-value: 1.30e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTL--DVTKKKQIDQ-FASEIER-- 74
Cdd:PRK12829   6 LKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATaARLPGAKVTATvaDVADPAQVERvFDTAVERfg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 -LDVLFNVAG-FVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGN-IINMSSVASsIKGVVNRCVYSTSK 151
Cdd:PRK12829  86 gLDVLVNNAGiAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAG-RLGYPGRTPYAASK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPK-----EARNDFLKRQKTGRFATAEEIALLCVYLAS 226
Cdd:PRK12829 165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLgigldEMEQEYLEKISLGRMVEPEDIAATALFLAS 244

                        250
                 ....*....|....*.
gi 511847639 227 DESAYVTGNPVIIDGG 242
Cdd:PRK12829 245 PAARYITGQAISVDGN 260
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 4-243 1.86e-59

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 188.09  E-value: 1.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESK-----LQELEECpGIQIRTL--DVTKKKQIDQFASEIE--- 73
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAgaealVAEIGAL-GGKALAVqgDVSDAESVERAVDEAKaef 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 -RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSKA 152
Cdd:PRK05557  82 gGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGL-MGNPGQANYAASKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERiqarpnPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYV 232
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETDMTDAL------PEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYI 234

                        250
                 ....*....|.
gi 511847639 233 TGNPVIIDGGW 243
Cdd:PRK05557 235 TGQTLHVNGGM 245
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-243 4.18e-59

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 187.40  E-value: 4.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE---CPGIQIR--TLDVTKKKQIDQFASEIE---- 73
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEalqKAGGKAIgvAMDVTDEEAINAGIDYAVetfg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAA 153
Cdd:PRK12429  81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLV-GSAGKAAYVSAKHG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARP-----NPKEARNDFL-KRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK12429 160 LIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDLAkergiSEEEVLEDVLlPLVPQKRFTTVEEIADYALFLASF 239

                        250
                 ....*....|....*.
gi 511847639 228 ESAYVTGNPVIIDGGW 243
Cdd:PRK12429 240 AAKGVTGQAWVVDGGW 255
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-245 1.31e-58

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 185.55  E-value: 1.31e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEleecPGIQIRTLDVTKkkQIDQFASEIERLDVLFNVAGFV 85
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLS----GNFHFLQLDLSD--DLEPLFDWVPSVDILCNTAGIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  86 H-HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIK---GVvnrcVYSTSKAAVIGLTKSL 161
Cdd:PRK06550  79 DdYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAgggGA----AYTASKHALAGFTKQL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 162 AADFIQQGIRCNCVCPGTVDTPSLQeriqarpnpkearNDF---------LKRQKTGRFATAEEIALLCVYLASDESAYV 232
Cdd:PRK06550 155 ALDYAKDGIQVFGIAPGAVKTPMTA-------------ADFepggladwvARETPIKRWAEPEEVAELTLFLASGKADYM 221

                        250
                 ....*....|...
gi 511847639 233 TGNPVIIDGGWSL 245
Cdd:PRK06550 222 QGTIVPIDGGWTL 234
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
3-183 5.04e-58

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 184.69  E-value: 5.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECP----GIQIRTLDVTKKKQIDQFASEIE---- 73
Cdd:COG0300    2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALaAELRaagaRVEVVALDVTDPDAVAALAEAVLarfg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAA 153
Cdd:COG0300   82 PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLR-GLPGMAAYAASKAA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGPVDTP 190
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 6-244 5.93e-57

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: 181.70  E-value: 5.93e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE---CPGIQIRTL--DVTKKKQIDQFASE----IERLD 76
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASelrAGGAGVLAVvaDLTDPEDIDRLVEKagdaFGRVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVVNRCVYSTSKAAVIG 156
Cdd:cd05344   81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSL-TVKEPEPNLVLSNVARAGLIG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARP-----NPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:cd05344  160 LVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAekegiSVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKASY 239

                        250
                 ....*....|...
gi 511847639 232 VTGNPVIIDGGWS 244
Cdd:cd05344  240 ITGQAILVDGGLT 252
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 10-242 1.21e-56

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 180.48  E-value: 1.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   10 VVTAAAQGIGRAAALAFAREGAKVIATDINESKL-----QELEECPG-IQIRTLDVTKKKQIDQFASEIE----RLDVLF 79
Cdd:TIGR01830   2 LVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGaeevvEELKALGVkALGVVLDVSDREDVKAVVEEIEeelgTIDILV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSI--KGVVNrcvYSTSKAAVIGL 157
Cdd:TIGR01830  82 NNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMgnAGQAN---YAASKAGVIGF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  158 TKSLAADFIQQGIRCNCVCPGTVDTP---SLQERIQARpnpkearndFLKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:TIGR01830 159 TKSLAKELASRNITVNAVAPGFIDTDmtdKLSEKVKKK---------ILSQIPLGRFGQPEEVANAVAFLASDEASYITG 229


                  ....*...
gi 511847639  235 NPVIIDGG 242
Cdd:TIGR01830 230 QVIHVDGG 237
PRK06172 PRK06172
SDR family oxidoreductase;
1-242 7.90e-56

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 179.18  E-value: 7.90e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN----ESKLQELEECPG--IQIRTlDVTK----KKQIDQFAS 70
Cdd:PRK06172   2 SMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDaaggEETVALIREAGGeaLFVAC-DVTRdaevKALVEQTIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  71 EIERLDVLFNVAGF-VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYST 149
Cdd:PRK06172  81 AYGRLDYAFNNAGIeIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLG-AAPKMSIYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEarndFLK-RQKTGRFATAEEIALLCVYLASDE 228
Cdd:PRK06172 160 SKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRKAE----FAAaMHPVGRIGKVEEVASAVLYLCSDG 235

                        250
                 ....*....|....
gi 511847639 229 SAYVTGNPVIIDGG 242
Cdd:PRK06172 236 ASFTTGHALMVDGG 249
PRK06500 PRK06500
SDR family oxidoreductase;
1-245 2.80e-55

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 177.46  E-value: 2.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG-----IQIRTLDVTKKKQI-DQFASEIER 74
Cdd:PRK06500   1 MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGesalvIRADAGDVAAQKALaQALAEAFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPkMLAQKSGNIINmSSVASSIkGVVNRCVYSTSKAAV 154
Cdd:PRK06500  81 LDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP-LLANPASIVLN-GSINAHI-GMPNSSVYAASKAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:PRK06500 158 LSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVG 237

                        250
                 ....*....|.
gi 511847639 235 NPVIIDGGWSL 245
Cdd:PRK06500 238 SEIIVDGGMSN 248
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 2-243 3.18e-55

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: 177.19  E-value: 3.18e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIR--TLDVTK----KKQIDQFASEIERL 75
Cdd:cd05341    1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARffHLDVTDedgwTAVVDTAREAFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVI 155
Cdd:cd05341   81 DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLV-GDPALAAYNASKGAVR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 156 GLTKSLAADFIQQ--GIRCNCVCPGTVDTPSLQERIqarpnPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:cd05341  160 GLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELL-----IAQGEMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVT 234

                        250
                 ....*....|
gi 511847639 234 GNPVIIDGGW 243
Cdd:cd05341  235 GSELVVDGGY 244
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-243 4.58e-55

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 176.98  E-value: 4.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKV-IATDINESKLQELEECPG-----IQIRTLDVTKKKQIDQFASEIE- 73
Cdd:PRK12825   1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVvVHYRSDEEAAEELVEAVEalgrrAQAVQADVTDKAALEAAVAAAVe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 ---RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVVNRCVYSTS 150
Cdd:PRK12825  81 rfgRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSV-AGLPGWPGRSNYAAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 151 KAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESA 230
Cdd:PRK12825 160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTD------MKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASD 233

                        250
                 ....*....|...
gi 511847639 231 YVTGNPVIIDGGW 243
Cdd:PRK12825 234 YITGQVIEVTGGV 246
PRK08589 PRK08589
SDR family oxidoreductase;
1-242 6.51e-55

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 177.28  E-value: 6.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINEsKLQELEEcpgiQIRT---------LDVTKKKQIDQFASE 71
Cdd:PRK08589   1 MKRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAE-AVSETVD----KIKSnggkakayhVDISDEQQVKDFASE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IE----RLDVLFNVAGFVHH-GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLaQKSGNIINMSSVaSSIKGVVNRCV 146
Cdd:PRK08589  76 IKeqfgRVDVLFNNAGVDNAaGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMM-EQGGSIINTSSF-SGQAADLYRSG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNpkEARNDFLKRQK----TGRFATAEEIALLCV 222
Cdd:PRK08589 154 YNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSED--EAGKTFRENQKwmtpLGRLGKPEEVAKLVV 231

                        250       260
                 ....*....|....*....|
gi 511847639 223 YLASDESAYVTGNPVIIDGG 242
Cdd:PRK08589 232 FLASDDSSFITGETIRIDGG 251
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 3-244 1.48e-54

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: 175.72  E-value: 1.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL---DVTKKKQI----DQFASEIERL 75
Cdd:cd05326    1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFvhcDVTVEADVraavDTAVARFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFV--HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRcVYSTSKAA 153
Cdd:cd05326   81 DIMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPH-AYTASKHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLqerIQARpNPKEARNDFLKR---QKTGRFATAEEIALLCVYLASDESA 230
Cdd:cd05326  160 VLGLTRSAATELGEHGIRVNCVSPYGVATPLL---TAGF-GVEDEAIEEAVRgaaNLKGTALRPEDIAAAVLYLASDDSR 235

                        250
                 ....*....|....
gi 511847639 231 YVTGNPVIIDGGWS 244
Cdd:cd05326  236 YVSGQNLVVDGGLT 249
PRK06398 PRK06398
aldose dehydrogenase; Validated
 1-244 2.67e-54

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 175.41  E-value: 2.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE--ECpgiqirtlDVTKKKQ----IDQFASEIER 74
Cdd:PRK06398   1 DLGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDyfKV--------DVSNKEQvikgIDYVISKYGR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAV 154
Cdd:PRK06398  73 IDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFA-VTRNAAAYVTSKHAV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQgIRCNCVCPGTVDTPSL----QERIQARPNPKEAR-NDFLKRQKTGRFATAEEIALLCVYLASDES 229
Cdd:PRK06398 152 LGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLewaaELEVGKDPEHVERKiREWGEMHPMKRVGKPEEVAYVVAFLASDLA 230

                        250
                 ....*....|....*
gi 511847639 230 AYVTGNPVIIDGGWS 244
Cdd:PRK06398 231 SFITGECVTVDGGLR 245
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 1-244 5.08e-54

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 174.53  E-value: 5.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTlDVTKKKQIDQ-FASEIE---RL 75
Cdd:PRK06057   2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAaDEVGGLFVPT-DVTDEDAVNAlFDTAAEtygSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFV--HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKAA 153
Cdd:PRK06057  81 DIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQISYTASKGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNpKEARNdfLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK06057 161 VLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDPE-RAARR--LVHVPMGRFAEPEEIAAAVAFLASDDASFIT 237

                        250
                 ....*....|.
gi 511847639 234 GNPVIIDGGWS 244
Cdd:PRK06057 238 ASTFLVDGGIS 248
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 4-243 6.26e-54

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: 174.08  E-value: 6.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL---QELEECPGIQIR--TLDVTKKKQIDQFASEIE----R 74
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAeeaQQLIEKEGVEATafTCDVSDEEAIKAAVEAIEedfgK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVVNRCVYSTSKAAV 154
Cdd:cd05347   83 IDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSL-LSELGGPPVPAYAASKGGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPnpkeARNDF-LKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:cd05347  162 AGLTKALATEWARHGIQVNAIAPGYFATE-MTEAVVADP----EFNDDiLKRIPAGRWGQPEDLVGAAVFLASDASDYVN 236

                        250
                 ....*....|
gi 511847639 234 GNPVIIDGGW 243
Cdd:cd05347  237 GQIIFVDGGW 246
PRK07063 PRK07063
SDR family oxidoreductase;
1-244 8.95e-53

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 171.39  E-value: 8.95e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-----EECPGIQIRTL--DVTKKKQID----QFA 69
Cdd:PRK07063   2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAaaaiaRDVAGARVLAVpaDVTDAASVAaavaAAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSV-ASSIkgvVNRCV-Y 147
Cdd:PRK07063  82 EAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASThAFKI---IPGCFpY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK07063 159 PVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLASD 238

                        250
                 ....*....|....*..
gi 511847639 228 ESAYVTGNPVIIDGGWS 244
Cdd:PRK07063 239 EAPFINATCITIDGGRS 255
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 3-245 1.11e-52

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 170.99  E-value: 1.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIR--TLDVTKKKQ----IDQFASEIERLD 76
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKglVCDVSDSQSveaaVAAVISAFGRID 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVIG 156
Cdd:PRK06841  92 ILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVV-ALERHVAYCASKAGVVG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTpSLQERIQARPNPKEARndflKRQKTGRFATAEEIALLCVYLASDESAYVTGNP 236
Cdd:PRK06841 171 MTKVLALEWGPYGITVNAISPTVVLT-ELGKKAWAGEKGERAK----KLIPAGRFAYPEEIAAAALFLASDAAAMITGEN 245


                 ....*....
gi 511847639 237 VIIDGGWSL 245
Cdd:PRK06841 246 LVIDGGYTI 254
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 2-242 1.57e-52

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: 170.26  E-value: 1.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG---IQIRTlDVTKKKQIDQFA----SEIER 74
Cdd:cd05345    1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGeaaIAIQA-DVTKRADVEAMVeaalSKFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVH-HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSI--KGVVnrcVYSTSK 151
Cdd:cd05345   80 LDILVNNAGITHrNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRprPGLT---WYNASK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQarPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:cd05345  157 GWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMG--EDTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASF 234

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:cd05345  235 ITGVALEVDGG 245
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 4-242 5.12e-52

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: 169.21  E-value: 5.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE---CPGIQIRTlDVTKKKQI-DQFASEIER---LD 76
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAqiaGGALALRV-DVTDEQQVaALFERAVEEfggLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVH-HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVI 155
Cdd:cd08944   80 LLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQS-GDPGYGAYGASKAAIR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARN-DFLKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:cd08944  159 NLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPGGfHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFITG 238


                 ....*...
gi 511847639 235 NPVIIDGG 242
Cdd:cd08944  239 QVLCVDGG 246
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 4-245 1.79e-51

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: 167.97  E-value: 1.79e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE----LEEC--PGIQIRTL--DVTKKKQIDQFASE---- 71
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEEtrqsCLQAgvSEKKILLVvaDLTEEEGQDRIISTtlak 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKsGNIINMSSVAS--SIKGVVNrcvYST 149
Cdd:cd05364   81 FGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGgrSFPGVLY---YCI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQArpnPKEARNDFLKRQKT----GRFATAEEIALLCVYLA 225
Cdd:cd05364  157 SKAALDQFTRCTALELAPKGVRVNSVSPGVIVTG-FHRRMGM---PEEQYIKFLSRAKEthplGRPGTVDEVAEAIAFLA 232

                        250       260
                 ....*....|....*....|
gi 511847639 226 SDESAYVTGNPVIIDGGWSL 245
Cdd:cd05364  233 SDASSFITGQLLPVDGGRHL 252
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-243 6.23e-51

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 166.30  E-value: 6.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE---ECPGIQIRT--LDVTKKKQIDQFASEIE-- 73
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAaalEAAGGRAHAiaADLADPASVQRFFDAAAaa 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 --RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvASSIKGVVNRCVYSTSK 151
Cdd:PRK12939  82 lgGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLAS-DTALWGAPKLGAYVASK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQEriqarpNPKEARNDFLKRQKT-GRFATAEEIALLCVYLASDESA 230
Cdd:PRK12939 161 GAVIGMTRSLARELGGRGITVNAIAPGLTATEATAY------VPADERHAYYLKGRAlERLQVPDDVAGAVLFLLSDAAR 234

                        250
                 ....*....|...
gi 511847639 231 YVTGNPVIIDGGW 243
Cdd:PRK12939 235 FVTGQLLPVNGGF 247
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-242 8.15e-51

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 166.36  E-value: 8.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE--LEECPGIQIRTLDVTKKKQIDQFASEIER---- 74
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLaaLEIGPAAIAVSLDVTRQDSIDRIVAAAVErfgg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVASSiKGVVNRCVYSTSKAA 153
Cdd:PRK07067  81 IDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGR-RGEALVSHYCATKAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTP------SLQERIQARPnPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK07067 160 VISYTQSAALALIRHGINVNAIAPGVVDTPmwdqvdALFARYENRP-PGEKKRLVGEAVPLGRMGVPDDLTGMALFLASA 238

                        250
                 ....*....|....*
gi 511847639 228 ESAYVTGNPVIIDGG 242
Cdd:PRK07067 239 DADYIVAQTYNVDGG 253
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-245 4.02e-50

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 164.12  E-value: 4.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLFN 80
Cdd:PRK07060   4 AFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRLDVGDDAAIRAALAAAGAFDGLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  81 VAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVAsSIKGVVNRCVYSTSKAAVIGLTK 159
Cdd:PRK07060  84 CAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgRGGSIVNVSSQA-ALVGLPDHLAYCASKAALDAITR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 160 SLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPnpkEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVII 239
Cdd:PRK07060 163 VLCVELGPHGIRVNSVNPTVTLTP-MAAEAWSDP---QKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPV 238


                 ....*.
gi 511847639 240 DGGWSL 245
Cdd:PRK07060 239 DGGYTA 244
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 6-243 6.78e-50

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 164.16  E-value: 6.78e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN-----ESKLQELEECPGIQIRTL--DVTKKKQIDQF----ASEIER 74
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGdaaeiEAVRAGLAAKHGVKVLYHgaDLSKPAAIEDMvayaQRQFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVVNRCVYSTSKAAV 154
Cdd:cd08940   82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASV-HGLVASANKSAYVAAKHGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERI----QARPNPKE--ARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:cd08940  161 VGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQIsalaQKNGVPQEqaARELLLEKQPSKQFVTPEQLGDTAVFLASDA 240

                        250
                 ....*....|....*
gi 511847639 229 SAYVTGNPVIIDGGW 243
Cdd:cd08940  241 ASQITGTAVSVDGGW 255
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 3-243 1.12e-49

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: 163.27  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN----ESKLQELEECPGIQIRTL--DVTK----KKQIDQFASEI 72
Cdd:cd05352    5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSapraEEKAEELAKKYGVKTKAYkcDVSSqesvEKTFKQIQKDF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkgvVNR----CVYS 148
Cdd:cd05352   85 GKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTI---VNRpqpqAAYN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:cd05352  162 ASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTD------LTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDA 235

                        250
                 ....*....|....*
gi 511847639 229 SAYVTGNPVIIDGGW 243
Cdd:cd05352  236 SSYTTGSDLIIDGGY 250
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-245 5.09e-49

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 161.59  E-value: 5.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEecpgIQIRTLDVTKKKQID----QFASEIERLD 76
Cdd:PRK08220   3 AMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP----FATFVLDVSDAAAVAqvcqRLLAETGPLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGvVNRCVYSTSKAAVIG 156
Cdd:PRK08220  79 VLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPR-IGMAAYGASKAALTS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPNPKEAR-NDFLKRQKTG----RFATAEEIALLCVYLASDESAY 231
Cdd:PRK08220 158 LAKCVGLELAPYGVRCNVVSPGSTDTD-MQRTLWVDEDGEQQViAGFPEQFKLGiplgKIARPQEIANAVLFLASDLASH 236

                        250
                 ....*....|....
gi 511847639 232 VTGNPVIIDGGWSL 245
Cdd:PRK08220 237 ITLQDIVVDGGATL 250
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-244 4.71e-48

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 158.94  E-value: 4.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpgiQIRTL---------DV----TKKKQIDQ 67
Cdd:PRK07478   1 MMRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVA----EIRAEggeavalagDVrdeaYAKALVAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  68 FASEIERLDVLFNVAGFV-HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCV 146
Cdd:PRK07478  77 AVERFGGLDIAFNNAGTLgEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFPGMAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQEriqarPNPKEARNDF------LKrqktgRFATAEEIALL 220
Cdd:PRK07478 157 YAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRA-----MGDTPEALAFvaglhaLK-----RMAQPEEIAQA 226

                        250       260
                 ....*....|....*....|....
gi 511847639 221 CVYLASDESAYVTGNPVIIDGGWS 244
Cdd:PRK07478 227 ALFLASDAASFVTGTALLVDGGVS 250
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 4-245 5.04e-47

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: 156.39  E-value: 5.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIatdIN----ESKLQELEEcpgiQIRTL---------DVTKKKQI-DQFA 69
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVV---VNyrskEDAAEEVVE----EIKAVggkaiavqaDVSKEEDVvALFQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIER---LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMSSVASSI--KGVVN 143
Cdd:cd05358   74 SAIKEfgtLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIpwPGHVN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 144 rcvYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQEriqARPNPkEARNDFLKRQKTGRFATAEEIALLCVY 223
Cdd:cd05358  154 ---YAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAE---AWDDP-EQRADLLSLIPMGRIGEPEEIAAAAAW 226

                        250       260
                 ....*....|....*....|..
gi 511847639 224 LASDESAYVTGNPVIIDGGWSL 245
Cdd:cd05358  227 LASDEASYVTGTTLFVDGGMTL 248
PRK07069 PRK07069
short chain dehydrogenase; Validated
 11-244 1.79e-46

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 154.87  E-value: 1.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  11 VTAAAQGIGRAAALAFAREGAKVIATDINESKL-----QELEECPGIQIR---TLDVTKKKQ----IDQFASEIERLDVL 78
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGldafaAEINAAHGEGVAfaaVQDVTDEAQwqalLAQAADAMGGLSVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAVIGLT 158
Cdd:PRK07069  84 VNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVA-AFKAEPDYTAYNASKAAVASLT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 159 KSLAADFIQQG--IRCNCVCPGTVDTPSLqERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNP 236
Cdd:PRK07069 163 KSIALDCARRGldVRCNSIHPTFIRTGIV-DPIFQRLGEEEATRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVTGAE 241


                 ....*...
gi 511847639 237 VIIDGGWS 244
Cdd:PRK07069 242 LVIDGGIC 249
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-243 1.24e-45

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 159.24  E-value: 1.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL--DVTKKKQI----DQFASEIERLDVLF 79
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALamDVSDEAQIregfEQLHREFGRIDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFV--HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGN-IINMSSVASsIKGVVNRCVYSTSKAAVIG 156
Cdd:PRK06484  85 NNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAG-LVALPKRTAYSASKAAVIS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQArpnPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNP 236
Cdd:PRK06484 164 LTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERA---GKLDPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGST 240


                 ....*..
gi 511847639 237 VIIDGGW 243
Cdd:PRK06484 241 LVVDGGW 247
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
7-242 3.43e-45

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 151.46  E-value: 3.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDI-NESKLQELEECPG---IQIRT--LDVTKKKQIDQFASEIE----RLD 76
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFsGNDCAKDWFEEYGfteDQVRLkeLDVTDTEECAEALAEIEeeegPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYSTSKAAVIG 156
Cdd:PRK12824  83 ILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNG-LKGQFGQTNYSAAKAGMIG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriQARPnpkearnDFLKRQKTG----RFATAEEIALLCVYLASDESAYV 232
Cdd:PRK12824 162 FTKALASEGARYGITVNCIAPGYIATPMVE---QMGP-------EVLQSIVNQipmkRLGTPEEIAAAVAFLVSEAAGFI 231

                        250
                 ....*....|
gi 511847639 233 TGNPVIIDGG 242
Cdd:PRK12824 232 TGETISINGG 241
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-243 3.90e-45

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 151.81  E-value: 3.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT--DINESKLQELEECPG--IQIRTLDVTKKKQIDQFASEI----ER 74
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITthGTNWDETRRLIEKEGrkVTFVQVDLTKPESAEKVVKEAleefGK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAV 154
Cdd:PRK06935  92 IDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASML-SFQGGKFVPAYTASKHGV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQErIQArpnpKEARND-FLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK06935 171 AGLTKAFANELAAYNIQVNAIAPGYIKTANTAP-IRA----DKNRNDeILKRIPAGRWGEPDDLMGAAVFLASRASDYVN 245

                        250
                 ....*....|
gi 511847639 234 GNPVIIDGGW 243
Cdd:PRK06935 246 GHILAVDGGW 255
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 7-244 2.57e-44

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: 149.59  E-value: 2.57e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-----LEECPGIQIRTL--DVTKKKQIDQFASE-IE---RL 75
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAakaalLEIAPDAEVLLIkaDVSDEAQVEAYVDAtVEqfgRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFV-HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYSTSKAAV 154
Cdd:cd05330   84 DGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGG-IRGVGNQSGYAAAKHGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERI-QARP-NPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYV 232
Cdd:cd05330  163 VGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLkQLGPeNPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAGYV 242

                        250
                 ....*....|..
gi 511847639 233 TGNPVIIDGGWS 244
Cdd:cd05330  243 NAAVVPIDGGQS 254
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-242 5.67e-44

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 148.02  E-value: 5.67e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL-QELEECPG--IQIRTLDVTK----KKQIDQFASEIE 73
Cdd:PRK12828   2 EHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLsQTLPGVPAdaLRIGGIDLVDpqaaRRAVDEVNRQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRcVYSTSKAA 153
Cdd:PRK12828  82 RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMG-AYAAAKAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqeriQARPNPKEArnDFlkrqktGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK12828 161 VARLTEALAAELLDRGITVNAVLPSIIDTP------PNRADMPDA--DF------SRWVTPEQIAAVIAFLLSDEAQAIT 226


                 ....*....
gi 511847639 234 GNPVIIDGG 242
Cdd:PRK12828 227 GASIPVDGG 235
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 2-242 1.13e-43

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: 148.21  E-value: 1.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESK------LQELEECpGIQIRTL--DVTK----KKQIDQFA 69
Cdd:cd05355   22 GKLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEddaeetKKLIEEE-GRKCLLIpgDLGDesfcRDLVKEVV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVH-HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVaSSIKGVVNRCVYS 148
Cdd:cd05355  101 KEFGKLDILVNNAAYQHpQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSV-TAYKGSPHLLDYA 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqerIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:cd05355  178 ATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTP-----LIPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQD 252

                        250
                 ....*....|....
gi 511847639 229 SAYVTGNPVIIDGG 242
Cdd:cd05355  253 SSYVTGQVLHVNGG 266
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 1-244 6.10e-43

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: 146.05  E-value: 6.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINEsklQELEEC-----------PGIQIRTLDVTKKKQIDQFA 69
Cdd:cd05329    1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQ---KELDECltewrekgfkvEGSVCDVSSRSERQELMDTV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEI--ERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVY 147
Cdd:cd05329   78 ASHfgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVI-AVPSGAPY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqeRIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:cd05329  157 GATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATP----LVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMP 232

                        250
                 ....*....|....*..
gi 511847639 228 ESAYVTGNPVIIDGGWS 244
Cdd:cd05329  233 AASYITGQIIAVDGGLT 249
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 6-242 8.11e-43

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: 145.60  E-value: 8.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL-----QELEECPGIQIRT-LDVTKKKQ----IDQFASEIERL 75
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAakstiQEISEAGYNAVAVgADVTDKDDvealIDQAVEKFGSF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMSSVASsIKGVVNRCVYSTSKAAV 154
Cdd:cd05366   82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAG-VQGFPNLGAYSASKFAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQ------ARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:cd05366  161 RGLTQTAAQELAPKGITVNAYAPGIVKTE-MWDYIDeevgeiAGKPEGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASED 239

                        250
                 ....*....|....
gi 511847639 229 SAYVTGNPVIIDGG 242
Cdd:cd05366  240 SDYITGQTILVDGG 253
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 3-245 8.16e-43

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: 145.76  E-value: 8.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE------CPGIQIRTLDVTKKKQIDQFASE-IE-- 73
Cdd:cd08933    6 RYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESelnragPGSCKFVPCDVTKEEDIKTLISVtVErf 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 -RLDVLFNVAGFvH--HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKmLAQKSGNIINMSSVASSIkGVVNRCVYSTS 150
Cdd:cd08933   86 gRIDCLVNNAGW-HppHQTTDETSAQEFRDLLNLNLISYFLASKYALPH-LRKSQGNIINLSSLVGSI-GQKQAAPYVAT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 151 KAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASdESA 230
Cdd:cd08933  163 KGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIKEGELAQLLGRMGTEAESGLAALFLAA-EAT 241

                        250
                 ....*....|....*
gi 511847639 231 YVTGNPVIIDGGWSL 245
Cdd:cd08933  242 FCTGIDLLLSGGAEL 256
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 7-204 9.13e-43

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 145.45  E-value: 9.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRT--LDVTKKKQIDQFASEIE----RLDVLFN 80
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVleLDVTDEESIKAAVKEVIerfgRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  81 VAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVIGLTKS 160
Cdd:cd05374   81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLV-PTPFLGPYCASKAALEALSES 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 511847639 161 LAADFIQQGIRCNCVCPGTVDTPsLQERIQARPNPKEARNDFLK 204
Cdd:cd05374  160 LRLELAPFGIKVTIIEPGPVRTG-FADNAAGSALEDPEISPYAP 202
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-242 1.08e-42

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 145.31  E-value: 1.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKV-IATDINESKLQELEEcPGIQIRTLDVTKKKQIDQFASEIE----RLD 76
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKELRE-KGVFTIKCDVGNRDQVKKSKEVVEkefgRVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIG 156
Cdd:PRK06463  82 VLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTTFYAITKAGIII 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTpSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNP 236
Cdd:PRK06463 162 LTRRLAFELGKYGIRVNAVAPGWVET-DMTLSGKSQEEAEKLRELFRNKTVLKTTGKPEDIANIVLFLASDDARYITGQV 240


                 ....*.
gi 511847639 237 VIIDGG 242
Cdd:PRK06463 241 IVADGG 246
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-243 1.14e-42

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 145.25  E-value: 1.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN--------ESKLQELEECPG------IQIRTLDVTKKkQID 66
Cdd:PRK12827   1 MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHpmrgraeaDAVAAGIEAAGGkalglaFDVRDFAATRA-ALD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  67 QFASEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFL-PKMLAQKSGNIINMSSVASSI--KGVVN 143
Cdd:PRK12827  80 AGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRARRGGRIVNIASVAGVRgnRGQVN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 144 rcvYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriQARPNPKearndFLKRQKTGRFATAEEIALLCVY 223
Cdd:PRK12827 160 ---YAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMAD---NAAPTEH-----LLNPVPVQRLGEPDEVAALVAF 228

                        250       260
                 ....*....|....*....|
gi 511847639 224 LASDESAYVTGNPVIIDGGW 243
Cdd:PRK12827 229 LVSDAASYVTGQVIPVDGGF 248
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 9-245 1.75e-42

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: 144.53  E-value: 1.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEleECPGIQIRTLDVTKKKQID----QFASEIERLDVLFNVAGF 84
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLE--YGDPLRLTPLDVADAAAVRevcsRLLAEHGPIDALVNCAGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  85 VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINmssVASSIKGV--VNRCVYSTSKAAVIGLTKSLA 162
Cdd:cd05331   79 LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVT---VASNAAHVprISMAAYGASKAALASLSKCLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 163 ADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTG----RFATAEEIALLCVYLASDESAYVTGNPVI 238
Cdd:cd05331  156 LELAPYGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIAGVPEQFRLGiplgKIAQPADIANAVLFLASDQAGHITMHDLV 235


                 ....*..
gi 511847639 239 IDGGWSL 245
Cdd:cd05331  236 VDGGATL 242
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 1-240 1.17e-41

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 142.84  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIA-----TDINESKLQELEE--CPGIQIRTlDVTK----KKQIDQFA 69
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVicgrnAEKGEAQAAELEAlgAKAVFVQA-DLSDvedcRRVVAAAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKS-GNIINMSSVaSSIKGVVNRCVYS 148
Cdd:PRK06198  80 EAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSM-SAHGGQPFLAAYC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlQERIQARPNpkEARNDFL----KRQKTGRFATAEEIALLCVYL 224
Cdd:PRK06198 159 ASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEG-EDRIQREFH--GAPDDWLekaaATQPFGRLLDPDEVARAVAFL 235

                        250
                 ....*....|....*.
gi 511847639 225 ASDESAYVTGnpVIID 240
Cdd:PRK06198 236 LSDESGLMTG--SVID 249
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-243 1.63e-41

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 142.73  E-value: 1.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINE----SKLQELEECPGIQIR-TLDVTKKKQ----IDQFASE 71
Cdd:PRK13394   2 MSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQdganAVADEINKAGGKAIGvAMDVTNEDAvnagIDKVAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKML-AQKSGNIINMSSVaSSIKGVVNRCVYSTS 150
Cdd:PRK13394  82 FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSV-HSHEASPLKSAYVTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 151 KAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIqarpnPKEARND-----------FLKRQKTGRFATAEEIAL 219
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQI-----PEQAKELgiseeevvkkvMLGKTVDGVFTTVEDVAQ 235

                        250       260
                 ....*....|....*....|....
gi 511847639 220 LCVYLASDESAYVTGNPVIIDGGW 243
Cdd:PRK13394 236 TVLFLSSFPSAALTGQSFVVSHGW 259
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 2-242 1.81e-41

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 143.25  E-value: 1.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKV-IA-----TDINESKlqELEECPGIQIRTL--DVTK----KKQIDQFA 69
Cdd:PRK06701  42 GKLKGKVALITGGDSGIGRAVAVLFAKEGADIaIVyldehEDANETK--QRVEKEGVKCLLIpgDVSDeafcKDAVEETV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGT-ILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaqKSGN-IINMSSVaSSIKGVVNRCVY 147
Cdd:PRK06701 120 RELGRLDILVNNAAFQYPQQsLEDITAEQLDKTFKTNIYSYFHMTKAALPHL---KQGSaIINTGSI-TGYEGNETLIDY 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqeriqARPNPKEARN--DFLKRQKTGRFATAEEIALLCVYLA 225
Cdd:PRK06701 196 SATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP-------LIPSDFDEEKvsQFGSNTPMQRPGQPEELAPAYVFLA 268

                        250
                 ....*....|....*..
gi 511847639 226 SDESAYVTGNPVIIDGG 242
Cdd:PRK06701 269 SPDSSYITGQMLHVNGG 285
PRK06114 PRK06114
SDR family oxidoreductase;
3-243 2.06e-41

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 141.84  E-value: 2.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINES-----KLQELEECPG--IQIrTLDVTKKKQ----IDQFASE 71
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDdglaeTAEHIEAAGRraIQI-AADVTSKADlraaVARTEAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkgvVNR----CVY 147
Cdd:PRK06114  84 LGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGII---VNRgllqAHY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqerIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK06114 161 NASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATP-----MNTRPEMVHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSD 235

                        250
                 ....*....|....*.
gi 511847639 228 ESAYVTGNPVIIDGGW 243
Cdd:PRK06114 236 AASFCTGVDLLVDGGF 251
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 3-242 2.40e-41

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: 141.90  E-value: 2.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTkkKQIDQFA----------SEI 72
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDAAHVHT--ADLETYAgaqgvvraavERF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGfvhhGTIL-----DCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsiKGvVNRCVY 147
Cdd:cd08937   79 GRVDVLINNVG----GTIWakpyeHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAT--RG-IYRIPY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPnPKEARNDF--------LKRQKTGRFATAEEIAL 219
Cdd:cd08937  152 SAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAP-MSEQEKVWyqrivdqtLDSSLMGRYGTIDEQVR 230

                        250       260
                 ....*....|....*....|...
gi 511847639 220 LCVYLASDESAYVTGNPVIIDGG 242
Cdd:cd08937  231 AILFLASDEASYITGTVLPVGGG 253
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 11-245 3.10e-41

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: 141.34  E-value: 3.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  11 VTAAAQGIGRAAALAFAREGAKVIatdIN-----ESKLQELEECPGIQIRTL----DVTKKKQIDQFASEIE----RLDV 77
Cdd:cd05359    3 VTGGSRGIGKAIALRLAERGADVV---INyrkskDAAAEVAAEIEELGGKAVvvraDVSQPQDVEEMFAAVKerfgRLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYSTSKAAVIGL 157
Cdd:cd05359   80 LVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGS-IRALPNYLAVGTAKAALEAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDTPSLqeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPV 237
Cdd:cd05359  159 VRYLAVELGPRGIRVNAVSPGVIDTDAL----AHFPNREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTL 234


                 ....*...
gi 511847639 238 IIDGGWSL 245
Cdd:cd05359  235 VVDGGLSI 242
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 8-183 3.63e-41

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: 140.84  E-value: 3.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE---LEECPGIQIRTL--DVTKKKQIDQFASEIER----LDVL 78
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEEtanNVRKAGGKVHYYkcDVSKREEVYEAAKKIKKevgdVTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAS--SIKGVVnrcVYSTSKAAVIG 156
Cdd:cd05339   81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGliSPAGLA---DYCASKAAAVG 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQ---GIRCNCVCPGTVDTP 183
Cdd:cd05339  158 FHESLRLELKAYgkpGIKTTLVCPYFINTG 187
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 4-244 6.61e-41

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: 141.06  E-value: 6.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQIR-TLDVTKKKQIDQFASEIE----R 74
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDkvakEITALGGRAIAlAADVLDRASLERAREEIVaqfgT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCE--------------EKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVA--SSI 138
Cdd:cd08935   83 VDILINGAGGNHPDATTDPEhyepeteqnffdldEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNafSPL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 139 KGVVnrcVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPN--PKEARNDFLKRQKTGRFATAEE 216
Cdd:cd08935  163 TKVP---AYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP-QNRKLLINPDgsYTDRSNKILGRTPMGRFGKPEE 238

                        250       260
                 ....*....|....*....|....*....
gi 511847639 217 IALLCVYLASDE-SAYVTGNPVIIDGGWS 244
Cdd:cd08935  239 LLGALLFLASEKaSSFVTGVVIPVDGGFS 267
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 3-244 1.09e-39

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 137.77  E-value: 1.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-LEECPGIQIRTL----DVTKKKQIDQFASEIE---- 73
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEaAAHLEALGIDALwiaaDVADEADIERLAEETLerfg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPK-MLAQKSGNIINMSSVAS---SIKGVVNRCVYST 149
Cdd:PRK08213  89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGlggNPPEVMDTIAYNT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPG---TVDTPSLQERIQArpnpkearnDFLKRQKTGRFATAEEIALLCVYLAS 226
Cdd:PRK08213 169 SKGAVINFTRALAAEWGPHGIRVNAIAPGffpTKMTRGTLERLGE---------DLLAHTPLGRLGDDEDLKGAALLLAS 239

                        250
                 ....*....|....*...
gi 511847639 227 DESAYVTGNPVIIDGGWS 244
Cdd:PRK08213 240 DASKHITGQILAVDGGVS 257
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
3-245 1.52e-39

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 137.16  E-value: 1.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVI-----ATDINESKLQELE----ECPGIQIRTLDVTKKKQI-DQFASEI 72
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAvnyarSRKAAEETAEEIEalgrKALAVKANVGDVEKIKEMfAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYSTSKA 152
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGS-IRYLENYTTVGVSKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERiqarPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYV 232
Cdd:PRK08063 160 ALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHF----PNREELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMI 235

                        250
                 ....*....|...
gi 511847639 233 TGNPVIIDGGWSL 245
Cdd:PRK08063 236 RGQTIIVDGGRSL 248
PRK08628 PRK08628
SDR family oxidoreductase;
3-243 2.18e-39

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 137.01  E-value: 2.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIR----TLDVTK----KKQIDQFASEIER 74
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEELRALQPRaefvQVDLTDdaqcRDAVEQTVAKFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGfVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKsGNIINMSS-VASSIKGvvNRCVYSTSKAA 153
Cdd:PRK08628  84 IDGLVNNAG-VNDGVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISSkTALTGQG--GTSGYAAAKGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTG-RFATAEEIALLCVYLASDESAYV 232
Cdd:PRK08628 160 QLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIATFDDPEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHT 239

                        250
                 ....*....|.
gi 511847639 233 TGNPVIIDGGW 243
Cdd:PRK08628 240 TGQWLFVDGGY 250
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 1-244 3.16e-39

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 136.68  E-value: 3.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIR--TLDVTKKKQID----QFASEIER 74
Cdd:PRK08265   1 MIGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARfiATDITDDAAIEravaTVVARFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVA-GFVHHGtiLDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQkSGNIINMSSVASSIkGVVNRCVYSTSKAA 153
Cdd:PRK08265  81 VDILVNLAcTYLDDG--LASSRADWLAALDVNLVSAAMLAQAAHPHLARG-GGAIVNFTSISAKF-AQTGRWLYPASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERiqarpnpkeARNDflkRQKT----------GRFATAEEIALLCVY 223
Cdd:PRK08265 157 IRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDEL---------SGGD---RAKAdrvaapfhllGRVGDPEEVAQVVAF 224

                        250       260
                 ....*....|....*....|.
gi 511847639 224 LASDESAYVTGNPVIIDGGWS 244
Cdd:PRK08265 225 LCSDAASFVTGADYAVDGGYS 245
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 4-244 3.21e-39

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 136.68  E-value: 3.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEleecPGIQIRTLDVTKKKQIDQFASEIE----RLDVLF 79
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH----ENYQFVPTDVSSAEEVNHTVAEIIekfgRIDGLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGfVHHGTIL----------DCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYST 149
Cdd:PRK06171  83 NNAG-INIPRLLvdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGL-EGSEGQSCYAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPGTVD-----TPSLQERIQ-ARPNPKEA-RNDFLKRQKT--GRFATAEEIALL 220
Cdd:PRK06171 161 TKAALNSFTRSWAKELGKHNIRVVGVAPGILEatglrTPEYEEALAyTRGITVEQlRAGYTKTSTIplGRSGKLSEVADL 240

                        250       260
                 ....*....|....*....|....
gi 511847639 221 CVYLASDESAYVTGNPVIIDGGWS 244
Cdd:PRK06171 241 VCYLLSDRASYITGVTTNIAGGKT 264
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 3-242 4.74e-39

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 135.94  E-value: 4.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQIRT--LDVTKKKQIDQFASEIERLD 76
Cdd:PRK06125   4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEalaaDLRAAHGVDVAVhaLDLSSPEAREQLAAEAGDID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAssikGVVNRCVY---STSKAA 153
Cdd:PRK06125  84 ILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAA----GENPDADYicgSAGNAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPS----LQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDES 229
Cdd:PRK06125 160 LMAFTRALGGKSLDDGVRVVGVNPGPVATDRmltlLKGRARAELGDESRWQELLAGLPLGRPATPEEVADLVAFLASPRS 239

                        250
                 ....*....|...
gi 511847639 230 AYVTGNPVIIDGG 242
Cdd:PRK06125 240 GYTSGTVVTVDGG 252
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 4-244 5.13e-39

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: 135.68  E-value: 5.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVA 82
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLvRECPGIEPVCVDLSDWDATEEALGSVGPVDLLVNNA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  83 GFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMSSVASSiKGVVNRCVYSTSKAAVIGLTKSL 161
Cdd:cd05351   85 AVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQ-RALTNHTVYCSTKAALDMLTKVM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 162 AADFIQQGIRCNCVCPGTVDTpSLQERIQARPNPKEArndFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIIDG 241
Cdd:cd05351  164 ALELGPHKIRVNSVNPTVVMT-DMGRDNWSDPEKAKK---MLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDG 239


                 ...
gi 511847639 242 GWS 244
Cdd:cd05351  240 GFL 242
PRK07774 PRK07774
SDR family oxidoreductase;
1-243 8.73e-39

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 135.26  E-value: 8.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQIRT-LDV----TKKKQIDQFASE 71
Cdd:PRK07774   1 MGRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAErvakQIVADGGTAIAVqVDVsdpdSAKAMADATVSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLFNVAGfVHHGTILDCEEK-DWDFS---MNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGvvnrCVY 147
Cdd:PRK07774  81 FGGIDYLVNNAA-IYGGMKLDLLITvPWDYYkkfMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYS----NFY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriqaRPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK07774 156 GLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATR-----TVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSD 230

                        250
                 ....*....|....*.
gi 511847639 228 ESAYVTGNPVIIDGGW 243
Cdd:PRK07774 231 EASWITGQIFNVDGGQ 246
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 6-242 9.78e-39

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: 134.77  E-value: 9.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEECPGIQ--IRTLDVTKKKQ----IDQFASEIERL 75
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALeqlkEELTNLYKNRviALELDITSKESikelIESYLEKFGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAG---FVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvassIKGVV---------- 142
Cdd:cd08930   82 DILINNAYpspKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIAS----IYGVIapdfriyent 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 143 ---NRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVdtpslqeriqarPNPKEarNDFLKR--QKT--GRFATAE 215
Cdd:cd08930  158 qmySPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGI------------LNNQP--SEFLEKytKKCplKRMLNPE 223

                        250       260
                 ....*....|....*....|....*..
gi 511847639 216 EIALLCVYLASDESAYVTGNPVIIDGG 242
Cdd:cd08930  224 DLRGAIIFLLSDASSYVTGQNLVIDGG 250
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 4-242 1.13e-38

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: 135.05  E-value: 1.13e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL--EECPGIQIRTLDVTKKKQIDQFASE-IER---LDV 77
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATaaEIGPAACAISLDVTDQASIDRCVAAlVDRwgsIDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVASSiKGVVNRCVYSTSKAAVIG 156
Cdd:cd05363   81 LVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGR-RGEALVGVYCATKAAVIS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTP------SLQERIQARPNpKEARNDFLKRQKTGRFATAEEIALLCVYLASDESA 230
Cdd:cd05363  160 LTQSAGLNLIRHGINVNAIAPGVVDGEhwdgvdAKFARYENRPR-GEKKRLVGEAVPFGRMGRAEDLTGMAIFLASTDAD 238

                        250
                 ....*....|..
gi 511847639 231 YVTGNPVIIDGG 242
Cdd:cd05363  239 YIVAQTYNVDGG 250
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
4-242 1.53e-38

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 141.52  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL----DVTKKKQIDQ-FASEIER---L 75
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALgvacDVTDEAAVQAaFEEAALAfggV 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKS-GNIINMSS---VASSiKGVVNrcvYSTSK 151
Cdd:PRK08324 500 DIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASknaVNPG-PNFGA---YGAAK 575

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPS-------LQERIQARP-NPKEARNDFLKRQKTGRFATAEEIALLCVY 223
Cdd:PRK08324 576 AAELHLVRQLALELGPDGIRVNGVNPDAVVRGSgiwtgewIEARAAAYGlSEEELEEFYRARNLLKREVTPEDVAEAVVF 655

                        250
                 ....*....|....*....
gi 511847639 224 LASDESAYVTGNPVIIDGG 242
Cdd:PRK08324 656 LASGLLSKTTGAIITVDGG 674
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 1-242 2.17e-38

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 133.98  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKViATDINESK------LQELEECPGIQIRT-LDVTK----KKQIDQFA 69
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKV-VINYNSSKeaaenlVNELGKEGHDVYAVqADVSKvedaNRLVEEAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGvVNRCVYST 149
Cdd:PRK12935  80 NHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGG-FGQTNYSA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERiqarpnPKEARNDFLKRQKTGRFATAEEIALLCVYLASDeS 229
Cdd:PRK12935 159 AKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEV------PEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRD-G 231

                        250
                 ....*....|...
gi 511847639 230 AYVTGNPVIIDGG 242
Cdd:PRK12935 232 AYITGQQLNINGG 244
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-243 1.17e-37

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 132.30  E-value: 1.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKlQELEECPGIQIRTLDVTKK-KQIDQFASEIER-------L 75
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPT-ETIEQVTALGRRFLSLTADlRKIDGIPALLERavaefghI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVAsSIKGVVNRCVYSTSKAAV 154
Cdd:PRK08993  87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASML-SFQGGIRVPSYTASKSGV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriQARPNpkEARN-DFLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:PRK08993 166 MGVTRLMANEWAKHNINVNAIAPGYMATNNTQ---QLRAD--EQRSaEILDRIPAGRWGLPSDLMGPVVFLASSASDYIN 240

                        250
                 ....*....|
gi 511847639 234 GNPVIIDGGW 243
Cdd:PRK08993 241 GYTIAVDGGW 250
PRK08267 PRK08267
SDR family oxidoreductase;
7-218 1.98e-37

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 131.98  E-value: 1.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE-ECPGIQIRT--LDVTKKKQ----IDQFASEIE-RLDVL 78
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAaELGAGNAWTgaLDVTDRAAwdaaLADFAAATGgRLDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvASSIKGVVNRCVYSTSKAAVIGLT 158
Cdd:PRK08267  82 FNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSS-ASAIYGQPGLAVYSATKFAVRGLT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 159 KSLAADFIQQGIRCNCVCPGTVDTPSLQEriqarpNPKEARNDFLKRqkTGRFATAEEIA 218
Cdd:PRK08267 161 EALDLEWRRHGIRVADVMPLFVDTAMLDG------TSNEVDAGSTKR--LGVRLTPEDVA 212
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 3-242 2.70e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 131.56  E-value: 2.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATdiNESKLQELEEcpGIQIRTLDVTKKKQIDQFASEI-ERL---DVL 78
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTT--ARSRPDDLPE--GVEFVAADLTTAEGCAAVARAVlERLggvDIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAG--FVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIG 156
Cdd:PRK06523  82 VHVLGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPESTTAYAAAKAALST 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTPS---LQERIQA-----RPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:PRK06523 162 YSKSLSKEVAPKGVRVNTVSPGWIETEAavaLAERLAEaagtdYEGAKQIIMDSLGGIPLGRPAEPEEVAELIAFLASDR 241

                        250
                 ....*....|....
gi 511847639 229 SAYVTGNPVIIDGG 242
Cdd:PRK06523 242 AASITGTEYVIDGG 255
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 7-242 3.95e-37

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: 130.50  E-value: 3.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESK-----LQELEECPGIQIRTLDVTKKKQI----DQFASEIERLDV 77
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPgaaaeLQAINPKVKATFVQCDVTSWEQLaaafKKAIEKFGRVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFV--HHGTILDCEEKDWDFSMNLNVRSMY---LMIKAFLPKMLAQKSGNIINMSSVASSIKGVVnRCVYSTSKA 152
Cdd:cd05323   81 LINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVInttYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQ-FPVYSASKH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLA-ADFIQQGIRCNCVCPGTVDTPSLqeriqarPNPKEARNDFLKRQKtgrFATAEEIALLCVYLASDESAy 231
Cdd:cd05323  160 GVVGFTRSLAdLLEYKTGVRVNAICPGFTNTPLL-------PDLVAKEAEMLPSAP---TQSPEVVAKAIVYLIEDDEK- 228

                        250
                 ....*....|.
gi 511847639 232 vTGNPVIIDGG 242
Cdd:cd05323  229 -NGAIWIVDGG 238
PRK07035 PRK07035
SDR family oxidoreductase;
4-242 7.07e-37

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 130.14  E-value: 7.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDinesklQELEECPGI--QIR---------TLDVTKKKQIDQFASEI 72
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSS------RKLDGCQAVadAIVaaggkaealACHIGEMEQIDALFAHI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 E----RLDVLFNVAGF-VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVnRCVY 147
Cdd:PRK07035  80 RerhgRLDILVNNAAAnPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDF-QGIY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK07035 159 SITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT----KFASALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASD 234

                        250
                 ....*....|....*
gi 511847639 228 ESAYVTGNPVIIDGG 242
Cdd:PRK07035 235 ASSYTTGECLNVDGG 249
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 1-242 1.09e-36

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 130.06  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKK-------KQIDQFASE-I 72
Cdd:PRK12823   3 NQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRAAGGEALALTADletyagaQAAMAAAVEaF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGfvhhGTIL-----DCEEKDWDFSMNlnvRSMY---LMIKAFLPKMLAQKSGNIINMSSVASsiKGVvNR 144
Cdd:PRK12823  83 GRIDVLINNVG----GTIWakpfeEYEEEQIEAEIR---RSLFptlWCCRAVLPHMLAQGGGAIVNVSSIAT--RGI-NR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 145 CVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTP-----------SLQERIQARpnpkEARNDFLKRQKTGRFAT 213
Cdd:PRK12823 153 VPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPprrvprnaapqSEQEKAWYQ----QIVDQTLDSSLMKRYGT 228

                        250       260
                 ....*....|....*....|....*....
gi 511847639 214 AEEIALLCVYLASDESAYVTGNPVIIDGG 242
Cdd:PRK12823 229 IDEQVAAILFLASDEASYITGTVLPVGGG 257
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 2-243 1.78e-36

(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: 128.98  E-value: 1.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQ-----IRTL---------DVTKKKQIDQ 67
Cdd:cd05353    1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADkvvdeIKAAggkavanydSVEDGEKIVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  68 FA-SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvASSIKGVVNRCV 146
Cdd:cd05353   81 TAiDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSS-AAGLYGNFGQAN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCP--GTVDTPSLQeriqaRPNPKEArndfLKrqktgrfatAEEIALLCVYL 224
Cdd:cd05353  160 YSAAKLGLLGLSNTLAIEGAKYNITCNTIAPaaGSRMTETVM-----PEDLFDA----LK---------PEYVAPLVLYL 221

                        250
                 ....*....|....*....
gi 511847639 225 ASDESAyVTGNPVIIDGGW 243
Cdd:cd05353  222 CHESCE-VTGGLFEVGAGW 239
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 7-242 2.20e-36

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: 128.73  E-value: 2.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVI-----ATDINESKLQELEEcPGIQIRTlDVTKKKQIDQFASEIE----RLDV 77
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVvnyyrSTESAEAVAAEAGE-RAIAIQA-DVRDRDQVQAMIEEAKnhfgPVDT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVA--GFVHHG----TILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSK 151
Cdd:cd05349   79 IVNNAliDFPFDPdqrkTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQ-NPVVPYHDYTTAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlqeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:cd05349  158 AALLGFTRNMAKELGPYGITVNMVSGGLLKVTD-----ASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARA 232

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:cd05349  233 VTGQNLVVDGG 243
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 4-239 2.92e-36

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: 128.42  E-value: 2.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE---ECPGIQIRTL--DVTKKKQID----QFASEIER 74
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALAdelEAEGGKALVLelDVTDEQQVDaaveRTVEALGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGvVNRCVYSTSKAAV 154
Cdd:cd08934   81 LDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAV-RNSAVYNATKFGV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPNpKEArndFLKRQKTGRFATAEEIALLCVYlASDESAYVTG 234
Cdd:cd08934  160 NAFSEGLRQEVTERGVRVVVIEPGTVDTE-LRDHITHTIT-KEA---YEERISTIRKLQAEDIAAAVRY-AVTAPHHVTV 233


                 ....*
gi 511847639 235 NPVII 239
Cdd:cd08934  234 NEILI 238
PRK09242 PRK09242
SDR family oxidoreductase;
1-244 2.92e-36

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 128.71  E-value: 2.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-----EECPGIQIRTL------DVTKKKQIDQFA 69
Cdd:PRK09242   4 RWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQArdelaEEFPEREVHGLaadvsdDEDRRAILDWVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYST 149
Cdd:PRK09242  84 DHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSG-LTHVRSGAPYGM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPNPKEArndFLKRQKTGRFATAEEIALLCVYLASDES 229
Cdd:PRK09242 163 TKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTP-LTSGPLSDPDYYEQ---VIERTPMRRVGEPEEVAAAVAFLCMPAA 238

                        250
                 ....*....|....*
gi 511847639 230 AYVTGNPVIIDGGWS 244
Cdd:PRK09242 239 SYITGQCIAVDGGFL 253
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-243 4.33e-36

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 128.10  E-value: 4.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINES-KLQELEECPGIQIR--TLDVTKKKQIDQFASE----IERLD 76
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEApETQAQVEALGRKFHfiTADLIQQKDIDSIVSQavevMGHID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKS-GNIINMSSVAsSIKGVVNRCVYSTSKAAVI 155
Cdd:PRK12481  86 ILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASML-SFQGGIRVPSYTASKSAVM 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDTPSlqeriQARPNPKEARND-FLKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:PRK12481 165 GLTRALATELSQYNINVNAIAPGYMATDN-----TAALRADTARNEaILERIPASRWGTPDDLAGPAIFLSSSASDYVTG 239


                 ....*....
gi 511847639 235 NPVIIDGGW 243
Cdd:PRK12481 240 YTLAVDGGW 248
PRK07074 PRK07074
SDR family oxidoreductase;
7-242 5.17e-36

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 127.96  E-value: 5.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELeecpgiqIRTL----------DVTKKKQID----QFASEI 72
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAF-------ADALgdarfvpvacDLTDAASLAaalaNAAAER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSikGVVNRCVYSTSKA 152
Cdd:PRK07074  76 GPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGM--AALGHPAYSAAKA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQktgRFATAEEIALLCVYLASDESAYV 232
Cdd:PRK07074 154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQVFEELKKWYPLQ---DFATPDDVANAVLFLASPAARAI 230

                        250
                 ....*....|
gi 511847639 233 TGNPVIIDGG 242
Cdd:PRK07074 231 TGVCLPVDGG 240
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 6-222 5.37e-36

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 127.37  E-value: 5.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-LEECPG--------IQIRTLDVTKKKQIDQ-FASEIERL 75
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEaVEEIEAeanasgqkVSYISADLSDYEEVEQaFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 ---DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKA 152
Cdd:cd08939   81 gppDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALV-GIYGYSAYCPSKF 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARpnPKEARndflKRQKTGRFATAEEIALLCV 222
Cdd:cd08939  160 ALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTK--PEETK----AIEGSSGPITPEEAARIIV 223
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 4-244 6.59e-36

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 128.48  E-value: 6.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQIR-TLDVTKKKQIDQFASEIE----R 74
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEavvaEIKAAGGEALAvKADVLDKESLEQARQQILedfgP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHG---------------TILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVA--SS 137
Cdd:PRK08277  88 CDILINGAGGNHPKattdnefhelieptkTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNafTP 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 138 IKGVVnrcVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslQER---IQARPNPKEARNDFLKRQKTGRFATA 214
Cdd:PRK08277 168 LTKVP---AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE--QNRallFNEDGSLTERANKILAHTPMGRFGKP 242

                        250       260       270
                 ....*....|....*....|....*....|.
gi 511847639 215 EEIALLCVYLASDE-SAYVTGNPVIIDGGWS 244
Cdd:PRK08277 243 EELLGTLLWLADEKaSSFVTGVVLPVDGGFS 273
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 4-242 8.59e-36

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: 127.21  E-value: 8.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVI-------ATDINESKLQELEECPGIQIrtlDVTKKKQIDQFASEI---- 72
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIisarkaeACADAAEELSAYGECIAIPA---DLSSEEGIEALVARVaers 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKS----GNIINMSSVASSIKGVVNRCVYS 148
Cdd:cd08942   81 DRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGLENYSYG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVdtPSLQERIQArpNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:cd08942  161 ASKAAVHQLTRKLAKELAGEHITVNAIAPGRF--PSKMTAFLL--NDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRA 236

                        250
                 ....*....|....
gi 511847639 229 SAYVTGNPVIIDGG 242
Cdd:cd08942  237 GAYLTGAVIPVDGG 250
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 4-182 1.06e-35

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


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 127.32  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EEC-----PGIQIRTLDVTKKKQIDQFASEIE---- 73
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVkSEClelgaPSPHVVPLDMSDLEDAEQVVEEALklfg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAA 153
Cdd:cd05332   81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKI-GVPFRTAYAASKHA 159

                        170       180
                 ....*....|....*....|....*....
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:cd05332  160 LQGFFDSLRAELSEPNISVTVVCPGLIDT 188
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 4-245 1.42e-35

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 127.15  E-value: 1.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIatdIN--------ESKLQELEECPG--IQIRTlDVTK----KKQIDQFA 69
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVV---INyrsdeeeaNDVAEEIKKAGGeaIAVKG-DVTVesdvVNLIQTAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVASSI--KGVVNrcv 146
Cdd:PRK08936  81 KEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIpwPLFVH--- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIqARPnpkEARNDFLKRQKTGRFATAEEIALLCVYLAS 226
Cdd:PRK08936 158 YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKF-ADP---KQRADVESMIPMGYIGKPEEIAAVAAWLAS 233

                        250
                 ....*....|....*....
gi 511847639 227 DESAYVTGNPVIIDGGWSL 245
Cdd:PRK08936 234 SEASYVTGITLFADGGMTL 252
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 4-242 1.62e-35

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 127.10  E-value: 1.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ---ELEECPGIQIRTL--DVTKKKQIDQFASEIER---- 74
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDkglAAYRELGIEAHGYvcDVTDEDGVQAMVSQIEKevgv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAV 154
Cdd:PRK07097  88 IDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSEL-GRETVSAYAAAKGGL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQE-RIQARPNPKEARNDF-LKRQKTGRFATAEEIALLCVYLASDESAYV 232
Cdd:PRK07097 167 KMLTKNIASEYGEANIQCNGIGPGYIATPQTAPlRELQADGSRHPFDQFiIAKTPAARWGDPEDLAGPAVFLASDASNFV 246

                        250
                 ....*....|
gi 511847639 233 TGNPVIIDGG 242
Cdd:PRK07097 247 NGHILYVDGG 256
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 4-242 1.74e-35

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 126.81  E-value: 1.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEC---PGIQIRTL--DVTK----KKQIDQFASEIER 74
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESlkgQGLSAHALafDVTDhdavRAAIDAFEAEIGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIK--GVVNrcvYSTSKA 152
Cdd:PRK07523  88 IDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALArpGIAP---YTATKG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQARPnpkeARNDFL-KRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:PRK07523 165 AVGNLTKGMATDWAKHGLQCNAIAPGYFDTP-LNAALVADP----EFSAWLeKRTPAGRWGKVEELVGACVFLASDASSF 239

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:PRK07523 240 VNGHVLYVDGG 250
PRK06128 PRK06128
SDR family oxidoreductase;
1-242 2.80e-35

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 127.28  E-value: 2.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINE-----SKLQELEECPGIQIRTL--DVTK----KKQIDQFA 69
Cdd:PRK06128  50 FGRLQGRKALITGADSGIGRATAIAFAREGADIALNYLPEeeqdaAEVVQLIQAEGRKAVALpgDLKDeafcRQLVERAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGF-VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSgnIINMSSVAS--SIKGVVNrcv 146
Cdd:PRK06128 130 KELGGLDILVNIAGKqTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGAS--IINTGSIQSyqPSPTLLD--- 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQEriqARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLAS 226
Cdd:PRK06128 205 YASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTP-LQP---SGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLAS 280

                        250
                 ....*....|....*.
gi 511847639 227 DESAYVTGNPVIIDGG 242
Cdd:PRK06128 281 QESSYVTGEVFGVTGG 296
PRK05650 PRK05650
SDR family oxidoreductase;
9-218 5.36e-35

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 125.92  E-value: 5.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpgiQIRTL---------DVTKKKQIDQFASEIER----L 75
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLK----LLREAggdgfyqrcDVRDYSQLTALAQACEEkwggI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAS--SIKGVVNrcvYSTSKAA 153
Cdd:PRK05650  79 DVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGlmQGPAMSS---YNVAKAG 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTgrfaTAEEIA 218
Cdd:PRK05650 156 VVALSETLLVELADDEIGVHVVCPSFFQTNLLDSFRGPNPAMKAQVGKLLEKSPI----TAADIA 216
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
6-242 5.54e-35

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 125.22  E-value: 5.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINE----SKLQELEECPGIQIR-TLDVTKKKQI----DQFASEIERLD 76
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEetaqAAADKLSKDGGKAIAvKADVSDRDQVfaavRQVVDTFGDLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMSSVAssikGVV---NRCVYSTSKA 152
Cdd:PRK08643  82 VVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINATSQA----GVVgnpELAVYSSTKF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQEriQARPNPKEARND-------FLKRQKTGRFATAEEIALLCVYLA 225
Cdd:PRK08643 158 AVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFD--IAHQVGENAGKPdewgmeqFAKDITLGRLSEPEDVANCVSFLA 235

                        250
                 ....*....|....*..
gi 511847639 226 SDESAYVTGNPVIIDGG 242
Cdd:PRK08643 236 GPDSDYITGQTIIVDGG 252
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 4-242 9.69e-35

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: 124.31  E-value: 9.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVI-----ATDINESKLQELEECPG--IQIRTlDVTKKKQIDQFASEIE--- 73
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVvnyasSKAAAEEVVAEIEAAGGkaIAVQA-DVSDPSQVARLFDAAEkaf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 -RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSIkGVVNRCVYSTSKA 152
Cdd:cd05362   80 gGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAA-YTPNYGAYAGSKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERiqarpNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYV 232
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAG-----KTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWV 231

                        250
                 ....*....|
gi 511847639 233 TGNPVIIDGG 242
Cdd:cd05362  232 NGQVIRANGG 241
PRK05855 PRK05855
SDR family oxidoreductase;
2-182 1.18e-34

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 130.10  E-value: 1.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpgiQIR---------TLDVTKKKQIDQFASEI 72
Cdd:PRK05855 311 GPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAE----LIRaagavahayRVDVSDADAMEAFAEWV 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ER----LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVAS-SIKGVVNrcV 146
Cdd:PRK05855 387 RAehgvPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAyAPSRSLP--A 464

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK05855 465 YATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK07831 PRK07831
SDR family oxidoreductase;
2-234 1.19e-34

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 124.76  E-value: 1.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAA-QGIGRAAALAFAREGAKVIATDINESKLQEL-----EECPGIQIRTL--DVTKKKQ----IDQFA 69
Cdd:PRK07831  13 GLLAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETadelaAELGLGRVEAVvcDVTSEAQvdalIDAAV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMSSVaSSIKGVVNRCVYS 148
Cdd:PRK07831  93 ERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGhGGVIVNNASV-LGWRAQHGQAHYA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLqeriqARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:PRK07831 172 AAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFL-----AKVTSAELLDELAAREAFGRAAEPWEVANVIAFLASDY 246


                 ....*.
gi 511847639 229 SAYVTG 234
Cdd:PRK07831 247 SSYLTG 252
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-182 1.25e-34

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 124.03  E-value: 1.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG-----IQIRTLDVTKKKQID----QFASE 71
Cdd:PRK07666   2 AQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEaygvkVVIATADVSDYEEVTaaieQLKNE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSK 151
Cdd:PRK07666  82 LGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQ-KGAAVTSAYSASK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK07666 161 FGVLGLTESLMQEVRKHNIRVTALTPSTVAT 191
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-245 1.44e-34

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 124.33  E-value: 1.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRT-------LDVTKKKQIDQFASEIERLD 76
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkklslveLDITDQESLEEFLSKSAEKY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNvaGFVH--------HGT-ILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvassIKGVVN---- 143
Cdd:PRK09186  82 GKID--GAVNcayprnkdYGKkFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISS----IYGVVApkfe 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 144 ---------RCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTV-DtpslqeriqarpNPKEArndFLKRQKT----- 208
Cdd:PRK09186 156 iyegtsmtsPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIlD------------NQPEA---FLNAYKKccngk 220

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 511847639 209 GRFaTAEEIALLCVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK09186 221 GML-DPDDICGTLVFLLSDQSKYITGQNIIVDDGFSL 256
PRK07062 PRK07062
SDR family oxidoreductase;
4-244 2.20e-34

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 124.00  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-----LEECPGIQI--RTLDVTKKKQIDQFASEIE--- 73
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASaearlREKFPGARLlaARCDVLDEADVAAFAAAVEarf 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 -RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSS----------VASSikgvv 142
Cdd:PRK07062  86 gGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSllalqpephmVATS----- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 143 nrcvysTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDF---LKRQKT---GRFATAEE 216
Cdd:PRK07062 161 ------AARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQSWEAWtaaLARKKGiplGRLGRPDE 234

                        250       260
                 ....*....|....*....|....*...
gi 511847639 217 IALLCVYLASDESAYVTGNPVIIDGGWS 244
Cdd:PRK07062 235 AARALFFLASPLSSYTTGSHIDVSGGFA 262
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-244 4.01e-34

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 123.78  E-value: 4.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE----LEECPGIQIRTLDVTKKKQI----DQFASEIER 74
Cdd:PLN02253  15 RLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNvcdsLGGEPNVCFFHCDVTVEDDVsravDFTVDKFGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHH--GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCvYSTSKA 152
Cdd:PLN02253  95 LDIMVNNAGLTGPpcPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHA-YTGSKH 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDT----PSLQERIQARPNPKEARNdFLKRQKT--GRFATAEEIALLCVYLAS 226
Cdd:PLN02253 174 AVLGLTRSVAAELGKHGIRVNCVSPYAVPTalalAHLPEDERTEDALAGFRA-FAGKNANlkGVELTVDDVANAVLFLAS 252

                        250
                 ....*....|....*...
gi 511847639 227 DESAYVTGNPVIIDGGWS 244
Cdd:PLN02253 253 DEARYISGLNLMIDGGFT 270
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-243 6.03e-34

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 127.66  E-value: 6.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQ--IRTLDVTKKKQIDQFASEIE----RLDVL 78
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEhlSVQADITDEAAVESAFAQIQarwgRLDVL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHH-GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVIGL 157
Cdd:PRK06484 348 VNNAGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLL-ALPPRNAYCASKAAVTML 424

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQArpnpkeARNDF---LKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:PRK06484 425 SRSLACEWAPAGIRVNTVAPGYIETPAVLALKAS------GRADFdsiRRRIPLGRLGDPEEVAEAIAFLASPAASYVNG 498


                 ....*....
gi 511847639 235 NPVIIDGGW 243
Cdd:PRK06484 499 ATLTVDGGW 507
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 4-234 6.08e-34

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 122.29  E-value: 6.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEECPGIQ--IRTLDV--TKKKQIDQFASEIE-- 73
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLeavyDEIEAAGGPQpaIIPLDLltATPQNYQQLADTIEeq 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 --RLD-VLFNvAGFVhhGTILDCEEKD---WDFSMNLNVRSMYLMIKAFLPKMLAQKSGNII-NMSSVASsiKGVVNRCV 146
Cdd:PRK08945  90 fgRLDgVLHN-AGLL--GELGPMEQQDpevWQDVMQVNVNATFMLTQALLPLLLKSPAASLVfTSSSVGR--QGRANWGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslQERIQARP--NPKEarndfLKrqktgrfaTAEEIALLCVYL 224
Cdd:PRK08945 165 YAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT---AMRASAFPgeDPQK-----LK--------TPEDIMPLYLYL 228

                        250
                 ....*....|
gi 511847639 225 ASDESAYVTG 234
Cdd:PRK08945 229 MGDDSRRKNG 238
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-182 7.54e-34

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 122.74  E-value: 7.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-LEECPGIQIRTLDVTKKKQIDQFASEIER----LDV 77
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKEtAAELGLVVGGPLDVTDPASFAAFLDAVEAdlgpIDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVIGL 157
Cdd:PRK07825  82 LVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKI-PVPGMATYCASKHAVVGF 160

                        170       180
                 ....*....|....*....|....*
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK07825 161 TDAARLELRGTGVHVSVVLPSFVNT 185
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 7-185 1.35e-33

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: 121.02  E-value: 1.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG---IQIRTLDVTKKKQ----IDQFASEI-ERLDVL 78
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGaenVVAGALDVTDRAAwaaaLADFAAATgGRLDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvASSIKGVVNRCVYSTSKAAVIGLT 158
Cdd:cd08931   81 FNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTAS-SSAIYGQPDLAVYSATKFAVRGLT 159

                        170       180
                 ....*....|....*....|....*..
gi 511847639 159 KSLAADFIQQGIRCNCVCPGTVDTPSL 185
Cdd:cd08931  160 EALDVEWARHGIRVADVWPWFVDTPIL 186
PRK07577 PRK07577
SDR family oxidoreductase;
7-245 1.57e-33

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 120.99  E-value: 1.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESklqelEECPGiQIRTLDVTKKKQIDQFASEI---ERLDVLFNVAG 83
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARSAI-----DDFPG-ELFACDLADIEQTAATLAQIneiHPVDAIVNNVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  84 FVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAssIKGVVNRCVYSTSKAAVIGLTKSLAA 163
Cdd:PRK07577  78 IALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA--IFGALDRTSYSAAKSALVGCTRTWAL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 164 DFIQQGIRCNCVCPGTVDTPSLQERiqaRPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIIDGGW 243
Cdd:PRK07577 156 ELAEYGITVNAVAPGPIETELFRQT---RPVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDGGG 232


                 ..
gi 511847639 244 SL 245
Cdd:PRK07577 233 SL 234
PRK12743 PRK12743
SDR family oxidoreductase;
7-245 2.10e-33

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 121.29  E-value: 2.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIAT------DINESKLQELEECPGIQIRTLDVTK----KKQIDQFASEIERLD 76
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITwhsdeeGAKETAEEVRSHGVRAEIRQLDLSDlpegAQALDKLIQRLGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVASSIKGVVNrCVYSTSKAAVI 155
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGA-SAYTAAKHALG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDTP-SLQERIQARPNPKEArndflkrQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:PRK12743 162 GLTKAMALELVEHGILVNAVAPGAIATPmNGMDDSDVKPDSRPG-------IPLGRPGDTHEIASLVAWLCSEGASYTTG 234

                        250
                 ....*....|.
gi 511847639 235 NPVIIDGGWSL 245
Cdd:PRK12743 235 QSLIVDGGFML 245
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-242 3.51e-33

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 120.45  E-value: 3.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-LEEC--PGIQIRT--LDVTKKKQI----DQFASEIE 73
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEaVAECgaLGTEVRGyaANVTDEEDVeatfAQIAEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEE---------KDWDFSMNLNVRSMYLMIKAFLPKMLAQKS-GNIINMSSVASSikGVVN 143
Cdd:PRK08217  82 QLNGLINNAGILRDGLLVKAKDgkvtskmslEQFQSVIDVNLTGVFLCGREAAAKMIESGSkGVIINISSIARA--GNMG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 144 RCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriQARPnpkEARNDFLKRQKTGRFATAEEIALLCVY 223
Cdd:PRK08217 160 QTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA---AMKP---EALERLEKMIPVGRLGEPEEIAHTVRF 233

                        250
                 ....*....|....*....
gi 511847639 224 LAsdESAYVTGNPVIIDGG 242
Cdd:PRK08217 234 II--ENDYVTGRVLEIDGG 250
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 5-242 4.84e-33

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: 120.34  E-value: 4.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEEcPGIQI--RTLDVTKKKQIDQF-ASEIER--- 74
Cdd:cd08945    2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLattvKELRE-AGVEAdgRTCDVRSVPEIEALvAAAVARygp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPK--MLAQKSGNIINMSSVASSiKGVVNRCVYSTSKA 152
Cdd:cd08945   81 IDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGK-QGVVHAAPYSASKH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQA------RPNPKEARNDFLKRQKTGRFATAEEIALLCVYLAS 226
Cdd:cd08945  160 GVVGFTKALGLELARTGITVNAVCPGFVETP-MAASVREhyadiwEVSTEEAFDRITARVPLGRYVTPEEVAGMVAYLIG 238

                        250
                 ....*....|....*.
gi 511847639 227 DESAYVTGNPVIIDGG 242
Cdd:cd08945  239 DGAAAVTAQALNVCGG 254
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 6-242 6.38e-33

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 120.14  E-value: 6.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE----------CPGIQIrtlDVTKKKQIDQFASEIE-- 73
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQeinaeygegmAYGFGA---DATSEQSVLALSRGVDei 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 --RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMSSvASSIKGVVNRCVYSTS 150
Cdd:PRK12384  79 fgRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINS-KSGKVGSKHNSGYSAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 151 KAAVIGLTKSLAADFIQQGIRCNCVCPGT-VDTP---SLQERIQARPN--PKEARNDFLKRQKTGRFATAEEIALLCVYL 224
Cdd:PRK12384 158 KFGGVGLTQSLALDLAEYGITVHSLMLGNlLKSPmfqSLLPQYAKKLGikPDEVEQYYIDKVPLKRGCDYQDVLNMLLFY 237

                        250
                 ....*....|....*...
gi 511847639 225 ASDESAYVTGNPVIIDGG 242
Cdd:PRK12384 238 ASPKASYCTGQSINVTGG 255
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 8-242 7.66e-33

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 119.60  E-value: 7.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL--------QELEECPGIQIRTLDVTKKKQIDQFA-SEIERLDVL 78
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAeavaaaiqQAGGQAIGLECNVTSEQDLEAVVKATvSQFGGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFV-HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVvNRCVYSTSKAAVIGL 157
Cdd:cd05365   81 VNNAGGGgPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNV-RIAAYGSSKAAVNHM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQarPNPKEARndfLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPV 237
Cdd:cd05365  160 TRNLAFDLGPKGIRVNAVAPGAVKTDALASVLT--PEIERAM---LKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVL 234


                 ....*
gi 511847639 238 IIDGG 242
Cdd:cd05365  235 TVSGG 239
PRK06194 PRK06194
hypothetical protein; Provisional
 1-240 8.46e-33

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 120.51  E-value: 8.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECpGIQI--RTLDVTKKKQIDQFASEIER 74
Cdd:PRK06194   1 MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDravaELRAQ-GAEVlgVRTDVSDAAQVEALADAALE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 ----LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ------KSGNIINMSSVASSIkGVVNR 144
Cdd:PRK06194  80 rfgaVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpaYEGHIVNTASMAGLL-APPAM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 145 CVYSTSKAAVIGLTKSLAADFIQQG--IRCNCVCPGTVDT---PSLQERIQARPNPKEARNDFLKRQK-TGRF-----AT 213
Cdd:PRK06194 159 GIYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTgiwQSERNRPADLANTAPPTRSQLIAQAmSQKAvgsgkVT 238

                        250       260
                 ....*....|....*....|....*..
gi 511847639 214 AEEIALLCVYLASDESAYVTGNPVIID 240
Cdd:PRK06194 239 AEEVAQLVFDAIRAGRFYIYSHPQALA 265
PRK07814 PRK07814
SDR family oxidoreductase;
3-242 9.58e-33

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 119.88  E-value: 9.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpgiQIRTL---------DVTKKKQIDQFA---- 69
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAE----QIRAAgrrahvvaaDLAHPEATAGLAgqav 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMSSVASSIKGvvnR--CV 146
Cdd:PRK07814  83 EAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAG---RgfAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQgIRCNCVCPGTVDTPSLqERIQARPnpkEARNDFLKRQKTGRFATAEEIALLCVYLAS 226
Cdd:PRK07814 160 YGTAKAALAHYTRLAALDLCPR-IRVNAIAPGSILTSAL-EVVAAND---ELRAPMEKATPLRRLGDPEDIAAAAVYLAS 234

                        250
                 ....*....|....*.
gi 511847639 227 DESAYVTGNPVIIDGG 242
Cdd:PRK07814 235 PAGSYLTGKTLEVDGG 250
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 6-197 1.29e-32

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: 118.86  E-value: 1.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEECPGIQIRTL--DVTKKKQI-DQFASEIERLDV- 77
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLdavaKEIEEKYGVETKTIaaDFSAGDDIyERIEKELEGLDIg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 -LFNVAGFVHH--GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKgVVNRCVYSTSKAAV 154
Cdd:cd05356   81 iLVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIP-TPLLATYSASKAFL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDT--PSLQERIQARPNPKE 197
Cdd:cd05356  160 DFFSRALYEEYKSQGIDVQSLLPYLVATkmSKIRKSSLFVPSPEQ 204
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 7-228 1.35e-32

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: 118.23  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE-ECPGIQIRTLDVTKKKQ----IDQFASEIERLDVLFNV 81
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSaSGGDVEAVPYDARDPEDaralVDALRDRFGRIDVLVHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  82 AGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsiKGVVN-RCVYSTSKAAVIGLTKS 160
Cdd:cd08932   81 AGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSG--KRVLAgNAGYSASKFALRALAHA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 161 LAADFIQQGIRCNCVCPGTVDTPSLQ--ERIQARPnpkearndflkrqkTGRFATAEEIALLCVYLASDE 228
Cdd:cd08932  159 LRQEGWDHGVRVSAVCPGFVDTPMAQglTLVGAFP--------------PEEMIQPKDIANLVRMVIELP 214
PRK07454 PRK07454
SDR family oxidoreductase;
11-183 1.78e-32

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 118.52  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  11 VTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPG-IQIRTLDVTK----KKQIDQFASEIERLDVLFNV 81
Cdd:PRK07454  11 ITGASSGIGKATALAFAKAGWDLALVARSQDALEalaaELRSTGVkAAAYSIDLSNpeaiAPGIAELLEQFGCPDVLINN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  82 AGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSKAAVIGLTKSL 161
Cdd:PRK07454  91 AGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAAR-NAFPQWGAYCVSKAALAAFTKCL 169

                        170       180
                 ....*....|....*....|..
gi 511847639 162 AADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK07454 170 AEEERSHGIRVCTITLGAVNTP 191
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 6-242 1.84e-32

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: 118.65  E-value: 1.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL----DVTKKKQI----DQFASEIERLDV 77
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALgvqcDVTSEAQVqsafEQAVLEFGGLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIGL 157
Cdd:cd08943   81 VVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARN----DFLKRQKTGRFATAEEIALLCVYLASDESAYVT 233
Cdd:cd08943  161 ARCLALEGGEDGIRVNTVNPDAVFRGSKIWEGVWRAARAKAYGlleeEYRTRNLLKREVLPEDVAEAVVAMASEDFGKTT 240


                 ....*....
gi 511847639 234 GNPVIIDGG 242
Cdd:cd08943  241 GAIVTVDGG 249
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 4-242 2.57e-32

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: 118.41  E-value: 2.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIatdINESKLQELEEC-PGIQIRTLDVTKKKQIDQFASEIERL------- 75
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVV---VSSRKQQNVDRAvATLQGEGLSVTGTVCHVGKAEDRERLvatavnl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 ----DVLF-NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTS 150
Cdd:cd08936   85 hggvDILVsNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVA-AFHPFPGLGPYNVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 151 KAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESA 230
Cdd:cd08936  164 KTALLGLTKNLAPELAPRNIRVNCLAPGLIKT----SFSSALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDAS 239

                        250
                 ....*....|..
gi 511847639 231 YVTGNPVIIDGG 242
Cdd:cd08936  240 YITGETVVVGGG 251
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 7-182 3.52e-32

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: 117.77  E-value: 3.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECP-----GIQIRTLDVTK----KKQIDQFASEIERLD 76
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELaDELGakfpvKVLPLQLDVSDresiEAALENLPEEFRDID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHhGT--ILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSKAAV 154
Cdd:cd05346   81 ILVNNAGLAL-GLdpAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGR-YPYAGGNVYCATKAAV 158

                        170       180
                 ....*....|....*....|....*...
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:cd05346  159 RQFSLNLRKDLIGTGIRVTNIEPGLVET 186
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 1-245 6.64e-32

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 116.94  E-value: 6.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG--IQIRTLDVTKKKQIDQFA----SEIER 74
Cdd:PRK12936   1 MFDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGerVKIFPANLSDRDEVKALGqkaeADLEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAV 154
Cdd:PRK12936  81 VDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVV-GVTGNPGQANYCASKAGM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPslqerIQARPNPKEaRNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIESA-----MTGKLNDKQ-KEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTG 233

                        250
                 ....*....|.
gi 511847639 235 NPVIIDGGWSL 245
Cdd:PRK12936 234 QTIHVNGGMAM 244
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 6-245 6.88e-32

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 117.00  E-value: 6.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLqELEECPGIQIR--TLDVTKKKQIDQFASEIE----RLDVLF 79
Cdd:cd05371    2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPG-ETVAKLGDNCRfvPVDVTSEKDVKAALALAKakfgRLDIVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHHGTILDCEEK------DWDFSMNLNVRSMYLMIKAFLPKMLAQ------KSGNIINMSSVASsIKGVVNRCVY 147
Cdd:cd05371   81 NCAGIAVAAKTYNKKGQqphsleLFQRVINVNLIGTFNVIRLAAGAMGKNepdqggERGVIINTASVAA-FEGQIGQAAY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQEriqarpNPKEARnDFLKRQKT--GRFATAEEIALLCVYLA 225
Cdd:cd05371  160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAG------LPEKVR-DFLAKQVPfpSRLGDPAEYAHLVQHII 232

                        250       260
                 ....*....|....*....|
gi 511847639 226 sdESAYVTGNPVIIDGGWSL 245
Cdd:cd05371  233 --ENPYLNGEVIRLDGAIRM 250
PRK07832 PRK07832
SDR family oxidoreductase;
7-205 2.10e-31

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 116.30  E-value: 2.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPG--IQIRTLDVTKKKQIDQFASEI----ERLD 76
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAqtvaDARALGGtvPEHRALDISDYDAVAAFAADIhaahGSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKML-AQKSGNIINMSSvASSIKGVVNRCVYSTSKAAVI 155
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVaAGRGGHLVNVSS-AAGLVALPWHAAYSASKFGLR 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDTPsLQERIQ----ARPNP--KEARNDFLKR 205
Cdd:PRK07832 160 GLSEVLRFDLARHGIGVSVVVPGAVKTP-LVNTVEiagvDREDPrvQKWVDRFRGH 214
PRK06124 PRK06124
SDR family oxidoreductase;
4-244 3.10e-31

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 115.58  E-value: 3.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpgiQIRT---------LDVTKKKQIDQFASEIE- 73
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVA----ALRAaggaaealaFDIADEEAVAAAFARIDa 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 ---RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTS 150
Cdd:PRK06124  85 ehgRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQV-ARAGDAVYPAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 151 KAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqeriqaRPNPKEARN----DFLK-RQKTGRFATAEEIALLCVYLA 225
Cdd:PRK06124 164 KQGLTGLMRALAAEFGPHGITSNAIAPGYFAT---------ETNAAMAADpavgPWLAqRTPLGRWGRPEEIAGAAVFLA 234

                        250
                 ....*....|....*....
gi 511847639 226 SDESAYVTGNPVIIDGGWS 244
Cdd:PRK06124 235 SPAASYVNGHVLAVDGGYS 253
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 4-234 3.51e-31

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: 114.98  E-value: 3.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL------EECPGIQIRTLDVTK--KKQIDQFASEIE-- 73
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVadhineEGGRQPQWFILDLLTctSENCQQLAQRIAvn 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 --RLDVLFNVAGFVhhGTILDCEE---KDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIInMSSVASSIKGVVNRCVYS 148
Cdd:cd05340   82 ypRLDGVLHNAGLL--GDVCPLSEqnpQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLV-FTSSSVGRQGRANWGAYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPslqERIQARP--NPKearndflkrqktgRFATAEEIALLCVYLAS 226
Cdd:cd05340  159 VSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTA---MRASAFPteDPQ-------------KLKTPADIMPLYLWLMG 222


                 ....*...
gi 511847639 227 DESAYVTG 234
Cdd:cd05340  223 DDSRRKTG 230
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 1-242 4.86e-31

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 115.93  E-value: 4.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN-------------ESKLQELEECPGIQI-RTLDVTKKKQ-- 64
Cdd:PRK07791   1 MGLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGvgldgsasggsaaQAVVDEIVAAGGEAVaNGDDIADWDGaa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  65 --IDQFASEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGN-----IINMSSvAS 136
Cdd:PRK07791  81 nlVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAEsKAGRavdarIINTSS-GA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 137 SIKGVVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPgtVDTPSLQERIQArpnpkearnDFLKRQKTGRF-ATA- 214
Cdd:PRK07791 160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP--AARTRMTETVFA---------EMMAKPEEGEFdAMAp 228

                        250       260
                 ....*....|....*....|....*...
gi 511847639 215 EEIALLCVYLASDESAYVTGNPVIIDGG 242
Cdd:PRK07791 229 ENVSPLVVWLGSAESRDVTGKVFEVEGG 256
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 4-245 6.11e-31

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: 114.61  E-value: 6.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQIRTL--DVTKKKQIDQFASEIE---- 73
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEaaaeEISSATGGRAHPIqcDVRDPEAVEAAVDETLkefg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAG--FvhhgtILDCEE---KDWDFSMNLNVRSMYLMIKAFLPKMLAQKS-GNIINMSS--VASSIKGVVNRc 145
Cdd:cd05369   81 KIDILINNAAgnF-----LAPAESlspNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISAtyAYTGSPFQVHS- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 146 vySTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIqarpNPKEARNDFLKRQ-KTGRFATAEEIALLCVYL 224
Cdd:cd05369  155 --AAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERL----APSGKSEKKMIERvPLGRLGTPEEIANLALFL 228

                        250       260
                 ....*....|....*....|.
gi 511847639 225 ASDESAYVTGNPVIIDGGWSL 245
Cdd:cd05369  229 LSDAASYINGTTLVVDGGQWL 249
PRK05867 PRK05867
SDR family oxidoreductase;
4-244 6.19e-31

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 114.75  E-value: 6.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPG--IQIRTlDVTKKKQI----DQFASEIE 73
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEkladEIGTSGGkvVPVCC-DVSQHQQVtsmlDQVTAELG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ-KSGNIINMSSVASSIKGVVNRCV-YSTSK 151
Cdd:PRK05867  86 GIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVPQQVShYCASK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpSLQERIQarpnpkEARNDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:PRK05867 166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILT-ELVEPYT------EYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSY 238

                        250
                 ....*....|...
gi 511847639 232 VTGNPVIIDGGWS 244
Cdd:PRK05867 239 MTGSDIVIDGGYT 251
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 6-244 3.29e-30

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: 112.67  E-value: 3.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG-----IQIRTLDVTKKKQIDQFASEI-ERLDVLF 79
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGpnlffVHGDVADETLVKFVVYAMLEKlGRIDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKsGNIINMSSvASSIKGVVNRCVYSTSKAAVIGLTK 159
Cdd:cd09761   81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIAS-TRAFQSEPDSEAYAASKGGLVALTH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 160 SLAADfIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEArndflKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVII 239
Cdd:cd09761  159 ALAMS-LGPDIRVNCISPGWINTTEQQEFTAAPLTQEDH-----AQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIV 232


                 ....*
gi 511847639 240 DGGWS 244
Cdd:cd09761  233 DGGMT 237
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 4-183 5.64e-30

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: 112.10  E-value: 5.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT-------DINESK---------LQELEE----CPGIQirtLDVTKKK 63
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAaktasegDNGSAKslpgtieetAEEIEAaggqALPIV---VDVRDED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  64 QI----DQFASEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIK 139
Cdd:cd05338   78 QVralvEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPP-LSLR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 511847639 140 GVVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGT-VDTP 183
Cdd:cd05338  157 PARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTaIETP 201
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 9-193 7.11e-30

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: 111.65  E-value: 7.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE-----CPGIQIRTLDVTKKKQ----IDQFASEIERLDVLF 79
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAellnpNPSVEVEILDVTDEERnqlvIAELEAELGGLDLVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYSTSKAAVIGLTK 159
Cdd:cd05350   81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAA-LRGLPGAAAYSASKAALSSLAE 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 511847639 160 SLAADFIQQGIRCNCVCPGTVDTPsLQERIQARP 193
Cdd:cd05350  160 SLRYDVKKRGIRVTVINPGFIDTP-LTANMFTMP 192
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-245 9.21e-30

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 111.97  E-value: 9.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL--DVTK----KKQIDQFASEIER 74
Cdd:PRK06200   1 MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVegDVTSyadnQRAVDQTVDAFGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILdcEEKDWD-----FS--MNLNVRSMYLMIKAFLPKmLAQKSGNIINMSSVASSIKGVVNRCvY 147
Cdd:PRK06200  81 LDCFVGNAGIWDYNTSL--VDIPAEtldtaFDeiFNVNVKGYLLGAKAALPA-LKASGGSMIFTLSNSSFYPGGGGPL-Y 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQgIRCNCVCPGTVDTP-------SLQE-RIQARPNpkeaRNDFLK-RQKTGRFATAEEIA 218
Cdd:PRK06200 157 TASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDlrgpaslGQGEtSISDSPG----LADMIAaITPLQFAPQPEDHT 231

                        250       260
                 ....*....|....*....|....*...
gi 511847639 219 LLCVYLASDE-SAYVTGNPVIIDGGWSL 245
Cdd:PRK06200 232 GPYVLLASRRnSRALTGVVINADGGLGI 259
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 7-182 1.78e-29

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: 110.02  E-value: 1.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGA-KVIATDINESKLQE-----LEECPGIQIRTLDVTKKKQIDQFASEIE----RLD 76
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAaveklRAEGLSVRFHQLDVTDDASIEAAADFVEekygGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFV---HHGTILDCEEkdWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKgvvnrCVYSTSKAA 153
Cdd:cd05324   81 ILVNNAGIAfkgFDDSTPTREQ--ARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLT-----SAYGVSKAA 153

                        170       180
                 ....*....|....*....|....*....
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:cd05324  154 LNALTRILAKELKETGIKVNACCPGWVKT 182
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 8-242 2.47e-29

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: 110.66  E-value: 2.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ-ELEECPGIQIRTLDVTkkkqidqfASEIERLDVLFNVAGfVH 86
Cdd:cd05328    1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVIaDLSTPEGRAAAIADVL--------ARCSGVLDGLVNCAG-VG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  87 HGTILDceekdwdFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASS-------------IKGVVNRCV------- 146
Cdd:cd05328   72 GTTVAG-------LVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalAAGTEARAValaehag 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 ------YSTSKAAVIGLTKSLAAD-FIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDflkRQKTGRFATAEEIAL 219
Cdd:cd05328  145 qpgylaYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGGESVDAF---VTPMGRRAEPDEIAP 221

                        250       260
                 ....*....|....*....|...
gi 511847639 220 LCVYLASDESAYVTGNPVIIDGG 242
Cdd:cd05328  222 VIAFLASDAASWINGANLFVDGG 244
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-242 6.86e-29

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 109.41  E-value: 6.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIatdIN----ESKLQELEECPG---IQIRTlDVTKKKQIDQ-FASEIER 74
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVV---VNyhqsEDAAEALADELGdraIALQA-DVTDREQVQAmFATATEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 ----LDVLFN--VAGFVHHGTILD-CEEKDW-DFSMNLN--VRSMYLMIKAFLPKMLAQKSGNIINMSSvassiKGVVNR 144
Cdd:PRK08642  78 fgkpITTVVNnaLADFSFDGDARKkADDITWeDFQQQLEgsVKGALNTIQAALPGMREQGFGRIINIGT-----NLFQNP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 145 CV----YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqerIQARPNPKEARNDFLkRQKT--GRFATAEEIA 218
Cdd:PRK08642 153 VVpyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT------TDASAATPDEVFDLI-AATTplRKVTTPQEFA 225

                        250       260
                 ....*....|....*....|....
gi 511847639 219 LLCVYLASDESAYVTGNPVIIDGG 242
Cdd:PRK08642 226 DAVLFFASPWARAVTGQNLVVDGG 249
PRK06949 PRK06949
SDR family oxidoreductase;
1-244 7.12e-29

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 109.47  E-value: 7.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGR---LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE---ECPG--IQIRTLDVTK----KKQIDQF 68
Cdd:PRK06949   1 MGRsinLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRaeiEAEGgaAHVVSLDVTDyqsiKAAVAHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  69 ASEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ--------KSGNIINMSSVASsIKG 140
Cdd:PRK06949  81 ETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARakgagntkPGGRIINIASVAG-LRV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 141 VVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEArnDFLKRQKTGRfatAEEIALL 220
Cdd:PRK06949 160 LPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQGQKLV--SMLPRKRVGK---PEDLDGL 234

                        250       260
                 ....*....|....*....|....
gi 511847639 221 CVYLASDESAYVTGNPVIIDGGWS 244
Cdd:PRK06949 235 LLLLAADESQFINGAIISADDGFG 258
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 4-242 8.27e-29

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 108.96  E-value: 8.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAA--QGIGRAAALAFAREGAKVIATDINE---SKLQEL-EECPGIQIRTLDVTKKKQIDQFASEIE---- 73
Cdd:COG0623    3 LKGKRGLITGVAndRSIAWGIAKALHEEGAELAFTYQGEalkKRVEPLaEELGSALVLPCDVTDDEQIDALFDEIKekwg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDvlfnvaGFVH----------HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSiKGVVN 143
Cdd:COG0623   83 KLD------FLVHsiafapkeelGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLM--NEGGSIVTLTYLGAE-RVVPN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 144 RCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlqeriqarpnpkeAR-----NDFLKRQKT----GRFATA 214
Cdd:COG0623  154 YNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLA-------------ASgipgfDKLLDYAEEraplGRNVTI 220

                        250       260
                 ....*....|....*....|....*...
gi 511847639 215 EEIALLCVYLASDESAYVTGNPVIIDGG 242
Cdd:COG0623  221 EEVGNAAAFLLSDLASGITGEIIYVDGG 248
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-245 8.63e-29

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 109.04  E-value: 8.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVI------ATDINESkLQELEECPGIQIRTL-DVTKKKQ----IDQFA 69
Cdd:PRK06077   1 MYSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnakkrAEEMNET-LKMVKENGGEGIGVLaDVSTREGcetlAKATI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVAsSIKGVVNRCVYST 149
Cdd:PRK06077  80 DRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVA-GIRPAYGLSIYGA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQgIRCNCVCPGTVDTpSLQERIQARPNPKEarNDFLKRQK-TGRFATAEEIALLCVYLASDE 228
Cdd:PRK06077 157 MKAAVINLTKYLALELAPK-IRVNAIAPGFVKT-KLGESLFKVLGMSE--KEFAEKFTlMGKILDPEEVAEFVAAILKIE 232

                        250
                 ....*....|....*..
gi 511847639 229 SayVTGNPVIIDGGWSL 245
Cdd:PRK06077 233 S--ITGQVFVLDSGESL 247
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 9-182 1.01e-28

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 108.54  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREG-AKVIATDINESKLQELEECPGIQIRT----LDVTKKKQ--IDQFASE--IERLDVLF 79
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLhileLDVTDEIAesAEAVAERlgDAGLDVLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVH-HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYS--TSKAAVIG 156
Cdd:cd05325   81 NNAGILHsYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDNTSGGWYSyrASKAALNM 160

                        170       180
                 ....*....|....*....|....*.
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:cd05325  161 LTKSLAVELKRDGITVVSLHPGWVRT 186
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 3-242 1.02e-28

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 109.17  E-value: 1.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINesklQELEECPGIQIRTL---------DVTKKKQID---QFA- 69
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDIN----ADAANHVVDEIQQLggqafacrcDITSEQELSalaDFAl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  70 SEIERLDVLFNVAGfvhhG---TILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGvVNRCV 146
Cdd:PRK06113  84 SKLGKVDILVNNAG----GggpKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKN-INMTS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQArpnpkEARNDFLKRQKTGRFATAEEIALLCVYLAS 226
Cdd:PRK06113 159 YASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITP-----EIEQKMLQHTPIRRLGQPQDIANAALFLCS 233

                        250
                 ....*....|....*.
gi 511847639 227 DESAYVTGNPVIIDGG 242
Cdd:PRK06113 234 PAASWVSGQILTVSGG 249
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-183 1.49e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 108.84  E-value: 1.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELeecPGIQIRTLDVTKKKQIDQFASEI----ERLDVLFNVA 82
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPI---PGVELLELDVTDDASVQAAVDEViaraGRIDVLVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  83 GFvhhGTILDCEEkdwdFSM-------NLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAssikGVVNR---CVYSTSKA 152
Cdd:PRK06179  82 GV---GLAGAAEE----SSIaqaqalfDTNVFGILRMTRAVLPHMRAQGSGRIINISSVL----GFLPApymALYAASKH 150

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK06179 151 AVEGYSESLDHEVRQFGIRVSLVEPAYTKTN 181
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 4-242 1.52e-28

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 108.30  E-value: 1.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE---CPGIQIRT--LDVTKKKQIDQFASEIER---- 74
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAklrQEGIKAHAapFNVTHKQEVEAAIEHIEKdigp 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAV 154
Cdd:PRK08085  87 IDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSEL-GRDTITPYAASKGAV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTpslqERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:PRK08085 166 KMLTRGMCVELARHNIQVNGIAPGYFKT----EMTKALVEDEAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNG 241


                 ....*...
gi 511847639 235 NPVIIDGG 242
Cdd:PRK08085 242 HLLFVDGG 249
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 4-242 1.80e-28

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 107.91  E-value: 1.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT-----DINESKLQELEECPG----IQIRTLDVTK-KKQIDQFASEIE 73
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyagsaAAADELVAEIEAAGGraiaVQADVADAAAvTRLFDAAETAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSIKgVVNRCVYSTSKAA 153
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALP-LPGYGPYAASKAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqeriQARPNPK--EARNDFLKRQKTGRFATAEEIALLCVYLASDESAY 231
Cdd:PRK12937 160 VEGLVHVLANELRGRGITVNAVAPGPVAT-------ELFFNGKsaEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAW 232

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:PRK12937 233 VNGQVLRVNGG 243
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 3-245 2.26e-27

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 105.51  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL--DVTK----KKQIDQFASEIERLD 76
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVegDVRSladnERAVARCVERFGKLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILD--CEEK---DWDFSMNLNVRSMYLMIKAFLPKMLAQKsGNIINMSSVASSIKGVVNRCvYSTSK 151
Cdd:cd05348   81 CFIGNAGIWDYSTSLVdiPEEKldeAFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGGGPL-YTASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQgIRCNCVCPGTVDT-----PSL---QERIQARPNPkearnDFLKR-QKTGRFATAEEIALLCV 222
Cdd:cd05348  159 HAVVGLVKQLAYELAPH-IRVNGVAPGGMVTdlrgpASLgqgETSISTPPLD-----DMLKSiLPLGFAPEPEDYTGAYV 232

                        250       260
                 ....*....|....*....|....
gi 511847639 223 YLAS-DESAYVTGNPVIIDGGWSL 245
Cdd:cd05348  233 FLASrGDNRPATGTVINYDGGMGV 256
PRK06181 PRK06181
SDR family oxidoreductase;
6-218 6.26e-27

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 104.29  E-value: 6.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTL----DVTKKKQ----IDQFASEIERLD 76
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLaQELADHGGEALvvptDVSDAEAcerlIEAAVARFGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWdFS--MNLN-VRSMYLmIKAFLPKMLAQKsGNIINMSSVASSIkGVVNRCVYSTSKAA 153
Cdd:PRK06181  81 ILVNNAGITMWSRFDELTDLSV-FErvMRVNyLGAVYC-THAALPHLKASR-GQIVVVSSLAGLT-GVPTRSGYAASKHA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPkeARNDFLKRQKTgrfATAEEIA 218
Cdd:PRK06181 157 LHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGDGKP--LGKSPMQESKI---MSAEECA 216
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 4-188 5.65e-26

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: 101.23  E-value: 5.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTLDVTKKKQIDQFASEIER----LDVL 78
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAkKELPNIHTIVLDVGDAESVEALAEALLSeypnLDIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEE--KDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRcVYSTSKAAVIG 156
Cdd:cd05370   83 INNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANP-VYCATKAALHS 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTVDTPSLQER 188
Cdd:cd05370  162 YTLALRHQLKDTGVEVVEIVPPAVDTELHEER 193
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 4-242 8.82e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 101.19  E-value: 8.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE-ECPGIQIRTL----DVTKKKQIDQFASE-IE---R 74
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAaEIDDLGRRALavptDITDEDQCANLVALaLErfgR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAgFVH--HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKmLAQKSGNIINMSSvASSIKGVVNRCVYSTSKA 152
Cdd:PRK07890  83 VDALVNNA-FRVpsMKPLADADFAHWRAVIELNVLGTLRLTQAFTPA-LAESGGSIVMINS-MVLRHSQPKYGAYKMAKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQAR-----PNPKEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK07890 160 ALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGYFRHQagkygVTVEQIYAETAANSDLKRLPTDDEVASAVLFLASD 239

                        250
                 ....*....|....*
gi 511847639 228 ESAYVTGNPVIIDGG 242
Cdd:PRK07890 240 LARAITGQTLDVNCG 254
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 6-242 1.28e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 100.52  E-value: 1.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEECPGiQIRT--LDVTKKKQIDQFASEIE----RL 75
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLeeakLEIEQFPG-QVLTvqMDVRNPEDVQKMVEQIDekfgRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAG--FVHHGtiLDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK-SGNIINMssVASSIKGVVNRCVYSTS-K 151
Cdd:PRK07677  80 DALINNAAgnFICPA--EDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGiKGNIINM--VATYAWDAGPGVIHSAAaK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 152 AAVIGLTKSLAADFIQQ-GIRCNCVCPGTVDTPSLQERIQARPnpkEARNDFLKRQKTGRFATAEEIALLCVYLASDESA 230
Cdd:PRK07677 156 AGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERTGGADKLWESE---EAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAA 232

                        250
                 ....*....|..
gi 511847639 231 YVTGNPVIIDGG 242
Cdd:PRK07677 233 YINGTCITMDGG 244
PRK07985 PRK07985
SDR family oxidoreductase;
2-242 3.13e-25

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 100.84  E-value: 3.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT-------DINESKlQELEEC-------PGiqirtlDVTK----KK 63
Cdd:PRK07985  45 GRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISylpveeeDAQDVK-KIIEECgrkavllPG------DLSDekfaRS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  64 QIDQFASEIERLDVLFNVAGF-VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPkmLAQKSGNIINMSSVaSSIKGVV 142
Cdd:PRK07985 118 LVHEAHKALGGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIP--LLPKGASIITTSSI-QAYQPSP 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 143 NRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPsLQeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCV 222
Cdd:PRK07985 195 HLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTA-LQ---ISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYV 270

                        250       260
                 ....*....|....*....|
gi 511847639 223 YLASDESAYVTGNPVIIDGG 242
Cdd:PRK07985 271 YLASQESSYVTAEVHGVCGG 290
PRK07326 PRK07326
SDR family oxidoreductase;
1-183 3.19e-25

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 99.31  E-value: 3.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEECPGIQIRTLDVTK----KKQIDQFASEI 72
Cdd:PRK07326   1 MMSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELeeaaAELNNKGNVLGLAADVRDeadvQRAVDAIVAAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKmLAQKSGNIINMSSVASSiKGVVNRCVYSTSKA 152
Cdd:PRK07326  81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPA-LKRGGGYIINISSLAGT-NFFAGGAAYNASKF 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK07326 159 GLVGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-243 3.32e-25

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 99.86  E-value: 3.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAA--AQGIGRAAALAFAREGAKVIAT-------------DINES-KLQELEECPGIQIRT--LDVTK- 61
Cdd:PRK12859   1 MNQLKNKVAVVTGVsrLDGIGAAICKELAEAGADIFFTywtaydkempwgvDQDEQiQLQEELLKNGVKVSSmeLDLTQn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  62 ---KKQIDQFASEIERLDVLFNVAGFV--HHGTILDCEEKDWDFsmNLNVRSMYLMIKAFlPKMLAQKSGN-IINMSSVA 135
Cdd:PRK12859  81 dapKELLNKVTEQLGYPHILVNNAAYStnNDFSNLTAEELDKHY--MVNVRATTLLSSQF-ARGFDKKSGGrIINMTSGQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 136 SsiKG-VVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIqarpnpkeaRNDFLKRQKTGRFATA 214
Cdd:PRK12859 158 F--QGpMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEI---------KQGLLPMFPFGRIGEP 226

                        250       260
                 ....*....|....*....|....*....
gi 511847639 215 EEIALLCVYLASDESAYVTGNPVIIDGGW 243
Cdd:PRK12859 227 KDAARLIKFLASEEAEWITGQIIHSEGGF 255
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-242 4.05e-25

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 98.89  E-value: 4.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVI------ATDINESKlQELEECPG----IQIRTLDVTK-KKQIDQFASEIERL 75
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVvhynrsEAEAQRLK-DELNALRNsavlVQADLSDFAAcADLVAAAFRAFGRC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMS-SVASsiKGVVNRCVYSTSKAAV 154
Cdd:cd05357   80 DVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIdAMTD--RPLTGYFAYCMSKAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQgIRCNCVCPGTVdtpSLQERiqarpNPKEARNDFLKRQKTGRFATAEEIALLCVYLASdeSAYVTG 234
Cdd:cd05357  158 EGLTRSAALELAPN-IRVNGIAPGLI---LLPED-----MDAEYRENALRKVPLKRRPSAEEIADAVIFLLD--SNYITG 226


                 ....*...
gi 511847639 235 NPVIIDGG 242
Cdd:cd05357  227 QIIKVDGG 234
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
7-242 4.21e-25

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 99.32  E-value: 4.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIA----TDINESKLQELEECPGI-------QIRTLDVTKKKqIDQFASEIERL 75
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpNSPRRVKWLEDQKALGFdfiasegNVGDWDSTKAA-FDKVKAEVGEI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSKAAVI 155
Cdd:PRK12938  83 DVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQ-KGQFGQTNYSTAKAGIH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDTPSLqeriqarpnpKEARNDFLKR----QKTGRFATAEEIALLCVYLASDESAY 231
Cdd:PRK12938 162 GFTMSLAQEVATKGVTVNTVSPGYIGTDMV----------KAIRPDVLEKivatIPVRRLGSPDEIGSIVAWLASEESGF 231

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:PRK12938 232 STGADFSLNGG 242
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-244 5.69e-25

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 98.99  E-value: 5.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQ--GIGRAAALAFAREGAKVIAT--------------DINESKLQELEECPGIQIRTLDV------TK 61
Cdd:PRK12748   3 LMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTywspydktmpwgmhDKEPVLLKEEIESYGVRCEHMEIdlsqpyAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  62 KKQIDQFASEIERLDVLFNVAGFVHHGTI--LDCEEKDWDFSmnLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvASSIK 139
Cdd:PRK12748  83 NRVFYAVSERLGDPSILINNAAYSTHTRLeeLTAEQLDKHYA--VNVRATMLLSSAFAKQYDGKAGGRIINLTS-GQSLG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 140 GVVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARndflkrqktGRFATAEEIAL 219
Cdd:PRK12748 160 PMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWITEELKHHLVPKFPQ---------GRVGEPVDAAR 230

                        250       260
                 ....*....|....*....|....*
gi 511847639 220 LCVYLASDESAYVTGNPVIIDGGWS 244
Cdd:PRK12748 231 LIAFLVSEEAKWITGQVIHSEGGFS 255
PRK12746 PRK12746
SDR family oxidoreductase;
1-245 6.14e-25

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 98.95  E-value: 6.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAkVIATDINESK------LQELEECPG------IQIRTLDVTkKKQIDQF 68
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGA-LVAIHYGRNKqaadetIREIESNGGkaflieADLNSIDGV-KKLVEQL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  69 ASEIE------RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQksGNIINMSSVASSIkGVV 142
Cdd:PRK12746  79 KNELQirvgtsEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRL-GFT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 143 NRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpSLQERIQARPnpkEARNDFLKRQKTGRFATAEEIALLCV 222
Cdd:PRK12746 156 GSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKT-DINAKLLDDP---EIRNFATNSSVFGRIGQVEDIADAVA 231

                        250       260
                 ....*....|....*....|...
gi 511847639 223 YLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK12746 232 FLASSDSRWVTGQIIDVSGGFCL 254
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 5-178 9.18e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 98.83  E-value: 9.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQI--RTLDVTKKKQIDQFASEIE----RLDVL 78
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRAlaRLLDVTDFDAIDAVVADAEatfgPIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAS--SIKGVvnrCVYSTSKAAVIG 156
Cdd:PRK06180  83 VNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGliTMPGI---GYYCGSKFALEG 159

                        170       180
                 ....*....|....*....|..
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPG 178
Cdd:PRK06180 160 ISESLAKEVAPFGIHVTAVEPG 181
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 3-161 9.64e-25

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: 98.31  E-value: 9.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTLDVTKKKQIDQFASEIER----LDV 77
Cdd:COG3967    2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAaAANPGLHTIVLDVADPASIAALAEQVTAefpdLNV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDcEEKDWDFS---MNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSV------ASSikgvvnrCVYS 148
Cdd:COG3967   82 LINNAGIMRAEDLLD-EAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGlafvplAVT-------PTYS 153

                        170
                 ....*....|...
gi 511847639 149 TSKAAVIGLTKSL 161
Cdd:COG3967  154 ATKAALHSYTQSL 166
PRK08264 PRK08264
SDR family oxidoreductase;
4-183 1.21e-24

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 97.65  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAF-AREGAKVIATDINESKLQELEecPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVA 82
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLlARGAAKVYAAARDPESVTDLG--PRVVPLQLDVTDPASVAAAAEAASDVTILVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  83 G-FVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAVIGLTKSL 161
Cdd:PRK08264  82 GiFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVL-SWVNFPNLGTYSASKAAAWSLTQAL 160

                        170       180
                 ....*....|....*....|..
gi 511847639 162 AADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK08264 161 RAELAPQGTRVLGVHPGPIDTD 182
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-237 1.77e-24

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 100.68  E-value: 1.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESK--LQELEECPGIQIRTLDVTK----KKQIDQFASEIERLDV 77
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGeaLAAVANRVGGTALALDITApdapARIAEHLAERHGGLDI 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVVNRCVYSTSKAAVIGL 157
Cdd:PRK08261 288 VVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSI-SGIAGNRGQTNYAASKAGVIGL 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDTpslqeriqarpnPKEARNDFLKRQKTGRFAT----------AEEIAllcvYLASD 227
Cdd:PRK08261 367 VQALAPLLAERGITINAVAPGFIET------------QMTAAIPFATREAGRRMNSlqqgglpvdvAETIA----WLASP 430

                        250
                 ....*....|
gi 511847639 228 ESAYVTGNPV 237
Cdd:PRK08261 431 ASGGVTGNVV 440
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 6-211 2.02e-24

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: 97.09  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGA-KVIATDINESKLQELEECPGIQIRT--LDVTKKKQIDQFASEIERLDVLFNVA 82
Cdd:cd05354    3 DKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPlrLDVTDPESIKAAAAQAKDVDVVINNA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  83 G-FVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYSTSKAAVIGLTKSL 161
Cdd:cd05354   83 GvLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVAS-LKNFPAMGTYSASKSAAYSLTQGL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 511847639 162 AADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKTGRF 211
Cdd:cd05354  162 RAELAAQGTLVLSVHPGPIDTRMAAGAGGPKESPETVAEAVLKALKAGEF 211
PRK07856 PRK07856
SDR family oxidoreductase;
4-242 2.77e-24

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 97.31  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEecpGIQIRTLDVTKKKQIDQFASEIE----RLDVLF 79
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGR---PAEFHAADVRDPDQVAALVDAIVerhgRLDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKS-GNIINMSSVaSSIKGVVNRCVYSTSKAAVIGLT 158
Cdd:PRK07856  81 NNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSV-SGRRPSPGTAAYGAAKAGLLNLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 159 KSLAADFIQQgIRCNCVCPGTVDTpslqERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVI 238
Cdd:PRK07856 160 RSLAVEWAPK-VRVNAVVVGLVRT----EQSELHYGDAEGIAAVAATVPLGRLATPADIAWACLFLASDLASYVSGANLE 234


                 ....
gi 511847639 239 IDGG 242
Cdd:PRK07856 235 VHGG 238
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 8-195 8.35e-24

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: 95.53  E-value: 8.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL----EECPGIQIR-TLDVTKKKQIDQFASEIE----RLDVL 78
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELarevRELGGEAIAvVADVADAAQVERAADTAVerfgRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSKAAVIGLT 158
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGY-RSAPLQAAYSASKHAVRGFT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 511847639 159 KSLAADFIQQG--IRCNCVCPGTVDTPSLQ---ERIQARPNP 195
Cdd:cd05360  161 ESLRAELAHDGapISVTLVQPTAMNTPFFGharSYMGKKPKP 202
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-245 8.54e-24

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 95.60  E-value: 8.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG----IQIRTLDVTKKKQIDQFASEIER--- 74
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSkygnIHYVVGDVSSTESARNVIEKAAKvln 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 -LDVLFNVAGFVHHGTILDCEEkdWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSIKGVVNRCVYSTSKAA 153
Cdd:PRK05786  81 aIDGLVVTVGGYVEDTVEEFSG--LEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIYKASPDQLSYAVAKAG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 154 VIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERiqarpnpkearnDFLKRQKTGRF-ATAEEIALLCVYLASDESAYV 232
Cdd:PRK05786 157 LAKAVEILASELLGRGIRVNGIAPTTISGDFEPER------------NWKKLRKLGDDmAPPEDFAKVIIWLLTDEADWV 224

                        250
                 ....*....|...
gi 511847639 233 TGNPVIIDGGWSL 245
Cdd:PRK05786 225 DGVVIPVDGGARL 237
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
30-242 9.14e-24

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 95.45  E-value: 9.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  30 GAKVIATDINESKLqELEECpgIQIrtlDVTKKKQIDQFASEI-ERLDVLFNVAGFvhHGTildceekdwdFSMNLNVRS 108
Cdd:PRK12428   9 GARVIGVDRREPGM-TLDGF--IQA---DLGDPASIDAAVAALpGRIDALFNIAGV--PGT----------APVELVARV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 109 MYLMIKAF----LPKMLAqkSGNIINMSSVASS--------IKGVVN-------------------RCvYSTSKAAVIGL 157
Cdd:PRK12428  71 NFLGLRHLtealLPRMAP--GGAIVNVASLAGAewpqrlelHKALAAtasfdegaawlaahpvalaTG-YQLSKEALILW 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLA-ADFIQQGIRCNCVCPGTVDTPSL--------QERIQARPNPKearndflkrqktGRFATAEEIALLCVYLASDE 228
Cdd:PRK12428 148 TMRQAqPWFGARGIRVNCVAPGPVFTPILgdfrsmlgQERVDSDAKRM------------GRPATADEQAAVLVFLCSDA 215

                        250
                 ....*....|....
gi 511847639 229 SAYVTGNPVIIDGG 242
Cdd:PRK12428 216 ARWINGVNLPVDGG 229
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 4-242 1.09e-23

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 95.69  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-----LEECPgIQIRTL--DVTKKKQIDQFASEIERL- 75
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKarekiKSESN-VDVSYIvaDLTKREDLERTVKELKNIg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 --DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAssIKGVV-NRCVYSTSKA 152
Cdd:PRK08339  85 epDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVA--IKEPIpNIALSNVVRI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPK-----EARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK08339 163 SMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKREgksveEALQEYAKPIPLGRLGEPEEIGYLVAFLASD 242

                        250
                 ....*....|....*
gi 511847639 228 ESAYVTGNPVIIDGG 242
Cdd:PRK08339 243 LGSYINGAMIPVDGG 257
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 1-190 1.09e-23

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 96.18  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE---CPGIQIRTL--DVTKKKQIDQFASEIERL 75
Cdd:PRK05876   1 MDGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNhlrAEGFDVHGVmcDVRHREEVTHLADEAFRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 ----DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIInmsSVASSIKGVVNRC---VYS 148
Cdd:PRK05876  81 lghvDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHV---VFTASFAGLVPNAglgAYG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTP--SLQERIQ 190
Cdd:PRK05876 158 VAKYGVVGLAETLAREVTADGIGVSVLCPMVVETNlvANSERIR 201
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 8-245 1.56e-23

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: 95.22  E-value: 1.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESK-----LQELE-ECPGIQIRTLDVTKKKQ----IDQFASEIERLDV 77
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDqatevVAEVLaAGRRAIYFQADIGELSDhealLDQAWEDFGRLDC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFV--HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK------SGNIINMSSvASSIKGVVNRCVYST 149
Cdd:cd05337   83 LVNNAGIAvrPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPdrfdgpHRSIIFVTS-INAYLVSPNRGEYCI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT-------PSLQERIQARPNPkearndflkrqkTGRFATAEEIALLCV 222
Cdd:cd05337  162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTdmtapvkEKYDELIAAGLVP------------IRRWGQPEDIAKAVR 229

                        250       260
                 ....*....|....*....|...
gi 511847639 223 YLASDESAYVTGNPVIIDGGWSL 245
Cdd:cd05337  230 TLASGLLPYSTGQPINIDGGLSM 252
PRK06914 PRK06914
SDR family oxidoreductase;
6-183 1.70e-23

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 95.48  E-value: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG-------IQIRTLDVTKKKQI---DQFASEIERL 75
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATqlnlqqnIKVQQLDVTDQNSIhnfQLVLKEIGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVI 155
Cdd:PRK06914  83 DLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRV-GFPGLSPYVSSKYALE 161

                        170       180
                 ....*....|....*....|....*...
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK06914 162 GFSESLRLELKPFGIDVALIEPGSYNTN 189
PRK12742 PRK12742
SDR family oxidoreductase;
1-244 1.80e-23

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 94.82  E-value: 1.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDI-NESKLQELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLF 79
Cdd:PRK12742   1 MGAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAgSKDAAERLAQETGATAVQTDSADRDAVIDVVRKSGALDILV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIGLTK 159
Cdd:PRK12742  81 VNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIIIGSVNGDRMPVAGMAAYAASKSALQGMAR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 160 SLAADFIQQGIRCNCVCPGTVDTPSlqeriqarpNP-----KEARNDFLKRQktgRFATAEEIALLCVYLASDESAYVTG 234
Cdd:PRK12742 159 GLARDFGPRGITINVVQPGPIDTDA---------NPangpmKDMMHSFMAIK---RHGRPEEVAGMVAWLAGPEASFVTG 226

                        250
                 ....*....|
gi 511847639 235 NPVIIDGGWS 244
Cdd:PRK12742 227 AMHTIDGAFG 236
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 6-182 2.15e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 95.10  E-value: 2.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIR--TLDVTKKKQ----IDQFASEIERLDVLF 79
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLplALDVTDRAAvfaaVETAVEHFGRLDIVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAVIGLTK 159
Cdd:PRK08263  83 NNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIG-GISAFPMSGIYHASKWALEGMSE 161

                        170       180
                 ....*....|....*....|...
gi 511847639 160 SLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK08263 162 ALAQEVAEFGIKVTLVEPGGYST 184
PRK07201 PRK07201
SDR family oxidoreductase;
2-170 2.36e-23

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 98.10  E-value: 2.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   2 GRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGI-QIRTLDVTKKKQIDQFASEI---- 72
Cdd:PRK07201 367 GPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDelvaEIRAKGGTaHAYTCDLTDSAAVDHTVKDIlaeh 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGFVHHGTILDCEEKDWDF--SMNLN----VRsmylMIKAFLPKMLAQKSGNIINMSSVassikGVVNR-- 144
Cdd:PRK07201 447 GHVDYLVNNAGRSIRRSVENSTDRFHDYerTMAVNyfgaVR----LILGLLPHMRERRFGHVVNVSSI-----GVQTNap 517

                        170       180
                 ....*....|....*....|....*...
gi 511847639 145 --CVYSTSKAAVIGLTKSLAADFIQQGI 170
Cdd:PRK07201 518 rfSAYVASKAALDAFSDVAASETLSDGI 545
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 6-242 2.63e-23

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 94.84  E-value: 2.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESK----LQELEECPGIQIRTL--DVTKKKQIDQFASEIE----RL 75
Cdd:cd05322    2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENaekvADEINAEYGEKAYGFgaDATNEQSVIALSKGVDeifkRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKS-GNIINMSSVASSIkGVVNRCVYSTSKAAV 154
Cdd:cd05322   82 DLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKV-GSKHNSGYSAAKFGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGT-VDTPSLQERIQARP-----NPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGNlLKSPMFQSLLPQYAkklgiKESEVEQYYIDKVPLKRGCDYQDVLNMLLFYASPK 240

                        250
                 ....*....|....
gi 511847639 229 SAYVTGNPVIIDGG 242
Cdd:cd05322  241 ASYCTGQSINITGG 254
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 7-182 3.41e-23

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: 93.73  E-value: 3.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL--EECPGIQIRTLDVTKKKQIDQFASEIER----LDVLFN 80
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAaaQELEGVLGLAGDVRDEADVRRAVDAMEEafggLDALVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  81 VAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAS--SIKGvvnRCVYSTSKAAVIGLT 158
Cdd:cd08929   81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGknAFKG---GAAYNASKFGLLGLS 157

                        170       180
                 ....*....|....*....|....
gi 511847639 159 KSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:cd08929  158 EAAMLDLREANIRVVNVMPGSVDT 181
PRK08416 PRK08416
enoyl-ACP reductase;
1-242 4.53e-23

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 94.07  E-value: 4.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT-----DINESKLQELEECPGIQIRT--LDVTKKkqiDQFASEIE 73
Cdd:PRK08416   3 SNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTynsnvEEANKIAEDLEQKYGIKAKAypLNILEP---ETYKELFK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFS--MNLNVRSM----YLMIKAFL-------PKMLAQKSGNIINMSSVASSIKg 140
Cdd:PRK08416  80 KIDEDFDRVDFFISNAIISGRAVVGGYTkfMRLKPKGLnniyTATVNAFVvgaqeaaKRMEKVGGGSIISLSSTGNLVY- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 141 VVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriqARPNPKEARNDFLKRQKTGRFATAEEIALL 220
Cdd:PRK08416 159 IENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALK----AFTNYEEVKAKTEELSPLNRMGQPEDLAGA 234

                        250       260
                 ....*....|....*....|..
gi 511847639 221 CVYLASDESAYVTGNPVIIDGG 242
Cdd:PRK08416 235 CLFLCSEKASWLTGQTIVVDGG 256
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-245 8.70e-23

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 93.10  E-value: 8.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINES-KLQE-LEECPGIQIRTL----DVTK----KKQIDQFASEIERLD 76
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDeELAAtQQELRALGVEVIffpaDVADlsahEAMLDAAQAAWGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGF--VHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGN------IINMSSVaSSIKGVVNRCVYS 148
Cdd:PRK12745  83 CLVNNAGVgvKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSV-NAIMVSPNRGEYC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriqarpnPKEARNDFLKRQKT---GRFATAEEIALLCVYLA 225
Cdd:PRK12745 162 ISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTA--------PVTAKYDALIAKGLvpmPRWGEPEDVARAVAALA 233

                        250       260
                 ....*....|....*....|
gi 511847639 226 SDESAYVTGNPVIIDGGWSL 245
Cdd:PRK12745 234 SGDLPYSTGQAIHVDGGLSI 253
PRK05717 PRK05717
SDR family oxidoreductase;
5-244 1.25e-22

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 93.03  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQ--IRTLDVTKKKQIDQFASEI----ERLDVL 78
Cdd:PRK05717   9 NGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENawFIAMDVADEAQVAAGVAEVlgqfGRLDAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFV--HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKsGNIINMSSVASSiKGVVNRCVYSTSKAAVIG 156
Cdd:PRK05717  89 VCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRAR-QSEPDTEAYAASKGGLLA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 157 LTKSLAADFIQQgIRCNCVCPGTVDTPSLQERiqaRPNPKEARNDflKRQKTGRFATAEEIALLCVYLASDESAYVTGNP 236
Cdd:PRK05717 167 LTHALAISLGPE-IRVNAVSPGWIDARDPSQR---RAEPLSEADH--AQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQE 240


                 ....*...
gi 511847639 237 VIIDGGWS 244
Cdd:PRK05717 241 FVVDGGMT 248
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 6-187 2.34e-22

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: 92.29  E-value: 2.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-----LEECPG--IQIRTLDVTKKKQIDQFASEI----ER 74
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEaaaeiKKETGNakVEVIQLDLSSLASVRQFAEEFlarfPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDceeKD-WDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSI-------------KG 140
Cdd:cd05327   81 LDILINNAGIMAPPRRLT---KDgFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAgpidfndldlennKE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 511847639 141 VVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQE 187
Cdd:cd05327  158 YSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRR 204
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 8-234 3.78e-22

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: 91.19  E-value: 3.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREG--AKVIATDINESKLQELEE--CPGIQIRT--LDVTKkkqIDQFASEIE-------R 74
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEelRPGLRVTTvkADLSD---AAGVEQLLEairkldgE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFV-HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKM-LAQKSGNIINMSSVAsSIKGVVNRCVYSTSKA 152
Cdd:cd05367   78 RDLLINNAGSLgPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkKRGLKKTVVNVSSGA-AVNPFKGWGLYCSSKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADfiQQGIRCNCVCPGTVDTPsLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDESaYV 232
Cdd:cd05367  157 ARDMFFRVLAAE--EPDVRVLSYAPGVVDTD-MQREIRETSADPETRSRFRSLKEKGELLDPEQSAEKLANLLEKDK-FE 232


                 ..
gi 511847639 233 TG 234
Cdd:cd05367  233 SG 234
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 6-234 5.21e-22

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: 90.46  E-value: 5.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESklQELEECPGIQIRTLDVTKKKQ-IDQFASEIERLDVLFNVAGF 84
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAEN--EEADASIIVLDSDSFTEQAKQvVASVARLSGKVDALICVAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  85 VHHGTILDCEE-KDWDFSMNLNVRSMYLMIKAFLPKMLaqKSGNIINMSSvassiKGVVNRC----VYSTSKAAVIGLTK 159
Cdd:cd05334   79 WAGGSAKSKSFvKNWDLMWKQNLWTSFIASHLATKHLL--SGGLLVLTGA-----KAALEPTpgmiGYGAAKAAVHQLTQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511847639 160 SLAADF--IQQGIRCNCVCPGTVDTPslQERiQARPNPkearnDFlkrqktGRFATAEEIALLCVYLASDESAYVTG 234
Cdd:cd05334  152 SLAAENsgLPAGSTANAILPVTLDTP--ANR-KAMPDA-----DF------SSWTPLEFIAELILFWASGAARPKSG 214
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 1-226 6.23e-22

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: 91.03  E-value: 6.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTL-----DVTKKKQIDQFASEIER 74
Cdd:cd05343    1 MERWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALaAECQSAGYPTLfpyqcDLSNEEQILSMFSAIRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 L----DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQK--SGNIINMSSVASSIKGVVNRC-VY 147
Cdd:cd05343   81 QhqgvDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGHRVPPVSVFhFY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAAD--FIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARNDFLKRQKtgrfatAEEIALLCVYLA 225
Cdd:cd05343  161 AATKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLK------PEDVANAVLYVL 234


                 .
gi 511847639 226 S 226
Cdd:cd05343  235 S 235
PRK09072 PRK09072
SDR family oxidoreductase;
3-171 1.14e-21

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 90.39  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE---CPG-IQIRTLDVTK---KKQIDQFASEIERL 75
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAArlpYPGrHRWVVADLTSeagREAVLARAREMGGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVI 155
Cdd:PRK09072  82 NVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSI-GYPGYASYCASKFALR 160

                        170
                 ....*....|....*.
gi 511847639 156 GLTKSLAADFIQQGIR 171
Cdd:PRK09072 161 GFSEALRRELADTGVR 176
PRK09135 PRK09135
pteridine reductase; Provisional
 1-245 1.56e-21

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 89.60  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVI------ATDINESKlQELE-ECPG----IQIRTLDVTKKKQ-IDQF 68
Cdd:PRK09135   1 MMTDSAKVALITGGARRIGAAIARTLHAAGYRVAihyhrsAAEADALA-AELNaLRPGsaaaLQADLLDPDALPElVAAC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  69 ASEIERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKmLAQKSGNIINMSSVASSiKGVVNRCVYS 148
Cdd:PRK09135  80 VAAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQ-LRKQRGAIVNITDIHAE-RPLKGYPVYC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQgIRCNCVCPGTVDTPSlqeriQARPNPKEARNDFLKRQKTGRFATAEEIAlLCVYLASDE 228
Cdd:PRK09135 158 AAKAALEMLTRSLALELAPE-VRVNAVAPGAILWPE-----DGNSFDEEARQAILARTPLKRIGTPEDIA-EAVRFLLAD 230

                        250
                 ....*....|....*..
gi 511847639 229 SAYVTGNPVIIDGGWSL 245
Cdd:PRK09135 231 ASFITGQILAVDGGRSL 247
PRK09730 PRK09730
SDR family oxidoreductase;
7-242 1.98e-21

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 89.52  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKV---------IATDIneskLQELEECPG--IQIRTlDVTKKKQI----DQFASE 71
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVavnyqqnlhAAQEV----VNLITQAGGkaFVLQA-DISDENQVvamfTAIDQH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLFNVAGFV-HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ---KSGNIINMSSVASSIKGVVNRCVY 147
Cdd:PRK09730  77 DEPLAALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEYVDY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT--------PSLQERIQARpnpkearndfLKRQKTGrfaTAEEIAL 219
Cdd:PRK09730 157 AASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTemhasggePGRVDRVKSN----------IPMQRGG---QPEEVAQ 223

                        250       260
                 ....*....|....*....|...
gi 511847639 220 LCVYLASDESAYVTGNPVIIDGG 242
Cdd:PRK09730 224 AIVWLLSDKASYVTGSFIDLAGG 246
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-242 4.13e-21

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 89.84  E-value: 4.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDI--NESKLQELEECPGIQIRTL----DVTKKKQIDQF---ASEIER 74
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVasALDASDVLDEIRAAGAKAVavagDISQRATADELvatAVGLGG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKaFLPKMLAQKS--------GNIINMSSVAsSIKGVVNRCV 146
Cdd:PRK07792  90 LDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTR-NAAAYWRAKAkaaggpvyGRIVNTSSEA-GLVGPVGQAN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPgTVDTPSLQERIQARPNPKEARNDFLkrqktgrfaTAEEIALLCVYLAS 226
Cdd:PRK07792 168 YGAAKAGITALTLSAARALGRYGVRANAICP-RARTAMTADVFGDAPDVEAGGIDPL---------SPEHVVPLVQFLAS 237

                        250
                 ....*....|....*.
gi 511847639 227 DESAYVTGNPVIIDGG 242
Cdd:PRK07792 238 PAAAEVNGQVFIVYGP 253
PRK06123 PRK06123
SDR family oxidoreductase;
7-242 8.44e-21

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 87.91  E-value: 8.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIAT-----DINESKLQELEECPGIQIRT-LDVTKKKQIDQ-FAS---EIERLD 76
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNylrnrDAAEAVVQAIRRQGGEALAVaADVADEADVLRlFEAvdrELGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILD-CEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQ---KSGNIINMSSVASSIKGVVNRCVYSTSKA 152
Cdd:PRK06123  83 ALVNNAGILEAQMRLEqMDAARLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGEYIDYAASKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqeRIQArPNPKEARNDFLKRQ-KTGRFATAEEIALLCVYLASDESAY 231
Cdd:PRK06123 163 AIDTMTIGLAKEVAAEGIRVNAVRPGVIYT-----EIHA-SGGEPGRVDRVKAGiPMGRGGTAEEVARAILWLLSDEASY 236

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:PRK06123 237 TTGTFIDVSGG 247
PRK06182 PRK06182
short chain dehydrogenase; Validated
 7-183 6.40e-20

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 85.78  E-value: 6.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECpGIQIRTLDVTK----KKQIDQFASEIERLDVLFNVA 82
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASL-GVHPLSLDVTDeasiKAAVDTIIAEEGRIDVLVNNA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  83 GFVHHGTILDC--EEKDWDFSMNL--NVRsmylMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNrCVYSTSKAAVIGLT 158
Cdd:PRK06182  83 GYGSYGAIEDVpiDEARRQFEVNLfgAAR----LTQLVLPHMRAQRSGRIINISSMGGKIYTPLG-AWYHATKFALEGFS 157

                        170       180
                 ....*....|....*....|....*...
gi 511847639 159 KSL---AADFiqqGIRCNCVCPGTVDTP 183
Cdd:PRK06182 158 DALrleVAPF---GIDVVVIEPGGIKTE 182
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 6-244 9.47e-20

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 84.94  E-value: 9.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAA--QGIGRAAALAFAREGAKVIAT---DINESKLQEL-EECPGI-QIRTLDVTKKKQIDQFASEIErlDVL 78
Cdd:cd05372    1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTyqpEALRKRVEKLaERLGESaLVLPCDVSNDEEIKELFAEVK--KDW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  79 FNVAGFVH----------HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSiKGVVNRCVYS 148
Cdd:cd05372   79 GKLDGLVHsiafapkvqlKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYLGSE-RVVPGYNVMG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLqeriQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:cd05372  156 VAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAA----SGITGFDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDL 231

                        250
                 ....*....|....*.
gi 511847639 229 SAYVTGNPVIIDGGWS 244
Cdd:cd05372  232 SSGITGEIIYVDGGYH 247
PRK05866 PRK05866
SDR family oxidoreductase;
3-183 1.49e-19

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 85.18  E-value: 1.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpGI-------QIRTLDVTKKKQIDQFASEIER- 74
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVAD--RItraggdaMAVPCDLSDLDAVDALVADVEKr 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 ---LDVLFNVAGFVHHGTILDCEEK--DWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSS--VASsikGVVNR-CV 146
Cdd:PRK05866 115 iggVDILINNAGRSIRRPLAESLDRwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwgVLS---EASPLfSV 191

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK05866 192 YNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATP 228
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 7-182 1.51e-19

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: 84.43  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGA---KVIATDINESKLQELEECPG------IQIRTLDVTKKKQIDQFASEIE--RL 75
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASDPSkrfKVYATMRDLKKKGRLWEAAGalaggtLETLQLDVCDSKSVAAAVERVTerHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNRCVYSTSKAAVI 155
Cdd:cd09806   81 DVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVG-GLQGLPFNDVYCASKFALE 159

                        170       180
                 ....*....|....*....|....*..
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:cd09806  160 GLCESLAVQLLPFNVHLSLIECGPVHT 186
PRK06947 PRK06947
SDR family oxidoreductase;
5-242 1.80e-19

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 84.09  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKViatDIN--------ESKLQELEECPGiqiRTL----DVTKKKQI----DQF 68
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSV---GINyardaaaaEETADAVRAAGG---RACvvagDVANEADViamfDAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  69 ASEIERLDVLFNVAGFVHHGTIL-DCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGN---IINMSSVASSIkGVVNR 144
Cdd:PRK06947  75 QSAFGRLDALVNNAGIVAPSMPLaDMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRL-GSPNE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 145 CV-YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqeRIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVY 223
Cdd:PRK06947 154 YVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIET-----EIHASGGQPGRAARLGAQTPLGRAGEADEVAETIVW 228

                        250
                 ....*....|....*....
gi 511847639 224 LASDESAYVTGNPVIIDGG 242
Cdd:PRK06947 229 LLSDAASYVTGALLDVGGG 247
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 1-183 2.10e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 85.02  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTL----DVTKKKQIDQFASEIE--- 73
Cdd:PRK05872   4 MTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLtvvaDVTDLAAMQAAAEEAVerf 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 -RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKsGNIINMSSVAsSIKGVVNRCVYSTSKA 152
Cdd:PRK05872  84 gGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLA-AFAAAPGMAAYCASKA 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK05872 162 GVEAFANALRLEVAHHGVTVGSAYLSWIDTD 192
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 9-233 2.67e-19

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: 82.18  E-value: 2.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGA-KVIATDinesklqeleecpgiqirtldvtkkkqidqfaseieRLDVLFNVAGFVHH 87
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLVVS------------------------------------RRDVVVHNAAILDD 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  88 GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVIGLTKSLAADFIQ 167
Cdd:cd02266   45 GRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLF-GAPGLGGYAASKAALDGLAQQWASEGWG 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511847639 168 QGIRCNCVCPGTVDTPSLQeriqarPNPKEARNDFLKRQKTGRFATAEEIA--LLCVYL-ASDESAYVT 233
Cdd:cd02266  124 NGLPATAVACGTWAGSGMA------KGPVAPEEILGNRRHGVRTMPPEEVAraLLNALDrPKAGVCYII 186
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 8-243 4.70e-19

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 83.01  E-value: 4.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE----ECPGIqiRTLDVTKKKQ-IDQFASEIERLDVLFNVA 82
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQafesENPGT--KALSEQKPEElVDAVLQAGGAIDVLVSND 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  83 GFV-HHGTILDCEEKDWDFSMN-LNVRSmYLMIKAFLPKMLAQKSGNIINMSSvASSIKGVVNRCVYSTSKAAVIGLTKS 160
Cdd:cd05361   81 YIPrPMNPIDGTSEADIRQAFEaLSIFP-FALLQAAIAQMKKAGGGSIIFITS-AVPKKPLAYNSLYGPARAAAVALAES 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 161 LAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPkEARNDFLKRQKTGRFATAEEIALLCVYLASDESAYVTGNPVIID 240
Cdd:cd05361  159 LAKELSRDNILVYAIGPNFFNSPTYFPTSDWENNP-ELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFA 237


                 ...
gi 511847639 241 GGW 243
Cdd:cd05361  238 GGY 240
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 8-180 1.08e-18

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 82.11  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRT--LDVTKKKQIDQFASEI----ERLDVLFNV 81
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIaqLDVRNRAAIEEMLASLpaewRNIDVLVNN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  82 AGFV-----HHGTILDceekDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKgVVNRCVYSTSKAAVIG 156
Cdd:PRK10538  82 AGLAlglepAHKASVE----DWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWP-YAGGNVYGATKAFVRQ 156

                        170       180
                 ....*....|....*....|....
gi 511847639 157 LTKSLAADFIQQGIRCNCVCPGTV 180
Cdd:PRK10538 157 FSLNLRTDLHGTAVRVTDIEPGLV 180
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 1-245 1.68e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 81.93  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQI-RTLDVTK----KKQIDQFASE 71
Cdd:PRK07576   4 MFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDaavaQLQQAGPEGLgVSADVRDyaavEAAFAQIADE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLfnVAG----FVhhGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPkMLAQKSGNIINMSSVASSIKGVVNRCVy 147
Cdd:PRK07576  84 FGPIDVL--VSGaagnFP--APAAGMSANGFKTVVDIDLLGTFNVLKAAYP-LLRRPGASIIQISAPQAFVPMPMQAHV- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPnpkEARNDFLKRQKTGRFATAEEIALLCVYLASD 227
Cdd:PRK07576 158 CAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAGTEGMARLAPSP---ELQAAVAQSVPLKRNGTKQDIANAALFLASD 234

                        250
                 ....*....|....*...
gi 511847639 228 ESAYVTGNPVIIDGGWSL 245
Cdd:PRK07576 235 MASYITGVVLPVDGGWSL 252
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-183 2.20e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 82.66  E-value: 2.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpgiQIRTL---------DVTKKKQIDQFASE 71
Cdd:PRK07109   3 LKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAA----EIRAAggealavvaDVADAEAVQAAADR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IE----RLDVLFNVAG---FVHHGTIlDCEEKDWDFSMNlnvrsmYL------MikAFLPKMLAQKSGNIINMSSvASSI 138
Cdd:PRK07109  79 AEeelgPIDTWVNNAMvtvFGPFEDV-TPEEFRRVTEVT------YLgvvhgtL--AALRHMRPRDRGAIIQVGS-ALAY 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 511847639 139 KGVVNRCVYSTSKAAVIGLTKSLAADFIQQG--IRCNCVCPGTVDTP 183
Cdd:PRK07109 149 RSIPLQSAYCAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNTP 195
PRK06139 PRK06139
SDR family oxidoreductase;
1-185 6.15e-18

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 81.31  E-value: 6.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-LEECPGIQIRTL----DVTKKKQI----DQFASE 71
Cdd:PRK06139   2 MGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAvAEECRALGAEVLvvptDVTDADQVkalaTQAASF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IERLDVLFNVAG------FvhHGTILDCEEKdwDFSMNL--NVRSMYlmikAFLPKMLAQKSGNIINMSSVASSIkGVVN 143
Cdd:PRK06139  82 GGRIDVWVNNVGvgavgrF--EETPIEAHEQ--VIQTNLigYMRDAH----AALPIFKKQGHGIFINMISLGGFA-AQPY 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 511847639 144 RCVYSTSKAAVIGLTKSLAADFIQQgiRCNCVC---PGTVDTPSL 185
Cdd:PRK06139 153 AAAYSASKFGLRGFSEALRGELADH--PDIHVCdvyPAFMDTPGF 195
PRK05693 PRK05693
SDR family oxidoreductase;
7-182 6.56e-18

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 80.61  E-value: 6.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECpGIQIRTLDVTKKKQIDQFASEIE----RLDVLFNVA 82
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA-GFTAVQLDVNDGAALARLAEELEaehgGLDVLINNA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  83 GFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPkMLAQKSGNIINMSSVaSSIKGVVNRCVYSTSKAAVIGLTKSLA 162
Cdd:PRK05693  81 GYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGSV-SGVLVTPFAGAYCASKAAVHALSDALR 158

                        170       180
                 ....*....|....*....|
gi 511847639 163 ADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK05693 159 LELAPFGVQVMEVQPGAIAS 178
PRK08340 PRK08340
SDR family oxidoreductase;
9-241 9.72e-18

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 79.85  E-value: 9.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQIRTLDVTKKKQIDQFASE----IERLDVLFN 80
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEkalkELKEYGEVYAVKADLSDKDDLKNLVKEawelLGGIDALVW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  81 VAG-------FVHHGTILDceekdWdfsmnLNVRSMYLMIKAFLPKMLAQK------SGNIINMSSVasSIKGVVNRCVY 147
Cdd:PRK08340  83 NAGnvrcepcMLHEAGYSD-----W-----LEAALLHLVAPGYLTTLLIQAwlekkmKGVLVYLSSV--SVKEPMPPLVL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 S-TSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARP-----NPKEA-RNDFLKRQKTGRFATAEEIALL 220
Cdd:PRK08340 151 AdVTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTPGARENLARIAeergvSFEETwEREVLERTPLKRTGRWEELGSL 230

                        250       260
                 ....*....|....*....|.
gi 511847639 221 CVYLASDESAYVTGNPVIIDG 241
Cdd:PRK08340 231 IAFLLSENAEYMLGSTIVFDG 251
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 4-245 1.93e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 79.08  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKL----QELEECPG---IQIRTLDVTKKKQI----DQFASEI 72
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLaaaaEEIEALKGagaVRYEPADVTDEDQVaravDAATAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ERLDVLFNVAGFVHH-GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSikgVVNRC--VYST 149
Cdd:PRK05875  85 GRLHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAAS---NTHRWfgAYGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKsLAADFI-QQGIRCNCVCPGTVDTpSLQERIQARPnpkEARNDFLKRQKTGRFATAEEIALLCVYLASDE 228
Cdd:PRK05875 162 TKSAVDHLMK-LAADELgPSWVRVNSIRPGLIRT-DLVAPITESP---ELSADYRACTPLPRVGEVEDVANLAMFLLSDA 236

                        250
                 ....*....|....*..
gi 511847639 229 SAYVTGNPVIIDGGWSL 245
Cdd:PRK05875 237 ASWITGQVINVDGGHML 253
PRK08278 PRK08278
SDR family oxidoreductase;
1-186 2.70e-17

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 78.79  E-value: 2.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAK-VIA--TDINESKL--------QELEECPG----IQirtLDVTKKKQI 65
Cdd:PRK08278   1 MMSLSGKTLFITGASRGIGLAIALRAARDGANiVIAakTAEPHPKLpgtihtaaEEIEAAGGqalpLV---GDVRDEDQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  66 DQ-FASEIER---LDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMS-SVASSIKG 140
Cdd:PRK08278  78 AAaVAKAVERfggIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSpPLNLDPKW 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 511847639 141 VVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGT-VDTPSLQ 186
Cdd:PRK08278 158 FAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPRTtIATAAVR 204
PRK07041 PRK07041
SDR family oxidoreductase;
10-242 2.72e-17

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 77.77  E-value: 2.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  10 VVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVAGFV 85
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAaaarALGGGAPVRTAALDITDEAAVDAFFAEAGPFDHVVITAADT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  86 HHGTILDCEEKDWDFSMNLNVRSMYLMIKAflPKMLAqkSGNIINMSSVAS-------SIKGVVNrcvystskAAVIGLT 158
Cdd:PRK07041  81 PGGPVRALPLAAAQAAMDSKFWGAYRVARA--ARIAP--GGSLTFVSGFAAvrpsasgVLQGAIN--------AALEALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 159 KSLAADFIQqgIRCNCVCPGTVDTPSLQeriQARPNPKEARNDFL-KRQKTGRFATAEEIALLCVYLAsdESAYVTGNPV 237
Cdd:PRK07041 149 RGLALELAP--VRVNTVSPGLVDTPLWS---KLAGDAREAMFAAAaERLPARRVGQPEDVANAILFLA--ANGFTTGSTV 221


                 ....*
gi 511847639 238 IIDGG 242
Cdd:PRK07041 222 LVDGG 226
PRK07024 PRK07024
SDR family oxidoreductase;
9-183 5.06e-17

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 77.66  E-value: 5.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKV--IA--TDINESKLQELEECPGIQIRTLDVTKKKQIDQFASE-IERL---DVLFN 80
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLglVArrTDALQAFAARLPKAARVSVYAADVRDADALAAAAADfIAAHglpDVVIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  81 VAGfVHHGTILDCEEkDWD-FS--MNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASsIKGVVNRCVYSTSKAAVIGL 157
Cdd:PRK07024  85 NAG-ISVGTLTEERE-DLAvFRevMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAG-VRGLPGAGAYSASKAAAIKY 161

                        170       180
                 ....*....|....*....|....*.
gi 511847639 158 TKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK07024 162 LESLRVELRPAGVRVVTIAPGYIRTP 187
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 4-227 8.71e-17

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: 77.10  E-value: 8.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT-----DINESKLQELEECPGIQI-RTLDVTKKKQIDQFASEIE---- 73
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITgrtilPQLPGTAEEIEARGGKCIpVRCDHSDDDEVEALFERVAreqq 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 -RLDVLFNVAgFVHHGTILDCEEK--------DWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAsSIKGVVNr 144
Cdd:cd09763   81 gRLDILVNNA-YAAVQLILVGVAKpfweepptIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTG-GLEYLFN- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 145 CVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYL 224
Cdd:cd09763  158 VAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT----ELVLEMPEDDEGSWHAKERDAFLNGETTEYSGRCVVAL 233


                 ...
gi 511847639 225 ASD 227
Cdd:cd09763  234 AAD 236
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 8.81e-17

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 76.90  E-value: 8.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVT--AAAQGIGRAAALAFAREGAKVIATDINESKL---QELEECPGIQIRT-LDVTKKKQIDQFASEIE- 73
Cdd:PRK07533   5 LLPLAGKRGLVVgiANEQSIAWGCARAFRALGAELAVTYLNDKARpyvEPLAEELDAPIFLpLDVREPGQLEAVFARIAe 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 ---RLDVLFNVAGFVH----HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSiKGVVNRCV 146
Cdd:PRK07533  85 ewgRLDFLLHSIAFAPkedlHGRVVDCSREGFALAMDVSCHSFIRMARLAEPLM--TNGGSLLTMSYYGAE-KVVENYNL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpslqeriqaR-----PNPKEARNDFLKRQKTGRFATAEEIALLC 221
Cdd:PRK07533 162 MGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKT---------RaasgiDDFDALLEDAAERAPLRRLVDIDDVGAVA 232

                        250       260
                 ....*....|....*....|...
gi 511847639 222 VYLASDESAYVTGNPVIIDGGWS 244
Cdd:PRK07533 233 AFLASDAARRLTGNTLYIDGGYH 255
PRK09291 PRK09291
SDR family oxidoreductase;
6-178 1.25e-16

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 76.58  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPG-----IQIRTLDVTkkkqidqfaSEIER------ 74
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAArrglaLRVEKLDLT---------DAIDRaqaaew 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 -LDVLFNVAGFVHHGTIldceekdWDFSMNLnVRSMY--------LMIKAFLPKMLAQKSGNIINMSSVASSIKGvVNRC 145
Cdd:PRK09291  73 dVDVLLNNAGIGEAGAV-------VDIPVEL-VRELFetnvfgplELTQGFVRKMVARGKGKVVFTSSMAGLITG-PFTG 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 511847639 146 VYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPG 178
Cdd:PRK09291 144 AYCASKHALEAIAEAMHAELKPFGIQVATVNPG 176
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 4-245 3.54e-16

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 75.50  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIA-----TDINESKLQE--------------LEECPGIQ--IRTLDVTKK 62
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhygnrKEEAEETVYEiqsnggsafsiganLESLHGVEalYSSLDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  63 KQIDQfaseiERLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSIKgVV 142
Cdd:PRK12747  82 NRTGS-----TKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRIS-LP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 143 NRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpSLQERIQARPNPKEARNDFlkrQKTGRFATAEEIALLCV 222
Cdd:PRK12747 154 DFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKT-DMNAELLSDPMMKQYATTI---SAFNRLGEVEDIADTAA 229

                        250       260
                 ....*....|....*....|...
gi 511847639 223 YLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK12747 230 FLASPDSRWVTGQLIDVSGGSCL 252
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 6-182 4.05e-16

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: 75.58  E-value: 4.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVI------------ATDINESKLQEleecpGIQIRTLDVTKKKQIDQFASEI- 72
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVImacrdmakceeaAAEIRRDTLNH-----EVIVRHLDLASLKSIRAFAAEFl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 ---ERLDVLFNVAGfvhhgtILDC---EEKDwDFSMNLNVRSM--YLMIKAFLPKMLAQKSGNIINMSSVA--------- 135
Cdd:cd09807   76 aeeDRLDVLINNAG------VMRCpysKTED-GFEMQFGVNHLghFLLTNLLLDLLKKSAPSRIVNVSSLAhkagkinfd 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 511847639 136 --SSIKGVVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:cd09807  149 dlNSEKSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK08219 PRK08219
SDR family oxidoreductase;
7-191 5.02e-16

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 74.58  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAReGAKVIATDINESKLQEL-EECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVAGFV 85
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELaAELPGATPFPVDLTDPEAIAAAVEQLGRLDVLVHNAGVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  86 HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKsGNIINMSSvASSIKGVVNRCVYSTSKAAVIGLTKSLAADf 165
Cdd:PRK08219  83 DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINS-GAGLRANPGWGSYAASKFALRALADALREE- 159

                        170       180
                 ....*....|....*....|....*..
gi 511847639 166 iQQG-IRCNCVCPGTVDTPsLQERIQA 191
Cdd:PRK08219 160 -EPGnVRVTSVHPGRTDTD-MQRGLVA 184
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 4-236 1.11e-15

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 75.72  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL--EECPGIQIRTLDVTKKK--QIDQFASEIERLDVLF 79
Cdd:COG3347  423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAaaELGGGYGADAVDATDVDvtAEAAVAAAFGFAGLDI 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHHGTILDCEEKDWDFSMNLNVRSM-------YLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCVYSTSKA 152
Cdd:COG3347  503 GGSDIGVANAGIASSSPEEETRLSFWLNNFahlstgqFLVARAAFQGTGGQGLGGSSVFAVSKNAAAAAYGAAAAATAKA 582

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTPS--------LQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCVYL 224
Cdd:COG3347  583 AAQHLLRALAAEGGANGINANRVNPDAVLDGSaiwasaarAERAAAYGIGNLLLEEVYRKRVALAVLVLAEDIAEAAAFF 662

                        250
                 ....*....|..
gi 511847639 225 ASDESAYVTGNP 236
Cdd:COG3347  663 ASDGGNKATGGR 674
PRK06101 PRK06101
SDR family oxidoreductase;
8-183 2.88e-15

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 72.59  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEE-CPGIQIRTLDVTKKKQIDQFASEIERLDV--LFNvAGf 84
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTqSANIFTLAFDVTDHPGTKAALSQLPFIPElwIFN-AG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  85 vhhgtilDCEEKD---WDFS-----MNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSIkgVVNRC-VYSTSKAAVI 155
Cdd:PRK06101  81 -------DCEYMDdgkVDATlmarvFNVNVLGVANCIEGIQPHL--SCGHRVVIVGSIASEL--ALPRAeAYGASKAAVA 149

                        170       180
                 ....*....|....*....|....*...
gi 511847639 156 GLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK06101 150 YFARTLQLDLRPKGIEVVTVFPGFVATP 177
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 4-180 3.53e-15

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 72.48  E-value: 3.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAK-VIATDINES--KL--------QELEECPG------IQIRTLDVTK---KK 63
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANvVIAAKTAEPhpKLpgtiytaaEEIEAAGGkalpciVDIRDEDQVRaavEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  64 QIDQFASeierLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVAS-SIKGVV 142
Cdd:cd09762   81 AVEKFGG----IDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNlNPKWFK 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 511847639 143 NRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTV 180
Cdd:cd09762  157 NHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPRTA 194
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 8-245 2.13e-14

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: 70.73  E-value: 2.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639    8 VIVVTAAAQGIGRAAALAFAREGAKVI-------------ATDINESKLQELEECPG--IQIRTLDVTKKKQIDQFASEI 72
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVlhyhrsaaaastlAAELNARRPNSAVTCQAdlSNSATLFSRCEAIIDACFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   73 ERLDVLFNVAGFVHHGTIL--DCEEKDWDFS---------MNLNVRSMYLMIKAFLPKML----AQKSGN--IINMSSVA 135
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLrgDAGEGVGDKKslevqvaelFGSNAIAPYFLIKAFAQRQAgtraEQRSTNlsIVNLCDAM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  136 SSIKgVVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQeriqarpnPKEARNDFLKRQKTG-RFATA 214
Cdd:TIGR02685 163 TDQP-LLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPDAM--------PFEVQEDYRRKVPLGqREASA 233

                         250       260       270
                  ....*....|....*....|....*....|.
gi 511847639  215 EEIALLCVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:TIGR02685 234 EQIADVVIFLVSPKAKYITGTCIKVDGGLSL 264
PRK08703 PRK08703
SDR family oxidoreductase;
1-201 3.27e-14

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 69.58  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL---------EECPGIQIRTLDvTKKKQIDQFASE 71
Cdd:PRK08703   1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVydaiveaghPEPFAIRFDLMS-AEEKEFEQFAAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  72 IE-----RLDVLFNVAGFVHHGTILDCEE-KDWDFSMNLNVRSMYLMIKAFLPkMLAQKSGNIINMSSVASSIKGVVNRC 145
Cdd:PRK08703  80 IAeatqgKLDGIVHCAGYFYALSPLDFQTvAEWVNQYRINTVAPMGLTRALFP-LLKQSPDASVIFVGESHGETPKAYWG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 511847639 146 VYSTSKAAVIGLTKSLAADFIQQG-IRCNCVCPGTVDTPslqERIqaRPNPKEARND 201
Cdd:PRK08703 159 GFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSP---QRI--KSHPGEAKSE 210
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 7-189 1.43e-13

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: 68.46  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIAT--DINESKLQELEECPGIQIRT--LDVTKKKQIDQfASEIERLDV----- 77
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGclTKNGPGAKELRRVCSDRLRTlqLDVTKPEQIKR-AAQWVKEHVgekgl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 --LFNVAGFVHHGTilDCEE---KDWDFSMNLNVRSMYLMIKAFLPkMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKA 152
Cdd:cd09805   80 wgLVNNAGILGFGG--DEELlpmDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRV-PFPAGGAYCASKA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPG-----TVDTPSLQERI 189
Cdd:cd09805  156 AVEAFSDSLRRELQPWGVKVSIIEPGnfktgITGNSELWEKQ 197
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 8-199 3.19e-13

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: 67.02  E-value: 3.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKV-IATDINESKLQ----ELEECPGIQI-RTLDVTKKKQIDQFASEIER----LDV 77
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVaLAARREAKLEAllvdIIRDAGGSAKaVPTDARDEDEVIALFDLIEEeigpLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 L-FNVAGFVHhGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIInMSSVASSIKGVVNRCVYSTSKAAVIG 156
Cdd:cd05373   81 LvYNAGANVW-FPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTII-FTGATASLRGRAGFAAFAGAKFALRA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 511847639 157 LTKSLAADFIQQGIR-CNCVCPGTVDTPSLQERIQARPNPKEAR 199
Cdd:cd05373  159 LAQSMARELGPKGIHvAHVIIDGGIDTDFIRERFPKRDERKEED 202
PRK12744 PRK12744
SDR family oxidoreductase;
4-244 3.27e-13

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 67.07  E-value: 3.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN--------ESKLQELEECpGIQIRTL--DVTKKKQIDQ-FASEI 72
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNsaaskadaEETVAAVKAA-GAKAVAFqaDLTTAAAVEKlFDDAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  73 E---RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIInmsSVASSIKGVVN--RCVY 147
Cdd:PRK12744  85 AafgRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIV---TLVTSLLGAFTpfYSAY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSL--QERIQARPNPKEAR--NDFLKRQKTgrfaTAEEIALLCVY 223
Cdd:PRK12744 160 AGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFypQEGAEAVAYHKTAAalSPFSKTGLT----DIEDIVPFIRF 235

                        250       260
                 ....*....|....*....|.
gi 511847639 224 LASDeSAYVTGNPVIIDGGWS 244
Cdd:PRK12744 236 LVTD-GWWITGQTILINGGYT 255
PRK09134 PRK09134
SDR family oxidoreductase;
7-242 7.47e-13

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 66.10  E-value: 7.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKViATDINESkLQELEECPGiQIRTL---------DVTKKKQ----IDQFASEIE 73
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDV-AVHYNRS-RDEAEALAA-EIRALgrravalqaDLADEAEvralVARASAALG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMssvassIKGVVNR-----CVYS 148
Cdd:PRK09134  87 PITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNM------IDQRVWNlnpdfLSYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLAADFIQQgIRCNCVCPGtvdtPSLqeriqarPNPKEARNDFLK-RQKT--GRFATAEEIALLCVYLA 225
Cdd:PRK09134 161 LSKAALWTATRTLAQALAPR-IRVNAIGPG----PTL-------PSGRQSPEDFARqHAATplGRGSTPEEIAAAVRYLL 228

                        250
                 ....*....|....*..
gi 511847639 226 SDESayVTGNPVIIDGG 242
Cdd:PRK09134 229 DAPS--VTGQMIAVDGG 243
PRK08017 PRK08017
SDR family oxidoreductase;
7-182 1.16e-12

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 65.49  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECpGIQIRTLDVTKKKQIDQFASEI-----ERLDVLFNV 81
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNSL-GFTGILLDLDDPESVERAADEVialtdNRLYGLFNN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  82 AGFVHHGTI--LDCEEKDWDFSMNLnvRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVIGLTK 159
Cdd:PRK08017  82 AGFGVYGPLstISRQQMEQQFSTNF--FGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLI-STPGRGAYAASKYALEAWSD 158

                        170       180
                 ....*....|....*....|...
gi 511847639 160 SLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK08017 159 ALRMELRHSGIKVSLIEPGPIRT 181
PRK05993 PRK05993
SDR family oxidoreductase;
7-182 2.04e-12

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 65.05  E-value: 2.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcPGIQIRTLDVTKKKQIDQFASEI-----ERLDVLFNV 81
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA-EGLEAFQLDYAEPESIAALVAQVlelsgGRLDALFNN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  82 AGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINmssvASSIKGVVN---RCVYSTSKAAVIGLT 158
Cdd:PRK05993  84 GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQ----CSSILGLVPmkyRGAYNASKFAIEGLS 159

                        170       180
                 ....*....|....*....|....
gi 511847639 159 KSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK05993 160 LTLRMELQGSGIHVSLIEPGPIET 183
PRK06196 PRK06196
oxidoreductase; Provisional
 4-186 2.59e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 65.09  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT----DINESKLQELEecpGIQIRTLDVTKKKQIDQFASEI----ERL 75
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVParrpDVAREALAGID---GVEVVMLDLADLESVRAFAERFldsgRRI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DVLFNVAGfvhhgtILDCEEK----DWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVVNRCV----- 146
Cdd:PRK06196 101 DILINNAG------VMACPETrvgdGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRSPIRWDDPhftrg 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 ------YSTSKAA----VIGLTKsLAADfiqQGIRCNCVCPGTVDTPsLQ 186
Cdd:PRK06196 175 ydkwlaYGQSKTAnalfAVHLDK-LGKD---QGVRAFSVHPGGILTP-LQ 219
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
4-245 5.36e-12

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 63.99  E-value: 5.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGK--VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELE----ECPGIQIRTLDVTKKKQIDQFASEIER--- 74
Cdd:PRK08415   3 MKGKkgLIVGVANNKSIAYGIAKACFEQGAELAFTYLNEALKKRVEpiaqELGSDYVYELDVSKPEHFKSLAESLKKdlg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 -LDVLFNVAGFVH----HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASsIKGVVNRCVYST 149
Cdd:PRK08415  83 kIDFIVHSVAFAPkealEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL--NDGASVLTLSYLGG-VKYVPHYNVMGV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 150 SKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQE----RIQARPNPKEARndfLKRQktgrfATAEEIALLCVYLA 225
Cdd:PRK08415 160 AKAALESSVRYLAVDLGKKGIRVNAISAGPIKTLAASGigdfRMILKWNEINAP---LKKN-----VSIEEVGNSGMYLL 231

                        250       260
                 ....*....|....*....|
gi 511847639 226 SDESAYVTGNPVIIDGGWSL 245
Cdd:PRK08415 232 SDLSSGVTGEIHYVDAGYNI 251
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-180 7.55e-12

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 63.84  E-value: 7.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKkqiDQFASEIERLDVLFNVAGFVHHG 88
Cdd:COG0451    2 ILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDP---EALAAALAGVDAVVHLAAPAGVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  89 tildceEKDWDFSMNLNVRSMYLMIKAflpkMLAQKSGNIINMSSvaSSIKGVVNRCV-----------YSTSKAAVIGL 157
Cdd:COG0451   79 ------EEDPDETLEVNVEGTLNLLEA----ARAAGVKRFVYASS--SSVYGDGEGPIdedtplrpvspYGASKLAAELL 146

                        170       180
                 ....*....|....*....|...
gi 511847639 158 TKSLAADFiqqGIRCNCVCPGTV 180
Cdd:COG0451  147 ARAYARRY---GLPVTILRPGNV 166
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 11-183 1.50e-11

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 61.77  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  11 VTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVAGFVHHGTI 90
Cdd:cd11730    3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPADVAAELEVWALAQELGPLDLLVYAAGAILGKPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  91 LDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGVvnrCVYSTSKAAVIGLTKSLAADFiqQGI 170
Cdd:cd11730   83 ARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPELVMLPGL---SAYAAAKAALEAYVEVARKEV--RGL 157

                        170
                 ....*....|...
gi 511847639 171 RCNCVCPGTVDTP 183
Cdd:cd11730  158 RLTLVRPPAVDTG 170
PRK06953 PRK06953
SDR family oxidoreductase;
7-182 2.50e-11

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 61.24  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECpGIQIRTLDVTKKKQIDQFASEI--ERLDVLFNVAGF 84
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQAL-GAEALALDVADPASVAGLAWKLdgEALDAAVYVAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  85 V--HHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPkMLAQKSGNIINMSSVASSIKGVVNRC--VYSTSKAAVIGLTKS 160
Cdd:PRK06953  81 YgpRTEGVEPITREDFDAVMHTNVLGPMQLLPILLP-LVEAAGGVLAVLSSRMGSIGDATGTTgwLYRASKAALNDALRA 159

                        170       180
                 ....*....|....*....|..
gi 511847639 161 LAADFiqQGIRCNCVCPGTVDT 182
Cdd:PRK06953 160 ASLQA--RHATCIALHPGWVRT 179
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 6-230 2.94e-11

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: 61.46  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQ----ELEECPG---IQIRTLDVTKKKQI----DQFASEIER 74
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEearkEIETESGnqnIFLHIVDMSDPKQVwefvEEFKEEGKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVAGFVHHGTILDceEKDWDFSMNLNVRSMYLMIKAFLP----------------KMLAQKSgNIINMSSVASSI 138
Cdd:cd09808   81 LHVLINNAGCMVNKRELT--EDGLEKNFATNTLGTYILTTHLIPvlekeedprvitvssgGMLVQKL-NTNNLQSERTAF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 139 KGVVnrcVYSTSKAAVIGLTKSLAADFiqQGIRCNCVCPGTVDTPSLQeriQARPnpkearnDFLKRQKTgRFATAEEIA 218
Cdd:cd09808  158 DGTM---VYAQNKRQQVIMTEQWAKKH--PEIHFSVMHPGWADTPAVR---NSMP-------DFHARFKD-RLRSEEQGA 221

                        250
                 ....*....|..
gi 511847639 219 LLCVYLASDESA 230
Cdd:cd09808  222 DTVVWLALSSAA 233
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 9-183 5.41e-11

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 59.90  E-value: 5.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQeleecpgiqirtLDVTKKKQIDQFASEIERLDVLFNVAGFVHHG 88
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQ------------VDITDEASIKALFEKVGHFDAIVSTAGDAEFA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  89 TILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaqKSGNIINMSSVASSIKGVVNRCVYSTSKAAVIGLTKSLAADfIQQ 168
Cdd:cd11731   69 PLAELTDADFQRGLNSKLLGQINLVRHGLPYL---NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIE-LPR 144

                        170
                 ....*....|....*
gi 511847639 169 GIRCNCVCPGTVDTP 183
Cdd:cd11731  145 GIRINAVSPGVVEES 159
PRK07102 PRK07102
SDR family oxidoreductase;
6-183 7.33e-11

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 60.32  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpGIQIRT--------LDVTkkkQIDQFASEIERLDV 77
Cdd:PRK07102   1 MKKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLAD--DLRARGavavstheLDIL---DTASHAAFLDSLPA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAgFVHHGTILDCE--EKDWDFS---MNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSKA 152
Cdd:PRK07102  76 LPDIV-LIAVGTLGDQAacEADPALAlreFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGD-RGRASNYVYGSAKA 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511847639 153 AVIGLTKSLAADFIQQGIRCNCVCPGTVDTP 183
Cdd:PRK07102 154 ALTAFLSGLRNRLFKSGVHVLTVKPGFVRTP 184
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 8.27e-11

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 60.37  E-value: 8.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTA--AAQGIGRAAALAFAREGAKVIATDIN---ESKLQELEECPGIQI-RTLDVTKKKQIDQFASEIER 74
Cdd:PRK08690   1 MGFLQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVVdklEERVRKMAAELDSELvFRCDVASDDEINQVFADLGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 ----LDVLFNVAGFVHH----GTILDCEEKD-WDFSMNLNVRSMYLMIKAFLPKMLAQKSGnIINMSSVASsIKGVVNRC 145
Cdd:PRK08690  81 hwdgLDGLVHSIGFAPKealsGDFLDSISREaFNTAHEISAYSLPALAKAARPMMRGRNSA-IVALSYLGA-VRAIPNYN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 146 VYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlqeriqarpnpKEARNDFLKRQKTG-------RFATAEEIA 218
Cdd:PRK08690 159 VMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLA-----------ASGIADFGKLLGHVaahnplrRNVTIEEVG 227

                        250       260
                 ....*....|....*....|....*..
gi 511847639 219 LLCVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK08690 228 NTAAFLLSDLSSGITGEITYVDGGYSI 254
PRK08177 PRK08177
SDR family oxidoreductase;
7-165 9.78e-11

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 59.66  E-value: 9.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKKQIDQFASEI--ERLDVLF---NV 81
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKLDMNDPASLDQLLQRLqgQRFDLLFvnaGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  82 AGFVHHGTILDCEEKDWDFSMNlNVRSMYLMIKAFLPKmLAQKSGNIINMSSVASSI---KGvVNRCVYSTSKAAVIGLT 158
Cdd:PRK08177  82 SGPAHQSAADATAAEIGQLFLT-NAIAPIRLARRLLGQ-VRPGQGVLAFMSSQLGSVelpDG-GEMPLYKASKAALNSMT 158


                 ....*..
gi 511847639 159 KSLAADF 165
Cdd:PRK08177 159 RSFVAEL 165
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-242 1.02e-10

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 60.12  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAA--QGIGRAAALAFAREGAKVIATDINESKLQELEEC--PGIQIRTLDVTKKKQIDQ-FASEIERL 75
Cdd:PRK06079   2 SGILSGKKIVVMGVAnkRSIAWGCAQAIKDQGATVIYTYQNDRMKKSLQKLvdEEDLLVECDVASDESIERaFATIKERV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  76 DvlfNVAGFVH----------HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPkmLAQKSGNIINMSSVASSiKGVVNRC 145
Cdd:PRK06079  82 G---KIDGIVHaiayakkeelGGNVTDTSRDGYALAQDISAYSLIAVAKYARP--LLNPGASIVTLTYFGSE-RAIPNYN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 146 VYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPKEARndflKRQKTGRFATAEEIALLCVYLA 225
Cdd:PRK06079 156 VMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGIKGHKDLLKESD----SRTVDGVGVTIEEVGNTAAFLL 231

                        250
                 ....*....|....*..
gi 511847639 226 SDESAYVTGNPVIIDGG 242
Cdd:PRK06079 232 SDLSTGVTGDIIYVDKG 248
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-240 1.44e-10

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 59.70  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIAtdINESKLQELEEC-----PGIQIRTLDVTKKKQIDQ----FASEIERLDV 77
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVIS--ISRTENKELTKLaeqynSNLTFHSLDLQDVHELETnfneILSSIQEDNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 ----LFNVAGFVHH-GTILDCEEKDWDFSMNLNVRSMYLMIKAFLpKMLAQKSGN--IINMSSVASS--IKGvvnRCVYS 148
Cdd:PRK06924  80 ssihLINNAGMVAPiKPIEKAESEELITNVHLNLLAPMILTSTFM-KHTKDWKVDkrVINISSGAAKnpYFG---WSAYC 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 149 TSKAAVIGLTKSLA--ADFIQQGIRCNCVCPGTVDTpSLQERIqaRPNPKEA---RNDFLKRQKTGRFATAEEIALLCVY 223
Cdd:PRK06924 156 SSKAGLDMFTQTVAteQEEEEYPVKIVAFSPGVMDT-NMQAQI--RSSSKEDftnLDRFITLKEEGKLLSPEYVAKALRN 232

                        250
                 ....*....|....*..
gi 511847639 224 LASDESayvTGNPVIID 240
Cdd:PRK06924 233 LLETED---FPNGEVID 246
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 6-182 2.26e-10

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 59.49  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEC-----PGIQIRTLDVTKKKQIDQ----FASEIERLD 76
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSiqskySKTQIKTVVVDFSGDIDEgvkrIKETIEGLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 V--LFNVAG-------FVHhgtildceEKDWDFSMNL---NVRSMYLMIKAFLPKMLAQKSGNIINM-SSVASSIKGVVN 143
Cdd:PLN02780 133 VgvLINNVGvsypyarFFH--------EVDEELLKNLikvNVEGTTKVTQAVLPGMLKRKKGAIINIgSGAAIVIPSDPL 204

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 511847639 144 RCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PLN02780 205 YAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVAT 243
PRK08251 PRK08251
SDR family oxidoreductase;
7-182 1.24e-09

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 56.87  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKvIA-----TDINESKLQELEEC-PGIQ--IRTLDVTKKKQI----DQFASEIER 74
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRD-LAlcarrTDRLEELKAELLARyPGIKvaVAALDVNDHDQVfevfAEFRDELGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LD-VLFNvAGF---VHHGTildceekdWDFSMNL-----NVRSMYLMIKAFLPKMLAQKSGNIINMSSVaSSIKGVV-NR 144
Cdd:PRK08251  82 LDrVIVN-AGIgkgARLGT--------GKFWANKataetNFVAALAQCEAAMEIFREQGSGHLVLISSV-SAVRGLPgVK 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 511847639 145 CVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK08251 152 AAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRS 189
PRK06720 PRK06720
hypothetical protein; Provisional
 3-124 1.13e-08

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 53.05  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   3 RLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDIN-ESKLQELEECP--GIQIRTLDVTKKKQ------IDQFASEIE 73
Cdd:PRK06720  13 KLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDqESGQATVEEITnlGGEALFVSYDMEKQgdwqrvISITLNAFS 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511847639  74 RLDVLFNVAGFVHHGTIL-DCEEKDwdfSMNLNVRSMYLMIKAFLPKMLAQK 124
Cdd:PRK06720  93 RIDMLFQNAGLYKIDSIFsRQQEND---SNVLCINDVWIEIKQLTSSFMKQQ 141
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
4-245 1.29e-08

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 53.96  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   4 LDGKVIVVTAAA--QGIGRAAALAFAREGAKVIAT---DINESKLQELEECPGIQ---IRTLDVTKKKQIDQ-FASEIER 74
Cdd:PRK08594   5 LEGKTYVVMGVAnkRSIAWGIARSLHNAGAKLVFTyagERLEKEVRELADTLEGQeslLLPCDVTSDEEITAcFETIKEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 LDVLFNVA---GFVH----HGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSiKGVVNRCVY 147
Cdd:PRK08594  85 VGVIHGVAhciAFANkedlRGEFLETSRDGFLLAQNISAYSLTAVAREAKKLM--TEGGSIVTLTYLGGE-RVVQNYNVM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 148 STSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlqeriqarpnpkeAR-----NDFLK----RQKTGRFATAEEIA 218
Cdd:PRK08594 162 GVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLS-------------AKgvggfNSILKeieeRAPLRRTTTQEEVG 228

                        250       260
                 ....*....|....*....|....*..
gi 511847639 219 LLCVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK08594 229 DTAAFLFSDLSRGVTGENIHVDSGYHI 255
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 9-242 1.48e-08

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 53.40  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINE-SKLQELEEcPGIQIRTLDVTKKKQIDQFASEI-ERLDVLFNVagfVH 86
Cdd:PRK06483   5 ILITGAGQRIGLALAWHLLAQGQPVIVSYRTHyPAIDGLRQ-AGAQCIQADFSTNAGIMAFIDELkQHTDGLRAI---IH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  87 HGTILDCEEKDWDFS------MNLNVRSMYLMIKAFLPKMLAQKSG--NIINMSS-VASsiKGVVNRCVYSTSKAAVIGL 157
Cdd:PRK06483  81 NASDWLAEKPGAPLAdvlarmMQIHVNAPYLLNLALEDLLRGHGHAasDIIHITDyVVE--KGSDKHIAYAASKAALDNM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 158 TKSLAADFIQQgIRCNCVCPGTvdtpslqerIQARPNPKEARndflkRQKT------GRFATAEEIALLCVYLAsdESAY 231
Cdd:PRK06483 159 TLSFAAKLAPE-VKVNSIAPAL---------ILFNEGDDAAY-----RQKAlaksllKIEPGEEEIIDLVDYLL--TSCY 221

                        250
                 ....*....|.
gi 511847639 232 VTGNPVIIDGG 242
Cdd:PRK06483 222 VTGRSLPVDGG 232
PRK06482 PRK06482
SDR family oxidoreductase;
11-182 3.61e-08

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 52.81  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  11 VTAAAQGIGRA-AALAFAReGAKVIATDINESKLQELEECPGIQIR--TLDVTK----KKQIDQFASEIERLDVLFNVAG 83
Cdd:PRK06482   7 ITGASSGFGRGmTERLLAR-GDRVAATVRRPDALDDLKARYGDRLWvlQLDVTDsaavRAVVDRAFAALGRIDVVVSNAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  84 FVHHGTI--LDCEEKDWDFSMNLnVRSMYLmIKAFLPKMLAQKSGNIINMSSVASSIkGVVNRCVYSTSKAAVIGLTKSL 161
Cdd:PRK06482  86 YGLFGAAeeLSDAQIRRQIDTNL-IGSIQV-IRAALPHLRRQGGGRIVQVSSEGGQI-AYPGFSLYHATKWGIEGFVEAV 162

                        170       180
                 ....*....|....*....|.
gi 511847639 162 AADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK06482 163 AQEVAPFGIEFTIVEPGPART 183
PRK07775 PRK07775
SDR family oxidoreductase;
10-182 5.51e-08

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 52.45  E-value: 5.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  10 VVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcpgiQIRT---------LDVTKKKQIDQFASEIER----LD 76
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVD----KIRAdggeavafpLDVTDPDSVKSFVAQAEEalgeIE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  77 VLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSvassikGVVNR-----CVYSTSK 151
Cdd:PRK07775  90 VLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGS------DVALRqrphmGAYGAAK 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 511847639 152 AAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK07775 164 AGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 167-242 7.40e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 51.94  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 167 QQGIRCNCVCPGTVDTPSLQERIQArpnpkeARNDFLKRQ----KTGRFATAEEIALLCVYLASDESAYVTGNPVIIDGG 242
Cdd:PRK06940 189 ERGARINSISPGIISTPLAQDELNG------PRGDGYRNMfaksPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262
PRK08862 PRK08862
SDR family oxidoreductase;
8-177 1.46e-07

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 50.49  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   8 VIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGI--QIRTLDVTKKKQ------IDQFASEIER-LDV 77
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTyEQCSALtdNVYSFQLKDFSQesirhlFDAIEQQFNRaPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHHGTILDCEEKDwDFSMNLN--VRSMYLMIKAFLPKMLAQKS-GNIINMSSVASsikgVVNRCVYSTSKAAV 154
Cdd:PRK08862  87 LVNNWTSSPLPSLFDEQPSE-SFIQQLSslASTLFTYGQVAAERMRKRNKkGVIVNVISHDD----HQDLTGVESSNALV 161

                        170       180
                 ....*....|....*....|...
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCP 177
Cdd:PRK08862 162 SGFTHSWAKELTPFNIRVGGVVP 184
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 1.72e-07

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 50.78  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALA--FAREGAKVIAT---DINESKLQELEECPGIQ-IRTLDVTKKKQIDQFASEIER 74
Cdd:PRK06603   3 TGLLQGKKGLITGIANNMSISWAIAqlAKKHGAELWFTyqsEVLEKRVKPLAEEIGCNfVSELDVTNPKSISNLFDDIKE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 ----LDVLFNVAGFVH----HGTILDCEEKDWDFSMNLNVRSMYLMIKAflPKMLAQKSGNIINMSSVASSiKGVVNRCV 146
Cdd:PRK06603  83 kwgsFDFLLHGMAFADknelKGRYVDTSLENFHNSLHISCYSLLELSRS--AEALMHDGGSIVTLTYYGAE-KVIPNYNV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlqeriqarpnpKEARNDF---LKRQKTG----RFATAEEIAL 219
Cdd:PRK06603 160 MGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLA-----------SSAIGDFstmLKSHAATaplkRNTTQEDVGG 228

                        250       260
                 ....*....|....*....|....*.
gi 511847639 220 LCVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK06603 229 AAVYLFSELSKGVTGEIHYVDCGYNI 254
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
1-182 3.00e-07

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 49.94  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTaaaqGIGRAAALAFA------REGAKVIATDINE-SKLQEL------EECPGIQirtLDVTKKKQIDQ 67
Cdd:PRK07889   2 MGLLEGKRILVT----GVITDSSIAFHvarvaqEQGAEVVLTGFGRaLRLTERiakrlpEPAPVLE---LDVTNEEHLAS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  68 FASEI-ERLDvlfNVAGFVHH----------GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINM---SS 133
Cdd:PRK07889  75 LADRVrEHVD---GLDGVVHSigfapqsalgGNFLDAPWEDVATALHVSAYSLKSLAKALLPLM--NEGGSIVGLdfdAT 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511847639 134 VASSI---KGVvnrcvystSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK07889 150 VAWPAydwMGV--------AKAALESTNRYLARDLGPRGIRVNLVAAGPIRT 193
PRK09009 PRK09009
SDR family oxidoreductase;
9-191 3.26e-07

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 49.68  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAA--LAFAREGAKVIATdinESKLQELEECPGIQIRTLDVTKKKQIDQFASEIERLDVLFNVAGFVH 86
Cdd:PRK09009   3 ILIVGGSGGIGKAMVkqLLERYPDATVHAT---YRHHKPDFQHDNVQWHALDVTDEAEIKQLSEQFTQLDWLINCVGMLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  87 HGTilDCEEK-----DWDF---SMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSIKGvvNRC----VYSTSKAAV 154
Cdd:PRK09009  80 TQD--KGPEKslqalDADFflqNITLNTLPSLLLAKHFTPKLKQSESAKFAVISAKVGSISD--NRLggwySYRASKAAL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFiQQGIRCNCVC---PGTVDTPsLQERIQA 191
Cdd:PRK09009 156 NMFLKTLSIEW-QRSLKHGVVLalhPGTTDTA-LSKPFQQ 193
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 8-224 3.54e-07

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: 49.91  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639    8 VIVVTAAAQGIGRAAALAFAR----EGAKVIATDINESKLQELEECPG-------IQIRTLDVTKKKQIDQFA------- 69
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGaersglrVVRVSLDLGAEAGLEQLLkalrelp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   70 --SEIERLdVLFNVAGFVHHGTILDCEEKDWDFSMN---LNVRSMYLMIKAFLPKMLAQKSGN--IINMSSVAsSIKGVV 142
Cdd:TIGR01500  82 rpKGLQRL-LLINNAGTLGDVSKGFVDLSDSTQVQNywaLNLTSMLCLTSSVLKAFKDSPGLNrtVVNISSLC-AIQPFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  143 NRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTpSLQERIQARPNPKEARNDFLKRQKTGRFATAEEIALLCV 222
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDT-DMQQQVREESVDPDMRKGLQELKAKGKLVDPKVSAQKLL 238


                  ..
gi 511847639  223 YL 224
Cdd:TIGR01500 239 SL 240
PRK07984 PRK07984
enoyl-ACP reductase FabI;
1-245 3.65e-07

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 49.90  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQ--GIGRAAALAFAREGAKVIATDINE---SKLQELEECPGIQI-RTLDVTKKKQIDQFASEIER 74
Cdd:PRK07984   1 MGFLSGKRILVTGVASklSIAYGIAQAMHREGAELAFTYQNDklkGRVEEFAAQLGSDIvLPCDVAEDASIDAMFAELGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  75 ldVLFNVAGFVHHGTILDCEEKDWDF-----------SMNLNVRSMYLMIKAfLPKMLAQKSGnIINMSSVASSiKGVVN 143
Cdd:PRK07984  81 --VWPKFDGFVHSIGFAPGDQLDGDYvnavtregfkiAHDISSYSFVAMAKA-CRSMLNPGSA-LLTLSYLGAE-RAIPN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 144 RCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVdtpslqeRIQARPNPKEARNDFLKRQKTG---RFATAEEIALL 220
Cdd:PRK07984 156 YNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPI-------RTLAASGIKDFRKMLAHCEAVTpirRTVTIEDVGNS 228

                        250       260
                 ....*....|....*....|....*
gi 511847639 221 CVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK07984 229 AAFLCSDLSAGISGEVVHVDGGFSI 253
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 6-167 1.83e-06

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 47.61  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGA-KVIATDINESKLQELEE-----CPGIQIRTL--DVtKKKQIDQFASEIERLDV 77
Cdd:cd05237    2 GKTILVTGGAGSIGSELVRQILKFGPkKLIVFDRDENKLHELVRelrsrFPHDKLRFIigDV-RDKERLRRAFKERGPDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  78 LFNVAGFVHhgtildceekdwdfsmnlnVRSMYL----MIKAflpkmlaqksgNIINMSSVAS-SIKGVVNR--CVySTS 150
Cdd:cd05237   81 VFHAAALKH-------------------VPSMEDnpeeAIKT-----------NVLGTKNVIDaAIENGVEKfvCI-STD 129

                        170       180
                 ....*....|....*....|.
gi 511847639 151 KAA----VIGLTKSLAADFIQ 167
Cdd:cd05237  130 KAVnpvnVMGATKRVAEKLLL 150
PRK07023 PRK07023
SDR family oxidoreductase;
10-227 5.51e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 46.16  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  10 VVTAAAQGIGRAAALAFAREGAKVIAtdINESKLQELEECPGIQIR--TLDVTKKKQIDQF-ASEIERLDV-------LF 79
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAVLG--VARSRHPSLAAAAGERLAevELDLSDAAAAAAWlAGDLLAAFVdgasrvlLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  80 NVAGFVHH-GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQKSGNIINMSSVASSiKGVVNRCVYSTSKAAVIGLT 158
Cdd:PRK07023  83 NNAGTVEPiGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAAR-NAYAGWSVYCATKAALDHHA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511847639 159 KSLAADfIQQGIRCNCVCPGTVDTpSLQERIQARPN---PKEARNDFLKRqkTGRFATAEEIAL-LCVYLASD 227
Cdd:PRK07023 162 RAVALD-ANRALRIVSLAPGVVDT-GMQATIRATDEerfPMRERFRELKA--SGALSTPEDAARrLIAYLLSD 230
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
135-245 8.55e-06

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 45.89  E-value: 8.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 135 ASSIKGVVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVdtpslqeRIQARPNPKEARNDFLKRQKT---GRF 211
Cdd:PRK06505 147 GGSTRVMPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPV-------RTLAGAGIGDARAIFSYQQRNsplRRT 219

                         90       100       110
                 ....*....|....*....|....*....|....
gi 511847639 212 ATAEEIALLCVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK06505 220 VTIDEVGGSALYLLSDLSSGVTGEIHFVDSGYNI 253
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-182 1.25e-05

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: 45.18  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL-EECPGIQIRTL-DVTKKKQIDQFASE---IERLDVLFNVAG 83
Cdd:cd08951   10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAkAACPGAAGVLIgDLSSLAETRKLADQvnaIGRFDAVIHNAG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  84 FVHHGTILDCEEkDWDFSMNLNVRSMYLMiKAFL--PKMLAQKSGNIINmsSVASSIKGV--VNRC-----VYSTSKAAV 154
Cdd:cd08951   90 ILSGPNRKTPDT-GIPAMVAVNVLAPYVL-TALIrrPKRLIYLSSGMHR--GGNASLDDIdwFNRGendspAYSDSKLHV 165

                        170       180
                 ....*....|....*....|....*...
gi 511847639 155 IGLTKSLAADFiqQGIRCNCVCPGTVDT 182
Cdd:cd08951  166 LTLAAAVARRW--KDVSSNAVHPGWVPT 191
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 5-141 1.92e-05

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: 45.05  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAR-EGAKVIAT------DINESKLQELEEC--PGIQI--RTLDVTKKKQIDQFASEIE 73
Cdd:cd08953  204 PGGVYLVTGGAGGIGRALARALARrYGARLVLLgrsplpPEEEWKAQTLAALeaLGARVlyISADVTDAAAVRRLLEKVR 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511847639  74 ----RLDVLFNVAGFVHHGTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMLAQksgnIINMSSVASSIKGV 141
Cdd:cd08953  284 erygAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDF----FVLFSSVSAFFGGA 351
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
1-243 3.92e-05

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 43.59  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGK--VIVVTAAAQGIGRAAALAFAREGAKVIAT---DINESKLQEL-EECPGIQIRTLDVTKKKQIDQFASEIE- 73
Cdd:PRK08159   5 SGLMAGKrgLILGVANNRSIAWGIAKACRAAGAELAFTyqgDALKKRVEPLaAELGAFVAGHCDVTDEASIDAVFETLEk 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 ---RLDVLFNVAGFVHH----GTILDCEEKDWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVASSiKGVVNRCV 146
Cdd:PRK08159  85 kwgKLDFVVHAIGFSDKdeltGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLM--TDGGSILTLTYYGAE-KVMPHYNV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 147 YSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSLQERIQARPNPK-EARNDFLKRQktgrfATAEEIALLCVYLA 225
Cdd:PRK08159 162 MGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGDFRYILKwNEYNAPLRRT-----VTIEEVGDSALYLL 236

                        250
                 ....*....|....*...
gi 511847639 226 SDESAYVTGNPVIIDGGW 243
Cdd:PRK08159 237 SDLSRGVTGEVHHVDSGY 254
PRK07806 PRK07806
SDR family oxidoreductase;
1-120 4.10e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 43.56  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESK-----LQELEECpGIQIRTL--DVTKKKQIDQFASEI- 72
Cdd:PRK07806   1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPrankvVAEIEAA-GGRASAVgaDLTDEESVAALMDTAr 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 511847639  73 ---ERLDVL-FNVAGfvhhGTILDCEEkdwDFSMNLNVRSMYLMIKAFLPKM 120
Cdd:PRK07806  80 eefGGLDALvLNASG----GMESGMDE---DYAMRLNRDAQRNLARAALPLM 124
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 8.20e-05

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 42.78  E-value: 8.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAA--QGIGRAAALAFAREGAKVIATDI------NESKLQELEE--CPGIqIRTLDVTKKKQIDQFAS 70
Cdd:PRK07370   1 MLDLTGKKALVTGIAnnRSIAWGIAQQLHAAGAELGITYLpdekgrFEKKVRELTEplNPSL-FLPCDVQDDAQIEETFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  71 EIE----RLDVLFNVAGFVhhgtilDCEEKDWDFS----------MNLNVRSMYLMIKAFLPKMlaQKSGNIINMSSVAS 136
Cdd:PRK07370  80 TIKqkwgKLDILVHCLAFA------GKEELIGDFSatsregfaraLEISAYSLAPLCKAAKPLM--SEGGSIVTLTYLGG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 137 sIKGVVNRCVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlqerIQARPNPKEARNDFLKRQKTGRFATAEE 216
Cdd:PRK07370 152 -VRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLA----SSAVGGILDMIHHVEEKAPLRRTVTQTE 226

                        250       260
                 ....*....|....*....|....*....
gi 511847639 217 IALLCVYLASDESAYVTGNPVIIDGGWSL 245
Cdd:PRK07370 227 VGNTAAFLLSDLASGITGQTIYVDAGYCI 255
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 8.98e-05

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 42.50  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTA--AAQGIGRAAALAFAREGAKVIATDINE---SKLQELEECPGIQ-IRTLDVTKKKQIDQ-FASEIE 73
Cdd:PRK06997   1 MGFLAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVGDrfkDRITEFAAEFGSDlVFPCDVASDEQIDAlFASLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  74 R---LDVLFNVAGFVHH----GTILD-CEEKDWDFSMNLNVRSMYLMIKAFLPkMLAQKsGNIINMSSVASSiKGVVNRC 145
Cdd:PRK06997  81 HwdgLDGLVHSIGFAPReaiaGDFLDgLSRENFRIAHDISAYSFPALAKAALP-MLSDD-ASLLTLSYLGAE-RVVPNYN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 146 VYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDTPSlqeriqarpnpKEARNDFLKRQK-------TGRFATAEEIA 218
Cdd:PRK06997 158 TMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLA-----------ASGIKDFGKILDfvesnapLRRNVTIEEVG 226

                        250       260
                 ....*....|....*....|....*.
gi 511847639 219 LLCVYLASDESAYVTGNPVIIDGGWS 244
Cdd:PRK06997 227 NVAAFLLSDLASGVTGEITHVDSGFN 252
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-83 1.08e-04

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


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 42.31  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAqGIGRAAALAFAREGAKVIATDINESKLQELEECPG---IQIRTLDVTKKKQIdqfaSEIERLDVLFNVA 82
Cdd:cd05188  135 GDTVLVLGAG-GVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGAdhvIDYKEEDLEEELRL----TGGGGADVVIDAV 209


                 .
gi 511847639  83 G 83
Cdd:cd05188  210 G 210
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 9-165 1.16e-04

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 42.28  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639    9 IVVTAAAQGIGRAAALAFAREGAKVIATDiNESKLQELEECPGIQIRTLDVTKKKQIDQFASEiERLDVLFNVAGFvhhG 88
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLD-RLTSASNTARLADLRFVEGDLTDRDALEKLLAD-VRPDAVIHLAAV---G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   89 TILDCEEKDWDFSMNlNVRSMYLMIKAflpkMLAQKSGNIINMSSVA------------SSIKGVVN-RCVYSTSKAAVI 155
Cdd:pfam01370  76 GVGASIEDPEDFIEA-NVLGTLNLLEA----ARKAGVKRFLFASSSEvygdgaeipqeeTTLTGPLApNSPYAAAKLAGE 150

                         170
                  ....*....|
gi 511847639  156 GLTKSLAADF 165
Cdd:pfam01370 151 WLVLAYAAAY 160
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 4-78 2.56e-04

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 41.60  E-value: 2.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511847639   4 LDGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLdvtkKKQI---DQFASEIERLDVL 78
Cdd:PRK07424 176 LKGKTVAVTGASGTLGQALLKELHQQGAKVVALTSNSDKITLEINGEDLPVKTL----HWQVgqeAALAELLEKVDIL 249
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 6-84 2.73e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 41.43  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-----LEECPGIQIR--TLDVTKKKQIDQFASEIER---- 74
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEamTLDLASLRSVQRFAEAFKAknsp 80

                         90
                 ....*....|.
gi 511847639  75 LDVLF-NVAGF 84
Cdd:cd09809   81 LHVLVcNAAVF 91
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-178 3.35e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 41.14  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   1 MGRLDGKVIVVTAAAQGIGRAAALAFAREGAKVIAT---------DINESklQELEECP---------GIQIRTlDVTKK 62
Cdd:PRK08303   3 MKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTgrstrarrsEYDRP--ETIEETAelvtaaggrGIAVQV-DHLVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  63 KQI----DQFASEIERLDVLFN-VAGfvhhGTIL-DCEEKDWDFSMNLNVRSMYLMIKA-------FLPKMLAQKSGNII 129
Cdd:PRK08303  80 EQVralvERIDREQGRLDILVNdIWG----GEKLfEWGKPVWEHSLDKGLRMLRLAIDThlitshfALPLLIRRPGGLVV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 511847639 130 NMSSVASSIKGVVNR--CVYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPG 178
Cdd:PRK08303 156 EITDGTAEYNATHYRlsVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPG 206
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-83 4.30e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 40.78  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   5 DGKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQE-----LEECPG--IQIRTLDVTK----KKQIDQFASEIE 73
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAaaariTAATPGadVTLQELDLTSlasvRAAADALRAAYP 94

                         90
                 ....*....|
gi 511847639  74 RLDVLFNVAG 83
Cdd:PRK06197  95 RIDLLINNAG 104
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
119-182 1.07e-03

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 39.31  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511847639 119 KMLAQKSGNIINMSSVASSikgVVNRC--VYSTSKAAVIGLTKSLAADFIQQGIRCNCVCPGTVDT 182
Cdd:PRK07904 132 KMRAQGFGQIIAMSSVAGE---RVRRSnfVYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRT 194
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-80 1.31e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 38.26  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639     2 GRLDGKVIVVTAaaqGI-GRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLdvtkKKQIDQFASEIERLDVLFN 80
Cdd:smart01002  17 GVPPAKVVVIGA---GVvGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTL----YSQAELLEEAVKEADLVIG 89
CDP_TE_SDR_e cd05258
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ...
 7-105 1.37e-03

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


Pssm-ID: 187568 [Multi-domain]  Cd Length: 337  Bit Score: 39.20  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVTAAAQGIGRAAALAFAREGAKVIATD--------INESKLQELEECPGIQIRTLDVTKKkqiDQFASEIERLDVL 78
Cdd:cd05258    1 MRVLITGGAGFIGSNLARFFLKQGWEVIGFDnlmrrgsfGNLAWLKANREDGGVRFVHGDIRNR---NDLEDLFEDIDLI 77

                         90       100
                 ....*....|....*....|....*..
gi 511847639  79 FNVAGFVHHGTILDceEKDWDFSMNLN 105
Cdd:cd05258   78 IHTAAQPSVTTSAS--SPRLDFETNAL 102
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 10-99 1.70e-03

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 38.31  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   10 VVTAAAQGIGRAAALAFAREGAKVIA--------TDINESKLQELEEcPGIQIRTL--DVTKKKQIDQFASEIERLdvLF 79
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARHLVllsrsaapRPDAQALIAELEA-RGVEVVVVacDVSDPDAVAALLAEIKAE--GP 80

                          90       100
                  ....*....|....*....|....*.
gi 511847639   80 NVAGFVH------HGTILDCEEKDWD 99
Cdd:pfam08659  81 PIRGVIHaagvlrDALLENMTDEDWR 106
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
 9-58 3.39e-03

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical 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: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 38.02  E-value: 3.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEcPGIQIRTLD 58
Cdd:cd05269    1 ILVTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAA-DGVEVRQGD 49
ADP_GME_SDR_e cd05248
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ...
 9-108 3.66e-03

ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ADP-L-glycero-D-mannoheptose 6-epimerase, an extended SDR, which catalyzes the NAD-dependent interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. This subgroup has the canonical active site tetrad and NAD(P)-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187559 [Multi-domain]  Cd Length: 317  Bit Score: 38.05  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREG-AKVIATD--INESKLQELEECpgiqirtlDVTKKKQIDQFASEIERLDVLFNVAGFV 85
Cdd:cd05248    2 IIVTGGAGFIGSNLVKALNERGiTDILVVDnlSNGEKFKNLVGL--------KIADYIDKDDFKDWVRKGDENFKIEAIF 73

                         90       100
                 ....*....|....*....|...
gi 511847639  86 HHGTILDCEEKDWDFSMNLNVRS 108
Cdd:cd05248   74 HQGACSDTTETDGKYMMDNNYQY 96
PRK05884 PRK05884
SDR family oxidoreductase;
9-234 3.95e-03

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 37.48  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   9 IVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEECPGIQIRTLDVTKKKQIDQFASEIER-LDVLFNV------ 81
Cdd:PRK05884   3 VLVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDAIVCDNTDPASLEEARGLFPHhLDTIVNVpapswd 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639  82 AGFVHHGTILDCEEKdWDFSMNLNVRSMYLMIKAFLPKMlaQKSGNIINM-------SSVASSIKgvvnrcvystskAAV 154
Cdd:PRK05884  83 AGDPRTYSLADTANA-WRNALDATVLSAVLTVQSVGDHL--RSGGSIISVvpenppaGSAEAAIK------------AAL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639 155 IGLTKSLAADFIQQGIRCNCVCPGTVDTPSLqERIQARPNPkearndflkrqktgrfaTAEEIALLCVYLASDESAYVTG 234
Cdd:PRK05884 148 SNWTAGQAAVFGTRGITINAVACGRSVQPGY-DGLSRTPPP-----------------VAAEIARLALFLTTPAARHITG 209
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 6-83 4.99e-03

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 37.54  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   6 GKVIVVTAAAQGIGRAAA-LAFAReGAKVIATdINESKLQELeecpgiqiRTLDVTK----KKQIDQFASEIERLDVLFN 80
Cdd:cd05289  145 GQTVLIHGAAGGVGSFAVqLAKAR-GARVIAT-ASAANADFL--------RSLGADEvidyTKGDFERAAAPGGVDAVLD 214


                 ...
gi 511847639  81 VAG 83
Cdd:cd05289  215 TVG 217
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 4-54 5.94e-03

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 36.80  E-value: 5.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 511847639   4 LDGKVIVVtaaaQGIG---RAAALAFAREGAKVIATDINESKLQELEECPGIQI 54
Cdd:cd01075   26 LEGKTVAV----QGLGkvgYKLAEHLLEEGAKLIVADINEEAVARAAELFGATV 75
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-46 6.35e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 37.19  E-value: 6.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQEL 46
Cdd:cd08268  145 GDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDAL 185
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 6-66 6.36e-03

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 37.26  E-value: 6.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511847639   6 GKVIVVTAAAQGIGRAAALAFAREGAKVIATDINESKLQELEEC----------PGIQIRTLDVTKKKQID 66
Cdd:cd05282  139 GDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELKALgadevidsspEDLAQRVKEATGGAGAR 209
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 6-48 7.27e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 37.05  E-value: 7.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 511847639   6 GKVIVVTAAAQGIGRAA-ALAfAREGAKVIATDINESKLQELEE 48
Cdd:COG0604  140 GETVLVHGAAGGVGSAAvQLA-KALGARVIATASSPEKAELLRA 182
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 7-93 9.64e-03

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 36.84  E-value: 9.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511847639   7 KVIVVtaAAQGIGR-AAALAFAReGAKVIATDINESKLQELEECpGIqIRTLDVTKKKQIDQFASEIER-LDVLFNVAGF 84
Cdd:cd08254  168 TVLVI--GLGGLGLnAVQIAKAM-GAAVIAVDIKEEKLELAKEL-GA-DEVLNSLDDSPKDKKAAGLGGgFDVIFDFVGT 242


                 ....*....
gi 511847639  85 vhHGTILDC 93
Cdd:cd08254  243 --QPTFEDA 249
 
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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