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Conserved domains on  [gi|489055331|ref|WP_002965489|]
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MULTISPECIES: SDR family oxidoreductase [Brucella]

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 ...
 6-244 1.93e-128

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: 362.94  E-value: 1.93e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGF 85
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCAGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAAVIGLTKAVAAD 165
Cdd:cd05368   81 VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTKAAVIGLTKSVAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 166 YVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAYNIDGGWS 243
Cdd:cd05368  161 FAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASdeSAYVTGTAVVIDGGWS 240


                 .
gi 489055331 244 I 244
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 ...
 6-244 1.93e-128

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: 362.94  E-value: 1.93e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGF 85
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCAGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAAVIGLTKAVAAD 165
Cdd:cd05368   81 VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTKAAVIGLTKSVAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 166 YVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAYNIDGGWS 243
Cdd:cd05368  161 FAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASdeSAYVTGTAVVIDGGWS 240


                 .
gi 489055331 244 I 244
Cdd:cd05368  241 L 241
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-244 1.83e-78

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: 236.61  E-value: 1.83e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EGiAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAaaelraAG-GRALAVAADVTDEAAVEALVAAAvaaf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKA 153
Cdd:COG1028   82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIA-GLRGSPGQAAYAASKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYT 231
Cdd:COG1028  161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTP----MTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASdaASYI 236

                        250
                 ....*....|...
gi 489055331 232 TGQAYNIDGGWSI 244
Cdd:COG1028  237 TGQVLAVDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 14-243 1.26e-63

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: 198.42  E-value: 1.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   14 AAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIA---GIVTRRLDVLDDAAVKALVAEI----GQIDILFNCAGFV 86
Cdd:pfam13561   3 ANESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAeelGAAVLPCDVTDEEQVEALVAAAvekfGRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   87 HN--GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASsVKGVSNRFVYGLTKAAVIGLTKAVAA 164
Cdd:pfam13561  83 PKlkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGA-ERVVPNYNAYGAAKAALEALTRYLAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  165 DYVGKGIRCNAICPGTVESPSlqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATYTTGQAYNIDGGW 242
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLA----ASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLAsdLASYITGQVLYVDGGY 235


                  .
gi 489055331  243 S 243
Cdd:pfam13561 236 T 236
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3-243 2.21e-57

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 182.67  E-value: 2.21e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALaaelrAAGGEARVLVFDVSDEAAVRALIEAAveaf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVK--GVSNrfvYGLT 151
Cdd:PRK05653  81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGnpGQTN---YSAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrlRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GAT 229
Cdd:PRK05653 158 KAGVIGFTKALALELASRGITVNAVAPGFIDTD------MTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLAsdAAS 231

                        250
                 ....*....|....
gi 489055331 230 YTTGQAYNIDGGWS 243
Cdd:PRK05653 232 YITGQVIPVNGGMY 245
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 8-241 1.36e-34

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 124.10  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331    8 KTALVTAAGQGIGQASALAFAEAGAKVYATDIN---ADALAKLEGIAG--IVTRRLDVLDDAAVKALV----AEIGQIDI 78
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNeetAKETAKEINQAGgkAVAYKLDVSDKDQVFSAIdqaaEKFGGFDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD-GAIINMASVASsVKGVSNRFVYGLTKAAVIG 157
Cdd:TIGR02415  81 MVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAG-HEGNPILSAYSSTKFAVRG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  158 LTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQ----GDYEAARA--AFIARQPIGRIGQPEEIADLAVYLAG--AT 229
Cdd:TIGR02415 160 LTQTAAQELAPKGITVNAYCPGIVKTP-MWEEIDEEtseiAGKPIGEGfeEFSSEIALGRPSEPEDVAGLVSFLASedSD 238

                         250
                  ....*....|..
gi 489055331  230 YTTGQAYNIDGG 241
Cdd:TIGR02415 239 YITGQSILVDGG 250
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
 10-244 1.03e-20

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 87.28  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKV---Y-ATDINADALAKLEGIAGI--VTRRLDVLDDAAVKALVAE----IGQIDIL 79
Cdd:NF012208   1 ALVTGSARGIGRAIALALAREGFDVavhYrRSAEAAEQTAQEAEALGVkaITLQADLTDPEQARSLVEEaaeaLGGLSVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMA-SVASSVKGVSNRFVYGLTKAAVIGL 158
Cdd:NF012208  81 VNNVGNYLHKPLLETTDEEWHEMLDSNLNATFYVTQAALPLMRAAGWGRIVNLGyAGAQNLLARPGITPYVIAKTGVIIY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESpSLQDRLRaqgdyeaaraafiaRQPIGRIGQPEEIADLAVYL--AGATYTTGQAY 236
Cdd:NF012208 161 SKALAKELAGDGITVNVVSPGVAEN-SVSQPLP--------------EIPAGRPATLEELADAVLFFvrPSSDYITGQVL 225


                 ....*...
gi 489055331 237 NIDGGWSI 244
Cdd:NF012208 226 EVAGGWNL 233
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-100 1.24e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.62  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331     8 KTALVTAAGQGIGQASALAFAEAGAK--------VYATDINADALAKLEGIAGIVT-RRLDVLDDAAVKALVAEI----G 74
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARrlvllsrsGPDAPGAAALLAELEAAGARVTvVACDVADRDALAAVLAAIpaveG 80

                           90       100
                   ....*....|....*....|....*.
gi 489055331    75 QIDILFNCAGFVHNGTILEMKDEELD 100
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFA 106
 
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 ...
 6-244 1.93e-128

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: 362.94  E-value: 1.93e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGF 85
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCAGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAAVIGLTKAVAAD 165
Cdd:cd05368   81 VHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTKAAVIGLTKSVAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 166 YVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAYNIDGGWS 243
Cdd:cd05368  161 FAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASdeSAYVTGTAVVIDGGWS 240


                 .
gi 489055331 244 I 244
Cdd:cd05368  241 L 241
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-244 1.83e-78

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: 236.61  E-value: 1.83e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EGiAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAaaelraAG-GRALAVAADVTDEAAVEALVAAAvaaf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKA 153
Cdd:COG1028   82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIA-GLRGSPGQAAYAASKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYT 231
Cdd:COG1028  161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTP----MTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASdaASYI 236

                        250
                 ....*....|...
gi 489055331 232 TGQAYNIDGGWSI 244
Cdd:COG1028  237 TGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 10-239 9.01e-67

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: 206.37  E-value: 9.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIA----GIVTRRLDVLDDAAVKALVAEI----GQIDILFN 81
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEalggNAVAVQADVSDEEDVEALVEEAleefGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  82 CAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIGLTKA 161
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVA-GLRPLPGQAAYAASKAALEGLTRS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 162 VAADYVGKGIRCNAICPGTVESPSLQDRLRaqgdyEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAYNID 239
Cdd:cd05233  160 LALELAPYGIRVNAVAPGLVDTPMLAKLGP-----EEAEKELAAAIPLGRLGTPEEVAEAVVFLASdeASYITGQVIPVD 234
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 14-243 1.26e-63

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: 198.42  E-value: 1.26e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   14 AAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIA---GIVTRRLDVLDDAAVKALVAEI----GQIDILFNCAGFV 86
Cdd:pfam13561   3 ANESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAeelGAAVLPCDVTDEEQVEALVAAAvekfGRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   87 HN--GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASsVKGVSNRFVYGLTKAAVIGLTKAVAA 164
Cdd:pfam13561  83 PKlkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGA-ERVVPNYNAYGAAKAALEALTRYLAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  165 DYVGKGIRCNAICPGTVESPSlqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATYTTGQAYNIDGGW 242
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLA----ASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLAsdLASYITGQVLYVDGGY 235


                  .
gi 489055331  243 S 243
Cdd:pfam13561 236 T 236
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 6-228 3.90e-58

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: 184.23  E-value: 3.90e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAEI----GQIDIL 79
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGgrALAVPLDVTDEAAVEAAVAAAvaefGRLDVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIGLT 159
Cdd:COG4221   84 VNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIA-GLRPYPGGAVYAATKAAVRGLS 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055331 160 KAVAADYVGKGIRCNAICPGTVESPSLQDRLRaqGDYEAARAAFIARQPIgrigQPEEIADLAVYLAGA 228
Cdd:COG4221  163 ESLRAELRPTGIRVTVIEPGAVDTEFLDSVFD--GDAEAAAAVYEGLEPL----TPEDVAEAVLFALTQ 225
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3-243 2.21e-57

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 182.67  E-value: 2.21e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALaaelrAAGGEARVLVFDVSDEAAVRALIEAAveaf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVK--GVSNrfvYGLT 151
Cdd:PRK05653  81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGnpGQTN---YSAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrlRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GAT 229
Cdd:PRK05653 158 KAGVIGFTKALALELASRGITVNAVAPGFIDTD------MTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLAsdAAS 231

                        250
                 ....*....|....
gi 489055331 230 YTTGQAYNIDGGWS 243
Cdd:PRK05653 232 YITGQVIPVNGGMY 245
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 3-244 2.65e-56

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 180.00  E-value: 2.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK--LEGIA----GIVTRRLDVLDDAAVKALVAEI--- 73
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEalVAEIGalggKALAVQGDVSDAESVERAVDEAkae 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 -GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTK 152
Cdd:PRK05557  81 fGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVV-GLMGNPGQANYAASK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRaqgdyEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATY 230
Cdd:PRK05557 160 AGVIGFTKSLARELASRGITVNAVAPGFIETD-MTDALP-----EDVKEAILAQIPLGRLGQPEEIASAVAFLASdeAAY 233

                        250
                 ....*....|....
gi 489055331 231 TTGQAYNIDGGWSI 244
Cdd:PRK05557 234 ITGQTLHVNGGMVM 247
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-244 4.19e-56

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 179.27  E-value: 4.19e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVY-ATDINADALAKLE------GIAGIVTRrLDVLDDAAVKALVAEI--- 73
Cdd:PRK05565   2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVViAYDINEEAAQELLeeikeeGGDAIAVK-ADVSSEEDVENLVEQIvek 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 -GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTK 152
Cdd:PRK05565  81 fGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLI-GASCEVLYSASK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQdrlraqgDYEAARAAFIARQ-PIGRIGQPEEIADLAVYLA--GAT 229
Cdd:PRK05565 160 GAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS-------SFSEEDKEGLAEEiPLGRLGKPEEIAKVVLFLAsdDAS 232

                        250
                 ....*....|....*
gi 489055331 230 YTTGQAYNIDGGWSI 244
Cdd:PRK05565 233 YITGQIITVDGGWTC 247
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-244 1.24e-55

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 177.85  E-value: 1.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKlegiAGIVTRRLDVLDDaaVKALVAEIGQIDILFNCAGFV 86
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLS----GNFHFLQLDLSDD--LEPLFDWVPSVDILCNTAGIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  87 HN-GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGvSNRFVYGLTKAAVIGLTKAVAAD 165
Cdd:PRK06550  79 DDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAG-GGGAAYTASKHALAGFTKQLALD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 166 YVGKGIRCNAICPGTVESPslqdrlRAQGDYEAAR-AAFIARQ-PIGRIGQPEEIADLAVYLA--GATYTTGQAYNIDGG 241
Cdd:PRK06550 158 YAKDGIQVFGIAPGAVKTP------MTAADFEPGGlADWVAREtPIKRWAEPEEVAELTLFLAsgKADYMQGTIVPIDGG 231


                 ...
gi 489055331 242 WSI 244
Cdd:PRK06550 232 WTL 234
FabG-like PRK07231
SDR family oxidoreductase;
4-244 2.14e-55

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 177.71  E-value: 2.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE----------GIAGIVTRRLDVldDAAVKALVAEI 73
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAaeilaggraiAVAADVSDEADV--EAAVAAALERF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVH-NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTK 152
Cdd:PRK07231  80 GSVDILVNNAGTTHrNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTA-GLRPRPGLGWYNASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLraQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATY 230
Cdd:PRK07231 159 GAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFM--GEPTPENRAKFLATIPLGRLGTPEDIANAALFLAsdEASW 236

                        250
                 ....*....|....
gi 489055331 231 TTGQAYNIDGGWSI 244
Cdd:PRK07231 237 ITGVTLVVDGGRCV 250
PRK07063 PRK07063
SDR family oxidoreductase;
1-244 7.05e-55

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 176.78  E-value: 7.05e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN-------ADALAKLEGIAGIVTRRLDVLDDAAVKALVA-- 71
Cdd:PRK07063   1 MMNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDaalaeraAAAIARDVAGARVLAVPADVTDAASVAAAVAaa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 --EIGQIDILFNCAGFVHNGTILEMKDEELD--FAVNLnvRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFV 147
Cdd:PRK07063  81 eeAFGPLDVLVNNAGINVFADPLAMTDEDWRrcFAVDL--DGAWNGCRAVLPGMVERGRGSIVNIASTHAF-KIIPGCFP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 148 YGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG 227
Cdd:PRK07063 158 YPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLAS 237

                        250
                 ....*....|....*....
gi 489055331 228 --ATYTTGQAYNIDGGWSI 244
Cdd:PRK07063 238 deAPFINATCITIDGGRSV 256
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-244 1.00e-54

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: 176.31  E-value: 1.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE-----------GIAGIVTRRLDVldDAAVKALVAEIGQ 75
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAAselraggagvlAVVADLTDPEDI--DRLVEKAGDAFGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVsNRFVYGLTKAAV 155
Cdd:cd05344   79 VDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEP-NLVLSNVARAGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGD-----YEAARAAFIARQPIGRIGQPEEIADLAVYLA--GA 228
Cdd:cd05344  158 IGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEkegisVEEAEKEVASQIPLGRVGKPEELAALIAFLAseKA 237

                        250
                 ....*....|....*.
gi 489055331 229 TYTTGQAYNIDGGWSI 244
Cdd:cd05344  238 SYITGQAILVDGGLTR 253
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 8-241 1.56e-54

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: 175.04  E-value: 1.56e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIA-----GIVTRRLDVLDDAAVKALVAEI----GQIDI 78
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIkalggNAAALEADVSDREAVEALVEKVeaefGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVaSSVKGVSNRFVYGLTKAAVIGL 158
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSV-VGLIGNPGQANYAASKAGVIGF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESPsLQDRLRaqgdyEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAY 236
Cdd:cd05333  160 TKSLAKELASRGITVNAVAPGFIDTD-MTDALP-----EKVKEKILKQIPLGRLGTPEEVANAVAFLASddASYITGQVL 233


                 ....*
gi 489055331 237 NIDGG 241
Cdd:cd05333  234 HVNGG 238
PRK06138 PRK06138
SDR family oxidoreductase;
4-244 5.23e-53

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 171.87  E-value: 5.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGIAGIVTRRLDVLDDAAVKALV----AEIGQ 75
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAervaAAIAAGGRAFARQGDVGSAEAVEALVdfvaARWGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASvASSVKGVSNRFVYGLTKAAV 155
Cdd:PRK06138  82 LDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTAS-QLALAGGRGRAAYVASKGAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTG 233
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALREALRARHPMNRFGTAEEVAQAALFLASdeSSFATG 240

                        250
                 ....*....|.
gi 489055331 234 QAYNIDGGWSI 244
Cdd:PRK06138 241 TTLVVDGGWLA 251
PRK12826 PRK12826
SDR family oxidoreductase;
4-241 9.72e-53

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 170.87  E-value: 9.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKALVAEI----G 74
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATaelveAAGGKARARQVDVRDRAALKAAVAAGvedfG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAA 154
Cdd:PRK12826  83 RLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPGLAHYAASKAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQgdyeaARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTT 232
Cdd:PRK12826 163 LVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQ-----WAEAIAAAIPLGRLGEPEDIAAAVLFLASdeARYIT 237


                 ....*....
gi 489055331 233 GQAYNIDGG 241
Cdd:PRK12826 238 GQTLPVDGG 246
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
4-241 1.84e-50

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 165.74  E-value: 1.84e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG----IVTRRLDVLDDAAVKALVAEI----GQ 75
Cdd:PRK08226   3 KLTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGrghrCTAVVADVRDPASVAAAIKRAkekeGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAAV 155
Cdd:PRK08226  83 IDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVADPGETAYALTKAAI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEAARAAF--IARQ-PIGRIGQPEEIADLAVYLAG--ATY 230
Cdd:PRK08226 163 VGLTKSLAVEYAQSGIRVNAICPGYVRTP-MAESIARQSNPEDPESVLteMAKAiPLRRLADPLEVGELAAFLASdeSSY 241

                        250
                 ....*....|.
gi 489055331 231 TTGQAYNIDGG 241
Cdd:PRK08226 242 LTGTQNVIDGG 252
PRK06172 PRK06172
SDR family oxidoreductase;
1-241 2.49e-50

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 164.92  E-value: 2.49e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD------ALAKLEGIAGIVTrRLDVLDDAAVKALVAEI- 73
Cdd:PRK06172   1 MSMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAggeetvALIREAGGEALFV-ACDVTRDAEVKALVEQTi 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 ---GQIDILFNCAGF-VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYG 149
Cdd:PRK06172  80 aayGRLDYAFNNAGIeIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLG-AAPKMSIYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqDRLRAQGDYEAARAAFI-ARQPIGRIGQPEEIADLAVYLA-- 226
Cdd:PRK06172 159 ASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDT----DMFRRAYEADPRKAEFAaAMHPVGRIGKVEEVASAVLYLCsd 234

                        250
                 ....*....|....*
gi 489055331 227 GATYTTGQAYNIDGG 241
Cdd:PRK06172 235 GASFTTGHALMVDGG 249
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-207 6.20e-50

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 163.89  E-value: 6.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKALVAEI----G 74
Cdd:COG0300    2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALaaelrAAGARVEVVALDVTDPDAVAALAEAVlarfG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAA 154
Cdd:COG0300   82 PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLR-GLPGMAAYAASKAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEAARAAFIARQ 207
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGPVDTP-FTARAGAPAGRPLLSPEEVARA 212
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 4-242 3.54e-49

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 161.98  E-value: 3.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE-----------GIAGIVTRRLDVldDAAVKALVAE 72
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAealqkaggkaiGVAMDVTDEEAI--NAGIDYAVET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTK 152
Cdd:PRK12429  79 FGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLV-GSAGKAAYVSAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESP----SLQDRLRAQG-DYEAARAAFIAR-QPIGRIGQPEEIADLAVYLA 226
Cdd:PRK12429 158 HGLIGLTKVVALEGATHGVTVNAICPGYVDTPlvrkQIPDLAKERGiSEEEVLEDVLLPlVPQKRFTTVEEIADYALFLA 237

                        250
                 ....*....|....*...
gi 489055331 227 G--ATYTTGQAYNIDGGW 242
Cdd:PRK12429 238 SfaAKGVTGQAWVVDGGW 255
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-242 4.29e-49

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 161.57  E-value: 4.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDI-NADALAKLEGIAG--IVTRRLDVLDDAAVKALVAE----I 73
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVvvhYRSDEeAAEELVEAVEALGrrAQAVQADVTDKAALEAAVAAaverF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVaSSVKGVSNRFVYGLTKA 153
Cdd:PRK12825  83 GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSV-AGLPGWPGRSNYAAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrlRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYT 231
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTD------MKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSdaSDYI 235

                        250
                 ....*....|.
gi 489055331 232 TGQAYNIDGGW 242
Cdd:PRK12825 236 TGQVIEVTGGV 246
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 4-244 1.74e-48

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: 159.86  E-value: 1.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADA---LAKLEGIAGI-----VTRRLDVldDAAVKALVAEIGQ 75
Cdd:cd05345    2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGaerVAADIGEAAIaiqadVTKRADV--EAMVEAALSKFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVH-NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAssvkGVSNR---FVYGLT 151
Cdd:cd05345   80 LDILVNNAGITHrNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTA----GLRPRpglTWYNAS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAqgDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--AT 229
Cdd:cd05345  156 KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGE--DTPENRAKFRATIPLGRLSTPDDIANAALYLASdeAS 233

                        250
                 ....*....|....*
gi 489055331 230 YTTGQAYNIDGGWSI 244
Cdd:cd05345  234 FITGVALEVDGGRCI 248
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 5-241 4.11e-48

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 159.45  E-value: 4.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGIAGIVTRrLDVLDDAAVKALVA----EIGQI 76
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALaataARLPGAKVTATV-ADVADPAQVERVFDtaveRFGGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAG-FVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK-DGAIINMASVASsVKGVSNRFVYGLTKAA 154
Cdd:PRK12829  88 DVLVNNAGiAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALSSVAG-RLGYPGRTPYAASKWA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPS----LQDRLRAQGD-YEAARAAFIARQPIGRIGQPEEIADLAVYLA--G 227
Cdd:PRK12829 167 VVGLVKSLAIELGPLGIRVNAILPGIVRGPRmrrvIEARAQQLGIgLDEMEQEYLEKISLGRMVEPEDIAATALFLAspA 246

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:PRK12829 247 ARYITGQAISVDGN 260
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-242 1.05e-47

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: 157.90  E-value: 1.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALA------KLEGIaGIVTRRLDVLDDAAVKALVAEI----G 74
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEeaqqliEKEGV-EATAFTCDVSDEEAIKAAVEAIeedfG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTKAA 154
Cdd:cd05347   82 KIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVP-AYAASKGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPSLQdRLRAqgdyEAARAAFI-ARQPIGRIGQPEEIADLAVYLA--GATYT 231
Cdd:cd05347  161 VAGLTKALATEWARHGIQVNAIAPGYFATEMTE-AVVA----DPEFNDDIlKRIPAGRWGQPEDLVGAAVFLAsdASDYV 235

                        250
                 ....*....|.
gi 489055331 232 TGQAYNIDGGW 242
Cdd:cd05347  236 NGQIIFVDGGW 246
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 8-194 2.59e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 155.08  E-value: 2.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331    8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAG-IVTRRLDVLDDAAVKALVAEI----GQIDI 78
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAvakeLGALGGkALFIQGDVTDRAQVKALVEQAverlGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIGL 158
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVA-GLVPYPGGSAYSASKAAVIGF 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 489055331  159 TKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQG 194
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 7-242 2.81e-46

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: 154.53  E-value: 2.81e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDIN--ADALAKLEGIAGIVTRRL-----DVLDDAAVKALVA----EIGQ 75
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGdaAEIEAVRAGLAAKHGVKVlyhgaDLSKPAAIEDMVAyaqrQFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAV 155
Cdd:cd08940   82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLV-ASANKSAYVAAKHGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQ------GDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG-- 227
Cdd:cd08940  161 VGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALaqkngvPQEQAARELLLEKQPSKQFVTPEQLGDTAVFLASda 240

                        250
                 ....*....|....*
gi 489055331 228 ATYTTGQAYNIDGGW 242
Cdd:cd08940  241 ASQITGTAVSVDGGW 255
PRK08589 PRK08589
SDR family oxidoreductase;
4-241 3.15e-46

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 154.94  E-value: 3.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN------ADALAKLEGIAGIVtrRLDVLDDAAVKALVAEI---- 73
Cdd:PRK08589   3 RLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAeavsetVDKIKSNGGKAKAY--HVDISDEQQVKDFASEIkeqf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHN-GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLErKDGAIINMASVASSVKGVsNRFVYGLTK 152
Cdd:PRK08589  81 GRVDVLFNNAGVDNAaGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAADL-YRSGYNAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEAARAAFIARQ---PIGRIGQPEEIADLAVYLAG-- 227
Cdd:PRK08589 159 GAVINFTKSIAIEYGRDGIRANAIAPGTIETP-LVDKLTGTSEDEAGKTFRENQKwmtPLGRLGKPEEVAKLVVFLASdd 237

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:PRK08589 238 SSFITGETIRIDGG 251
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-241 1.60e-44

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 150.03  E-value: 1.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEgiagIVTRRLDVLDDAAVKALV----AEIGQI 76
Cdd:PRK08220   2 NAMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP----FATFVLDVSDAAAVAQVCqrllAETGPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVsNRFVYGLTKAAVI 156
Cdd:PRK08220  78 DVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRI-GMAAYGASKAALT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 157 GLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEAARAAFIARQ-----PIGRIGQPEEIADLAVYLA--GAT 229
Cdd:PRK08220 157 SLAKCVGLELAPYGVRCNVVSPGSTDTD-MQRTLWVDEDGEQQVIAGFPEQfklgiPLGKIARPQEIANAVLFLAsdLAS 235

                        250
                 ....*....|..
gi 489055331 230 YTTGQAYNIDGG 241
Cdd:PRK08220 236 HITLQDIVVDGG 247
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
2-241 4.50e-44

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 149.02  E-value: 4.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADA--LAKLEGIAGIVTRRLDVLD----DAAVKALVAEIGQ 75
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARarLAALEIGPAAIAVSLDVTRqdsiDRIVAAAVERFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLER-KDGAIINMASVASSvKGVSNRFVYGLTKAA 154
Cdd:PRK07067  81 IDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGR-RGEALVSHYCATKAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPSLQ--DRL------RAQGDYEAARAAFIarqPIGRIGQPEEIADLAVYLA 226
Cdd:PRK07067 160 VISYTQSAALALIRHGINVNAIAPGVVDTPMWDqvDALfaryenRPPGEKKRLVGEAV---PLGRMGVPDDLTGMALFLA 236

                        250
                 ....*....|....*..
gi 489055331 227 G--ATYTTGQAYNIDGG 241
Cdd:PRK07067 237 SadADYIVAQTYNVDGG 253
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-242 1.19e-43

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: 147.53  E-value: 1.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTR--RLDVLDDA----AVKALVAEIGQI 76
Cdd:cd05341    1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARffHLDVTDEDgwtaVVDTAREAFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAVI 156
Cdd:cd05341   81 DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLV-GDPALAAYNASKGAVR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 157 GLTKAVAADY--VGKGIRCNAICPGTVESPSLQDRLRAQGDyeaarAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTT 232
Cdd:cd05341  160 GLTKSAALECatQGYGIRVNSVHPGYIYTPMTDELLIAQGE-----MGNYPNTPMGRAGEPDEIAYAVVYLASdeSSFVT 234

                        250
                 ....*....|
gi 489055331 233 GQAYNIDGGW 242
Cdd:cd05341  235 GSELVVDGGY 244
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-244 3.66e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 146.34  E-value: 3.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN---ADALAKLEGiAGIVTRRLDVLDDAAVKALVAEI----GQI 76
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSedvAEVAAQLLG-GNAKGLVCDVSDSQSVEAAVAAVisafGRI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAVI 156
Cdd:PRK06841  91 DILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVV-ALERHVAYCASKAGVV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 157 GLTKAVAADYVGKGIRCNAICPGTVESpSLQDRLRAQGDYEAARAAFiarqPIGRIGQPEEIADLAVYLA--GATYTTGQ 234
Cdd:PRK06841 170 GMTKVLALEWGPYGITVNAISPTVVLT-ELGKKAWAGEKGERAKKLI----PAGRFAYPEEIAAAALFLAsdAAAMITGE 244

                        250
                 ....*....|
gi 489055331 235 AYNIDGGWSI 244
Cdd:PRK06841 245 NLVIDGGYTI 254
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-244 1.34e-42

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 145.36  E-value: 1.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDdaAVKALVAEIGQIDILFNCAG 84
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDYFKVDVSNKEQVIK--GIDYVISKYGRIDILVNNAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  85 FVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAVIGLTKAVAA 164
Cdd:PRK06398  82 IESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFA-VTRNAAAYVTSKHAVLGLTRSIAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 165 DYVGKgIRCNAICPGTVESPSLQ--DRLRAQGDYEAaraafIARQ--------PIGRIGQPEEIADLAVYLAG--ATYTT 232
Cdd:PRK06398 161 DYAPT-IRCVAVCPGSIRTPLLEwaAELEVGKDPEH-----VERKirewgemhPMKRVGKPEEVAYVVAFLASdlASFIT 234

                        250
                 ....*....|..
gi 489055331 233 GQAYNIDGGWSI 244
Cdd:PRK06398 235 GECVTVDGGLRA 246
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 2-244 4.37e-41

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 141.30  E-value: 4.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD---ALAKLEGiAGIVTRRLDVLDDAAVKALVAEI----G 74
Cdd:PRK08265   1 MIGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADngaAVAASLG-ERARFIATDITDDAAIERAVATVvarfG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCA-GFVHNGtiLEMKDEELDFAVNLNVRSMIRTIRAVLPGMlERKDGAIINMASVASSVkGVSNRFVYGLTKA 153
Cdd:PRK08265  80 RVDILVNLAcTYLDDG--LASSRADWLAALDVNLVSAAMLAQAAHPHL-ARGGGAIVNFTSISAKF-AQTGRWLYPASKA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLqDRLrAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATYT 231
Cdd:PRK08265 156 AIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVM-DEL-SGGDRAKADRVAAPFHLLGRVGDPEEVAQVVAFLCsdAASFV 233

                        250
                 ....*....|...
gi 489055331 232 TGQAYNIDGGWSI 244
Cdd:PRK08265 234 TGADYAVDGGYSA 246
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-242 1.05e-40

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 140.26  E-value: 1.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYAT--DINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAEI----GQ 75
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITthGTNWDETRRLIEKEGrkVTFVQVDLTKPESAEKVVKEAleefGK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVsnrFV--YGLTKA 153
Cdd:PRK06935  92 IDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGK---FVpaYTASKH 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQdRLRAQgdyEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATYT 231
Cdd:PRK06935 169 GVAGLTKAFANELAAYNIQVNAIAPGYIKTANTA-PIRAD---KNRNDEILKRIPAGRWGEPDDLMGAAVFLAsrASDYV 244

                        250
                 ....*....|.
gi 489055331 232 TGQAYNIDGGW 242
Cdd:PRK06935 245 NGHILAVDGGW 255
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 10-241 1.74e-40

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: 139.14  E-value: 1.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVtrRLDVLDDAAVKALV----AEIGQIDILFNCAGF 85
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRLT--PLDVADAAAVREVCsrllAEHGPIDALVNCAGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTKAAVIGLTKAVAAD 165
Cdd:cd05331   79 LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMA-AYGASKAALASLSKCLGLE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 166 YVGKGIRCNAICPGTVESPSLQDRLraQGDYEAAR------AAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAYN 237
Cdd:cd05331  158 LAPYGVRCNVVSPGSTDTAMQRTLW--HDEDGAAQviagvpEQFRLGIPLGKIAQPADIANAVLFLASdqAGHITMHDLV 235


                 ....
gi 489055331 238 IDGG 241
Cdd:cd05331  236 VDGG 239
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
8-241 1.74e-40

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 139.13  E-value: 1.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK-LEGIAG-----IVTRRLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKdWFEEYGftedqVRLKELDVTDTEECAEALAEIeeeeGPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIG 157
Cdd:PRK12824  83 ILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVN-GLKGQFGQTNYSAAKAGMIG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVESPSLQdrlrAQGDYEAARaafIARQ-PIGRIGQPEEIADLAVYLA--GATYTTGQ 234
Cdd:PRK12824 162 FTKALASEGARYGITVNCIAPGYIATPMVE----QMGPEVLQS---IVNQiPMKRLGTPEEIAAAVAFLVseAAGFITGE 234


                 ....*..
gi 489055331 235 AYNIDGG 241
Cdd:PRK12824 235 TISINGG 241
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 5-241 3.29e-40

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: 138.78  E-value: 3.29e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD-ALAKLEGIA-GIVTRRLDVLDDAAVKAL----VAEIGQIDI 78
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGaAQAVVAQIAgGALALRVDVTDEQQVAALferaVEEFGGLDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVH-NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAVIG 157
Cdd:cd08944   81 LVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQS-GDPGYGAYGASKAAIRN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVESPSLQDrlrAQGDYEAARAAFIARQPI----GRIGQPEEIADLAVYLAG--ATYT 231
Cdd:cd08944  160 LTRTLAAELRHAGIRCNALAPGLIDTPLLLA---KLAGFEGALGPGGFHLLIhqlqGRLGRPEDVAAAVVFLLSddASFI 236

                        250
                 ....*....|
gi 489055331 232 TGQAYNIDGG 241
Cdd:cd08944  237 TGQVLCVDGG 246
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-244 3.58e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 138.31  E-value: 3.58e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILF 80
Cdd:PRK07060   3 MAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRLDVGDDAAIRAALAAAGAFDGLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLE-RKDGAIINMASVASSVkGVSNRFVYGLTKAAVIGLT 159
Cdd:PRK07060  83 NCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAaGRGGSIVNVSSQAALV-GLPDHLAYCASKAALDAIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 160 KAVAADYVGKGIRCNAICPGTVESPSLQDRLraqgDYEAARAAFIARQPIGRIGQPEEIADLAVYL--AGATYTTGQAYN 237
Cdd:PRK07060 162 RVLCVELGPHGIRVNSVNPTVTLTPMAAEAW----SDPQKSGPMLAAIPLGRFAEVDDVAAPILFLlsDAASMVSGVSLP 237


                 ....*..
gi 489055331 238 IDGGWSI 244
Cdd:PRK07060 238 VDGGYTA 244
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 5-244 4.31e-40

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: 138.70  E-value: 4.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL--------------AKLEGIAGIVTRRLDVldDAAVKALV 70
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLeetrqsclqagvseKKILLVVADLTEEEGQ--DRIISTTL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  71 AEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKdGAIINMASVAS--SVKGVsnrFVY 148
Cdd:cd05364   79 AKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGgrSFPGV---LYY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 149 GLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSlqdrLRAQGDYEAARAAFIAR----QPIGRIGQPEEIADLAVY 224
Cdd:cd05364  155 CISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGF----HRRMGMPEEQYIKFLSRaketHPLGRPGTVDEVAEAIAF 230

                        250       260
                 ....*....|....*....|..
gi 489055331 225 LA--GATYTTGQAYNIDGGWSI 244
Cdd:cd05364  231 LAsdASSFITGQLLPVDGGRHL 252
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-241 4.35e-40

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 138.66  E-value: 4.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK-----LEGIAG-IVTRRLDVLDDAAVKALV----AEIGQI 76
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKstiqeISEAGYnAVAVGADVTDKDDVEALIdqavEKFGSF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK-DGAIINMASVASsVKGVSNRFVYGLTKAAV 155
Cdd:cd05366   82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAG-VQGFPNLGAYSASKFAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQG-----DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--A 228
Cdd:cd05366  161 RGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGeiagkPEGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASedS 240

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:cd05366  241 DYITGQTILVDGG 253
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-242 9.05e-40

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 137.41  E-value: 9.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGIAG-IVTRRLDVLDDAAVKALVAEI-- 73
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEArelaAALEAAGGrAHAIAADLADPASVQRFFDAAaa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 --GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASvASSVKGVSNRFVYGLT 151
Cdd:PRK12939  81 alGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLAS-DTALWGAPKLGAYVAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--AT 229
Cdd:PRK12939 160 KGAVIGMTRSLARELGGRGITVNAIAPGLTAT-----EATAYVPADERHAYYLKGRALERLQVPDDVAGAVLFLLSdaAR 234

                        250
                 ....*....|...
gi 489055331 230 YTTGQAYNIDGGW 242
Cdd:PRK12939 235 FVTGQLLPVNGGF 247
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-242 1.60e-39

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: 137.08  E-value: 1.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINA----DALAKLEGIAGIVTR--RLDVLDDAAVKALVAEI-- 73
Cdd:cd05352    3 LFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSApraeEKAEELAKKYGVKTKayKCDVSSQESVEKTFKQIqk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 --GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVS-NRFVYGL 150
Cdd:cd05352   83 dfGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNRPqPQAAYNA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrLRAQGDYEaARAAFIARQPIGRIGQPEEIADLAVYLA--GA 228
Cdd:cd05352  163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTD-----LTDFVDKE-LRKKWESYIPLKRIALPEELVGAYLYLAsdAS 236

                        250
                 ....*....|....
gi 489055331 229 TYTTGQAYNIDGGW 242
Cdd:cd05352  237 SYTTGSDLIIDGGY 250
PRK06500 PRK06500
SDR family oxidoreductase;
4-243 2.03e-39

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 136.62  E-value: 2.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK06500   3 RLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGesALVIRADAGDVAAQKALAQALaeafGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGAIINmASVASSVkGVSNRFVYGLTKAAVIG 157
Cdd:PRK06500  83 AVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP-LLANPASIVLN-GSINAHI-GMPNSSVYAASKAALLS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEAARAAFIARQ-PIGRIGQPEEIADLAVYLAG--ATYTTGQ 234
Cdd:PRK06500 160 LAKTLSGELLPRGIRVNAVSPGPVQTP-LYGKLGLPEATLDAVAAQIQALvPLGRFGTPEEIAKAVLYLASdeSAFIVGS 238


                 ....*....
gi 489055331 235 AYNIDGGWS 243
Cdd:PRK06500 239 EIIVDGGMS 247
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 4-244 2.43e-39

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 136.61  E-value: 2.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGiAGIVTRRL--DVLDDAAVKALVAEI---- 73
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELeeaaAHLEA-LGIDALWIaaDVADEADIERLAEETlerf 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLP-GMLERKDGAIINMASVA---SSVKGVSNRFVYG 149
Cdd:PRK08213  88 GHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASVAglgGNPPEVMDTIAYN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrlRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--G 227
Cdd:PRK08213 168 TSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTK------MTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLAsdA 241

                        250
                 ....*....|....*..
gi 489055331 228 ATYTTGQAYNIDGGWSI 244
Cdd:PRK08213 242 SKHITGQILAVDGGVSA 258
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 8-243 1.60e-38

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: 134.57  E-value: 1.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGI---AGIVTRRLDVLDDAAVKALV----AEIGQI 76
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLeaakAALLEIapdAEVLLIKADVSDEAQVEAYVdatvEQFGRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKD-EELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASsVKGVSNRFVYGLTKAAV 155
Cdd:cd05330   84 DGFFNNAGIEGKQNLTEDFGaDEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGG-IRGVGNQSGYAAAKHGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQG--DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYT 231
Cdd:cd05330  163 VGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQLGpeNPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSddAGYV 242

                        250
                 ....*....|..
gi 489055331 232 TGQAYNIDGGWS 243
Cdd:cd05330  243 NAAVVPIDGGQS 254
PRK07774 PRK07774
SDR family oxidoreductase;
4-244 3.71e-38

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 133.33  E-value: 3.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKAL----VAEIG 74
Cdd:PRK07774   3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVakqivADGGTAIAVQVDVSDPDSAKAMadatVSAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNcagfvhNGTIL-EMKdeeLDFAVNL-----------NVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGV 142
Cdd:PRK07774  83 GIDYLVN------NAAIYgGMK---LDLLITVpwdyykkfmsvNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYSN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 143 snrfVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSlqDRLRAQGDYeaaRAAFIARQPIGRIGQPEEIADLA 222
Cdd:PRK07774 154 ----FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEA--TRTVTPKEF---VADMVKGIPLSRMGTPEDLVGMC 224

                        250       260
                 ....*....|....*....|....
gi 489055331 223 VYLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK07774 225 LFLLSdeASWITGQIFNVDGGQII 248
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 4-241 4.00e-38

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: 133.96  E-value: 4.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDINADA-----LAKLEGIAGIVTRRlDVLDDA----AVKALVA 71
Cdd:cd05355   23 KLKGKKALITGGDSGIGRAVAIAFAREGADVainYLPEEEDDAeetkkLIEEEGRKCLLIPG-DLGDESfcrdLVKEVVK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNG-TILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVaSSVKGVSNRFVYGL 150
Cdd:cd05355  102 EFGKLDILVNNAAYQHPQeSIEDITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSV-TAYKGSPHLLDYAA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDrlrAQGDYEAArAAFIARQPIGRIGQPEEIADLAVYLAG--A 228
Cdd:cd05355  179 TKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTP-LIP---SSFPEEKV-SEFGSQVPMGRAGQPAEVAPAYVFLASqdS 253

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:cd05355  254 SYVTGQVLHVNGG 266
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 1-243 4.83e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 133.32  E-value: 4.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEI----GQI 76
Cdd:PRK06057   1 LSQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLFVPTDVTDEDAVNALFDTAaetyGSV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFV--HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAA 154
Cdd:PRK06057  81 DIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQISYTASKGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDrLRAQGDYEAARAafIARQPIGRIGQPEEIADLAVYLAG--ATYTT 232
Cdd:PRK06057 161 VLAMSRELGVQFARQGIRVNALCPGPVNTPLLQE-LFAKDPERAARR--LVHVPMGRFAEPEEIAAAVAFLASddASFIT 237

                        250
                 ....*....|.
gi 489055331 233 GQAYNIDGGWS 243
Cdd:PRK06057 238 ASTFLVDGGIS 248
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 4-244 6.32e-38

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 134.01  E-value: 6.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK-------LEGIAGIVTRRlDVLDDA----AVKALVAE 72
Cdd:PRK06701  43 KLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANetkqrveKEGVKCLLIPG-DVSDEAfckdAVEETVRE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGF-VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVaSSVKGVSNRFVYGLT 151
Cdd:PRK06701 122 LGRLDILVNNAAFqYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTGSI-TGYEGNETLIDYSAT 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYeaarAAFIARQPIGRIGQPEEIADLAVYLAG--AT 229
Cdd:PRK06701 199 KGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP-LIPSDFDEEKV----SQFGSNTPMQRPGQPEELAPAYVFLASpdSS 273

                        250
                 ....*....|....*
gi 489055331 230 YTTGQAYNIDGGWSI 244
Cdd:PRK06701 274 YITGQMLHVNGGVIV 288
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 4-243 7.23e-38

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: 132.58  E-value: 7.23e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD---ALAKLEGIAGIVTRRLDVLDDAAVKALVAEI----GQI 76
Cdd:cd05326    1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDagqAVAAELGDPDISFVHCDVTVEADVRAAVDTAvarfGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFV--HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTKAA 154
Cdd:cd05326   81 DIMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPH-AYTASKHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTT 232
Cdd:cd05326  160 VLGLTRSAATELGEHGIRVNCVSPYGVATPLLTA-GFGVEDEAIEEAVRGAANLKGTALRPEDIAAAVLYLASddSRYVS 238

                        250
                 ....*....|.
gi 489055331 233 GQAYNIDGGWS 243
Cdd:cd05326  239 GQNLVVDGGLT 249
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-241 1.05e-37

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 132.49  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKleGIA-----GIVTR--RLDVLDDAAVKALVA----EI 73
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDK--GLAayrelGIEAHgyVCDVTDEDGVQAMVSqiekEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKA 153
Cdd:PRK07097  86 GVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSEL-GRETVSAYAAAKG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEaaRAAF----IARQPIGRIGQPEEIADLAVYLA--G 227
Cdd:PRK07097 165 GLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGS--RHPFdqfiIAKTPAARWGDPEDLAGPAVFLAsdA 242

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:PRK07097 243 SNFVNGHILYVDGG 256
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-242 1.87e-37

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 137.29  E-value: 1.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAEI----GQIDIL 79
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGdeHLSVQADITDEAAVESAFAQIqarwGRLDVL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHN-GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASSVkGVSNRFVYGLTKAAVIGL 158
Cdd:PRK06484 348 VNNAGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLL-ALPPRNAYCASKAAVTML 424

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESPSLQdRLRAQGdyEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAY 236
Cdd:PRK06484 425 SRSLACEWAPAGIRVNTVAPGYIETPAVL-ALKASG--RADFDSIRRRIPLGRLGDPEEVAEAIAFLASpaASYVNGATL 501


                 ....*.
gi 489055331 237 NIDGGW 242
Cdd:PRK06484 502 TVDGGW 507
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 5-243 2.83e-37

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: 131.81  E-value: 2.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL---AKLEGIAGIVTRRL--DVLDDAAVK----ALVAEIGQ 75
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGdkvAKEITALGGRAIALaaDVLDRASLErareEIVAQFGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVH--------------NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKg 141
Cdd:cd08935   83 VDILINGAGGNHpdattdpehyepetEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 142 VSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQ-GDYEAARAAFIARQPIGRIGQPEEIAD 220
Cdd:cd08935  162 LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPdGSYTDRSNKILGRTPMGRFGKPEELLG 241

                        250       260
                 ....*....|....*....|....*.
gi 489055331 221 LAVYLA---GATYTTGQAYNIDGGWS 243
Cdd:cd08935  242 ALLFLAsekASSFVTGVVIPVDGGFS 267
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-241 1.98e-36

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 129.13  E-value: 1.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEI----GQI 76
Cdd:PRK06463   1 YSMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVekefGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAAVI 156
Cdd:PRK06463  81 DVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTTFYAITKAGII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 157 GLTKAVAADYVGKGIRCNAICPGTVESpSLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQ 234
Cdd:PRK06463 161 ILTRRLAFELGKYGIRVNAVAPGWVET-DMTLSGKSQEEAEKLRELFRNKTVLKTTGKPEDIANIVLFLASddARYITGQ 239


                 ....*..
gi 489055331 235 AYNIDGG 241
Cdd:PRK06463 240 VIVADGG 246
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 4-243 2.43e-36

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 128.72  E-value: 2.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGI---AGIVTRRL--DVLDDAAVKALVAEI----- 73
Cdd:cd05329    3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEwreKGFKVEGSvcDVSSRSERQELMDTVashfg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKA 153
Cdd:cd05329   83 GKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVI-AVPSGAPYGATKG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEaaraAFIARQPIGRIGQPEEIADLAVYLA--GATYT 231
Cdd:cd05329  162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLD----KVIERTPLKRFGEPEEVAALVAFLCmpAASYI 237

                        250
                 ....*....|..
gi 489055331 232 TGQAYNIDGGWS 243
Cdd:cd05329  238 TGQIIAVDGGLT 249
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-241 2.94e-36

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 128.62  E-value: 2.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE------GIAGIVTRRLDVLDDAAVKALVAEIG 74
Cdd:PRK06125   1 MDLHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAadlraaHGVDVAVHALDLSSPEAREQLAAEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAssvkGVSNRFVY--GLT- 151
Cdd:PRK06125  81 DIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAA----GENPDADYicGSAg 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPS----LQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG 227
Cdd:PRK06125 157 NAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRmltlLKGRARAELGDESRWQELLAGLPLGRPATPEEVADLVAFLAS 236

                        250
                 ....*....|....*.
gi 489055331 228 --ATYTTGQAYNIDGG 241
Cdd:PRK06125 237 prSGYTSGTVVTVDGG 252
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-242 3.32e-36

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 128.86  E-value: 3.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN---ADALAKLEGIAG--IVTRRLDVLDDAAVKALVA---- 71
Cdd:PRK13394   1 MMSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNqdgANAVADEINKAGgkAIGVAMDVTNEDAVNAGIDkvae 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGML-ERKDGAIINMASVASSVkGVSNRFVYGL 150
Cdd:PRK13394  81 RFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHE-ASPLKSAYVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQG-----DYEAARA-AFIARQPIGRIGQPEEIADLAVY 224
Cdd:PRK13394 160 AKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQAkelgiSEEEVVKkVMLGKTVDGVFTTVEDVAQTVLF 239

                        250       260
                 ....*....|....*....|
gi 489055331 225 LAG--ATYTTGQAYNIDGGW 242
Cdd:PRK13394 240 LSSfpSAALTGQSFVVSHGW 259
PRK09242 PRK09242
SDR family oxidoreductase;
4-244 5.86e-36

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 127.94  E-value: 5.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEG----------IAGIVTrrlDVLDDAAVKALVAEI 73
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDelaeefpereVHGLAA---DVSDDEDRRAILDWV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 ----GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKgVSNRFVYG 149
Cdd:PRK09242  83 edhwDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTH-VRSGAPYG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEaaraAFIARQPIGRIGQPEEIADLAVYLA--G 227
Cdd:PRK09242 162 MTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYE----QVIERTPMRRVGEPEEVAAAVAFLCmpA 237

                        250
                 ....*....|....*..
gi 489055331 228 ATYTTGQAYNIDGGWSI 244
Cdd:PRK09242 238 ASYITGQCIAVDGGFLR 254
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 8-226 1.16e-35

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: 127.01  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEG------IAGIVTRRLDVLDDAAVKALVA----EIGQID 77
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADelgakfPVKVLPLQLDVSDRESIEAALEnlpeEFRDID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHnGT--ILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVYGLTKAAV 155
Cdd:cd05346   81 ILVNNAGLAL-GLdpAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGR-YPYAGGNVYCATKAAV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESP-SLqdrLRAQGDYEAARAAFIARQPIgrigQPEEIADLAVYLA 226
Cdd:cd05346  159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEfSL---VRFHGDKEKADKVYEGVEPL----TPEDIAETILWVA 223
PRK06114 PRK06114
SDR family oxidoreductase;
4-242 1.91e-35

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 126.43  E-value: 1.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDI-NADALA-----------KLEGIAGIVTRRLDVldDAAVKALVA 71
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLrTDDGLAetaehieaagrRAIQIAADVTSKADL--RAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvkgVSNRFV---- 147
Cdd:PRK06114  83 ELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGI---IVNRGLlqah 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 148 YGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEaaraAFIARQPIGRIGQPEEIADLAVYLA- 226
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATP-MNTRPEMVHQTK----LFEEQTPMQRMAKVDEMVGPAVFLLs 234

                        250
                 ....*....|....*..
gi 489055331 227 -GATYTTGQAYNIDGGW 242
Cdd:PRK06114 235 dAASFCTGVDLLVDGGF 251
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-242 2.02e-35

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 131.51  E-value: 2.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGI--VTRRLDVLDDAAVKALVAEI----GQIDILF 80
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPdhHALAMDVSDEAQIREGFEQLhrefGRIDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFV--HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDG-AIINMASVASsVKGVSNRFVYGLTKAAVIG 157
Cdd:PRK06484  85 NNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGaAIVNVASGAG-LVALPKRTAYSASKAAVIS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAqGDYEaaRAAFIARQPIGRIGQPEEIADLAVYLA--GATYTTGQA 235
Cdd:PRK06484 164 LTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERA-GKLD--PSAVRSRIPLGRLGRPEEIAEAVFFLAsdQASYITGST 240


                 ....*..
gi 489055331 236 YNIDGGW 242
Cdd:PRK06484 241 LVVDGGW 247
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 6-241 3.70e-35

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: 125.73  E-value: 3.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALA-----------KLEGIAGIVTRRLDVldDAAVKALVAEIG 74
Cdd:cd08945    2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLAttvkelreagvEADGRTCDVRSVPEI--EALVAAAVARYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLP--GMLERKDGAIINMASVASSvKGVSNRFVYGLTK 152
Cdd:cd08945   80 PIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKagGMLERGTGRIINIASTGGK-QGVVHAAPYSASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRA------QGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA 226
Cdd:cd08945  159 HGVVGFTKALGLELARTGITVNAVCPGFVETP-MAASVREhyadiwEVSTEEAFDRITARVPLGRYVTPEEVAGMVAYLI 237

                        250
                 ....*....|....*..
gi 489055331 227 G--ATYTTGQAYNIDGG 241
Cdd:cd08945  238 GdgAAAVTAQALNVCGG 254
PRK07062 PRK07062
SDR family oxidoreductase;
1-243 5.25e-35

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 125.54  E-value: 5.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE-------GIAGIVTRRLDVLDDAAVKALVAEI 73
Cdd:PRK07062   2 MQIQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEarlrekfPGARLLAARCDVLDEADVAAFAAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 ----GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKD-GAIINMAS----------VASS 138
Cdd:PRK07062  82 earfGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLP-LLRASAaASIVCVNSllalqpephmVATS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 139 VkgvsnrfvyglTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAF---IARQ---PIGRI 212
Cdd:PRK07062 161 A-----------ARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQSWEAWtaaLARKkgiPLGRL 229

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489055331 213 GQPEEIADLAVYLAG--ATYTTGQAYNIDGGWS 243
Cdd:PRK07062 230 GRPDEAARALFFLASplSSYTTGSHIDVSGGFA 262
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 4-244 6.20e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 125.04  E-value: 6.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EG-----IAGivtrrlDVLDDAAVKALVA- 71
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLvaeiraEGgeavaLAG------DVRDEAYAKALVAl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 ---EIGQIDILFNCAGFVHN-GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIInmasVASSVKGVSNRF- 146
Cdd:PRK07478  77 aveRFGGLDIAFNNAGTLGEmGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLI----FTSTFVGHTAGFp 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 147 ---VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSlqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAV 223
Cdd:PRK07478 153 gmaAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPM----GRAMGDTPEALAFVAGLHALKRMAQPEEIAQAAL 228

                        250       260
                 ....*....|....*....|...
gi 489055331 224 YLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK07478 229 FLASdaASFVTGTALLVDGGVSI 251
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-241 6.55e-35

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: 125.19  E-value: 6.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVyATDINADALAKLEGIAGIVTRRL-------DVLDDAAVKALVAEI---- 73
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANV-VVNYRSKEDAAEEVVEEIKAVGGkaiavqaDVSKEEDVVALFQSAikef 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLE-RKDGAIINMASVASSV--KGVSNrfvYGL 150
Cdd:cd05358   80 GTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIpwPGHVN---YAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLraqgDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--A 228
Cdd:cd05358  157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAW----DDPEQRADLLSLIPMGRIGEPEEIAAAAAWLASdeA 232

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:cd05358  233 SYVTGTTLFVDGG 245
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 1-241 7.06e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 125.02  E-value: 7.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYAT------DINADA------LAKLEGIAGIVTRRLDVLddaavka 68
Cdd:PRK06523   3 FFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTarsrpdDLPEGVefvaadLTTAEGCAAVARAVLERL------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  69 lvaeiGQIDILFNCAG--FVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRF 146
Cdd:PRK06523  76 -----GGVDILVHVLGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPESTT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 147 VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPS---LQDRLRAQ--GDYEAARAAFIARQ---PIGRIGQPEEI 218
Cdd:PRK06523 151 AYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAavaLAERLAEAagTDYEGAKQIIMDSLggiPLGRPAEPEEV 230

                        250       260
                 ....*....|....*....|....*
gi 489055331 219 ADLAVYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK06523 231 AELIAFLASdrAASITGTEYVIDGG 255
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 5-241 7.13e-35

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: 125.04  E-value: 7.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN---ADALAKLEG-----IAGIVTRRLDVldDAAVKALVAEIGQI 76
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINleaARATAAEIGpaacaISLDVTDQASI--DRCVAALVDRWGSI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLER-KDGAIINMASVASSvKGVSNRFVYGLTKAAV 155
Cdd:cd05363   79 DILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGR-RGEALVGVYCATKAAV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQ-----PIGRIGQPEEIADLAVYLAG--A 228
Cdd:cd05363  158 ISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFARYENRPRGEKKRLvgeavPFGRMGRAEDLTGMAIFLAStdA 237

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:cd05363  238 DYIVAQTYNVDGG 250
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 4-241 7.80e-35

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: 124.95  E-value: 7.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDD--------AAVKALVAEIGQ 75
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDAAHVHTADletyagaqGVVRAAVERFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGfvhnGTIL-----EMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAssVKGVsNRFVYGL 150
Cdd:cd08937   81 VDVLINNVG----GTIWakpyeHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIA--TRGI-YRIPYSA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAF-------IARQPIGRIGQPEEIADLAV 223
Cdd:cd08937  154 AKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEQEKVWYqrivdqtLDSSLMGRYGTIDEQVRAIL 233

                        250       260
                 ....*....|....*....|
gi 489055331 224 YLAG--ATYTTGQAYNIDGG 241
Cdd:cd08937  234 FLASdeASYITGTVLPVGGG 253
PRK05867 PRK05867
SDR family oxidoreductase;
5-243 9.47e-35

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 124.76  E-value: 9.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE-----GIAGIVTRRLDVLDDAAVKALV----AEIGQ 75
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLAdeigtSGGKVVPVCCDVSQHQQVTSMLdqvtAELGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLER-KDGAIINMASVASSVKGVSNRFV-YGLTKA 153
Cdd:PRK05867  87 IDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVPQQVShYCASKA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESpslqDRLRAQGDYEAARAAFIarqPIGRIGQPEEIADLAVYLAGA--TYT 231
Cdd:PRK05867 167 AVIHLTKAMAVELAPHKIRVNSVSPGYILT----ELVEPYTEYQPLWEPKI---PLGRLGRPEELAGLYLYLASEasSYM 239

                        250
                 ....*....|..
gi 489055331 232 TGQAYNIDGGWS 243
Cdd:PRK05867 240 TGSDIVIDGGYT 251
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 1-243 9.67e-35

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: 124.51  E-value: 9.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYA-TDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDIL 79
Cdd:cd05351    1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAvSRTQADLDSLVRECPGIEPVCVDLSDWDATEEALGSVGPVDLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK-DGAIINMASVASSVkGVSNRFVYGLTKAAVIGL 158
Cdd:cd05351   81 VNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQR-ALTNHTVYCSTKAALDML 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVespsLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAY 236
Cdd:cd05351  160 TKVMALELGPHKIRVNSVNPTVV----MTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLSdkSSMTTGSTL 235


                 ....*..
gi 489055331 237 NIDGGWS 243
Cdd:cd05351  236 PVDGGFL 242
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 5-241 1.20e-34

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: 124.52  E-value: 1.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYAT----DINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQI---- 76
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISarkaEACADAAEELSAYGECIAIPADLSSEEGIEALVARVAERsdrl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGA-----IINMASVASSVKGVSNRFVYGLT 151
Cdd:cd08942   84 DVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLP-LLRAAATAenparVINIGSIAGIVVSGLENYSYGAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLraqgDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--AT 229
Cdd:cd08942  163 KAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLL----NDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASraGA 238

                        250
                 ....*....|..
gi 489055331 230 YTTGQAYNIDGG 241
Cdd:cd08942  239 YLTGAVIPVDGG 250
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 8-241 1.36e-34

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 124.10  E-value: 1.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331    8 KTALVTAAGQGIGQASALAFAEAGAKVYATDIN---ADALAKLEGIAG--IVTRRLDVLDDAAVKALV----AEIGQIDI 78
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNeetAKETAKEINQAGgkAVAYKLDVSDKDQVFSAIdqaaEKFGGFDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD-GAIINMASVASsVKGVSNRFVYGLTKAAVIG 157
Cdd:TIGR02415  81 MVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAG-HEGNPILSAYSSTKFAVRG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  158 LTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQ----GDYEAARA--AFIARQPIGRIGQPEEIADLAVYLAG--AT 229
Cdd:TIGR02415 160 LTQTAAQELAPKGITVNAYCPGIVKTP-MWEEIDEEtseiAGKPIGEGfeEFSSEIALGRPSEPEDVAGLVSFLASedSD 238

                         250
                  ....*....|..
gi 489055331  230 YTTGQAYNIDGG 241
Cdd:TIGR02415 239 YITGQSILVDGG 250
PRK07069 PRK07069
short chain dehydrogenase; Validated
 10-243 1.59e-34

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 124.05  E-value: 1.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDIN----ADALA-KLEGIAGIVTR---RLDVLDDAAVKALVAE----IGQID 77
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINdaagLDAFAaEINAAHGEGVAfaaVQDVTDEAQWQALLAQaadaMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIG 157
Cdd:PRK07069  82 VLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVA-AFKAEPDYTAYNASKAAVAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 158 LTKAVAADYVGKG--IRCNAICPGTVESPSLQDRLRAQGDYEAARAafIARQ-PIGRIGQPEEIADLAVYLAG--ATYTT 232
Cdd:PRK07069 161 LTKSIALDCARRGldVRCNSIHPTFIRTGIVDPIFQRLGEEEATRK--LARGvPLGRLGEPDDVAHAVLYLASdeSRFVT 238

                        250
                 ....*....|.
gi 489055331 233 GQAYNIDGGWS 243
Cdd:PRK07069 239 GAELVIDGGIC 249
PRK06124 PRK06124
SDR family oxidoreductase;
5-244 1.99e-34

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 124.05  E-value: 1.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINA-------DALAKLEGIAGIVTrrLDVLDDAAVKALVAEI---- 73
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAatleaavAALRAAGGAAEALA--FDIADEEAVAAAFARIdaeh 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKA 153
Cdd:PRK06124  87 GRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQV-ARAGDAVYPAAKQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGT---------VESPSLQDRLRaqgdyeaaraafiARQPIGRIGQPEEIADLAVY 224
Cdd:PRK06124 166 GLTGLMRALAAEFGPHGITSNAIAPGYfatetnaamAADPAVGPWLA-------------QRTPLGRWGRPEEIAGAAVF 232

                        250       260
                 ....*....|....*....|..
gi 489055331 225 LA--GATYTTGQAYNIDGGWSI 244
Cdd:PRK06124 233 LAspAASYVNGHVLAVDGGYSV 254
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 10-241 2.17e-34

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 123.45  E-value: 2.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDIN-------ADALAKLEGIAgiVTRRLDVLDD----AAVKALVAEIGQIDI 78
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKsegaeavAAAIQQAGGQA--IGLECNVTSEqdleAVVKATVSQFGGITI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTI-LEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVsNRFVYGLTKAAVIG 157
Cdd:cd05365   80 LVNNAGGGGPKPFdMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNV-RIAAYGSSKAAVNH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVespsLQDRLRAQGDYEAARaAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQA 235
Cdd:cd05365  159 MTRNLAFDLGPKGIRVNAVAPGAV----KTDALASVLTPEIER-AMLKHTPLGRLGEPEDIANAALFLCSpaSAWVSGQV 233


                 ....*.
gi 489055331 236 YNIDGG 241
Cdd:cd05365  234 LTVSGG 239
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 2-241 2.21e-34

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 123.80  E-value: 2.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL-----------AKLEGIAGIVTRRLDVldDAAVKALV 70
Cdd:PRK06113   6 NLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAAnhvvdeiqqlgGQAFACRCDITSEQEL--SALADFAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  71 AEIGQIDILFNCAGFvHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVsNRFVYGL 150
Cdd:PRK06113  84 SKLGKVDILVNNAGG-GGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNI-NMTSYAS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQgdyeaARAAFIARQPIGRIGQPEEIADLAVYLA--GA 228
Cdd:PRK06113 162 SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPE-----IEQKMLQHTPIRRLGQPQDIANAALFLCspAA 236

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:PRK06113 237 SWVSGQILTVSGG 249
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 8-226 2.74e-34

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: 123.11  E-value: 2.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEG--IAGIVTRRLDVLDDAAVKALVAEI----GQIDILFN 81
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGEllNDNLEVLELDVTDEESIKAAVKEVierfGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  82 CAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAVIGLTKA 161
Cdd:cd05374   81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLV-PTPFLGPYCASKAALEALSES 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055331 162 VAADYVGKGIRCNAICPGTVESPSL------QDRLRAQGDYEAARAAFIAR--QPIGRIGQPEEIADLAVYLA 226
Cdd:cd05374  160 LRLELAPFGIKVTIIEPGPVRTGFAdnaagsALEDPEISPYAPERKEIKENaaGVGSNPGDPEKVADVIVKAL 232
PRK07074 PRK07074
SDR family oxidoreductase;
8-241 6.80e-34

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 122.57  E-value: 6.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE---GIAGIVTRRLDVLDDAAVKAL----VAEIGQIDILF 80
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFAdalGDARFVPVACDLTDAASLAAAlanaAAERGPVDVLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvkGVSNRFVYGLTKAAVIGLTK 160
Cdd:PRK07074  83 ANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGM--AALGHPAYSAAKAGLIHYTK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 161 AVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGD-YEAARAAFiarqPIGRIGQPEEIADLAVYLAG--ATYTTGQAYN 237
Cdd:PRK07074 161 LLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQvFEELKKWY----PLQDFATPDDVANAVLFLASpaARAITGVCLP 236


                 ....
gi 489055331 238 IDGG 241
Cdd:PRK07074 237 VDGG 240
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 10-244 8.16e-34

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: 122.08  E-value: 8.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK--LEGIAG----IVTRRLDVLDDAAVKALVAEI----GQIDIL 79
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAevAAEIEElggkAVVVRADVSQPQDVEEMFAAVkerfGRLDVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVYGLTKAAVIGLT 159
Cdd:cd05359   81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSI-RALPNYLAVGTAKAALEALV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 160 KAVAADYVGKGIRCNAICPGTVESpslqDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATYTTGQAYN 237
Cdd:cd05359  160 RYLAVELGPRGIRVNAVSPGVIDT----DALAHFPNREDLLEAAAANTPAGRVGTPQDVADAVGFLCsdAARMITGQTLV 235


                 ....*..
gi 489055331 238 IDGGWSI 244
Cdd:cd05359  236 VDGGLSI 242
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 5-242 8.43e-34

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 122.14  E-value: 8.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVY-------ATDINADALAKLEGIAGIVTRRL--DVLDDAAVK----ALVA 71
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIvldihpmRGRAEADAVAAGIEAAGGKALGLafDVRDFAATRaaldAGVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVL-PGMLERKDGAIINMASVASsVKGVSNRFVYGL 150
Cdd:PRK12827  84 EFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRARRGGRIVNIASVAG-VRGNRGQVNYAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDrlraqgdyEAARAAFIARQPIGRIGQPEEIADLAVYLA--GA 228
Cdd:PRK12827 163 SKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADN--------AAPTEHLLNPVPVQRLGEPDEVAALVAFLVsdAA 234

                        250
                 ....*....|....
gi 489055331 229 TYTTGQAYNIDGGW 242
Cdd:PRK12827 235 SYVTGQVIPVDGGF 248
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-241 1.14e-33

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 121.76  E-value: 1.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDIN-------ADALAKLEGIAgiVTRRLDVLDD----AAVKALVAEIGQ 75
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNeetaqaaADKLSKDGGKA--IAVKADVSDRdqvfAAVRQVVDTFGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGA-IINMASVASSVkGVSNRFVYGLTKAA 154
Cdd:PRK08643  80 LNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGGkIINATSQAGVV-GNPELAVYSSTKFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQG-----DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG-- 227
Cdd:PRK08643 159 VRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGenagkPDEWGMEQFAKDITLGRLSEPEDVANCVSFLAGpd 238

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:PRK08643 239 SDYITGQTIIVDGG 252
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-243 1.81e-33

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 121.66  E-value: 1.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALaKLEGIAGIVTrrlDVLDDAAVKALVAEI----GQIDI 78
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDG-QHENYQFVPT---DVSSAEEVNHTVAEIiekfGRIDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGfVHNGTIL----------EMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVY 148
Cdd:PRK06171  81 LVNNAG-INIPRLLvdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGL-EGSEGQSCY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 149 GLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRlraqgDYEAA------------RAAFIARQ--PIGRIGQ 214
Cdd:PRK06171 159 AATKAALNSFTRSWAKELGKHNIRVVGVAPGILEATGLRTP-----EYEEAlaytrgitveqlRAGYTKTStiPLGRSGK 233

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489055331 215 PEEIADLAVYLAG--ATYTTGQAYNIDGGWS 243
Cdd:PRK06171 234 LSEVADLVCYLLSdrASYITGVTTNIAGGKT 264
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-223 2.22e-33

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 120.56  E-value: 2.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDINADALAKLEGIAGI--VTRRLDVLD----DAAVKALVA 71
Cdd:PRK07666   1 MAQSLQGKNALITGAGRGIGRAVAIALAKEGVNVgllARTEENLKAVAEEVEAYGVkvVIATADVSDyeevTAAIEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVYGLT 151
Cdd:PRK07666  81 ELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQ-KGAAVTSAYSAS 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEaaraafiarqpigRIGQPEEIADLAV 223
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPD-------------KVMQPEDLAEFIV 218
PRK07814 PRK07814
SDR family oxidoreductase;
4-241 2.32e-33

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 121.42  E-value: 2.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYatdINADALAKLEGIAGIVT---RR-----LDVLDDAAVKALVA---- 71
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVL---IAARTESQLDEVAEQIRaagRRahvvaADLAHPEATAGLAGqave 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD-GAIINMASVASSVKGVSnrFV-YG 149
Cdd:PRK07814  84 AFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGgGSVINISSTMGRLAGRG--FAaYG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKgIRCNAICPGTVespsLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--G 227
Cdd:PRK07814 162 TAKAALAHYTRLAALDLCPR-IRVNAIAPGSI----LTSALEVVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLAspA 236

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:PRK07814 237 GSYLTGKTLEVDGG 250
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 8-225 4.83e-33

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 119.39  E-value: 4.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEG-IAGIVTRRLDVLDDAA----VKALVAEIGQIDILFNC 82
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAsGGDVEAVPYDARDPEDaralVDALRDRFGRIDVLVHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  83 AGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVaSSVKGVSNRFVYGLTKAAVIGLTKAV 162
Cdd:cd08932   81 AGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSL-SGKRVLAGNAGYSASKFALRALAHAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055331 163 AADYVGKGIRCNAICPGTVESPSLQdrlraqgdyeaaRAAFIARQPIGRIGQPEEIADLAVYL 225
Cdd:cd08932  160 RQEGWDHGVRVSAVCPGFVDTPMAQ------------GLTLVGAFPPEEMIQPKDIANLVRMV 210
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-241 7.37e-33

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 119.72  E-value: 7.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVY----ATDINADALAKLEGIAG--IVTRRLDV--LDDAA--VKALVAE 72
Cdd:PRK12935   2 VQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVinynSSKEAAENLVNELGKEGhdVYAVQADVskVEDANrlVEEAVNH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSnRFVYGLTK 152
Cdd:PRK12935  82 FGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFG-QTNYSAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLraqgdyEAARAAFIARQPIGRIGQPEEIADLAVYLA-GATYT 231
Cdd:PRK12935 161 AGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVP------EEVRQKIVAKIPKKRFGQADEIAKGVVYLCrDGAYI 234

                        250
                 ....*....|
gi 489055331 232 TGQAYNIDGG 241
Cdd:PRK12935 235 TGQQLNINGG 244
PRK06128 PRK06128
SDR family oxidoreductase;
4-241 7.73e-33

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 120.73  E-value: 7.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDINADALAKLEGI--AGIVTRRL--DVLDDAAVKALVA----E 72
Cdd:PRK06128  52 RLQGRKALITGADSGIGRATAIAFAREGADIalnYLPEEEQDAAEVVQLIqaEGRKAVALpgDLKDEAFCRQLVEravkE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGF-VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMlerKDGA-IINMASVaSSVKGVSNRFVYGL 150
Cdd:PRK06128 132 LGGLDILVNIAGKqTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL---PPGAsIINTGSI-QSYQPSPTLLDYAS 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDrlrAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--A 228
Cdd:PRK06128 208 TKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTP-LQP---SGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASqeS 283

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:PRK06128 284 SYVTGEVFGVTGG 296
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-241 1.22e-32

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 124.96  E-value: 1.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAGIVTRRLDVLDDAAVKALVAEI----GQI 76
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAaaaeLGGPDRALGVACDVTDEAAVQAAFEEAalafGGV 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK-DGAIINMASVASSVKGVSNrFVYGLTKAAV 155
Cdd:PRK08324 500 DIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPNF-GAYGAAKAAE 578

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPS-------LQDRLRAQG-DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG 227
Cdd:PRK08324 579 LHLVRQLALELGPDGIRVNGVNPDAVVRGSgiwtgewIEARAAAYGlSEEELEEFYRARNLLKREVTPEDVAEAVVFLAS 658

                        250
                 ....*....|....*.
gi 489055331 228 --ATYTTGQAYNIDGG 241
Cdd:PRK08324 659 glLSKTTGAIITVDGG 674
PRK07454 PRK07454
SDR family oxidoreductase;
8-226 1.22e-32

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 118.91  E-value: 1.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKALVAEI----GQIDI 78
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALaaelrSTGVKAAAYSIDLSNPEAIAPGIAELleqfGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASsvkgvSNRF----VYGLTKAA 154
Cdd:PRK07454  87 LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAA-----RNAFpqwgAYCVSKAA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEaaRAAFIArqpigrigqPEEIADLAVYLA 226
Cdd:PRK07454 162 LAAFTKCLAEEERSHGIRVCTITLGAVNTP-LWDTETVQADFD--RSAMLS---------PEQVAQTILHLA 221
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 9-188 1.85e-32

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: 118.50  E-value: 1.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVTAAGQGIGQASALAFAEAGAKVYATDIN---ADALAKLEGIAGI--------VTRRLDVldDAAVKALVAEIGQID 77
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINekgAEETANNVRKAGGkvhyykcdVSKREEV--YEAAKKIKKEVGDVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAS--SVKGVSnrfVYGLTKAAV 155
Cdd:cd05339   79 ILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGliSPAGLA---DYCASKAAA 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489055331 156 IGLTKAVAAD---YVGKGIRCNAICPGTVESPSLQD 188
Cdd:cd05339  156 VGFHESLRLElkaYGKPGIKTTLVCPYFINTGMFQG 191
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 4-226 4.96e-32

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 117.80  E-value: 4.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAK-VYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:PRK06198   3 RLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQaaeleALGAKAVFVQADLSDVEDCRRVVAAAdeaf 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK-DGAIINMASVaSSVKGVSNRFVYGLTK 152
Cdd:PRK06198  83 GRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSM-SAHGGQPFLAAYCASK 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPS---LQDRLRAQGDYEAARAAfiARQPIGRIGQPEEIADLAVYLA 226
Cdd:PRK06198 162 GALATLTRNAAYALLRNRIRVNGLNIGWMATEGedrIQREFHGAPDDWLEKAA--ATQPFGRLLDPDEVARAVAFLL 236
PRK07831 PRK07831
SDR family oxidoreductase;
5-234 6.57e-32

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 117.44  E-value: 6.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAA-GQGIGQASALAFAEAGAKVYATDIN-------ADALAKLEGIAGIVTRRLDVLDDAAVKALVA----E 72
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHerrlgetADELAAELGLGRVEAVVCDVTSEAQVDALIDaaveR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD-GAIINMASVAS--SVKGVSNrfvYG 149
Cdd:PRK07831  95 LGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHgGVIVNNASVLGwrAQHGQAH---YA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPG--------TVESPSLQDRLraqgdyeAARAAFiarqpiGRIGQPEEIADL 221
Cdd:PRK07831 172 AAKAGVMALTRCSALEAAEYGVRINAVAPSiamhpflaKVTSAELLDEL-------AAREAF------GRAAEPWEVANV 238

                        250
                 ....*....|....*
gi 489055331 222 AVYLAG--ATYTTGQ 234
Cdd:PRK07831 239 IAFLASdySSYLTGE 253
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-241 8.44e-32

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 116.43  E-value: 8.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD----ALAKLEGIAGIVTRrLDVLDDAAVKALVAEI--- 73
Cdd:PRK12828   1 MEHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAplsqTLPGVPADALRIGG-IDLVDPQAARRAVDEVnrq 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 -GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTK 152
Cdd:PRK12828  80 fGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMG-AYAAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLqdrlraQGDYEAARaafiarqpIGRIGQPEEIADLAVYLAG--ATY 230
Cdd:PRK12828 159 AGVARLTEALAAELLDRGITVNAVLPSIIDTPPN------RADMPDAD--------FSRWVTPEQIAAVIAFLLSdeAQA 224

                        250
                 ....*....|.
gi 489055331 231 TTGQAYNIDGG 241
Cdd:PRK12828 225 ITGASIPVDGG 235
PRK08267 PRK08267
SDR family oxidoreductase;
8-222 1.01e-31

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 116.96  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE---GIAGIVTRRLDVLDDAAVKALVAEI-----GQIDIL 79
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAaelGAGNAWTGALDVTDRAAWDAALADFaaatgGRLDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGA-IINMASvASSVKGVSNRFVYGLTKAAVIGL 158
Cdd:PRK08267  82 FNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALP-YLKATPGArVINTSS-ASAIYGQPGLAVYSATKFAVRGL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESPSLqdrlraQGDYEAARAAFIARQPIgRIgQPEEIADLA 222
Cdd:PRK08267 160 TEALDLEWRRHGIRVADVMPLFVDTAML------DGTSNEVDAGSTKRLGV-RL-TPEDVAEAV 215
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-241 2.15e-31

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 116.02  E-value: 2.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYatdINADALAKLEGIA------GIVTRRL--DVLDDAAVKALV----AE 72
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVI---LNGRDPAKLAAAAeslkgqGLSAHALafDVTDHDAVRAAIdafeAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVK--GVSNrfvYGL 150
Cdd:PRK07523  85 IGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALArpGIAP---YTA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEaarAAFIARQPIGRIGQPEEIADLAVYLA--GA 228
Cdd:PRK07523 162 TKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTP-LNAALVADPEFS---AWLEKRTPAGRWGKVEELVGACVFLAsdAS 237

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:PRK07523 238 SFVNGHVLYVDGG 250
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 5-241 2.26e-31

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 115.78  E-value: 2.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVyatDINADALAKLEGIAGIVTRRLDVL-----DDAAVKAL----VAEIGQ 75
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIV---GLHGTRVEKLEALAAELGERVKIFpanlsDRDEVKALgqkaEADLEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAV 155
Cdd:PRK12936  81 VDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVV-GVTGNPGQANYCASKAGM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESpSLQDRLRaqgdyEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTG 233
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIES-AMTGKLN-----DKQKEAIMGAIPMKRMGTGAEVASAVAYLASseAAYVTG 233


                 ....*...
gi 489055331 234 QAYNIDGG 241
Cdd:PRK12936 234 QTIHVNGG 241
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 1-241 2.35e-31

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 115.81  E-value: 2.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN------ADALAKLEGIAGIVTRRLDVLDDA--AVKALVAE 72
Cdd:PRK12823   2 MNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelvhevAAELRAAGGEALALTADLETYAGAqaAMAAAVEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGfvhnGTIL-----EMKDEELDFAVNlnvRSMIRTI---RAVLPGMLERKDGAIINMASVASsvKGVsN 144
Cdd:PRK12823  82 FGRIDVLINNVG----GTIWakpfeEYEEEQIEAEIR---RSLFPTLwccRAVLPHMLAQGGGAIVNVSSIAT--RGI-N 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 145 RFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAF-------IARQPIGRIGQPEE 217
Cdd:PRK12823 152 RVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPPRRVPRNAAPQSEQEKAWYqqivdqtLDSSLMKRYGTIDE 231

                        250       260
                 ....*....|....*....|....*.
gi 489055331 218 IADLAVYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK12823 232 QVAAILFLASdeASYITGTVLPVGGG 257
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-241 5.75e-31

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 114.94  E-value: 5.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE------GIAGIVTRRLDVLDDAAVKALVAE-- 72
Cdd:cd08933    3 SGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALEselnraGPGSCKFVPCDVTKEEDIKTLISVtv 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 --IGQIDILFNCAGFvH--NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGAIINMASVASSVkGVSNRFVY 148
Cdd:cd08933   83 erFGRIDCLVNNAGW-HppHQTTDETSAQEFRDLLNLNLISYFLASKYALP-HLRKSQGNIINLSSLVGSI-GQKQAAPY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 149 GLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG- 227
Cdd:cd08933  160 VATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIKEGELAQLLGRMGTEAESGLAALFLAAe 239

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:cd08933  240 ATFCTGIDLLLSGG 253
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 5-241 7.12e-31

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: 114.29  E-value: 7.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDIN-ADALA---KLEGIAGIVTRRlDVLDDAAVKAL----VAEI 73
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVvvnYASSKAaAEEVVaeiEAAGGKAIAVQA-DVSDPSQVARLfdaaEKAF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASSVkGVSNRFVYGLTKA 153
Cdd:cd05362   80 GGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAA-YTPNYGAYAGSKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYT 231
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTD-----MFYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASpdGRWV 231

                        250
                 ....*....|
gi 489055331 232 TGQAYNIDGG 241
Cdd:cd05362  232 NGQVIRANGG 241
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-241 1.67e-30

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 113.52  E-value: 1.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE---GIAGIVTR--RLDVLDDAAVKALVAEI----G 74
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVaecGALGTEVRgyAANVTDEEDVEATFAQIaedfG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKD---------EELDFAVNLNVRSMIRTIRAVLPGMLERKD-GAIINMASVASSVK-GVS 143
Cdd:PRK08217  82 QLNGLINNAGILRDGLLVKAKDgkvtskmslEQFQSVIDVNLTGVFLCGREAAAKMIESGSkGVIINISSIARAGNmGQT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 144 NrfvYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdRLRAQGDYEaARAAFIARQPIGRIGQPEEIADLAV 223
Cdd:PRK08217 162 N---YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIET-----EMTAAMKPE-ALERLEKMIPVGRLGEPEEIAHTVR 232

                        250
                 ....*....|....*...
gi 489055331 224 YLAGATYTTGQAYNIDGG 241
Cdd:PRK08217 233 FIIENDYVTGRVLEIDGG 250
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-181 1.78e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 113.88  E-value: 1.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-EGIAGIVTRRLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETaAELGLVVGGPLDVTDPASFAAFLDAVeadlGPID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAS--SVKGVSnrfVYGLTKAAV 155
Cdd:PRK07825  81 VLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGkiPVPGMA---TYCASKHAV 157

                        170       180
                 ....*....|....*....|....*.
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTV 181
Cdd:PRK07825 158 VGFTDAARLELRGTGVHVSVVLPSFV 183
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 7-241 3.25e-30

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: 112.81  E-value: 3.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL------------AKLEGIAGIVTRRLDVldDAAVKALVAEIG 74
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALeqlkeeltnlykNRVIALELDITSKESI--KELIESYLEKFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAG---FVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSV---------KGV 142
Cdd:cd08930   80 RIDILINNAYpspKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIapdfriyenTQM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 143 SNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTV---ESPSLQDRLRaqgdyeaaraafiARQPIGRIGQPEEIA 219
Cdd:cd08930  160 YSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIlnnQPSEFLEKYT-------------KKCPLKRMLNPEDLR 226

                        250       260
                 ....*....|....*....|....
gi 489055331 220 DLAVYLAG--ATYTTGQAYNIDGG 241
Cdd:cd08930  227 GAIIFLLSdaSSYVTGQNLVIDGG 250
PRK05855 PRK05855
SDR family oxidoreductase;
4-195 3.29e-30

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 117.77  E-value: 3.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL---AKLEGIAGIV--TRRLDVLDDAAVKALV----AEIG 74
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAertAELIRAAGAVahAYRVDVSDADAMEAFAewvrAEHG 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLER-KDGAIINMASVAS--SVKGVSnrfVYGLT 151
Cdd:PRK05855 392 VPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAyaPSRSLP---AYATS 468

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVE------------SPSLQDRLRAQGD 195
Cdd:PRK05855 469 KAAVLMLSECLRAELAAAGIGVTAICPGFVDtnivattrfagaDAEDEARRRGRAD 524
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 8-241 3.54e-30

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: 112.39  E-value: 3.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDIN-----ADALAKLEGIAGIVTRRLDVLDD----AAVKALVAEIGQIDI 78
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNenpgaAAELQAINPKVKATFVQCDVTSWeqlaAAFKKAIEKFGRVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFV----HNGTILEMKDEELDFAVNLNvrSMIRTIRAVLPGMLERK---DGAIINMASVASSVKGVSNRfVYGLT 151
Cdd:cd05323   81 LINNAGILdeksYLFAGKLPPPWEKTIDVNLT--GVINTTYLALHYMDKNKggkGGVIVNIGSVAGLYPAPQFP-VYSAS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVA-ADYVGKGIRCNAICPGTVESPSLQDrlraqgdyeaARAAFIARQPIGRIGQPEEIADLAVYLAGATY 230
Cdd:cd05323  158 KHGVVGFTRSLAdLLEYKTGVRVNAICPGFTNTPLLPD----------LVAKEAEMLPSAPTQSPEVVAKAIVYLIEDDE 227

                        250
                 ....*....|.
gi 489055331 231 TTGQAYNIDGG 241
Cdd:cd05323  228 KNGAIWIVDGG 238
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 1-241 5.55e-30

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 112.51  E-value: 5.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDIN-----ADALAKLEGIAGIVtrRLDVLDDAAVKALV-- 70
Cdd:PRK08936   1 MYSDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVvinYRSDEEeandvAEEIKKAGGEAIAV--KGDVTVESDVVNLIqt 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  71 --AEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLER-KDGAIINMASVASSVKGVSnrFV 147
Cdd:PRK08936  79 avKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPL--FV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 148 -YGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLraqgDYEAARAAFIARQPIGRIGQPEEIADLAVYLA 226
Cdd:PRK08936 157 hYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKF----ADPKQRADVESMIPMGYIGKPEEIAAVAAWLA 232

                        250
                 ....*....|....*..
gi 489055331 227 G--ATYTTGQAYNIDGG 241
Cdd:PRK08936 233 SseASYVTGITLFADGG 249
PRK07035 PRK07035
SDR family oxidoreductase;
5-244 1.20e-29

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 111.26  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGA-------KVYATDINADALAKLEGIAGIVTRRLDVLDDaaVKALVAEI---- 73
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAhvivssrKLDGCQAVADAIVAAGGKAEALACHIGEMEQ--IDALFAHIrerh 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAG----FvhnGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGvSNRFVYG 149
Cdd:PRK07035  84 GRLDILVNNAAanpyF---GHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPG-DFQGIYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAAraafIARQPIGRIGQPEEIADLAVYLA--G 227
Cdd:PRK07035 160 ITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQA----LAHIPLRRHAEPSEMAGAVLYLAsdA 235

                        250
                 ....*....|....*..
gi 489055331 228 ATYTTGQAYNIDGGWSI 244
Cdd:PRK07035 236 SSYTTGECLNVDGGYLS 252
PRK06949 PRK06949
SDR family oxidoreductase;
2-226 2.29e-29

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 110.62  E-value: 2.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE-------GIAGIVtrRLDVLDDAAVKALVA--- 71
Cdd:PRK06949   4 SINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRaeieaegGAAHVV--SLDVTDYQSIKAAVAhae 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 -EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGA--------IINMASVASsVKGV 142
Cdd:PRK06949  82 tEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAG-LRVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 143 SNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDyeaarAAFIARQPIGRIGQPEEIADLA 222
Cdd:PRK06949 161 PQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQG-----QKLVSMLPRKRVGKPEDLDGLL 235


                 ....
gi 489055331 223 VYLA 226
Cdd:PRK06949 236 LLLA 239
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 1-243 3.59e-29

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 110.76  E-value: 3.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL-AKLEGIA-------GIVTrrlDVLDDAAVKALVAE 72
Cdd:PRK08277   4 NLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAeAVVAEIKaaggealAVKA---DVLDKESLEQARQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 I----GQIDILFNCAGFVHNG---------------TILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMA 133
Cdd:PRK08277  81 IledfGPCDILINGAGGNHPKattdnefhelieptkTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 134 SVA-----SSVKGvsnrfvYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPslQDR---LRAQGDYEAARAAFIA 205
Cdd:PRK08277 161 SMNaftplTKVPA------YSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE--QNRallFNEDGSLTERANKILA 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489055331 206 RQPIGRIGQPEEIADLAVYLA---GATYTTGQAYNIDGGWS 243
Cdd:PRK08277 233 HTPMGRFGKPEELLGTLLWLAdekASSFVTGVVLPVDGGFS 273
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-224 7.31e-29

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: 109.16  E-value: 7.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGIAGIV-TRRLDVLD----DAAVKALVAEIGQ 75
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLealaDELEAEGGKAlVLELDVTDeqqvDAAVERTVEALGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGvSNRFVYGLTKAAV 155
Cdd:cd08934   81 LDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAV-RNSAVYNATKFGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDYEAARAAFIARQPIgrigQPEEIADLAVY 224
Cdd:cd08934  160 NAFSEGLRQEVTERGVRVVVIEPGTVDTE-LRDHITHTITKEAYEERISTIRKL----QAEDIAAAVRY 223
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 4-242 1.08e-28

(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: 108.56  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADA----------------LAKLEGIAgiVTRRLDVLD-DAAV 66
Cdd:cd05353    2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRkgsgksssaadkvvdeIKAAGGKA--VANYDSVEDgEKIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  67 KALVAEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASvASSVKGVSNRF 146
Cdd:cd05353   80 KTAIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSS-AAGLYGNFGQA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 147 VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPG-------TVESPSLQDRLRaqgdyeaaraafiarqpigrigqPEEIA 219
Cdd:cd05353  159 NYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAagsrmteTVMPEDLFDALK-----------------------PEYVA 215

                        250       260
                 ....*....|....*....|....
gi 489055331 220 DLAVYLAGA-TYTTGQAYNIDGGW 242
Cdd:cd05353  216 PLVLYLCHEsCEVTGGLFEVGAGW 239
PRK08628 PRK08628
SDR family oxidoreductase;
1-242 1.08e-28

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 108.89  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTR----RLDVLDDA----AVKALVAE 72
Cdd:PRK08628   1 MDLNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEELRALQPRaefvQVDLTDDAqcrdAVEQTVAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGfVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKdGAIINMASvASSVKGVSNRFVYGLTK 152
Cdd:PRK08628  81 FGRIDGLVNNAG-VNDGVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISS-KTALTGQGGTSGYAAAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAAFIARQPIG-RIGQPEEIADLAVYL--AGAT 229
Cdd:PRK08628 158 GAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIATFDDPEAKLAAITAKIPLGhRMTTAEEIADTAVFLlsERSS 237

                        250
                 ....*....|...
gi 489055331 230 YTTGQAYNIDGGW 242
Cdd:PRK08628 238 HTTGQWLFVDGGY 250
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-242 1.20e-28

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 108.81  E-value: 1.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAG---------------AKVYAT-----DINADaLAKLEGIAGIVTRRldvldda 64
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGcdivginiveptetiEQVTALgrrflSLTAD-LRKIDGIPALLERA------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  65 avkalVAEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLER-KDGAIINMASVASSVKGVS 143
Cdd:PRK08993  80 -----VAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 144 NRfVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQdRLRAQgdyEAARAAFIARQPIGRIGQPEEIADLAV 223
Cdd:PRK08993 155 VP-SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQ-QLRAD---EQRSAEILDRIPAGRWGLPSDLMGPVV 229

                        250       260
                 ....*....|....*....|.
gi 489055331 224 YLA--GATYTTGQAYNIDGGW 242
Cdd:PRK08993 230 FLAssASDYINGYTIAVDGGW 250
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 8-186 1.93e-28

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: 107.54  E-value: 1.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG---IVTRRLDVLDDAAVKALVAEI-----GQIDIL 79
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGaenVVAGALDVTDRAAWAAALADFaaatgGRLDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGA-IINMASvASSVKGVSNRFVYGLTKAAVIGL 158
Cdd:cd08931   81 FNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALP-YLKATPGArVINTAS-SSAIYGQPDLAVYSATKFAVRGL 158

                        170       180
                 ....*....|....*....|....*...
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESPSL 186
Cdd:cd08931  159 TEALDVEWARHGIRVADVWPWFVDTPIL 186
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 8-230 4.61e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 107.68  E-value: 4.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINadaLAKLEGIAGIVTRRLDVLDDAAVKALVAEI----GQIDILFNCA 83
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRN---PARAAPIPGVELLELDVTDDASVQAAVDEViaraGRIDVLVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 GFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMasvaSSVKGvsnrFV-------YGLTKAAVI 156
Cdd:PRK06179  82 GVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINI----SSVLG----FLpapymalYAASKHAVE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055331 157 GLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQ---GDYEAARAAFIA--RQPIGRIGQPEEIADLAVYLAGATY 230
Cdd:PRK06179 154 GYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDsplAEYDRERAVVSKavAKAVKKADAPEVVADTVVKAALGPW 232
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 7-242 5.32e-28

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: 106.99  E-value: 5.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINA---DALAKLEG----IAGIVTRRLDVldDAAVKALVAEIGQIDIL 79
Cdd:cd05371    2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNspgETVAKLGDncrfVPVDVTSEKDV--KAALALAKAKFGRLDIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKD------EELDFAVNLNVRSMIRTIRAVLPGML--------ERkdGAIINMASVASsVKGVSNR 145
Cdd:cd05371   80 VNCAGIAVAAKTYNKKGqqphslELFQRVINVNLIGTFNVIRLAAGAMGknepdqggER--GVIINTASVAA-FEGQIGQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 146 FVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLqdrlraQGDYEAARaAFIARQ--PIGRIGQPEEIADLAV 223
Cdd:cd05371  157 AAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLL------AGLPEKVR-DFLAKQvpFPSRLGDPAEYAHLVQ 229

                        250
                 ....*....|....*....
gi 489055331 224 YLAGATYTTGQAYNIDGGW 242
Cdd:cd05371  230 HIIENPYLNGEVIRLDGAI 248
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 2-244 8.10e-28

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 106.58  E-value: 8.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL--------EGIAGIVTRRLDvlDDAAVKALVAEI 73
Cdd:PRK06200   1 MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLrqrfgdhvLVVEGDVTSYAD--NQRAVDQTVDAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAG-FVHNGTILEMKDEELDFA----VNLNVRSMIRTIRAVLPGMLERKdGAIINMASVASSVKGvSNRFVY 148
Cdd:PRK06200  79 GKLDCFVGNAGiWDYNTSLVDIPAETLDTAfdeiFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPG-GGGPLY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 149 GLTKAAVIGLTKAVAADyVGKGIRCNAICPGTVESP-----SLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAV 223
Cdd:PRK06200 157 TASKHAVVGLVRQLAYE-LAPKIRVNGVAPGGTVTDlrgpaSLGQGETSISDSPGLADMIAAITPLQFAPQPEDHTGPYV 235

                        250       260
                 ....*....|....*....|....
gi 489055331 224 YLA---GATYTTGQAYNIDGGWSI 244
Cdd:PRK06200 236 LLAsrrNSRALTGVVINADGGLGI 259
PRK07577 PRK07577
SDR family oxidoreductase;
8-244 9.57e-28

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 105.96  E-value: 9.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADalaklEGIAG--IVTRRLDVLDDAAVKALVAEIGQIDILFNCAGF 85
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARSAI-----DDFPGelFACDLADIEQTAATLAQINEIHPVDAIVNNVGI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAssVKGVSNRFVYGLTKAAVIGLTKAVAAD 165
Cdd:PRK07577  79 ALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA--IFGALDRTSYSAAKSALVGCTRTWALE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 166 YVGKGIRCNAICPGTVESpSLQDRLRAQGDYEAARaaFIARQPIGRIGQPEEIADLAVYLA--GATYTTGQAYNIDGGWS 243
Cdd:PRK07577 157 LAEYGITVNAVAPGPIET-ELFRQTRPVGSEEEKR--VLASIPMRRLGTPEEVAAAIAFLLsdDAGFITGQVLGVDGGGS 233


                 .
gi 489055331 244 I 244
Cdd:PRK07577 234 L 234
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 8-241 9.96e-28

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: 106.00  E-value: 9.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKV---YATDIN-ADALAKLEGiAGIVTRRLDVLDDAAVKALVAEI----GQIDIL 79
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVvvnYYRSTEsAEAVAAEAG-ERAIAIQADVRDRDQVQAMIEEAknhfGPVDTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCA--GFVHNG----TILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASvassvKGVSNRFV----YG 149
Cdd:cd05349   80 VNNAliDFPFDPdqrkTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGT-----NLFQNPVVpyhdYT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSlqdrlRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG-- 227
Cdd:cd05349  155 TAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTD-----ASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASpw 229

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:cd05349  230 ARAVTGQNLVVDGG 243
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-242 1.26e-27

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 106.14  E-value: 1.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDInADALAKLEGIAGIVTR----RLDVLDDAAVKALVAE----IGQI 76
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGV-AEAPETQAQVEALGRKfhfiTADLIQQKDIDSIVSQavevMGHI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGA-IINMASVASSVKGVSNRfVYGLTKAAV 155
Cdd:PRK12481  85 DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGkIINIASMLSFQGGIRVP-SYTASKSAV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQdRLRAQgdyEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATYTTG 233
Cdd:PRK12481 164 MGLTRALATELSQYNINVNAIAPGYMATDNTA-ALRAD---TARNEAILERIPASRWGTPDDLAGPAIFLSssASDYVTG 239


                 ....*....
gi 489055331 234 QAYNIDGGW 242
Cdd:PRK12481 240 YTLAVDGGW 248
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-241 3.20e-27

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: 104.98  E-value: 3.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVY------------ATDINADALAKLEGIAGivtrrlDVLDDAAVKALVAE 72
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAiagrkpevleaaAEEISSATGGRAHPIQC------DVRDPEAVEAAVDE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 I----GQIDILFNCAG--FVhngtileMKDEELDF-----AVNLNVRSMIRTIRAVLPGMLERKDGA-IINMaSVASSVK 140
Cdd:cd05369   75 TlkefGKIDILINNAAgnFL-------APAESLSPngfktVIDIDLNGTFNTTKAVGKRLIEAKHGGsILNI-SATYAYT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 141 GVSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQgdyEAARAAFIARQPIGRIGQPEEIAD 220
Cdd:cd05369  147 GSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPS---GKSEKKMIERVPLGRLGTPEEIAN 223

                        250       260
                 ....*....|....*....|...
gi 489055331 221 LAVYLA--GATYTTGQAYNIDGG 241
Cdd:cd05369  224 LALFLLsdAASYINGTTLVVDGG 246
PRK12743 PRK12743
SDR family oxidoreductase;
8-241 3.75e-27

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 104.73  E-value: 3.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKV---YATDiNADALAKLEGIAGI----VTRRLDVLD----DAAVKALVAEIGQI 76
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIgitWHSD-EEGAKETAEEVRSHgvraEIRQLDLSDlpegAQALDKLIQRLGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELD--FAVNLN---------VRSMIRTIRAvlpgmlerkdGAIINMASVASSVKGVSNR 145
Cdd:PRK12743  82 DVLVNNAGAMTKAPFLDMDFDEWRkiFTVDVDgaflcsqiaARHMVKQGQG----------GRIINITSVHEHTPLPGAS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 146 fVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrLRAQGDyEAARAAFIARQPIGRIGQPEEIADLAVYL 225
Cdd:PRK12743 152 -AYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATP-----MNGMDD-SDVKPDSRPGIPLGRPGDTHEIASLVAWL 224

                        250
                 ....*....|....*...
gi 489055331 226 A--GATYTTGQAYNIDGG 241
Cdd:PRK12743 225 CseGASYTTGQSLIVDGG 242
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 5-241 6.38e-27

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 104.05  E-value: 6.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKV---YA-TDINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAE----IG 74
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVavnYAgSAAAADELVAEIEAAGgrAIAVQADVADAAAVTRLFDAaetaFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMAS--VASSVKGVSnrfVYGLTK 152
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTsvIALPLPGYG---PYAASK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATY 230
Cdd:PRK12937 158 AAVEGLVHVLANELRGRGITVNAVAPGPVAT-----ELFFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGpdGAW 232

                        250
                 ....*....|.
gi 489055331 231 TTGQAYNIDGG 241
Cdd:PRK12937 233 VNGQVLRVNGG 243
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-184 8.26e-27

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: 103.49  E-value: 8.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGIAG-----IVTRRLDVLD----DAAVKALVAEI 73
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLeeavEEIEAEANasgqkVSYISADLSDyeevEQAFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKA 153
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALV-GIYGYSAYCPSKF 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESP 184
Cdd:cd08939  160 ALRGLAESLRQELKPYNIRVSVVYPPDTDTP 190
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-244 2.76e-26

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 102.49  E-value: 2.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYatdINA-----DALAKLEGIAGIVTRRLDVLDDAA--------VKALVA 71
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVV---VNAkkraeEMNETLKMVKENGGEGIGVLADVStregcetlAKATID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVA--SSVKGVSnrfVYG 149
Cdd:PRK06077  81 RYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAgiRPAYGLS---IYG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKgIRCNAICPGTVESP---SLQDRLRAQGDYEAARAAFiarqpIGRIGQPEEIADLAVYLA 226
Cdd:PRK06077 156 AMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKlgeSLFKVLGMSEKEFAEKFTL-----MGKILDPEEVAEFVAAIL 229

                        250
                 ....*....|....*...
gi 489055331 227 GATYTTGQAYNIDGGWSI 244
Cdd:PRK06077 230 KIESITGQVFVLDSGESL 247
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 6-219 6.31e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 101.92  E-value: 6.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAEI----GQIDIL 79
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPdrALARLLDVTDFDAIDAVVADAeatfGPIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAS--SVKGVSnrfVYGLTKAAVIG 157
Cdd:PRK06180  83 VNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGliTMPGIG---YYCGSKFALEG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVES----PSLQDRLRAQGDYEA-------ARAAFIARQPigriGQPEEIA 219
Cdd:PRK06180 160 ISESLAKEVAPFGIHVTAVEPGSFRTdwagRSMVRTPRSIADYDAlfgpirqAREAKSGKQP----GDPAKAA 228
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 5-181 1.12e-25

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: 100.55  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVY-----ATDINADALAKLEGIAGIVTR------------RLDVLDDAAVK 67
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVvaaktASEGDNGSAKSLPGTIEETAEeieaaggqalpiVVDVRDEDQVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  68 ALVAEI----GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVaSSVKGVS 143
Cdd:cd05338   81 ALVEATvdqfGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPP-LSLRPAR 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489055331 144 NRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTV 181
Cdd:cd05338  160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTA 197
PRK07326 PRK07326
SDR family oxidoreductase;
5-184 1.43e-25

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 100.09  E-value: 1.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE----------GIAGIVTRRLDVldDAAVKALVAEIG 74
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAaelnnkgnvlGLAADVRDEADV--QRAVDAIVAAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGmLERKDGAIINMASVASsvkgvSNRF----VYGL 150
Cdd:PRK07326  82 GLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPA-LKRGGGYIINISSLAG-----TNFFaggaAYNA 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESP 184
Cdd:PRK07326 156 SKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 7-241 1.81e-25

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: 100.16  E-value: 1.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAGIVTRRLDVLDDAAVKA----LVAEIGQIDI 78
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKvaeaAQGGPRALGVQCDVTSEAQVQSafeqAVLEFGGLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAAVIGL 158
Cdd:cd08943   81 VVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESPSLQDrlraQGDYEAARAA--------FIARQPIGRIGQPEEIADLAVYLAG--A 228
Cdd:cd08943  161 ARCLALEGGEDGIRVNTVNPDAVFRGSKIW----EGVWRAARAKayglleeeYRTRNLLKREVLPEDVAEAVVAMASedF 236

                        250
                 ....*....|...
gi 489055331 229 TYTTGQAYNIDGG 241
Cdd:cd08943  237 GKTTGAIVTVDGG 249
PRK08264 PRK08264
SDR family oxidoreductase;
5-207 5.49e-25

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 98.81  E-value: 5.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGA-KVYATDINADALAKLEgiAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCA 83
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAaKVYAAARDPESVTDLG--PRVVPLQLDVTDPASVAAAAEAASDVTILVNNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 G-FVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIGLTKAV 162
Cdd:PRK08264  82 GiFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVL-SWVNFPNLGTYSASKAAAWSLTQAL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489055331 163 AADYVGKGIRCNAICPGTVESpslqdRLRAQGDYEAARAAFIARQ 207
Cdd:PRK08264 161 RAELAPQGTRVLGVHPGPIDT-----DMAAGLDAPKASPADVARQ 200
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 10-202 8.38e-25

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: 98.14  E-value: 8.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAG-AKVYATDINADALAKLEGIAGIVTRR----LDVLD--DAAVKALVAEIGQ--IDILF 80
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLhileLDVTDeiAESAEAVAERLGDagLDVLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHN-GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVK--GVSNRFVYGLTKAAVIG 157
Cdd:cd05325   81 NNAGILHSyGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGdnTSGGWYSYRASKAALNM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARAA 202
Cdd:cd05325  161 LTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAKNKGPITPEESV 205
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
4-244 1.47e-24

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 97.87  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDINA--DALAKLEGI-AGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIavnYARSRKAaeETAEEIEALgRKALAVKANVGDVEKIKEMFAQIdeef 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKA 153
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLG-SIRYLENYTTVGVSKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARaafiARQPIGRIGQPEEIADLAVYLAG--ATYT 231
Cdd:PRK08063 160 ALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELLEDAR----AKTPAGRMVEPEDVANAVLFLCSpeADMI 235

                        250
                 ....*....|...
gi 489055331 232 TGQAYNIDGGWSI 244
Cdd:PRK08063 236 RGQTIIVDGGRSL 248
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 1-241 1.64e-24

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 98.00  E-value: 1.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK------------LEGIAGIVTRRLDVldDAAVKA 68
Cdd:PRK08339   2 LKIDLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKarekiksesnvdVSYIVADLTKREDL--ERTVKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  69 LvAEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVY 148
Cdd:PRK08339  80 L-KNIGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIK-EPIPNIALS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 149 GLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSL----QDRLRAQG-DYEAARAAFIARQPIGRIGQPEEIADLAV 223
Cdd:PRK08339 158 NVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRViqlaQDRAKREGkSVEEALQEYAKPIPLGRLGEPEEIGYLVA 237

                        250       260
                 ....*....|....*....|
gi 489055331 224 YLAG--ATYTTGQAYNIDGG 241
Cdd:PRK08339 238 FLASdlGSYINGAMIPVDGG 257
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-241 1.92e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 97.44  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAG-IVTRRLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEakleIEQFPGqVLTVQMDVRNPEDVQKMVEQIdekfGRID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGfvhnGTILeMKDEELDF-----AVNLNVRSMIRTIRAVLPGMLERK-DGAIINMasVASSVKGVSNRFVYGLT 151
Cdd:PRK07677  81 ALINNAA----GNFI-CPAEDLSVngwnsVIDIVLNGTFYCSQAVGKYWIEKGiKGNIINM--VATYAWDAGPGVIHSAA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 -KAAVIGLTKAVAADYVGK-GIRCNAICPGTVESPSLQDRLRAQgdyEAARAAFIARQPIGRIGQPEEIADLAVYLAG-- 227
Cdd:PRK07677 154 aKAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERTGGADKLWES---EEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSde 230

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:PRK07677 231 AAYINGTCITMDGG 244
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 1-241 2.67e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 97.57  E-value: 2.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK-------LEGIAGIVTRRLDVLDD----AAVKAL 69
Cdd:PRK05875   1 MQLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAaaeeieaLKGAGAVRYEPADVTDEdqvaRAVDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  70 VAEIGQIDILFNCAGFVHN-GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvkgVSNRF-- 146
Cdd:PRK05875  81 TAWHGRLHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAAS---NTHRWfg 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 147 VYGLTKAAVIGLTKaVAADYVGKG-IRCNAICPGTVESpslqDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYL 225
Cdd:PRK05875 158 AYGVTKSAVDHLMK-LAADELGPSwVRVNSIRPGLIRT----DLVAPITESPELSADYRACTPLPRVGEVEDVANLAMFL 232

                        250
                 ....*....|....*...
gi 489055331 226 AG--ATYTTGQAYNIDGG 241
Cdd:PRK05875 233 LSdaASWITGQVINVDGG 250
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-243 3.59e-24

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 97.07  E-value: 3.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAA--GQGIGQASALAFAEAGAKVYAT---DINADALAKLEGIAGIVTRR-------------LDVLDDAA- 65
Cdd:PRK12748   3 LMKKIALVTGAsrLNGIGAAVCRRLAAKGIDIFFTywsPYDKTMPWGMHDKEPVLLKEeiesygvrcehmeIDLSQPYAp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  66 ---VKALVAEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASvASSVKGV 142
Cdd:PRK12748  83 nrvFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTS-GQSLGPM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 143 SNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLraqgdyeaaRAAFIARQPIGRIGQPEEIADLA 222
Cdd:PRK12748 162 PDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWITEEL---------KHHLVPKFPQGRVGEPVDAARLI 232

                        250       260
                 ....*....|....*....|...
gi 489055331 223 VYLAG--ATYTTGQAYNIDGGWS 243
Cdd:PRK12748 233 AFLVSeeAKWITGQVIHSEGGFS 255
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 7-243 7.47e-24

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: 95.72  E-value: 7.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAEI----GQIDILF 80
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGpnLFFVHGDVADETLVKFVVYAMleklGRIDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKdGAIINMASvASSVKGVSNRFVYGLTKAAVIGLTK 160
Cdd:cd09761   81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIAS-TRAFQSEPDSEAYAASKGGLVALTH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 161 AVAADyVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAAraafiARQPIGRIGQPEEIADLAVYLA--GATYTTGQAYNI 238
Cdd:cd09761  159 ALAMS-LGPDIRVNCISPGWINTTEQQEFTAAPLTQEDH-----AQHPAGRVGTPKDIANLVLFLCqqDAGFITGETFIV 232


                 ....*
gi 489055331 239 DGGWS 243
Cdd:cd09761  233 DGGMT 237
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 7-241 1.04e-23

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 95.87  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE-------GIAGIVTRRLDVLDDAAVKALVAEI----GQ 75
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAqeinaeyGEGMAYGFGADATSEQSVLALSRGVdeifGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK-DGAIINMASvASSVKGVSNRFVYGLTKAA 154
Cdd:PRK12384  82 VDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINS-KSGKVGSKHNSGYSAAKFG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGT-VESPSLQDRL----RAQG-DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG- 227
Cdd:PRK12384 161 GVGLTQSLALDLAEYGITVHSLMLGNlLKSPMFQSLLpqyaKKLGiKPDEVEQYYIDKVPLKRGCDYQDVLNMLLFYASp 240

                        250
                 ....*....|....*
gi 489055331 228 -ATYTTGQAYNIDGG 241
Cdd:PRK12384 241 kASYCTGQSINVTGG 255
PRK07985 PRK07985
SDR family oxidoreductase;
4-241 1.61e-23

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 96.22  E-value: 1.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDINADA--LAKLEGIAG--IVTRRLDVLDDAAVKALVAE---- 72
Cdd:PRK07985  46 RLKDRKALVTGGDSGIGRAAAIAYAREGADVaisYLPVEEEDAqdVKKIIEECGrkAVLLPGDLSDEKFARSLVHEahka 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGF-VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgmLERKDGAIINMASVaSSVKGVSNRFVYGLT 151
Cdd:PRK07985 126 LGGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIP--LLPKGASIITTSSI-QAYQPSPHLLDYAAT 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPsLQdrlRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--AT 229
Cdd:PRK07985 203 KAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTA-LQ---ISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASqeSS 278

                        250
                 ....*....|..
gi 489055331 230 YTTGQAYNIDGG 241
Cdd:PRK07985 279 YVTAEVHGVCGG 290
PRK12742 PRK12742
SDR family oxidoreductase;
7-243 1.67e-23

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 94.82  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDI-NADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGF 85
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAgSKDAAERLAQETGATAVQTDSADRDAVIDVVRKSGALDILVVNAGI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 VHNGTILEMKDEELDFAVNLNVRSMIRTirAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKAAVIGLTKAVAAD 165
Cdd:PRK12742  86 AVFGDALELDADDIDRLFKINIHAPYHA--SVEAARQMPEGGRIIIIGSVNGDRMPVAGMAAYAASKSALQGMARGLARD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 166 YVGKGIRCNAICPGTVESpslqDRLRAQGDYEAARAAFIArqpIGRIGQPEEIADLAVYLAG--ATYTTGQAYNIDGGWS 243
Cdd:PRK12742 164 FGPRGITINVVQPGPIDT----DANPANGPMKDMMHSFMA---IKRHGRPEEVAGMVAWLAGpeASFVTGAMHTIDGAFG 236
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-244 1.68e-23

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 95.03  E-value: 1.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDIN-----ADALAKLEGIAGIVTR-RLDVLD----DAAVKALVAEIGQID 77
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPddeelAATQQELRALGVEVIFfPADVADlsahEAMLDAAQAAWGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGF--VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD------GAIINMASVaSSVKGVSNRFVYG 149
Cdd:PRK12745  83 CLVNNAGVgvKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSV-NAIMVSPNRGEYC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDrlrAQGDYEAARAAFIArqPIGRIGQPEEIADLAVYLAGA- 228
Cdd:PRK12745 162 ISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAP---VTAKYDALIAKGLV--PMPRWGEPEDVARAVAALASGd 236

                        250
                 ....*....|....*..
gi 489055331 229 -TYTTGQAYNIDGGWSI 244
Cdd:PRK12745 237 lPYSTGQAIHVDGGLSI 253
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 2-244 1.94e-23

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 95.02  E-value: 1.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD----ALAKLEGIAGIVT-RRLDVLDDAAVKA----LVAE 72
Cdd:PRK07576   4 MFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEkvdaAVAQLQQAGPEGLgVSADVRDYAAVEAafaqIADE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGAIINMASVASSVKGVSNRFVyGLTK 152
Cdd:PRK07576  84 FGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYP-LLRRPGASIIQISAPQAFVPMPMQAHV-CAAK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQgdyEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATY 230
Cdd:PRK07576 162 AGVDMLTRTLALEWGPEGIRVNSIVPGPIAGTEGMARLAPS---PELQAAVAQSVPLKRNGTKQDIANAALFLAsdMASY 238

                        250
                 ....*....|....
gi 489055331 231 TTGQAYNIDGGWSI 244
Cdd:PRK07576 239 ITGVVLPVDGGWSL 252
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 5-241 2.31e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 94.82  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINA----DALAKL--EGIAGI-----VTRRLDVldDAAVKALVAEI 73
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAeraeLAVAKLrqEGIKAHaapfnVTHKQEV--EAAIEHIEKDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKA 153
Cdd:PRK08085  85 GPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSEL-GRDTITPYAASKG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESpslqDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GATYT 231
Cdd:PRK08085 164 AVKMLTRGMCVELARHNIQVNGIAPGYFKT----EMTKALVEDEAFTAWLCKRTPAARWGDPQELIGAAVFLSskASDFV 239

                        250
                 ....*....|
gi 489055331 232 TGQAYNIDGG 241
Cdd:PRK08085 240 NGHLLFVDGG 249
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 1-241 3.16e-23

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: 94.53  E-value: 3.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIR--LDGKTALVTAAGQGIGQASALAFAEAGAKVYAT---DINAD-ALAKLEG----IAGIVTRRLDVLD-DAAVKAL 69
Cdd:cd08936    2 VTRRdpLANKVALVTASTDGIGLAIARRLAQDGAHVVVSsrkQQNVDrAVATLQGeglsVTGTVCHVGKAEDrERLVATA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  70 VAEIGQIDILF-NCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVY 148
Cdd:cd08936   82 VNLHGGVDILVsNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVA-AFHPFPGLGPY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 149 GLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqDRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG- 227
Cdd:cd08936  161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT----SFSSALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSe 236

                        250
                 ....*....|....*
gi 489055331 228 -ATYTTGQAYNIDGG 241
Cdd:cd08936  237 dASYITGETVVVGGG 251
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 7-183 3.65e-23

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: 93.82  E-value: 3.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL----EGIAGIVTRRLDV---LDDAAVKALVAEIGQIDI- 78
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVakeiEEKYGVETKTIAAdfsAGDDIYERIEKELEGLDIg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 -LFNCAGFVHN--GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKgVSNRFVYGLTKAAV 155
Cdd:cd05356   81 iLVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIP-TPLLATYSASKAFL 159

                        170       180
                 ....*....|....*....|....*...
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVES 183
Cdd:cd05356  160 DFFSRALYEEYKSQGIDVQSLLPYLVAT 187
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 8-241 7.94e-23

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: 92.73  E-value: 7.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVY------ATDINA--DALAKLEGIAgiVTRRLDVLDDAAVKALVA----EIGQ 75
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVvhynrsEAEAQRlkDELNALRNSA--VLVQADLSDFAACADLVAaafrAFGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMaSVASSVKGVSNRFVYGLTKAAV 155
Cdd:cd05357   79 CDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINI-IDAMTDRPLTGYFAYCMSKAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKgIRCNAICPGTVespslqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAGATYTTGQA 235
Cdd:cd05357  158 EGLTRSAALELAPN-IRVNGIAPGLI--------LLPEDMDAEYRENALRKVPLKRRPSAEEIADAVIFLLDSNYITGQI 228


                 ....*.
gi 489055331 236 YNIDGG 241
Cdd:cd05357  229 IKVDGG 234
PRK05693 PRK05693
SDR family oxidoreductase;
8-215 8.75e-23

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 93.70  E-value: 8.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGiAGIVTRRLDVLDDAAVKA----LVAEIGQIDILFNCA 83
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAA-AGFTAVQLDVNDGAALARlaeeLEAEHGGLDVLINNA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 GFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGAIINMASVaSSVKGVSNRFVYGLTKAAVIGLTKAVA 163
Cdd:PRK05693  81 GYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGSV-SGVLVTPFAGAYCASKAAVHALSDALR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055331 164 ADYVGKGIRCNAICPGTVES------------------------PSLQDRLRAQGDyEAARAAFIARQPIGRIGQP 215
Cdd:PRK05693 159 LELAPFGVQVMEVQPGAIASqfasnasreaeqllaeqspwwplrEHIQARARASQD-NPTPAAEFARQLLAAVQQS 233
PRK05866 PRK05866
SDR family oxidoreductase;
2-171 8.82e-23

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 94.04  E-value: 8.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLegiAGIVTRR--------LDVLDDAAVKALVA-- 71
Cdd:PRK05866  35 PVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAV---ADRITRAggdamavpCDLSDLDAVDALVAdv 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 --EIGQIDILFNCAGFVHNGTILEMKDEELDF--AVNLNVRSMIRTIRAVLPGMLERKDGAIINMAS--VASsvkGVSNR 145
Cdd:PRK05866 112 ekRIGGVDILINNAGRSIRRPLAESLDRWHDVerTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwgVLS---EASPL 188

                        170       180
                 ....*....|....*....|....*..
gi 489055331 146 F-VYGLTKAAVIGLTKAVAADYVGKGI 171
Cdd:PRK05866 189 FsVYNASKAALSAVSRVIETEWGDRGV 215
PRK07856 PRK07856
SDR family oxidoreductase;
2-241 1.13e-22

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 92.69  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   2 TIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAgivTRRLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK07856   1 NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRPAE---FHAADVRDPDQVAALVDAIverhGRLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD-GAIINMASVaSSVKGVSNRFVYGLTKAAVI 156
Cdd:PRK07856  78 VLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSV-SGRRPSPGTAAYGAAKAGLL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 157 GLTKAVAADYVGKgIRCNAICPGTVESPSLQDRLraqGDyEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQ 234
Cdd:PRK07856 157 NLTRSLAVEWAPK-VRVNAVVVGLVRTEQSELHY---GD-AEGIAAVAATVPLGRLATPADIAWACLFLASdlASYVSGA 231


                 ....*..
gi 489055331 235 AYNIDGG 241
Cdd:PRK07856 232 NLEVHGG 238
PLN02253 PLN02253
xanthoxin dehydrogenase
 4-243 1.91e-22

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 92.96  E-value: 1.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAGIVTRRLDVL--DDA--AVKALVAEIGQ 75
Cdd:PLN02253  15 RLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNvcdsLGGEPNVCFFHCDVTveDDVsrAVDFTVDKFGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHN--GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTKA 153
Cdd:PLN02253  95 LDIMVNNAGLTGPpcPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPH-AYTGSKH 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVES----PSLQDRLRAQgDYEAARAAFIARQP--IGRIGQPEEIADLAVYLAG 227
Cdd:PLN02253 174 AVLGLTRSVAAELGKHGIRVNCVSPYAVPTalalAHLPEDERTE-DALAGFRAFAGKNAnlKGVELTVDDVANAVLFLAS 252

                        250
                 ....*....|....*...
gi 489055331 228 --ATYTTGQAYNIDGGWS 243
Cdd:PLN02253 253 deARYISGLNLMIDGGFT 270
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 7-205 2.48e-22

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: 91.70  E-value: 2.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGA-KVYATDINADALAKL--EGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCA 83
Cdd:cd05354    3 DKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLvaKYGDKVVPLRLDVTDPESIKAAAAQAKDVDVVINNA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 GFVHNGTILEMKDEE-LDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIGLTKAV 162
Cdd:cd05354   83 GVLKPATLLEEGALEaLKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVA-SLKNFPAMGTYSASKSAAYSLTQGL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489055331 163 AADYVGKGIRCNAICPGTVESpslqdRLRAQGDYEAARAAFIA 205
Cdd:cd05354  162 RAELAAQGTLVLSVHPGPIDT-----RMAAGAGGPKESPETVA 199
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 8-181 2.77e-22

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: 91.14  E-value: 2.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGA-KVYAT--DINA--DALAKL--EGIAgIVTRRLDVLDDAAVKALVAEI----GQI 76
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTarDVERgqAAVEKLraEGLS-VRFHQLDVTDDASIEAAADFVeekyGGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTI-LEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVsnrfvYGLTKAAV 155
Cdd:cd05324   80 DILVNNAGIAFKGFDdSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA-----YGVSKAAL 154

                        170       180
                 ....*....|....*....|....*.
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTV 181
Cdd:cd05324  155 NALTRILAKELKETGIKVNACCPGWV 180
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 9-244 3.15e-22

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: 91.76  E-value: 3.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVTAAGQGIGQASALAFAEAGAKVYATDI----NADALAKLEGIAGIVTR--RLDVLDDAAVKALVAEI----GQIDI 78
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAAGRRAIyfQADIGELSDHEALLDQAwedfGRLDC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFV--HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD------GAIINMASvASSVKGVSNRFVYGL 150
Cdd:cd05337   83 LVNNAGIAvrPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTS-INAYLVSPNRGEYCI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDrlrAQGDYEAARAAfiARQPIGRIGQPEEIADLAVYLA--GA 228
Cdd:cd05337  162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAP---VKEKYDELIAA--GLVPIRRWGQPEDIAKAVRTLAsgLL 236

                        250
                 ....*....|....*.
gi 489055331 229 TYTTGQAYNIDGGWSI 244
Cdd:cd05337  237 PYSTGQPINIDGGLSM 252
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
64-241 3.86e-22

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 91.23  E-value: 3.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  64 AAVKALVAEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVaSSVKGVS 143
Cdd:PRK12938  70 AAFDKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSV-NGQKGQF 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 144 NRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqDRLRAQgdYEAARAAFIARQPIGRIGQPEEIADLAV 223
Cdd:PRK12938 149 GQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGT----DMVKAI--RPDVLEKIVATIPVRRLGSPDEIGSIVA 222

                        170       180
                 ....*....|....*....|
gi 489055331 224 YLAG--ATYTTGQAYNIDGG 241
Cdd:PRK12938 223 WLASeeSGFSTGADFSLNGG 242
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 10-184 4.20e-22

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: 90.85  E-value: 4.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVK----ALVAEIGQIDILF 80
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELkaellNPNPSVEVEILDVTDEERNQlviaELEAELGGLDLVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAG--FVHNGTILEMKDEELDFAVNLNvrSMIRTIRAVLPGMLERKDGAIINMASVASsVKGVSNRFVYGLTKAAVIGL 158
Cdd:cd05350   81 INAGvgKGTSLGDLSFKAFRETIDTNLL--GAAAILEAALPQFRAKGRGHLVLISSVAA-LRGLPGAAAYSASKAALSSL 157

                        170       180
                 ....*....|....*....|....*.
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESP 184
Cdd:cd05350  158 AESLRYDVKKRGIRVTVINPGFIDTP 183
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-241 4.91e-22

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: 91.02  E-value: 4.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVTAAGQGIGQASALAFAEAGAKVYATDI-NADALAKLEGIAGIVTRRLDVLDDAAvkalvaeiGQIDILFNCAGFVH 87
Cdd:cd05328    1 TIVITGAASGIGAATAELLEDAGHTVIGIDLrEADVIADLSTPEGRAAAIADVLARCS--------GVLDGLVNCAGVGG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  88 NGTilemkdeeLDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSN----------------------- 144
Cdd:cd05328   73 TTV--------AGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQDKlelakalaagtearavalaehag 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 145 ---RFVYGLTKAAVIGLTKAVAADY-VGKGIRCNAICPGTVESPSLQDrLRAQGDYEAARAAFIArqPIGRIGQPEEIAD 220
Cdd:cd05328  145 qpgYLAYAGSKEALTVWTRRRAATWlYGAGVRVNTVAPGPVETPILQA-FLQDPRGGESVDAFVT--PMGRRAEPDEIAP 221

                        250       260
                 ....*....|....*....|...
gi 489055331 221 LAVYLAG--ATYTTGQAYNIDGG 241
Cdd:cd05328  222 VIAFLASdaASWINGANLFVDGG 244
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-241 5.16e-22

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 90.92  E-value: 5.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKV----YATDINADALAKLEGIAGIVTRRlDVLDDAAVKALVAE----IG 74
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVvvnyHQSEDAAEALADELGDRAIALQA-DVTDREQVQAMFATatehFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 Q-IDILFNCA--GFVHNG----TILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASvassvKGVSNRFV 147
Cdd:PRK08642  80 KpITTVVNNAlaDFSFDGdarkKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGT-----NLFQNPVV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 148 ----YGLTKAAVIGLTKAVAADYVGKGIRCNAICPGtvespslqdrLRAQGDYEAARAAFI-----ARQPIGRIGQPEEI 218
Cdd:PRK08642 155 pyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGG----------LLRTTDASAATPDEVfdliaATTPLRKVTTPQEF 224

                        250       260
                 ....*....|....*....|....*
gi 489055331 219 ADLAVYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK08642 225 ADAVLFFASpwARAVTGQNLVVDGG 249
PRK06194 PRK06194
hypothetical protein; Provisional
 4-181 8.91e-22

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 91.23  E-value: 8.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EGiAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:PRK06194   3 DFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAvaelraQG-AEVLGVRTDVSDAAQVEALADAAlerf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD------GAIINMASVASSVkGVSNRFV 147
Cdd:PRK06194  82 GAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASMAGLL-APPAMGI 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489055331 148 YGLTKAAVIGLTKAVAADY--VGKGIRCNAICPGTV 181
Cdd:PRK06194 161 YNVSKHAVVSLTETLYQDLslVTDQVGASVLCPYFV 196
PRK06181 PRK06181
SDR family oxidoreductase;
7-195 9.77e-22

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 90.42  E-value: 9.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE------GIAGIVTrRLDVLDDAAVKAL----VAEIGQI 76
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAqeladhGGEALVV-PTDVSDAEACERLieaaVARFGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEE-LDFAVNLNVRSMIRTIRAVLPGMLERKdGAIINMASVAsSVKGVSNRFVYGLTKAAV 155
Cdd:PRK06181  80 DILVNNAGITMWSRFDELTDLSvFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLA-GLTGVPTRSGYAASKHAL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGD 195
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGDGK 197
PRK05650 PRK05650
SDR family oxidoreductase;
11-220 1.11e-21

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 90.48  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  11 LVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDD----AAVKALVAEIGQIDILFN 81
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETlkllrEAGGDGFYQRCDVRDYsqltALAQACEEKWGGIDVIVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  82 CAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKG--VSNrfvYGLTKAAVIGLT 159
Cdd:PRK05650  84 NAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGpaMSS---YNVAKAGVVALS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055331 160 KAVAADYVGKGIRCNAICPGTVESpSLQDRLRAQGD-YEAARAAFIARQPIgrigQPEEIAD 220
Cdd:PRK05650 161 ETLLVELADDEIGVHVVCPSFFQT-NLLDSFRGPNPaMKAQVGKLLEKSPI----TAADIAD 217
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 4-224 1.13e-21

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: 90.26  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EGIAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:cd05343    3 RWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALaaecqsAGYPTLFPYQCDLSNEEQILSMFSAIrtqh 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK--DGAIINMASVAS-SVKGVSNRFVYGL 150
Cdd:cd05343   83 QGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGhRVPPVSVFHFYAA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055331 151 TKAAVIGLTKAVAAD--YVGKGIRCNAICPGTVESPSLQdrlRAQGDYEAARAAFIARQPigrIGQPEEIADLAVY 224
Cdd:cd05343  163 TKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEFAF---KLHDNDPEKAAATYESIP---CLKPEDVANAVLY 232
PRK07832 PRK07832
SDR family oxidoreductase;
8-220 1.39e-21

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 90.49  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAGIVT--RRLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQtvadARALGGTVPehRALDISDYDAVAAFAADIhaahGSMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLE-RKDGAIINMASVASSVkGVSNRFVYGLTKAAVI 156
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAaGRGGHLVNVSSAAGLV-ALPWHAAYSASKFGLR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055331 157 GLTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQG-DYEAARAAFIARQPIGRIGQPEEIAD 220
Cdd:PRK07832 160 GLSEVLRFDLARHGIGVSVVVPGAVKTP-LVNTVEIAGvDREDPRVQKWVDRFRGHAVTPEKAAE 223
PRK08416 PRK08416
enoyl-ACP reductase;
1-241 1.93e-21

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 89.83  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKV---YATDIN-ADALAK-LEGIAGIVTR--RLDVLDDAAVKALVAEI 73
Cdd:PRK08416   2 MSNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIaftYNSNVEeANKIAEdLEQKYGIKAKayPLNILEPETYKELFKKI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQ----IDILFNCA---------GFvhnGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVK 140
Cdd:PRK08416  82 DEdfdrVDFFISNAiisgravvgGY---TKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNLVY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 141 gVSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqDRLRAQGDYEAARAAFIARQPIGRIGQPEEIAD 220
Cdd:PRK08416 159 -IENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDT----DALKAFTNYEEVKAKTEELSPLNRMGQPEDLAG 233

                        250       260
                 ....*....|....*....|...
gi 489055331 221 LAVYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK08416 234 ACLFLCSekASWLTGQTIVVDGG 256
PRK09135 PRK09135
pteridine reductase; Provisional
 6-244 3.08e-21

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 88.83  E-value: 3.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKV---YATDI-NADALAK-LEGI-AG-IVTRRLDVLDDAAVKALVAEI----G 74
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVaihYHRSAaEADALAAeLNALrPGsAAALQADLLDPDALPELVAACvaafG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILfncagfVHN---------GTILEMKDEELdFAVNLNVRSMIrtIRAVLPgMLERKDGAIINMASVASSvKGVSNR 145
Cdd:PRK09135  85 RLDAL------VNNassfyptplGSITEAQWDDL-FASNLKAPFFL--SQAAAP-QLRKQRGAIVNITDIHAE-RPLKGY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 146 FVYGLTKAAVIGLTKAVAADyVGKGIRCNAICPGTV---ESPSLQDrlraqgdyEAARAAFIARQPIGRIGQPEEIADlA 222
Cdd:PRK09135 154 PVYCAAKAALEMLTRSLALE-LAPEVRVNAVAPGAIlwpEDGNSFD--------EEARQAILARTPLKRIGTPEDIAE-A 223

                        250       260
                 ....*....|....*....|....
gi 489055331 223 V--YLAGATYTTGQAYNIDGGWSI 244
Cdd:PRK09135 224 VrfLLADASFITGQILAVDGGRSL 247
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 5-196 3.38e-21

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: 88.52  E-value: 3.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEG-IAGIVTRRLDVLD----DAAVKALVAEIGQIDIL 79
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKeLPNIHTIVLDVGDaesvEALAEALLSEYPNLDIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKD--EELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTKAAVIG 157
Cdd:cd05370   83 INNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANP-VYCATKAALHS 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489055331 158 LTKAVAADYVGKGIRCNAICPGTVESPsLQDRLRAQGDY 196
Cdd:cd05370  162 YTLALRHQLKDTGVEVVEIVPPAVDTE-LHEERRNPDGG 199
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-244 5.55e-21

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: 88.56  E-value: 5.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE--------GIAGIVTRRLDvlDDAAVKALVAEIGQ 75
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRadfgdavvGVEGDVRSLAD--NERAVARCVERFGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAG-FVHNGTILEMKDEELDFA----VNLNVRSMIRTIRAVLPGMLERKdGAIINMASVASSVKGvSNRFVYGL 150
Cdd:cd05348   79 LDCFIGNAGiWDYSTSLVDIPEEKLDEAfdelFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPG-GGGPLYTA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKgIRCNAICPG-----------------TVESPSLQDRLRAQgdyeaaraafiarQPIGRIG 213
Cdd:cd05348  157 SKHAVVGLVKQLAYELAPH-IRVNGVAPGgmvtdlrgpaslgqgetSISTPPLDDMLKSI-------------LPLGFAP 222

                        250       260       270
                 ....*....|....*....|....*....|....
gi 489055331 214 QPEEIADLAVYLAGATYT---TGQAYNIDGGWSI 244
Cdd:cd05348  223 EPEDYTGAYVFLASRGDNrpaTGTVINYDGGMGV 256
PRK07201 PRK07201
SDR family oxidoreductase;
4-171 7.34e-21

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 90.78  E-value: 7.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAklEGIAGIVTRRL-------DVLDDAAVKALVAEI--- 73
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALD--ELVAEIRAKGGtahaytcDLTDSAAVDHTVKDIlae 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 -GQIDILFNCAGFVHNGTILEMKDEELDF--AVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAssVKGVSNRF-VYG 149
Cdd:PRK07201 446 hGHVDYLVNNAGRSIRRSVENSTDRFHDYerTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIG--VQTNAPRFsAYV 523

                        170       180
                 ....*....|....*....|..
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGI 171
Cdd:PRK07201 524 ASKAALDAFSDVAASETLSDGI 545
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 11-224 7.80e-21

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 87.89  E-value: 7.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  11 LVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG--IVTRRLDVLDDAAVKALV----AEIGQIDILFNCAG 84
Cdd:PRK10538   4 LVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGdnLYIAQLDVRNRAAIEEMLaslpAEWRNIDVLVNNAG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  85 FV------HNGTIlemkdEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTKAAVIGL 158
Cdd:PRK10538  84 LAlglepaHKASV-----EDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGN-VYGATKAFVRQF 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESPSLQDrLRAQGDYEAARAAFIARQPIgrigQPEEIADlAVY 224
Cdd:PRK10538 158 SLNLRTDLHGTAVRVTDIEPGLVGGTEFSN-VRFKGDDGKAEKTYQNTVAL----TPEDVSE-AVW 217
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
 10-244 1.03e-20

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 87.28  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKV---Y-ATDINADALAKLEGIAGI--VTRRLDVLDDAAVKALVAE----IGQIDIL 79
Cdd:NF012208   1 ALVTGSARGIGRAIALALAREGFDVavhYrRSAEAAEQTAQEAEALGVkaITLQADLTDPEQARSLVEEaaeaLGGLSVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  80 FNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMA-SVASSVKGVSNRFVYGLTKAAVIGL 158
Cdd:NF012208  81 VNNVGNYLHKPLLETTDEEWHEMLDSNLNATFYVTQAALPLMRAAGWGRIVNLGyAGAQNLLARPGITPYVIAKTGVIIY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 159 TKAVAADYVGKGIRCNAICPGTVESpSLQDRLRaqgdyeaaraafiaRQPIGRIGQPEEIADLAVYL--AGATYTTGQAY 236
Cdd:NF012208 161 SKALAKELAGDGITVNVVSPGVAEN-SVSQPLP--------------EIPAGRPATLEELADAVLFFvrPSSDYITGQVL 225


                 ....*...
gi 489055331 237 NIDGGWSI 244
Cdd:NF012208 226 EVAGGWNL 233
PRK06182 PRK06182
short chain dehydrogenase; Validated
 8-184 1.11e-20

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 87.71  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEgIAGIVTRRLDVLDDAAVKALVAEI----GQIDILFNCA 83
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA-SLGVHPLSLDVTDEASIKAAVDTIiaeeGRIDVLVNNA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 GFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRFvYGLTKAAVIGLTKAVA 163
Cdd:PRK06182  83 GYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAW-YHATKFALEGFSDALR 161

                        170       180
                 ....*....|....*....|.
gi 489055331 164 ADYVGKGIRCNAICPGTVESP 184
Cdd:PRK06182 162 LEVAPFGIDVVVIEPGGIKTE 182
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-182 1.21e-20

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 89.90  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINA--DALAKLEGIAGIVTRRLDVLDDAAVKALVAEI----GQIDI 78
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAagEALAAVANRVGGTALALDITAPDAPARIAEHLaerhGGLDI 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVA--SSVKGVSNrfvYGLTKAAVI 156
Cdd:PRK08261 288 VVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISgiAGNRGQTN---YAASKAGVI 364

                        170       180
                 ....*....|....*....|....*.
gi 489055331 157 GLTKAVAADYVGKGIRCNAICPGTVE 182
Cdd:PRK08261 365 GLVQALAPLLAERGITINAVAPGFIE 390
PRK12746 PRK12746
SDR family oxidoreductase;
5-244 1.56e-20

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 87.40  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKV--------YATDINADALAKLEGIAGIVTRRLDVLDDaaVKALVAEI--- 73
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVaihygrnkQAADETIREIESNGGKAFLIEADLNSIDG--VKKLVEQLkne 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 -------GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgmLERKDGAIINMASvASSVKGVSNRF 146
Cdd:PRK12746  82 lqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLP--LLRAEGRVINISS-AEVRLGFTGSI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 147 VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLraqgDYEAARAAFIARQPIGRIGQPEEIADLAVYLA 226
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLL----DDPEIRNFATNSSVFGRIGQVEDIADAVAFLA 234

                        250       260
                 ....*....|....*....|
gi 489055331 227 GAT--YTTGQAYNIDGGWSI 244
Cdd:PRK12746 235 SSDsrWVTGQIIDVSGGFCL 254
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-241 1.90e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 86.94  E-value: 1.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYatdINADALAKLEGIAG--------IVTRRLDVLDDAAVKALV----AE 72
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVV---LAARTAERLDEVAAeiddlgrrALAVPTDITDEDQCANLValalER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAgFVHNgtilEMKD-EELDFA-----VNLNVRSMIRTIRAVLPGMLERKdGAIIN---MASVASSVKGVS 143
Cdd:PRK07890  80 FGRVDALVNNA-FRVP----SMKPlADADFAhwravIELNVLGTLRLTQAFTPALAESG-GSIVMinsMVLRHSQPKYGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 144 nrfvYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQG-----DYEAARAAFIARQPIGRIGQPEEI 218
Cdd:PRK07890 154 ----YKMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGYFRHQAgkygvTVEQIYAETAANSDLKRLPTDDEV 229

                        250       260
                 ....*....|....*....|....*
gi 489055331 219 ADLAVYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK07890 230 ASAVLFLASdlARAITGQTLDVNCG 254
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-242 1.94e-20

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 86.76  E-value: 1.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAG--QGIGQASALAFAEAGAKVYAT-------------DINADALAKLEGIAGIV---TRRLDVLDDAA 65
Cdd:PRK12859   3 QLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTywtaydkempwgvDQDEQIQLQEELLKNGVkvsSMELDLTQNDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  66 VKALVAEI----GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIrTIRAVLPGMLERKDGA-IINMASVASSVK 140
Cdd:PRK12859  83 PKELLNKVteqlGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATT-LLSSQFARGFDKKSGGrIINMTSGQFQGP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 141 GVSNrFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRaqgdyEAARAAFiarqPIGRIGQPEEIAD 220
Cdd:PRK12859 162 MVGE-LAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEIK-----QGLLPMF----PFGRIGEPKDAAR 231

                        250       260
                 ....*....|....*....|....
gi 489055331 221 LAVYLAG--ATYTTGQAYNIDGGW 242
Cdd:PRK12859 232 LIKFLASeeAEWITGQIIHSEGGF 255
PRK07041 PRK07041
SDR family oxidoreductase;
11-244 2.66e-20

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 85.86  E-value: 2.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  11 LVTAAGQGIGQASALAFAEAGAKVYATDINAD----ALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGFV 86
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDrlaaAARALGGGAPVRTAALDITDEAAVDAFFAEAGPFDHVVITAADT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  87 HNGTILEMKDEELDFAVNLNVRSMIRTIRAVlpgmlERKDGAIINMASVASSVKGVSNRFVYGLTKAAVIGLTKAVAADY 166
Cdd:PRK07041  81 PGGPVRALPLAAAQAAMDSKFWGAYRVARAA-----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALEL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055331 167 VGkgIRCNAICPGTVESPsLQDRLrAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAGATYTTGQAYNIDGGWSI 244
Cdd:PRK07041 156 AP--VRVNTVSPGLVDTP-LWSKL-AGDAREAMFAAAAERLPARRVGQPEDVANAILFLAANGFTTGSTVLVDGGHAI 229
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 4-155 6.26e-20

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: 85.21  E-value: 6.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-EGIAGIVTRRLDVLDDAAVKALVAEI----GQIDI 78
Cdd:COG3967    2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAaAANPGLHTIVLDVADPASIAALAEQVtaefPDLNV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055331  79 LFNCAGFVHNGTILE--MKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRfVYGLTKAAV 155
Cdd:COG3967   82 LINNAGIMRAEDLLDeaEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTP-TYSATKAAL 159
PRK06914 PRK06914
SDR family oxidoreductase;
7-232 1.49e-19

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 85.08  E-value: 1.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG-------IVTRRLDVLDDAAVKA---LVAEIGQI 76
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATqlnlqqnIKVQQLDVTDQNSIHNfqlVLKEIGRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSV--KGVSNrfvYGLTKAA 154
Cdd:PRK06914  83 DLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVgfPGLSP---YVSSKYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVESP----SLQDRLRAQGD------YEAARAAFIARQpIGRIGQPEEIADLAVY 224
Cdd:PRK06914 160 LEGFSESLRLELKPFGIDVALIEPGSYNTNiwevGKQLAENQSETtspykeYMKKIQKHINSG-SDTFGNPIDVANLIVE 238


                 ....*...
gi 489055331 225 LAGATYTT 232
Cdd:PRK06914 239 IAESKRPK 246
PRK09730 PRK09730
SDR family oxidoreductase;
8-241 1.84e-19

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 84.13  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKV---YATDINA--DALAKLEGIAGIVTR-RLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVavnYQQNLHAaqEVVNLITQAGGKAFVlQADISDENQVVAMFTAIdqhdEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILE-MKDEELDFAVNLNVRSMIRTIRAVLPGMLER---KDGAIINMASVASSVKGVSNRFVYGLTKA 153
Cdd:PRK09730  82 ALVNNAGILFTQCTVEnLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEYVDYAASKG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdRLRAQGDyEAARAAFIARQ-PIGRIGQPEEIADLAVYLAG--ATY 230
Cdd:PRK09730 162 AIDTLTTGLSLEVAAQGIRVNCVRPGFIYT-----EMHASGG-EPGRVDRVKSNiPMQRGGQPEEVAQAIVWLLSdkASY 235

                        250
                 ....*....|.
gi 489055331 231 TTGQAYNIDGG 241
Cdd:PRK09730 236 VTGSFIDLAGG 246
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 5-244 2.10e-19

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: 83.92  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVT--AAGQGIGQASALAFAEAGAKV---YATDINADALAKL-EGIAGIVTRRLDVLDDAAVKALVAEI----G 74
Cdd:COG0623    3 LKGKRGLITgvANDRSIAWGIAKALHEEGAELaftYQGEALKKRVEPLaEELGSALVLPCDVTDDEQIDALFDEIkekwG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHN----GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASSvKGVSNRFVYGL 150
Cdd:COG0623   83 KLDFLVHSIAFAPKeelgGRFLDTSREGFLLAMDISAYSLVALAKAAEPLM--NEGGSIVTLTYLGAE-RVVPNYNVMGV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSlqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA--GA 228
Cdd:COG0623  160 AKAALEASVRYLAADLGPKGIRVNAISAGPIKTLA----ASGIPGFDKLLDYAEERAPLGRNVTIEEVGNAAAFLLsdLA 235

                        250
                 ....*....|....*.
gi 489055331 229 TYTTGQAYNIDGGWSI 244
Cdd:COG0623  236 SGITGEIIYVDGGYHI 251
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 7-179 3.29e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 83.93  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG--IVTRRLDVLDDAAVKALVAE----IGQIDILF 80
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGdrLLPLALDVTDRAAVFAAVETavehFGRLDIVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIGLTK 160
Cdd:PRK08263  83 NNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIG-GISAFPMSGIYHASKWALEGMSE 161

                        170
                 ....*....|....*....
gi 489055331 161 AVAADYVGKGIRCNAICPG 179
Cdd:PRK08263 162 ALAQEVAEFGIKVTLVEPG 180
PRK09134 PRK09134
SDR family oxidoreductase;
8-241 9.69e-19

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 82.28  E-value: 9.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKV---YATDIN-ADALAKLEGIAG--IVTRRLDVLDDAAVKALVAE----IGQID 77
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVavhYNRSRDeAEALAAEIRALGrrAVALQADLADEAEVRALVARasaaLGPIT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMasVASSVKGVSNRFV-YGLTKAAVI 156
Cdd:PRK09134  90 LLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNM--IDQRVWNLNPDFLsYTLSKAALW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 157 GLTKAVAADYVGKgIRCNAICPGtvesPSLQDRLRAQGDYEAARAAFiarqPIGRIGQPEEIADLAVYLAGATYTTGQAY 236
Cdd:PRK09134 168 TATRTLAQALAPR-IRVNAIGPG----PTLPSGRQSPEDFARQHAAT----PLGRGSTPEEIAAAVRYLLDAPSVTGQMI 238


                 ....*
gi 489055331 237 NIDGG 241
Cdd:PRK09134 239 AVDGG 243
PRK07775 PRK07775
SDR family oxidoreductase;
6-179 9.91e-19

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 82.49  E-value: 9.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGakvYATDINADALAKLEGIAG--------IVTRRLDVLDDAAVKALVAE----I 73
Cdd:PRK07775   9 DRRPALVAGASSGIGAATAIELAAAG---FPVALGARRVEKCEELVDkiradggeAVAFPLDVTDPDSVKSFVAQaeeaL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMAS-VASSVKGVSNrfVYGLTK 152
Cdd:PRK07775  86 GEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSdVALRQRPHMG--AYGAAK 163

                        170       180
                 ....*....|....*....|....*..
gi 489055331 153 AAVIGLTKAVAADYVGKGIRCNAICPG 179
Cdd:PRK07775 164 AGLEAMVTNLQMELEGTGVRASIVHPG 190
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 9-242 2.70e-18

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: 81.08  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVTAAGQGIGQASALAFAEAGAKVYATD---INADALAKLEG-IAGivTRRLDVLDDA-AVKALVAEIGQIDILFNCA 83
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVCHDasfADAAERQAFESeNPG--TKALSEQKPEeLVDAVLQAGGAIDVLVSND 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 GFVHN-GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASvASSVKGVSNRFVYGLTKAAVIGLTKAV 162
Cdd:cd05361   81 YIPRPmNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITS-AVPKKPLAYNSLYGPARAAAVALAESL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 163 AADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAaRAAFIARQPIGRIGQPEEIADLAVYLAGAT--YTTGQAYNIDG 240
Cdd:cd05361  160 AKELSRDNILVYAIGPNFFNSPTYFPTSDWENNPEL-RERVKRDVPLGRLGRPDEMGALVAFLASRRadPITGQFFAFAG 238


                 ..
gi 489055331 241 GW 242
Cdd:cd05361  239 GY 240
PRK09186 PRK09186
flagellin modification protein A; Provisional
 5-244 3.09e-18

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 80.80  E-value: 3.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL-AKLEGIAGIVTRR------LDVLDDAAVKALVAEI---- 73
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALnELLESLGKEFKSKklslveLDITDQESLEEFLSKSaeky 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCA---GFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMasvaSSVKGVSN-RF--- 146
Cdd:PRK09186  82 GKIDGAVNCAyprNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNI----SSIYGVVApKFeiy 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 147 ---------VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVespslqdrlrAQGDYEAARAAFiaRQPIGRIG--QP 215
Cdd:PRK09186 158 egtsmtspvEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGI----------LDNQPEAFLNAY--KKCCNGKGmlDP 225

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489055331 216 EEIADLAVYLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK09186 226 DDICGTLVFLLSdqSKYITGQNIIVDDGFSL 256
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 5-194 3.47e-18

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 81.16  E-value: 3.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEG----IAGIVTrrlDVLDDAAVKALVAE---- 72
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQavnhLRAegfdVHGVMC---DVRHREEVTHLADEafrl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGA-IINMASVASSVKGvSNRFVYGLT 151
Cdd:PRK05876  81 LGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGhVVFTASFAGLVPN-AGLGAYGVA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489055331 152 KAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQG 194
Cdd:PRK05876 160 KYGVVGLAETLAREVTADGIGVSVLCPMVVETNLVANSERIRG 202
PRK09072 PRK09072
SDR family oxidoreductase;
3-172 4.48e-18

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 80.76  E-value: 4.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL----EGIAGIVTRRLDVL---DDAAVKALVAEIGQ 75
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALaarlPYPGRHRWVVADLTseaGREAVLARAREMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAV 155
Cdd:PRK09072  81 INVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSI-GYPGYASYCASKFAL 159

                        170
                 ....*....|....*..
gi 489055331 156 IGLTKAVAADYVGKGIR 172
Cdd:PRK09072 160 RGFSEALRRELADTGVR 176
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-183 5.31e-18

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: 79.86  E-value: 5.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVY-----ATDINADALAKLEGIAGIVTrrlDVLDDAAVKALVA----EIGQIDI 78
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGicardEARLAAAAAQELEGVLGLAG---DVRDEADVRRAVDameeAFGGLDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASsvkgvSNRF----VYGLTKAA 154
Cdd:cd08929   78 LVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAG-----KNAFkggaAYNASKFG 152

                        170       180
                 ....*....|....*....|....*....
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVES 183
Cdd:cd08929  153 LLGLSEAAMLDLREANIRVVNVMPGSVDT 181
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 5-237 5.43e-18

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: 79.93  E-value: 5.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EGIAGIVTRRLDVLDDAA--VKALVAEI--- 73
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVadhineEGGRQPQWFILDLLTCTSenCQQLAQRIavn 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 -GQIDILFNCAGFVHNGTILEMKDEElDFA----VNLNVRSMIrtIRAVLPGMLERKDGAIInMASVASSVKGVSNRFVY 148
Cdd:cd05340   82 yPRLDGVLHNAGLLGDVCPLSEQNPQ-VWQdv*qVNVNATFML--TQALLPLLLKSDAGSLV-FTSSSVGRQGRANWGAY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 149 GLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPslqdrLRAQgdyeaaraAFIARQPIgRIGQPEEIADLAVYLAG- 227
Cdd:cd05340  158 AVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTA-----MRAS--------AFPTEDPQ-KLKTPADIMPLYLWLMGd 223

                        250
                 ....*....|.
gi 489055331 228 -ATYTTGQAYN 237
Cdd:cd05340  224 dSRRKTGMTFD 234
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 5-241 6.35e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 80.49  E-value: 6.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDI-------NADALAKLEGIAGIVTR---------RLDVLDDAA--V 66
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsASGGSAAQAVVDEIVAAggeavangdDIADWDGAAnlV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  67 KALVAEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIR-AVLPGMLERKDG-----AIINMASvASSVK 140
Cdd:PRK07791  84 DAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRhAAAYWRAESKAGravdaRIINTSS-GAGLQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 141 GVSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAIcpgtveSPSLQDRLRaqgdyEAARAAFIARQPIGRIG--QPEEI 218
Cdd:PRK07791 163 GSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAI------APAARTRMT-----ETVFAEMMAKPEEGEFDamAPENV 231

                        250       260
                 ....*....|....*....|....*
gi 489055331 219 ADLAVYLAGA--TYTTGQAYNIDGG 241
Cdd:PRK07791 232 SPLVVWLGSAesRDVTGKVFEVEGG 256
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 12-226 6.67e-18

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 79.73  E-value: 6.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  12 VTAAGQGIGQASALAFAEAGAKVYATDINADALAKL---------EGIAGIVtrrlDVLDDAAVKAL----VAEIGQIDI 78
Cdd:cd05360    5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELarevrelggEAIAVVA----DVADAAQVERAadtaVERFGRIDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVYGLTKAAVIGL 158
Cdd:cd05360   81 WVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGY-RSAPLQAAYSASKHAVRGF 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055331 159 TKAVAADYV--GKGIRCNAICPGTVESPSlqdrlraqgdYEAARAAFIAR-QPIGRIGQPEEIADLAVYLA 226
Cdd:cd05360  160 TESLRAELAhdGAPISVTLVQPTAMNTPF----------FGHARSYMGKKpKPPPPIYQPERVAEAIVRAA 220
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-178 1.25e-17

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 80.21  E-value: 1.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDI--NADALAKLEGIAGIVTRRL----DVLDDAAVKALVA--- 71
Cdd:PRK07792   6 NTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVasALDASDVLDEIRAAGAKAVavagDISQRATADELVAtav 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKD-------GAIINMASVASSVkGVSN 144
Cdd:PRK07792  86 GLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKaaggpvyGRIVNTSSEAGLV-GPVG 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489055331 145 RFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICP 178
Cdd:PRK07792 165 QANYGAAKAGITALTLSAARALGRYGVRANAICP 198
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 5-183 1.38e-17

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: 79.17  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EGIAGIVTRRLDVLDDAAVKALVAEI----G 74
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVksecleLGAPSPHVVPLDMSDLEDAEQVVEEAlklfG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAA 154
Cdd:cd05332   81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKI-GVPFRTAYAASKHA 159

                        170       180
                 ....*....|....*....|....*....
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVES 183
Cdd:cd05332  160 LQGFFDSLRAELSEPNISVTVVCPGLIDT 188
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 10-238 3.18e-17

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: 76.79  E-value: 3.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGA-KVYATDinadalaklegiagivtrRLDVLddaavkalvaeigqidilFNCAGFVHN 88
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLVVS------------------RRDVV------------------VHNAAILDD 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  89 GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAVIGLTKAVAADYVG 168
Cdd:cd02266   45 GRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLF-GAPGLGGYAASKAALDGLAQQWASEGWG 123

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 169 KGIRCNAICPGTVESPSLQDRLraqgdyEAARAAFIARQPIGRIGQPEEIADlAVYLAGATYTTGQAYNI 238
Cdd:cd02266  124 NGLPATAVACGTWAGSGMAKGP------VAPEEILGNRRHGVRTMPPEEVAR-ALLNALDRPKAGVCYII 186
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 4-208 3.61e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 78.47  E-value: 3.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGIAGIVTRRLDVLDDAAVKALVAEI----GQ 75
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELaalaAELGGDDRVLTVVADVTDLAAMQAAAEEAverfGG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKdGAIINMASVAS--SVKGVSnrfVYGLTKA 153
Cdd:PRK05872  86 IDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAfaAAPGMA---AYCASKA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDrlrAQGDYEAARaAFIARQP 208
Cdd:PRK05872 162 GVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRD---ADADLPAFR-ELRARLP 212
PRK06123 PRK06123
SDR family oxidoreductase;
8-241 6.13e-17

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 77.13  E-value: 6.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGakvYATDIN-------ADAL-AKLEGIAGI-VTRRLDVLDDAAVKALVA----EIG 74
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERG---YAVCLNylrnrdaAEAVvQAIRRQGGEaLAVAADVADEADVLRLFEavdrELG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILE-MKDEELDFAVNLNVRSMIRTIRAVLPGMLER---KDGAIINMASVASSVKGVSNRFVYGL 150
Cdd:PRK06123  80 RLDALVNNAGILEAQMRLEqMDAARLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGEYIDYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 151 TKAAV----IGLTKAVAADyvgkGIRCNAICPGTVESpslqdRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLA 226
Cdd:PRK06123 160 SKGAIdtmtIGLAKEVAAE----GIRVNAVRPGVIYT-----EIHASGGEPGRVDRVKAGIPMGRGGTAEEVARAILWLL 230

                        250
                 ....*....|....*..
gi 489055331 227 G--ATYTTGQAYNIDGG 241
Cdd:PRK06123 231 SdeASYTTGTFIDVSGG 247
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-181 6.18e-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: 77.49  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATdiNADALAKLEGIAGIVT--------RRLDVLDDAAVKALVAEI--- 73
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYIT--GRTILPQLPGTAEEIEarggkcipVRCDHSDDDEVEALFERVare 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 --GQIDILFNCAgFVHNGTIL--------EMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMasvaSSVKGVS 143
Cdd:cd09763   79 qqGRLDILVNNA-YAAVQLILvgvakpfwEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVII----SSTGGLE 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489055331 144 NRF--VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTV 181
Cdd:cd09763  154 YLFnvAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFV 193
PRK06947 PRK06947
SDR family oxidoreductase;
6-241 1.73e-16

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 76.00  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKV---YATDINA---------DALAKLEGIAGIVTRRLDVLddAAVKALVAEI 73
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVginYARDAAAaeetadavrAAGGRACVVAGDVANEADVI--AMFDAVQSAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVhnGTILEMKDEELD-----FAVN-----LNVRSMIRTIRAVLPGmlerKDGAIINMASVASSVkGVS 143
Cdd:PRK06947  79 GRLDALVNNAGIV--APSMPLADMDAArlrrmFDTNvlgayLCAREAARRLSTDRGG----RGGAIVNVSSIASRL-GSP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 144 NRFV-YGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLA 222
Cdd:PRK06947 152 NEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIET-----EIHASGGQPGRAARLGAQTPLGRAGEADEVAETI 226

                        250       260
                 ....*....|....*....|.
gi 489055331 223 VYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK06947 227 VWLLSdaASYVTGALLDVGGG 247
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-241 3.77e-16

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 74.80  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE------GIAGIVTRRLDVLDDA-AVKALVAEI-GQ 75
Cdd:PRK05786   2 RLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKktlskyGNIHYVVGDVSSTESArNVIEKAAKVlNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKdeELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASSVKGVSNRFVYGLTKAAV 155
Cdd:PRK05786  82 IDGLVVTVGGYVEDTVEEFS--GLEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIYKASPDQLSYAVAKAGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGTVESPSLQDR----LRAQGDYEAAraafiarqpigrigqPEEIADLAVYLAG--AT 229
Cdd:PRK05786 158 AKAVEILASELLGRGIRVNGIAPTTISGDFEPERnwkkLRKLGDDMAP---------------PEDFAKVIIWLLTdeAD 222

                        250
                 ....*....|..
gi 489055331 230 YTTGQAYNIDGG 241
Cdd:PRK05786 223 WVDGVVIPVDGG 234
PRK05717 PRK05717
SDR family oxidoreductase;
6-243 7.60e-16

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 74.54  E-value: 7.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAG----IVTrrLDVLDDAAVKALVAEI----GQID 77
Cdd:PRK05717   9 NGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGenawFIA--MDVADEAQVAAGVAEVlgqfGRLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 ILFNCAGFV--HNGTI--LEMKDEELDFAVNLNVRSMIRTIRAvlpGMLERKDGAIINMASVASSvKGVSNRFVYGLTKA 153
Cdd:PRK05717  87 ALVCNAAIAdpHNTTLesLSLAHWNRVLAVNLTGPMLLAKHCA---PYLRAHNGAIVNLASTRAR-QSEPDTEAYAASKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADyVGKGIRCNAICPGTVESpslqdRLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYT 231
Cdd:PRK05717 163 GLLALTHALAIS-LGPEIRVNAVSPGWIDA-----RDPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSrqAGFV 236

                        250
                 ....*....|..
gi 489055331 232 TGQAYNIDGGWS 243
Cdd:PRK05717 237 TGQEFVVDGGMT 248
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-226 9.27e-16

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: 74.18  E-value: 9.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVY--------ATDINADALAKLEGiAGIVTRRLDVLD----DAAVKALVAEIG 74
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIiacrneekGEEAAAEIKKETGN-AKVEVIQLDLSSlasvRQFAEEFLARFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTiLEMKDE-ELDFAVN------LNvrsmirtiRAVLPGMLERKDGAIINMASVASSV-------- 139
Cdd:cd05327   80 RLDILINNAGIMAPPR-RLTKDGfELQFAVNylghflLT--------NLLLPVLKASAPSRIVNVSSIAHRAgpidfndl 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 140 -----KGVSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARaAFIARqpigrigQ 214
Cdd:cd05327  151 dlennKEYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLR-PFLKK-------S 222

                        250
                 ....*....|..
gi 489055331 215 PEEIADLAVYLA 226
Cdd:cd05327  223 PEQGAQTALYAA 234
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
5-244 1.09e-15

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 73.82  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVT--AAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRR----LDVLDDAAVKALVAEI----G 74
Cdd:PRK07533   8 LAGKRGLVVgiANEQSIAWGCARAFRALGAELAVTYLNDKARPYVEPLAEELDAPiflpLDVREPGQLEAVFARIaeewG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGF-----VHnGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASSvKGVSNRFVYG 149
Cdd:PRK07533  88 RLDFLLHSIAFapkedLH-GRVVDCSREGFALAMDVSCHSFIRMARLAEPLM--TNGGSLLTMSYYGAE-KVVENYNLMG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdrlRAQ---GDYEAARAAFIARQPIGRIGQPEEIADLAVYLA 226
Cdd:PRK07533 164 PVKAALESSVRYLAAELGPKGIRVHAISPGPLKT-------RAAsgiDDFDALLEDAAERAPLRRLVDIDDVGAVAAFLA 236

                        250       260
                 ....*....|....*....|
gi 489055331 227 --GATYTTGQAYNIDGGWSI 244
Cdd:PRK07533 237 sdAARRLTGNTLYIDGGYHI 256
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 7-244 1.37e-15

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: 73.77  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVT--AAGQGIGQASALAFAEAGAKV---YATDINADALAKL----EGIAGIVtrRLDVLDDAAVKALVAEI---- 73
Cdd:cd05372    1 GKRILITgiANDRSIAWGIAKALHEAGAELaftYQPEALRKRVEKLaerlGESALVL--PCDVSNDEEIKELFAEVkkdw 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVHN----GTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASSvKGVSNRFVYG 149
Cdd:cd05372   79 GKLDGLVHSIAFAPKvqlkGPFLDTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYLGSE-RVVPGYNVMG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSlqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG-- 227
Cdd:cd05372  156 VAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLA----ASGITGFDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSdl 231

                        250
                 ....*....|....*..
gi 489055331 228 ATYTTGQAYNIDGGWSI 244
Cdd:cd05372  232 SSGITGEIIYVDGGYHI 248
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 7-241 5.04e-15

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: 72.11  E-value: 5.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD-ALAKLEGIAG-----IVTRRLDVLDDAAVKALVAEI----GQI 76
Cdd:cd05322    2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSEnAEKVADEINAeygekAYGFGADATNEQSVIALSKGVdeifKRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERK-DGAIINMASVASSVkGVSNRFVYGLTKAAV 155
Cdd:cd05322   82 DLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKV-GSKHNSGYSAAKFGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 156 IGLTKAVAADYVGKGIRCNAICPGT-VESPSLQDRLRAQG-----DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG-- 227
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGNlLKSPMFQSLLPQYAkklgiKESEVEQYYIDKVPLKRGCDYQDVLNMLLFYASpk 240

                        250
                 ....*....|....
gi 489055331 228 ATYTTGQAYNIDGG 241
Cdd:cd05322  241 ASYCTGQSINITGG 254
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 5-241 8.44e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 71.64  E-value: 8.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGA---------------KVYATDINADAL----AKLEGIAGIvtrrlDVLDDAA 65
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGAlvaihygnrkeeaeeTVYEIQSNGGSAfsigANLESLHGV-----EALYSSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  66 VKALVAEIG--QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINMASVASSVKgVS 143
Cdd:PRK12747  77 DNELQNRTGstKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRIS-LP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 144 NRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPS----LQDRLRAQgdYEAARAAFiarqpiGRIGQPEEIA 219
Cdd:PRK12747 154 DFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMnaelLSDPMMKQ--YATTISAF------NRLGEVEDIA 225

                        250       260
                 ....*....|....*....|....
gi 489055331 220 DLAVYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK12747 226 DTAAFLASpdSRWVTGQLIDVSGG 249
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 5-199 8.68e-15

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 73.03  E-value: 8.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILF 80
Cdd:COG3347  423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAaaaeLGGGYGADAVDATDVDVTAEAAVAAAFGFAGLDI 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHN--GTILEMKDEELDFAVNLNVRSMIRT-----IRAVLPGMLERKDGAIINMASVASSVKGVSNRFVYGLTKA 153
Cdd:COG3347  503 GGSDIGVAnaGIASSSPEEETRLSFWLNNFAHLSTgqflvARAAFQGTGGQGLGGSSVFAVSKNAAAAAYGAAAAATAKA 582

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAA 199
Cdd:COG3347  583 AAQHLLRALAAEGGANGINANRVNPDAVLDGSAIWASAARAERAAA 628
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 5-237 8.70e-15

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 71.44  E-value: 8.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINadaLAKLEGI-----------AGIVTRRLDVLDDAAVKALVAEI 73
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRT---EEKLEAVydeieaaggpqPAIIPLDLLTATPQNYQQLADTI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 ----GQIDilfncaGFVHNGTIL------EMKDEEL-DFAVNLNVRSMIRTIRAVLPGMLERKDGAIInmaSVASSV--K 140
Cdd:PRK08945  87 eeqfGRLD------GVLHNAGLLgelgpmEQQDPEVwQDVMQVNVNATFMLTQALLPLLLKSPAASLV---FTSSSVgrQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 141 GVSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdRLRAQgdyeaaraAFIARQPiGRIGQPEEIAD 220
Cdd:PRK08945 158 GRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT-----AMRAS--------AFPGEDP-QKLKTPEDIMP 223

                        250
                 ....*....|....*....
gi 489055331 221 LAVYLAG--ATYTTGQAYN 237
Cdd:PRK08945 224 LYLYLMGddSRRKNGQSFD 242
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
29-241 1.12e-14

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 70.80  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  29 EAGAKVYATDINADALakleGIAGIVtrRLDVLDDAAVKALVAEI-GQIDILFNCAGFVHNGtilemkDEELDFAVN-LN 106
Cdd:PRK12428   7 FLGARVIGVDRREPGM----TLDGFI--QADLGDPASIDAAVAALpGRIDALFNIAGVPGTA------PVELVARVNfLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 107 VRSMIRtirAVLPGMleRKDGAIINMASVASS--------------------------VKGVSNRFVYGLTKAAVIGLT- 159
Cdd:PRK12428  75 LRHLTE---ALLPRM--APGGAIVNVASLAGAewpqrlelhkalaatasfdegaawlaAHPVALATGYQLSKEALILWTm 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 160 KAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDyeaARAAFIARqPIGRIGQPEEIADLAVYLA--GATYTTGQAYN 237
Cdd:PRK12428 150 RQAQPWFGARGIRVNCVAPGPVFTPILGDFRSMLGQ---ERVDSDAK-RMGRPATADEQAAVLVFLCsdAARWINGVNLP 225


                 ....
gi 489055331 238 IDGG 241
Cdd:PRK12428 226 VDGG 229
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 8-181 4.40e-14

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: 69.41  E-value: 4.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGA---KVYATDINADALAKLEGIAG------IVTRRLDVLDDAAVKALVAEI--GQI 76
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASDPSkrfKVYATMRDLKKKGRLWEAAGalaggtLETLQLDVCDSKSVAAAVERVteRHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVI 156
Cdd:cd09806   81 DVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVG-GLQGLPFNDVYCASKFALE 159

                        170       180
                 ....*....|....*....|....*
gi 489055331 157 GLTKAVAADYVGKGIRCNAICPGTV 181
Cdd:cd09806  160 GLCESLAVQLLPFNVHLSLIECGPV 184
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 9-234 4.80e-14

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: 69.24  E-value: 4.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVTAAGQGIGQASALAFAEAG--AKVYATDINADALAKLEGIAG----IVTRRLDVLDDAAVKALVAEI----GQIDI 78
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELRpglrVTTVKADLSDAAGVEQLLEAIrkldGERDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFV-HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGM-LERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVI 156
Cdd:cd05367   81 LINNAGSLgPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFkKRGLKKTVVNVSSGA-AVNPFKGWGLYCSSKAARD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055331 157 GLTKAVAADYvgKGIRCNAICPGTVESPsLQDRLRAQGDYEAARAAFIARQPIGRIGQPEEIAD-LAVYLAGATYTTGQ 234
Cdd:cd05367  160 MFFRVLAAEE--PDVRVLSYAPGVVDTD-MQREIRETSADPETRSRFRSLKEKGELLDPEQSAEkLANLLEKDKFESGA 235
PRK08219 PRK08219
SDR family oxidoreductase;
8-220 1.04e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 68.04  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAgAKVYATDINADALAKL-EGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGFV 86
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELaAELPGATPFPVDLTDPEAIAAAVEQLGRLDVLVHNAGVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  87 HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAI-INMASVASSVKGVSnrfVYGLTKAAVIGLTKAVAAD 165
Cdd:PRK08219  83 DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVfINSGAGLRANPGWG---SYAASKFALRALADALREE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489055331 166 YVGKgIRCNAICPGTVESPsLQDRLRAQ--GDYEAARaaFIarqpigrigQPEEIAD 220
Cdd:PRK08219 160 EPGN-VRVTSVHPGRTDTD-MQRGLVAQegGEYDPER--YL---------RPETVAK 203
PRK08340 PRK08340
SDR family oxidoreductase;
11-240 3.64e-13

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 67.14  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  11 LVTAAGQGIGQASALAFAEAGAKVYATDINADALAK----LEGIAGIVTRRLDVLDDAAVKALVAE----IGQIDILFNC 82
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKalkeLKEYGEVYAVKADLSDKDDLKNLVKEawelLGGIDALVWN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  83 AG-------FVHNGTILEMKDEELDFAVnlnVRSMIRTIraVLPGMLERK-DGAIINMASVasSVKGVSNRFVYG-LTKA 153
Cdd:PRK08340  84 AGnvrcepcMLHEAGYSDWLEAALLHLV---APGYLTTL--LIQAWLEKKmKGVLVYLSSV--SVKEPMPPLVLAdVTRA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDY------EAARAAFIARQPIGRIGQPEEIADLAVYLAG 227
Cdd:PRK08340 157 GLVQLAKGVSRTYGGKGIRAYTVLLGSFDTPGARENLARIAEErgvsfeETWEREVLERTPLKRTGRWEELGSLIAFLLS 236

                        250
                 ....*....|....*
gi 489055331 228 --ATYTTGQAYNIDG 240
Cdd:PRK08340 237 enAEYMLGSTIVFDG 251
PRK12744 PRK12744
SDR family oxidoreductase;
5-243 1.09e-12

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 65.53  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN-----ADALAKLEGI----AGIVTRRLDVLDDAAVKAL----VA 71
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNsaaskADAEETVAAVkaagAKAVAFQADLTTAAAVEKLfddaKA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVlpGMLERKDGAIInmaSVASSVKGVSNRF--VYG 149
Cdd:PRK12744  86 AFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEA--GRHLNDNGKIV---TLVTSLLGAFTPFysAYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSL--QDRLRAQGdYEAARAAFIARQPIGrIGQPEEIADLAVYLA- 226
Cdd:PRK12744 161 GSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFypQEGAEAVA-YHKTAAALSPFSKTG-LTDIEDIVPFIRFLVt 238

                        250
                 ....*....|....*..
gi 489055331 227 GATYTTGQAYNIDGGWS 243
Cdd:PRK12744 239 DGWWITGQTILINGGYT 255
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
5-244 1.52e-12

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 65.54  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALV--TAAGQGIGQASALAFAEAGAKVYATDINaDALAK-LEGIAGIVTRR----LDVLDDAAVKALVAEI---- 73
Cdd:PRK08415   3 MKGKKGLIvgVANNKSIAYGIAKACFEQGAELAFTYLN-EALKKrVEPIAQELGSDyvyeLDVSKPEHFKSLAESLkkdl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVH----NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMlerKDGAIINMASVASSVKGVSNRFVYG 149
Cdd:PRK08415  82 GKIDFIVHSVAFAPkealEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL---NDGASVLTLSYLGGVKYVPHYNVMG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdrLRAQG--DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG 227
Cdd:PRK08415 159 VAKAALESSVRYLAVDLGKKGIRVNAISAGPIKT------LAASGigDFRMILKWNEINAPLKKNVSIEEVGNSGMYLLS 232

                        250
                 ....*....|....*....
gi 489055331 228 --ATYTTGQAYNIDGGWSI 244
Cdd:PRK08415 233 dlSSGVTGEIHYVDAGYNI 251
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 2.08e-12

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 64.75  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALV--TAAGQGIGQASALAFAEAGAKV---YATDINADALAKL----EGIAGIVTRrLDVLDDAAVKALVA 71
Cdd:PRK08594   1 MMLSLEGKTYVVmgVANKRSIAWGIARSLHNAGAKLvftYAGERLEKEVRELadtlEGQESLLLP-CDVTSDEEITACFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  72 EI----GQIDILFNCAGFVH----NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLErkDGAIINMASVASSvKGVS 143
Cdd:PRK08594  80 TIkeevGVIHGVAHCIAFANkedlRGEFLETSRDGFLLAQNISAYSLTAVAREAKKLMTE--GGSIVTLTYLGGE-RVVQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 144 NRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSlqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAV 223
Cdd:PRK08594 157 NYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLS----AKGVGGFNSILKEIEERAPLRRTTTQEEVGDTAA 232

                        250       260
                 ....*....|....*....|...
gi 489055331 224 YLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK08594 233 FLFSdlSRGVTGENIHVDSGYHI 255
PRK08278 PRK08278
SDR family oxidoreductase;
5-239 2.18e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 64.92  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEG----IAGIVTRR--------LDVLDDAAVKALVAE 72
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKLPGtihtAAEEIEAAggqalplvGDVRDEDQVAAAVAK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 ----IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMA-SVASSVKGVSNRFV 147
Cdd:PRK08278  84 averFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSpPLNLDPKWFAPHTA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 148 YGLTKAAVIGLTKAVAADYVGKGIRCNAICPGT-VESPSLQDRLRAQGDYEAARAafiarqpigrigqPEEIAD--LAVY 224
Cdd:PRK08278 164 YTMAKYGMSLCTLGLAEEFRDDGIAVNALWPRTtIATAAVRNLLGGDEAMRRSRT-------------PEIMADaaYEIL 230

                        250
                 ....*....|....*
gi 489055331 225 LAGATYTTGQAYnID 239
Cdd:PRK08278 231 SRPAREFTGNFL-ID 244
PRK06101 PRK06101
SDR family oxidoreductase;
9-189 3.09e-12

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 64.12  E-value: 3.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGI-AGIVTRRLDVLDDAAVKALVAEIGQI--DILFNcAG- 84
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTQsANIFTLAFDVTDHPGTKAALSQLPFIpeLWIFN-AGd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  85 --FVHNGTIlemkDEELDFAV-NLNVRSMIRTIRAVLPgMLERKDGAIInMASVASSVkGVSNRFVYGLTKAAVIGLTKA 161
Cdd:PRK06101  82 ceYMDDGKV----DATLMARVfNVNVLGVANCIEGIQP-HLSCGHRVVI-VGSIASEL-ALPRAEAYGASKAAVAYFART 154

                        170       180
                 ....*....|....*....|....*...
gi 489055331 162 VAADYVGKGIRCNAICPGTVESPsLQDR 189
Cdd:PRK06101 155 LQLDLRPKGIEVVTVFPGFVATP-LTDK 181
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 5-239 3.90e-12

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: 64.00  E-value: 3.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEG----------------IAGIVTRRLDVLDDAAVKA 68
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGtiytaaeeieaaggkaLPCIVDIRDEDQVRAAVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  69 LVAEIGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAS-SVKGVSNRFV 147
Cdd:cd09762   81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNlNPKWFKNHTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 148 YGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGDYEAARaafiarqpigrigQPEEIADLA--VYL 225
Cdd:cd09762  161 YTMAKYGMSMCVLGMAEEFKPGGIAVNALWPRTAIATAAMNMLGGVDVAACCR-------------KPEIMADAAyaILT 227

                        250
                 ....*....|....
gi 489055331 226 AGATYTTGQAYnID 239
Cdd:cd09762  228 KPSSEFTGNFL-ID 240
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-171 4.74e-12

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 64.50  E-value: 4.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALA----KLEGIAGIVTRRLDVLD-----DAAVKALVAEIGQID 77
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKdvsdSIQSKYSKTQIKTVVVDfsgdiDEGVKRIKETIEGLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  78 --ILFN-------CAGFVHngtilEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSNRF-V 147
Cdd:PLN02780 133 vgVLINnvgvsypYARFFH-----EVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDPLYaV 207

                        170       180
                 ....*....|....*....|....
gi 489055331 148 YGLTKAAVIGLTKAVAADYVGKGI 171
Cdd:PLN02780 208 YAATKAYIDQFSRCLYVEYKKSGI 231
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 10-239 4.83e-12

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 62.98  E-value: 4.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDINADALAklegiagivtrrLDVLDDAAVKALVAEIGQIDILFNCAGFVHNG 89
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQ------------VDITDEASIKALFEKVGHFDAIVSTAGDAEFA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  90 TILEMKDEELDFAVNLNVRSMIRTIRAVLPGMlerKDGAIINMASVASSVKGVSNRFVYGLTKAAVIGLTKAVAADyVGK 169
Cdd:cd11731   69 PLAELTDADFQRGLNSKLLGQINLVRHGLPYL---NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIE-LPR 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 170 GIRCNAICPGTVESPslqdrLRAQGDYEAARAAfiarqpigriGQPEEIADLAVYLAGATYtTGQAYNID 239
Cdd:cd11731  145 GIRINAVSPGVVEES-----LEAYGDFFPGFEP----------VPAEDVAKAYVRSVEGAF-TGQVLHVD 198
PRK06482 PRK06482
SDR family oxidoreductase;
7-179 5.58e-12

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 63.98  E-value: 5.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRR--LDVLDDAAVKALV----AEIGQIDILF 80
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVlqLDVTDSAAVRAVVdrafAALGRIDVVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVK--GVSnrfVYGLTKAAVIGL 158
Cdd:PRK06482  82 SNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAypGFS---LYHATKWGIEGF 158

                        170       180
                 ....*....|....*....|.
gi 489055331 159 TKAVAADYVGKGIRCNAICPG 179
Cdd:PRK06482 159 VEAVAQEVAPFGIEFTIVEPG 179
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 4-226 1.17e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 63.40  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-EGIAGIVTRRL----DVLDDAAVKA----LVAEIG 74
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALaAEIRAAGGEALavvaDVADAEAVQAaadrAEEELG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVYGLTKAA 154
Cdd:PRK07109  85 PIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAY-RSIPLQSAYCAAKHA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489055331 155 VIGLTKAVAADYV--GKGIRCNAICPGTVESPSLqDRLRAQGDYEAaraafiarQPIGRIGQPEEIADLAVYLA 226
Cdd:PRK07109 164 IRGFTDSLRCELLhdGSPVSVTMVQPPAVNTPQF-DWARSRLPVEP--------QPVPPIYQPEVVADAILYAA 228
PRK07024 PRK07024
SDR family oxidoreductase;
12-184 1.39e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 62.64  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  12 VTAAGQGIGQASALAFAEAGAKVYATDINADAL----AKLEGIAGIVTRRLDVLD----DAAVKALVAEIGQIDILFNCA 83
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGLVARRTDALqafaARLPKAARVSVYAADVRDadalAAAAADFIAAHGLPDVVIANA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 GfVHNGTILEMKdEELD-FA--VNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASsVKGVSNRFVYGLTKAAVIGLTK 160
Cdd:PRK07024  87 G-ISVGTLTEER-EDLAvFRevMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAG-VRGLPGAGAYSASKAAAIKYLE 163

                        170       180
                 ....*....|....*....|....
gi 489055331 161 AVAADYVGKGIRCNAICPGTVESP 184
Cdd:PRK07024 164 SLRVELRPAGVRVVTIAPGYIRTP 187
PRK05993 PRK05993
SDR family oxidoreductase;
8-183 2.98e-11

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 61.58  E-value: 2.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGiAGIVTRRLDVLDDAAVKALVAEI-----GQIDILFNC 82
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEA-EGLEAFQLDYAEPESIAALVAQVlelsgGRLDALFNN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  83 AGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINmasvASSVKGVSN---RFVYGLTKAAVIGLT 159
Cdd:PRK05993  84 GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQ----CSSILGLVPmkyRGAYNASKFAIEGLS 159

                        170       180
                 ....*....|....*....|....
gi 489055331 160 KAVAADYVGKGIRCNAICPGTVES 183
Cdd:PRK05993 160 LTLRMELQGSGIHVSLIEPGPIET 183
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 11-241 4.26e-11

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 60.72  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  11 LVTAAGQGIGQASALAFAEAGAKV---YATDinADALAKLEGiAGIVTRRLDVLDDAAVKALVAEIGQidilfNCAGF-- 85
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVivsYRTH--YPAIDGLRQ-AGAQCIQADFSTNAGIMAFIDELKQ-----HTDGLra 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 -VHNGTilEMKDEELDFAVNLNVRSMIR-------TIRAVLPGMLERKDGA---IINMAS-VASsvKGVSNRFVYGLTKA 153
Cdd:PRK06483  78 iIHNAS--DWLAEKPGAPLADVLARMMQihvnapyLLNLALEDLLRGHGHAasdIIHITDyVVE--KGSDKHIAYAASKA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 154 AVIGLTKAVAADYVGKgIRCNAICPGTVespslqdrLRAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAGATYTTG 233
Cdd:PRK06483 154 ALDNMTLSFAAKLAPE-VKVNSIAPALI--------LFNEGDDAAYRQKALAKSLLKIEPGEEEIIDLVDYLLTSCYVTG 224


                 ....*...
gi 489055331 234 QAYNIDGG 241
Cdd:PRK06483 225 RSLPVDGG 232
PRK06139 PRK06139
SDR family oxidoreductase;
1-188 4.42e-11

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 61.66  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL-----EGIAGIVTRRLDVLDDAAVKALVAE--- 72
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVaeecrALGAEVLVVPTDVTDADQVKALATQaas 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  73 -IGQIDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvkgVSNRF--VYG 149
Cdd:PRK06139  81 fGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGF---AAQPYaaAYS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGK-GIRCNAICPGTVESPSLQD 188
Cdd:PRK06139 158 ASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTPGFRH 197
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 9-225 6.95e-11

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: 60.47  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVTAAGQGIGQASALAFAEAGAKV-YATDINADALAKLEGIA-----GIVTRRLDVLDDAAVKALV----AEIGQIDI 78
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVaLAARREAKLEALLVDIIrdaggSAKAVPTDARDEDEVIALFdlieEEIGPLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVAsSVKGVSNRFVYGLTKAAVIGL 158
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATA-SLRGRAGFAAFAGAKFALRAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055331 159 TKAVAADYVGKGIR-CNAICPGTVESPSLQDRLRAQGDYEAARAafiarqpigrIGQPEEIADLAVYL 225
Cdd:cd05373  160 AQSMARELGPKGIHvAHVIIDGGIDTDFIRERFPKRDERKEEDG----------ILDPDAIAEAYWQL 217
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-238 1.58e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.99  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   9 TALVT-AAGQgIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAeigQIDILFNCAGFVH 87
Cdd:COG0451    1 RILVTgGAGF-IGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEALAAALA---GVDAVVHLAAPAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  88 NGtileMKDEELDFAVNlnvrsmIRTIRAVLPGMLERKDGAIINMASvaSSVKGVSNRFV-----------YGLTKAAVI 156
Cdd:COG0451   77 VG----EEDPDETLEVN------VEGTLNLLEAARAAGVKRFVYASS--SSVYGDGEGPIdedtplrpvspYGASKLAAE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 157 GLTKAVAADYvgkGIRCNAICPGTVESPslqdrlRAQGDYEAARAAFIARQPIGRIGQP---------EEIADLAVYLAG 227
Cdd:COG0451  145 LLARAYARRY---GLPVTILRPGNVYGP------GDRGVLPRLIRRALAGEPVPVFGDGdqrrdfihvDDVARAIVLALE 215

                        250
                 ....*....|.
gi 489055331 228 ATYTTGQAYNI 238
Cdd:COG0451  216 APAAPGGVYNV 226
PRK09291 PRK09291
SDR family oxidoreductase;
7-179 1.60e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 59.63  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYA--------TDINADalAKLEGIAgIVTRRLDVLDDAAVKAlvAEIGQIDI 78
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAgvqiapqvTALRAE--AARRGLA-LRVEKLDLTDAIDRAQ--AAEWDVDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGvSNRFVYGLTKAAVIGL 158
Cdd:PRK09291  77 LLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITG-PFTGAYCASKHALEAI 155

                        170       180
                 ....*....|....*....|.
gi 489055331 159 TKAVAADYVGKGIRCNAICPG 179
Cdd:PRK09291 156 AEAMHAELKPFGIQVATVNPG 176
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 7-183 2.57e-10

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 59.02  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYatdINADALAKLEGIAG----------IVTRRLDVLDDAAVKALVAEI--- 73
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVI---MACRDMAKCEEAAAeirrdtlnheVIVRHLDLASLKSIRAFAAEFlae 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 -GQIDILFNCAGFVHNGTILEMKDEELDFAVNlNVRSMIRTIraVLPGMLERKDGA-IINMASVA-----------SSVK 140
Cdd:cd09807   78 eDRLDVLINNAGVMRCPYSKTEDGFEMQFGVN-HLGHFLLTN--LLLDLLKKSAPSrIVNVSSLAhkagkinfddlNSEK 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489055331 141 GVSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVES 183
Cdd:cd09807  155 SYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
5-244 6.72e-10

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 57.80  E-value: 6.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVT--AAGQGIGQASALAFAEAGAKVYATDInADALAKLEGIAGIVTRRL--------DVLDDAAVKALVAEI- 73
Cdd:PRK07370   4 LTGKKALVTgiANNRSIAWGIAQQLHAAGAELGITYL-PDEKGRFEKKVRELTEPLnpslflpcDVQDDAQIEETFETIk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 ---GQIDILFNCAGFVH----NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLErkDGAIINMASVASsVKGVSNRF 146
Cdd:PRK07370  83 qkwGKLDILVHCLAFAGkeelIGDFSATSREGFARALEISAYSLAPLCKAAKPLMSE--GGSIVTLTYLGG-VRAIPNYN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 147 VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPG---TVESPSLQDRLRAQGDYEaaraafiARQPIGRIGQPEEIADLAV 223
Cdd:PRK07370 160 VMGVAKAALEASVRYLAAELGPKNIRVNAISAGpirTLASSAVGGILDMIHHVE-------EKAPLRRTVTQTEVGNTAA 232

                        250       260
                 ....*....|....*....|...
gi 489055331 224 YLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK07370 233 FLLSdlASGITGQTIYVDAGYCI 255
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 7-184 1.43e-09

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: 56.18  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKlegiAGIVTRRLDVLDDAA--VKALVAEI-GQIDILFNCA 83
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEAD----ASIIVLDSDSFTEQAkqVVASVARLsGKVDALICVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  84 GFVHNGTILEMKD-EELDFAVNLNVRSMIRTIRAVLPGMLErkdGAIINMASVASSVKGVSNRFVYGLTKAAVIGLTKAV 162
Cdd:cd05334   77 GGWAGGSAKSKSFvKNWDLMWKQNLWTSFIASHLATKHLLS---GGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSL 153

                        170       180
                 ....*....|....*....|....
gi 489055331 163 AADYVGK--GIRCNAICPGTVESP 184
Cdd:cd05334  154 AAENSGLpaGSTANAILPVTLDTP 177
PRK08017 PRK08017
SDR family oxidoreductase;
8-195 1.83e-09

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 56.25  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE--GIAGIVtrrLDVLDDAAVKALVAEI-----GQIDILF 80
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNslGFTGIL---LDLDDPESVERAADEVialtdNRLYGLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVkGVSNRFVYGLTKAAVIGLTK 160
Cdd:PRK08017  80 NNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLI-STPGRGAYAASKYALEAWSD 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489055331 161 AVAADYVGKGIRCNAICPGTVESPSLQDRLRAQGD 195
Cdd:PRK08017 159 ALRMELRHSGIKVSLIEPGPIRTRFTDNVNQTQSD 193
PRK06196 PRK06196
oxidoreductase; Provisional
 3-84 2.31e-09

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 56.61  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   3 IRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINAD-ALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQ----ID 77
Cdd:PRK06196  22 HDLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDvAREALAGIDGVEVVMLDLADLESVRAFAERFLDsgrrID 101


                 ....*..
gi 489055331  78 ILFNCAG 84
Cdd:PRK06196 102 ILINNAG 108
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-183 3.06e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 56.16  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAK-------LEGIAGIVTR--------RLDVLDDAA 65
Cdd:PRK08303   2 MMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTRARRSeydrpetIEETAELVTAaggrgiavQVDHLVPEQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  66 VKALVAEI----GQIDILFN--CAG---FVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVA 136
Cdd:PRK08303  82 VRALVERIdreqGRLDILVNdiWGGeklFEWGKPVWEHSLDKGLRMLRLAIDTHLITSHFALPLLIRRPGGLVVEITDGT 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489055331 137 SSVKGVSNR--FVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVES 183
Cdd:PRK08303 162 AEYNATHYRlsVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRS 210
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 10-184 4.19e-09

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 54.84  E-value: 4.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGFVHNG 89
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARPADVAAELEVWALAQELGPLDLLVYAAGAILGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  90 TILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSVKGVSnrfVYGLTKAAVIGLTKAVAADYvgK 169
Cdd:cd11730   81 PLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPELVMLPGLS---AYAAAKAALEAYVEVARKEV--R 155

                        170
                 ....*....|....*
gi 489055331 170 GIRCNAICPGTVESP 184
Cdd:cd11730  156 GLRLTLVRPPAVDTG 170
PRK08703 PRK08703
SDR family oxidoreductase;
5-184 1.27e-08

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 53.78  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKL------EGIAGIVTRRLDVLD--DAAVKALVAEI--- 73
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVydaiveAGHPEPFAIRFDLMSaeEKEFEQFAATIaea 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 --GQIDILFNCAGFVHngTILEMKDEELDFAVN---LNVRSMIRTIRAVLPGMLERKDGAII----NMASVASSVKGvsn 144
Cdd:PRK08703  84 tqGKLDGIVHCAGYFY--ALSPLDFQTVAEWVNqyrINTVAPMGLTRALFPLLKQSPDASVIfvgeSHGETPKAYWG--- 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489055331 145 rfVYGLTKAAVIGLTKAVAADYVGKG-IRCNAICPGTVESP 184
Cdd:PRK08703 159 --GFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSP 197
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
5-244 2.75e-08

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 53.05  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTA--AGQGIGQASALAFAEAGAKVYATDINADALAKLEGIA----GIVTRRLDVLDDAAVKALVAEIGQ--- 75
Cdd:PRK08690   4 LQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVVDKLEERVRKMAaeldSELVFRCDVASDDEINQVFADLGKhwd 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 -IDILFNCAGFVH----NGTILE-MKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGAIINMaSVASSVKGVSNRFVYG 149
Cdd:PRK08690  84 gLDGLVHSIGFAPkealSGDFLDsISREAFNTAHEISAYSLPALAKAARP-MMRGRNSAIVAL-SYLGAVRAIPNYNVMG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdrLRAQG--DYEAARAAFIARQPIGRIGQPEEIADLAVYLAG 227
Cdd:PRK08690 162 MAKASLEAGIRFTAACLGKEGIRCNGISAGPIKT------LAASGiaDFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLS 235

                        250
                 ....*....|....*....
gi 489055331 228 --ATYTTGQAYNIDGGWSI 244
Cdd:PRK08690 236 dlSSGITGEITYVDGGYSI 254
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
5-244 4.39e-08

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 52.32  E-value: 4.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVT--AAGQGIGQASALAFAEAGAKVYATdINADALAK-----LEGIAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:PRK06603   6 LQGKKGLITgiANNMSISWAIAQLAKKHGAELWFT-YQSEVLEKrvkplAEEIGCNFVSELDVTNPKSISNLFDDIkekw 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVH----NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMlerKDGAIINMASVASSVKGVSNRFVYG 149
Cdd:PRK06603  85 GSFDFLLHGMAFADknelKGRYVDTSLENFHNSLHISCYSLLELSRSAEALM---HDGGSIVTLTYYGAEKVIPNYNVMG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESPSLQdrlrAQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG-- 227
Cdd:PRK06603 162 VAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASS----AIGDFSTMLKSHAATAPLKRNTTQEDVGGAAVYLFSel 237

                        250
                 ....*....|....*..
gi 489055331 228 ATYTTGQAYNIDGGWSI 244
Cdd:PRK06603 238 SKGVTGEIHYVDCGYNI 254
PRK06953 PRK06953
SDR family oxidoreductase;
8-183 5.55e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 51.61  E-value: 5.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIaGIVTRRLDVLDDAAVKALVAEIG--QIDILFNCAGF 85
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQAL-GAEALALDVADPASVAGLAWKLDgeALDAAVYVAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 V--HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPgMLERKDGAIINMASVASSVKGV--SNRFVYGLTKAAVIGLTKA 161
Cdd:PRK06953  81 YgpRTEGVEPITREDFDAVMHTNVLGPMQLLPILLP-LVEAAGGVLAVLSSRMGSIGDAtgTTGWLYRASKAALNDALRA 159

                        170       180
                 ....*....|....*....|..
gi 489055331 162 VAADYvgKGIRCNAICPGTVES 183
Cdd:PRK06953 160 ASLQA--RHATCIALHPGWVRT 179
PRK06720 PRK06720
hypothetical protein; Provisional
 1-97 7.86e-08

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 50.74  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN-------ADALAKLEGIAGIVTRRLDVLDD--AAVKALVA 71
Cdd:PRK06720  10 MKMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDqesgqatVEEITNLGGEALFVSYDMEKQGDwqRVISITLN 89

                         90       100
                 ....*....|....*....|....*.
gi 489055331  72 EIGQIDILFNCAGFVHNGTILEMKDE 97
Cdd:PRK06720  90 AFSRIDMLFQNAGLYKIDSIFSRQQE 115
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 9.22e-08

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 51.67  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALV--TAAGQGIGQASALAFAEAGAKVyATDINADALAK-LEGIAGIVTRRL----DVLDDAAVKALVAEI 73
Cdd:PRK06505   1 MEGLMQGKRGLImgVANDHSIAWGIAKQLAAQGAEL-AFTYQGEALGKrVKPLAESLGSDFvlpcDVEDIASVDAVFEAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 ----GQIDILFNCAGFVHNGtilEMKDEELDFAVNLNVRSMI-----RTIRAVLPGMLERKDGAIINMaSVASSVKGVSN 144
Cdd:PRK06505  80 ekkwGKLDFVVHAIGFSDKN---ELKGRYADTTRENFSRTMViscfsFTEIAKRAAKLMPDGGSMLTL-TYGGSTRVMPN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 145 RFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVespslqdRLRAQGDYEAARAAFIARQ---PIGRIGQPEEIADL 221
Cdd:PRK06505 156 YNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPV-------RTLAGAGIGDARAIFSYQQrnsPLRRTVTIDEVGGS 228

                        250       260
                 ....*....|....*....|....*
gi 489055331 222 AVYLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK06505 229 ALYLLSdlSSGVTGEIHFVDSGYNI 253
PRK07984 PRK07984
enoyl-ACP reductase FabI;
5-244 2.60e-07

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 50.29  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVT--AAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRL----DVLDDAAVKALVAEIGQIDI 78
Cdd:PRK07984   4 LSGKRILVTgvASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIvlpcDVAEDASIDAMFAELGKVWP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNcaGFVHngTILEMKDEELD-----------FAVNLNVRS-----MIRTIRAVLpgmleRKDGAIINMASVASSvKGV 142
Cdd:PRK07984  84 KFD--GFVH--SIGFAPGDQLDgdyvnavtregFKIAHDISSysfvaMAKACRSML-----NPGSALLTLSYLGAE-RAI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 143 SNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdrLRAQG--DYEAARAAFIARQPIGRIGQPEEIAD 220
Cdd:PRK07984 154 PNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRT------LAASGikDFRKMLAHCEAVTPIRRTVTIEDVGN 227

                        250       260
                 ....*....|....*....|....*.
gi 489055331 221 LAVYLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK07984 228 SAAFLCSdlSAGISGEVVHVDGGFSI 253
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
5-244 5.31e-07

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 49.36  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALV--TAAGQGIGQASALAFAEAGAKVyATDINADALAK-----LEGIAGIVTRRLDVLDDAAVKALVAEI---- 73
Cdd:PRK08159   8 MAGKRGLIlgVANNRSIAWGIAKACRAAGAEL-AFTYQGDALKKrveplAAELGAFVAGHCDVTDEASIDAVFETLekkw 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 GQIDILFNCAGFVH----NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMlerKDGAIINMASVASSVKGVSNRFVYG 149
Cdd:PRK08159  87 GKLDFVVHAIGFSDkdelTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLM---TDGGSILTLTYYGAEKVMPHYNVMG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 150 LTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdrLRAQ--GDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG 227
Cdd:PRK08159 164 VAKAALEASVKYLAVDLGPKNIRVNAISAGPIKT------LAASgiGDFRYILKWNEYNAPLRRTVTIEEVGDSALYLLS 237

                        250
                 ....*....|....*....
gi 489055331 228 --ATYTTGQAYNIDGGWSI 244
Cdd:PRK08159 238 dlSRGVTGEVHHVDSGYHV 256
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 169-241 1.18e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 48.48  E-value: 1.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489055331 169 KGIRCNAICPGTVESPSLQDRLraQGDYEAARAAFIARQPIGRIGQPEEIADLAVYLAG--ATYTTGQAYNIDGG 241
Cdd:PRK06940 190 RGARINSISPGIISTPLAQDEL--NGPRGDGYRNMFAKSPAGRPGTPDEIAALAEFLMGprGSFITGSDFLVDGG 262
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-183 1.36e-06

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 47.79  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALV--TAAGQGIGQASALAFAEAGAKV---YATDINADALAKLEGiAGIVTRRLDVLDDAAVKALVAEI-- 73
Cdd:PRK06079   1 MSGILSGKKIVVmgVANKRSIAWGCAQAIKDQGATViytYQNDRMKKSLQKLVD-EEDLLVECDVASDESIERAFATIke 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  74 --GQIDilfncaGFVH----------NGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMlerKDGAIINMASVASSVKG 141
Cdd:PRK06079  80 rvGKID------GIVHaiayakkeelGGNVTDTSRDGYALAQDISAYSLIAVAKYARPLL---NPGASIVTLTYFGSERA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489055331 142 VSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVES 183
Cdd:PRK06079 151 IPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKT 192
PRK08177 PRK08177
SDR family oxidoreductase;
8-165 3.89e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 46.56  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTRRLDVLDDAAVKALVAEI-GQ-IDILFNCAGF 85
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKLDMNDPASLDQLLQRLqGQrFDLLFVNAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  86 V--HNGTILEMKDEELDFAVNLNVRSMIRTIRAVLpGMLERKDGAIINMASVASSVK-GVS-NRFVYGLTKAAVIGLTKA 161
Cdd:PRK08177  82 SgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLL-GQVRPGQGVLAFMSSQLGSVElPDGgEMPLYKASKAALNSMTRS 160


                 ....
gi 489055331 162 VAAD 165
Cdd:PRK08177 161 FVAE 164
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-100 4.32e-06

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: 46.98  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGQGIGQASALAFAE-AGAKVYAT---------DINADALAKLEGIAGIVT-RRLDVLDDAAVKALVAEI- 73
Cdd:cd08953  204 PGGVYLVTGGAGGIGRALARALARrYGARLVLLgrsplppeeEWKAQTLAALEALGARVLyISADVTDAAAVRRLLEKVr 283

                         90       100       110
                 ....*....|....*....|....*....|
gi 489055331  74 ---GQIDILFNCAGFVHNGTILEMKDEELD 100
Cdd:cd08953  284 eryGAIDGVIHAAGVLRDALLAQKTAEDFE 313
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 147-244 8.92e-06

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: 45.69  E-value: 8.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  147 VYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESP-----SLQDRLRaqgdyeaaraafiARQPIG-RIGQPEEIAD 220
Cdd:TIGR02685 172 MYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPdampfEVQEDYR-------------RKVPLGqREASAEQIAD 238

                          90       100
                  ....*....|....*....|....*.
gi 489055331  221 LAVYLAG--ATYTTGQAYNIDGGWSI 244
Cdd:TIGR02685 239 VVIFLVSpkAKYITGTCIKVDGGLSL 264
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 8-179 1.49e-05

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: 44.96  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYAT--DINADALAKLEGIAG--IVTRRLDV-----LDDAA--VKALVAEIGqI 76
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGclTKNGPGAKELRRVCSdrLRTLQLDVtkpeqIKRAAqwVKEHVGEKG-L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  77 DILFNCAGFVHNGTilemkDEEL----DF--AVNLNVRSMIRTIRAVLPgMLERKDGAIINMASVASSVkGVSNRFVYGL 150
Cdd:cd09805   80 WGLVNNAGILGFGG-----DEELlpmdDYrkCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRV-PFPAGGAYCA 152

                        170       180
                 ....*....|....*....|....*....
gi 489055331 151 TKAAVIGLTKAVAADYVGKGIRCNAICPG 179
Cdd:cd09805  153 SKAAVEAFSDSLRRELQPWGVKVSIIEPG 181
PRK08251 PRK08251
SDR family oxidoreductase;
8-183 3.22e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 43.77  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   8 KTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLE--------GIAgIVTRRLDVLDDAAV----KALVAEIGQ 75
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKaellarypGIK-VAVAALDVNDHDQVfevfAEFRDELGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMLERKDGAIINMASVaSSVKGV-SNRFVYGLTKAA 154
Cdd:PRK08251  82 LDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSV-SAVRGLpGVKAAYAASKAG 160

                        170       180
                 ....*....|....*....|....*....
gi 489055331 155 VIGLTKAVAADYVGKGIRCNAICPGTVES 183
Cdd:PRK08251 161 VASLGEGLRAELAKTPIKVSTIEPGYIRS 189
PRK07806 PRK07806
SDR family oxidoreductase;
5-123 3.25e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 43.94  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDIN----ADALAKLEGIAGI--VTRRLDVLDDAAVKAL----VAEIG 74
Cdd:PRK07806   4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprANKVVAEIEAAGGraSAVGADLTDEESVAALmdtaREEFG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489055331  75 QIDIL-FNCAGFVHNGTilemkDEelDFAVNLNVRSMIRTIRAVLPGMLE 123
Cdd:PRK07806  84 GLDALvLNASGGMESGM-----DE--DYAMRLNRDAQRNLARAALPLMPA 126
PRK07102 PRK07102
SDR family oxidoreductase;
7-184 3.47e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 43.76  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINADALAKLEgiAGIVTR--------RLDVLDDAAVKALVaeiGQIDI 78
Cdd:PRK07102   1 MKKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLA--DDLRARgavavsthELDILDTASHAAFL---DSLPA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  79 LFNCAGFVHnGTILEMKDEELDFA-----VNLNVRSMIRTIRAVLPGMLERKDGAIINMASVASSvKGVSNRFVYGLTKA 153
Cdd:PRK07102  76 LPDIVLIAV-GTLGDQAACEADPAlalreFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGD-RGRASNYVYGSAKA 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489055331 154 AVIGLTKAVAADYVGKGIRCNAICPGTVESP 184
Cdd:PRK07102 154 ALTAFLSGLRNRLFKSGVHVLTVKPGFVRTP 184
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-100 3.66e-05

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: 42.93  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331    9 TALVTAAGQGIGQASALAFAEAGAK--------VYATDINADALAKLEGI-AGIVTRRLDVLDDAAVKALVAEI----GQ 75
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARhlvllsrsAAPRPDAQALIAELEARgVEVVVVACDVSDPDAVAALLAEIkaegPP 81

                          90       100
                  ....*....|....*....|....*
gi 489055331   76 IDILFNCAGFVHNGTILEMKDEELD 100
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWR 106
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 57-182 3.83e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 43.26  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  57 RLDVLDDAAVKALVAEIGQIDILFNCAGFVHNGTILEMKDEelDFAVNLNVRSM--IRTIRAVLP------------GML 122
Cdd:PRK07578  37 QVDITDPASIRALFEKVGKVDAVVSAAGKVHFAPLAEMTDE--DFNVGLQSKLMgqVNLVLIGQHylndggsftltsGIL 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 123 ERKdgaIINMASVASSVKGVSNRFVygltKAAVIGLtkavaadyvGKGIRCNAICPGTVE 182
Cdd:PRK07578 115 SDE---PIPGGASAATVNGALEGFV----KAAALEL---------PRGIRINVVSPTVLT 158
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 7-84 1.63e-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: 41.92  E-value: 1.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489055331   7 GKTALVTAAGqGIGQASALAFAEAGAKVYATDINADALAKLEGIAGIVTrrLDVLDDAAVKALVAEIGQ-IDILFNCAG 84
Cdd:cd05188  135 GDTVLVLGAG-GVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHV--IDYKEEDLEEELRLTGGGgADVVIDAVG 210
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
59-244 2.04e-04

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 41.35  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  59 DVLDDAAVKALVAEIGQ----IDILFNCAGFVHN----GTILE-MKDEELDFAVNLNVRSMIRTIRAVLPgMLERKdgAI 129
Cdd:PRK06997  64 DVASDEQIDALFASLGQhwdgLDGLVHSIGFAPReaiaGDFLDgLSRENFRIAHDISAYSFPALAKAALP-MLSDD--AS 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 130 INMASVASSVKGVSNRFVYGLTKAAVIGLTKAVAADYVGKGIRCNAICPGTVESpslqdrLRAQG--DYEAARAAFIARQ 207
Cdd:PRK06997 141 LLTLSYLGAERVVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKT------LAASGikDFGKILDFVESNA 214

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489055331 208 PIGRIGQPEEIADLAVYLAG--ATYTTGQAYNIDGGWSI 244
Cdd:PRK06997 215 PLRRNVTIEEVGNVAAFLLSdlASGVTGEITHVDSGFNA 253
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 7-226 2.15e-04

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: 41.43  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   7 GKTALVTAAGQGIGQASALAFAEAGAKVYATDINA----DALAKLEGIAG---IVTRRLDVLDDAAVKALVAEIGQ---- 75
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQtraeEARKEIETESGnqnIFLHIVDMSDPKQVWEFVEEFKEegkk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  76 IDILFNCAGFVHNGTILEMKDEELDFAVN-----LNVRSMI---------RTIRAVLPGMLERKdgaiINMASVASSVKG 141
Cdd:cd09808   81 LHVLINNAGCMVNKRELTEDGLEKNFATNtlgtyILTTHLIpvlekeedpRVITVSSGGMLVQK----LNTNNLQSERTA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331 142 VSNRFVYGLTKAAVIGLTKAVAADYvgKGIRCNAICPGTVESPSLQDrlraqgdyeaARAAFIARQPiGRIGQPEEIADL 221
Cdd:cd09808  157 FDGTMVYAQNKRQQVIMTEQWAKKH--PEIHFSVMHPGWADTPAVRN----------SMPDFHARFK-DRLRSEEQGADT 223


                 ....*
gi 489055331 222 AVYLA 226
Cdd:cd09808  224 VVWLA 228
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 32-93 4.91e-04

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 40.59  E-value: 4.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489055331  32 AKVYATDINADALAKL-EGIAGIVTRRLDVLDDAAVKALvaeIGQIDILFNCAGFVHNGTILE 93
Cdd:COG1748    1 YEVTLADRSLEKAEALaASGPKVEAAQLDASDPEALAAL---IAGADLVINALPPYLNLTVAE 60
PRK09009 PRK09009
SDR family oxidoreductase;
18-90 5.87e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 40.05  E-value: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  18 GIGQA--SALAFAEAGAKVYAT------DINADalaklegiaGIVTRRLDVLDDAAVKALVAEIGQIDILFNCAGFVHNG 89
Cdd:PRK09009  11 GIGKAmvKQLLERYPDATVHATyrhhkpDFQHD---------NVQWHALDVTDEAEIKQLSEQFTQLDWLINCVGMLHTQ 81


                 .
gi 489055331  90 T 90
Cdd:PRK09009  82 D 82
PRK07023 PRK07023
SDR family oxidoreductase;
10-219 9.69e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 39.23  E-value: 9.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  10 ALVTAAGQGIGQASALAFAEAGAKVYATDINAD-ALAKLEGiAGIVTRRLDVLDDAAVKALVAEI--------GQIDILF 80
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRHpSLAAAAG-ERLAEVELDLSDAAAAAAWLAGDllaafvdgASRVLLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  81 NCAGFVHN-GTILEMKDEELDFAVNLNVRSMIRTIRAVL---PGMLERKdgaIINMASVAS--SVKGVSnrfVYGLTKAA 154
Cdd:PRK07023  83 NNAGTVEPiGPLATLDAAAIARAVGLNVAAPLMLTAALAqaaSDAAERR---ILHISSGAArnAYAGWS---VYCATKAA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055331 155 VIGLTKAVAADYVGkGIRCNAICPGTVESpSLQDRLRAQGDYE-AARAAFIARQPIGRIGQPEEIA 219
Cdd:PRK07023 157 LDHHARAVALDANR-ALRIVSLAPGVVDT-GMQATIRATDEERfPMRERFRELKASGALSTPEDAA 220
PRK05854 PRK05854
SDR family oxidoreductase;
5-84 1.04e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 39.66  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   5 LDGKTALVTAAGQGIGQASALAFAEAGAKVYATDINA----DALAKLEGI---AGIVTRRLDVLDDAAVKA----LVAEI 73
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRakgeAAVAAIRTAvpdAKLSLRALDLSSLASVAAlgeqLRAEG 91

                         90
                 ....*....|.
gi 489055331  74 GQIDILFNCAG 84
Cdd:PRK05854  92 RPIHLLINNAG 102
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 8-100 1.24e-03

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 38.62  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331     8 KTALVTAAGQGIGQASALAFAEAGAK--------VYATDINADALAKLEGIAGIVT-RRLDVLDDAAVKALVAEI----G 74
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARrlvllsrsGPDAPGAAALLAELEAAGARVTvVACDVADRDALAAVLAAIpaveG 80

                           90       100
                   ....*....|....*....|....*.
gi 489055331    75 QIDILFNCAGFVHNGTILEMKDEELD 100
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFA 106
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 11-104 3.32e-03

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. 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: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 37.99  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  11 LVT-AAGQgIGQASALAFAEAGAKVYATDINADALAKLegiagivtrrlDVLDDAAVKALVAEIgQIDILFNCAGF--VH 87
Cdd:cd05254    3 LITgATGM-LGRALVRLLKERGYEVIGTGRSRASLFKL-----------DLTDPDAVEEAIRDY-KPDVIINCAAYtrVD 69

                         90
                 ....*....|....*..
gi 489055331  88 NgtiLEmKDEELDFAVN 104
Cdd:cd05254   70 K---CE-SDPELAYRVN 82
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 6-73 4.87e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. 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 includes various 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: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 37.55  E-value: 4.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   6 DGKTALVTAAGqGIGQASALAFAEAGAKVYATDINAD--ALAKLEGiagiVTRRLDVLDDaAVKALVAEI 73
Cdd:cd08261  159 AGDTVLVVGAG-PIGLGVIQVAKARGARVIVVDIDDErlEFARELG----ADDTINVGDE-DVAARLREL 222
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 4-100 6.02e-03

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 37.36  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   4 RLDGKTALVTAAGQGIGQASALAFAEAGAK----VYATDINADALAKLE----GIAGIVTRRLDVLDDAAVKALVAEIGQ 75
Cdd:cd05274  147 GGLDGTYLITGGLGGLGLLVARWLAARGARhlvlLSRRGPAPRAAARAAllraGGARVSVVRCDVTDPAALAALLAELAA 226

                         90       100
                 ....*....|....*....|....*...
gi 489055331  76 ---IDILFNCAGFVHNGTILEMKDEELD 100
Cdd:cd05274  227 ggpLAGVIHAAGVLRDALLAELTPAAFA 254
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
1-179 9.85e-03

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 36.46  E-value: 9.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331   1 MTIRLDGKTALVTaagqGIGQASALAFA------EAGAKVYATDINaDALAKLEGIAgivtRRL---------DVLDDAA 65
Cdd:PRK07889   1 MMGLLEGKRILVT----GVITDSSIAFHvarvaqEQGAEVVLTGFG-RALRLTERIA----KRLpepapvlelDVTNEEH 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055331  66 VKALVAEIGQ----IDILFNCAGF----VHNGTILEMKDEELDFAVNLNVRSMIRTIRAVLPGMleRKDGAIINM---AS 134
Cdd:PRK07889  72 LASLADRVREhvdgLDGVVHSIGFapqsALGGNFLDAPWEDVATALHVSAYSLKSLAKALLPLM--NEGGSIVGLdfdAT 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489055331 135 VASSVkgvsnrfvY---GLTKAAVIGLTKAVAADYVGKGIRCNAICPG 179
Cdd:PRK07889 150 VAWPA--------YdwmGVAKAALESTNRYLARDLGPRGIRVNLVAAG 189
 
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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