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Conserved domains on  [gi|2462599489|ref|XP_054207102|]
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3-oxoacyl-[acyl-carrier-protein] reductase isoform X7 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 5-144 2.19e-56

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


The actual alignment was detected with superfamily member cd05333:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 240  Bit Score: 176.20  E-value: 2.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05333   105 INVNLTGVFNVTQAVIRAMIKRRSGRIINIS----------SVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITV 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  85 NVVAPGFVHTDMTKDLKE---EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd05333   175 NAVAPGFIDTDMTDALPEkvkEKILKQIPLGRLGTPEEVANAVAFLAsdDASYITGQVLHVNGGM 239
 
Name Accession Description Interval E-value
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 5-144 2.19e-56

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: 176.20  E-value: 2.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05333   105 INVNLTGVFNVTQAVIRAMIKRRSGRIINIS----------SVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITV 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  85 NVVAPGFVHTDMTKDLKE---EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd05333   175 NAVAPGFIDTDMTDALPEkvkEKILKQIPLGRLGTPEEVANAVAFLAsdDASYITGQVLHVNGGM 239
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-146 8.30e-56

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 174.96  E-value: 8.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK05653  110 IDVNLTGTFNVVRAALPPMIKARYGRIVNIS----------SVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITV 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLKE---EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK05653  180 NAVAPGFIDTDMTEGLPEevkAEILKEIPLGRLGQPEEVANAVAFLAsdAASYITGQVIPVNGGMYM 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-144 1.77e-55

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: 174.20  E-value: 1.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:COG1028   110 VLDVNLKGPFLLTRAALPHMRERGGGRIVNIS----------SIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIR 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  84 VNVVAPGFVHTDMTKDLKE-----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:COG1028   180 VNAVAPGPIDTPMTRALLGaeevrEALAARIPLGRLGTPEEVAAAVLFLAsdAASYITGQVLAVDGGL 247
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 5-144 4.12e-55

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 172.78  E-value: 4.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:TIGR01830 104 IDTNLTGVFNLTQAVLRIMIKQRSGRIINIS----------SVVGLMGNAGQANYAASKAGVIGFTKSLAKELASRNITV 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKK---NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:TIGR01830 174 NAVAPGFIDTDMTDKLSEKVKKKilsQIPLGRFGQPEEVANAVAFLAsdEASYITGQVIHVDGGM 238
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 5-144 4.56e-47

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 152.20  E-value: 4.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:pfam13561 101 LDVNLYSLFLLAKAALPLM--KEGGSIVNLS----------SIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRV 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLK-----EEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:pfam13561 169 NAISPGPIKTLAASGIPgfdelLAAAEARAPLGRLGTPEEVANAAAFLAsdLASYITGQVLYVDGGY 235
 
Name Accession Description Interval E-value
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 5-144 2.19e-56

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: 176.20  E-value: 2.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05333   105 INVNLTGVFNVTQAVIRAMIKRRSGRIINIS----------SVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITV 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  85 NVVAPGFVHTDMTKDLKE---EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd05333   175 NAVAPGFIDTDMTDALPEkvkEKILKQIPLGRLGTPEEVANAVAFLAsdDASYITGQVLHVNGGM 239
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-146 8.30e-56

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 174.96  E-value: 8.30e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK05653  110 IDVNLTGTFNVVRAALPPMIKARYGRIVNIS----------SVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITV 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLKE---EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK05653  180 NAVAPGFIDTDMTEGLPEevkAEILKEIPLGRLGQPEEVANAVAFLAsdAASYITGQVIPVNGGMYM 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-144 1.77e-55

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: 174.20  E-value: 1.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:COG1028   110 VLDVNLKGPFLLTRAALPHMRERGGGRIVNIS----------SIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIR 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  84 VNVVAPGFVHTDMTKDLKE-----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:COG1028   180 VNAVAPGPIDTPMTRALLGaeevrEALAARIPLGRLGTPEEVAAAVLFLAsdAASYITGQVLAVDGGL 247
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 5-144 4.12e-55

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


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 172.78  E-value: 4.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:TIGR01830 104 IDTNLTGVFNLTQAVLRIMIKQRSGRIINIS----------SVVGLMGNAGQANYAASKAGVIGFTKSLAKELASRNITV 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKK---NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:TIGR01830 174 NAVAPGFIDTDMTDKLSEKVKKKilsQIPLGRFGQPEEVANAVAFLAsdEASYITGQVIHVDGGM 238
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-144 3.34e-53

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 168.06  E-value: 3.34e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK05557  113 TNLTGVFNLTKAVARPMMKQRSGRIINIS----------SVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNA 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  87 VAPGFVHTDMTKDLKE---EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK05557  183 VAPGFIETDMTDALPEdvkEAILAQIPLGRLGQPEEIASAVAFLAsdEAAYITGQTLHVNGGM 245
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-141 7.55e-49

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: 156.68  E-value: 7.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05233   102 LDVNLTGVFLLTRAALPHMKKQGGGRIVNIS----------SVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRV 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEH----LKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVD 141
Cdd:cd05233   172 NAVAPGLVDTPMLAKLGPEEaekeLAAAIPLGRLGTPEEVAEAVVFLAsdEASYITGQVIPVD 234
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 5-144 4.56e-47

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 152.20  E-value: 4.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:pfam13561 101 LDVNLYSLFLLAKAALPLM--KEGGSIVNLS----------SIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRV 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLK-----EEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:pfam13561 169 NAISPGPIKTLAASGIPgfdelLAAAEARAPLGRLGTPEEVANAAAFLAsdLASYITGQVLYVDGGY 235
PRK12826 PRK12826
SDR family oxidoreductase;
5-146 2.91e-46

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 150.45  E-value: 2.91e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL-KGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK12826  111 IDVNLTGTFLLTQAALPALIRAGGGRIVLTS----------SVAGPrVGYPGLAHYAASKAGLVGFTRALALELAARNIT 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  84 VNVVAPGFVHTDMTKDLKE----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK12826  181 VNSVHPGGVDTPMAGNLGDaqwaEAIAAAIPLGRLGEPEDIAAAVLFLAsdEARYITGQTLPVDGGATL 249
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-147 3.98e-44

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 145.01  E-value: 3.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK12825  114 VNLSGVFHLLRAVVPPMRKQRGGRIVNIS----------SVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNM 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  87 VAPGFVHTDMTKDLKEEHL---KKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQLI 147
Cdd:PRK12825  184 VAPGDIDTDMKEATIEEAReakDAETPLGRSGTPEDIARAVAFLCsdASDYITGQVIEVTGGVDVI 249
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-143 8.66e-44

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 144.21  E-value: 8.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK05565  113 VNLTGVMLLTRYALPYMIKRKSGVIVNIS----------SIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNA 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  87 VAPGFVHTDMTKDLKEEH---LKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK05565  183 VAPGAIDTEMWSSFSEEDkegLAEEIPLGRLGKPEEIAKVVLFLAsdDASYITGQIITVDGG 244
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-146 3.72e-37

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 127.38  E-value: 3.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQ-QGGSIVNVghrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK08217  122 NLTGVFLCGREAAAKMIESgSKGVIINI-----------SSIARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAA 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  87 VAPGFVHTDMTKDLKEE---HLKKNIPLGRFGETIEVAHAVVFLLESPYITGHVLVVDGGLQL 146
Cdd:PRK08217  191 IAPGVIETEMTAAMKPEaleRLEKMIPVGRLGEPEEIAHTVRFIIENDYVTGRVLEIDGGLRL 253
FabG-like PRK07231
SDR family oxidoreductase;
7-144 5.60e-36

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 124.17  E-value: 5.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK07231  112 VNVKSPYLWTQAAVPAMRGEGGGAIVNVA----------STAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNA 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  87 VAPGFVHTDMTKDL-------KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK07231  182 VAPVVVETGLLEAFmgeptpeNRAKFLATIPLGRLGTPEDIANAALFLAsdEASWITGVTLVVDGGR 248
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
5-147 7.39e-36

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 123.72  E-value: 7.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK12824  108 INTNLNSVFNVTQPLFAAMCEQGYGRIINIS----------SVNGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITV 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKK---NIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGLQLI 147
Cdd:PRK12824  178 NCIAPGYIATPMVEQMGPEVLQSivnQIPMKRLGTPEEIAAAVAFLVSeaAGFITGETISINGGLYMH 245
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-143 6.18e-35

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


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 121.70  E-value: 6.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05347   112 VNLNGVFFVSQAVARHMIKQGHGKIINIC----------SLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNA 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  87 VAPGFVHTDMTKDLKEEH-----LKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05347   182 IAPGYFATEMTEAVVADPefnddILKRIPAGRWGQPEDLVGAAVFLAsdASDYVNGQIIFVDGG 245
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 5-103 4.04e-33

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 115.40  E-value: 4.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:pfam00106 105 IDVNLTGVFNLTRAVLPAMIKGSGGRIVNIS----------SVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRV 174

                          90
                  ....*....|....*....
gi 2462599489  85 NVVAPGFVHTDMTKDLKEE 103
Cdd:pfam00106 175 NAVAPGGVDTDMTKELRED 193
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-147 4.67e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 116.97  E-value: 4.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGS-MLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV----YSASKGGLVGFSRALAKEVAR 79
Cdd:PRK08213  117 MNLNVRGLfLLSQAVAKRSMIPRGYGRIINVA----------SVAGLGGNPPEVMdtiaYNTSKGAVINFTRALAAEWGP 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  80 KKIRVNVVAPGFVHTDMTKDL---KEEHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGLQLI 147
Cdd:PRK08213  187 HGIRVNAIAPGFFPTKMTRGTlerLGEDLLAHTPLGRLGDDEDLKGAALLLASdaSKHITGQILAVDGGVSAV 259
PRK06172 PRK06172
SDR family oxidoreductase;
8-144 1.04e-32

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 116.00  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK06172  116 NVKGVWLCMKYQIPLMLAQGGGAIVNTA----------SVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAV 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  88 APGFVHTDMTK------DLKEEHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGL 144
Cdd:PRK06172  186 CPAVIDTDMFRrayeadPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSdgASFTTGHALMVDGGA 250
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-143 2.65e-32

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 119.57  E-value: 2.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK06484  112 NLTGAYLVAREALRLMIEQgHGAAIVNVA----------SGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNA 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  87 VAPGFVHTDMTKDLKEEHL------KKNIPLGRFGETIEVAHAVVFL--LESPYITGHVLVVDGG 143
Cdd:PRK06484  182 VLPGYVRTQMVAELERAGKldpsavRSRIPLGRLGRPEEIAEAVFFLasDQASYITGSTLVVDGG 246
PRK06124 PRK06124
SDR family oxidoreductase;
5-144 6.80e-32

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 114.04  E-value: 6.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK06124  116 LETDLVAPILLSRLAAQRMKRQGYGRIIAI----------TSIAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGITS 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  85 NVVAPGFVHTD----MTKD-LKEEHLKKNIPLGRFGETIEVAHAVVFlLESP---YITGHVLVVDGGL 144
Cdd:PRK06124  186 NAIAPGYFATEtnaaMAADpAVGPWLAQRTPLGRWGRPEEIAGAAVF-LASPaasYVNGHVLAVDGGY 252
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 4-139 7.15e-31

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: 110.66  E-value: 7.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:COG4221   106 MIDVNVKGVLYVTRAALPAMRARGSGHIVNIS----------SIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIR 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEEHLKKNIPLGRFGETI---EVAHAVVFLLESPyitGHVLV 139
Cdd:COG4221   176 VTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLtpeDVAEAVLFALTQP---AHVNV 231
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-144 1.92e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 109.81  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQ-QQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:PRK12827  117 VNLDGFFNVTQAALPPMIRaRRGGRIVNIA----------SVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVN 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  86 VVAPGFVHTDM-TKDLKEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK12827  187 AVAPGAINTPMaDNAAPTEHLLNPVPVQRLGEPDEVAALVAFLVsdAASYVTGQVIPVDGGF 248
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-143 6.83e-30

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 108.52  E-value: 6.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK12939  111 VMNVNVRGTFLMLRAALPHLRDSGRGRIVNLA----------SDTALWGAPKLGAYVASKGAVIGMTRSLARELGGRGIT 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEEH----LKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK12939  181 VNAIAPGLTATEATAYVPADErhayYLKGRALERLQVPDDVAGAVLFLLsdAARFVTGQLLPVNGG 246
PRK06138 PRK06138
SDR family oxidoreductase;
8-144 6.86e-30

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 108.70  E-value: 6.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremllhKRSIVGLKGNSGqsvYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK06138  112 NVGGVFLWAKYAIPIMQRQGGGSIVNTAS-------QLALAGGRGRAA---YVASKGAIASLTRAMALDHATDGIRVNAV 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  88 APGFVHTDMTK---------DLKEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK06138  182 APGTIDTPYFRrifarhadpEALREALRARHPMNRFGTAEEVAQAALFLAsdESSFATGTTLVVDGGW 249
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 5-143 2.15e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 107.11  E-value: 2.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMI-QQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK07060  105 MAVNARGAALVARHVARAMIaAGRGGSIVNVS----------SQAALVGLPDHLAYCASKAALDAITRVLCVELGPHGIR 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  84 VNVVAPGFVHTDMTKDL-----KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK07060  175 VNSVNPTVTLTPMAAEAwsdpqKSGPMLAAIPLGRFAEVDDVAAPILFLLsdAASMVSGVSLPVDGG 241
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 5-143 3.82e-29

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


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 106.70  E-value: 3.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKK--I 82
Cdd:cd05341   107 LDINLTGVFLGTRAVIPPMKEAGGGSIINMS----------SIEGLVGDPALAAYNASKGAVRGLTKSAALECATQGygI 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  83 RVNVVAPGFVHTDMT----KDLKEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05341   177 RVNSVHPGYIYTPMTdellIAQGEMGNYPNTPMGRAGEPDEIAYAVVYLAsdESSFVTGSELVVDGG 243
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-146 1.08e-28

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: 105.54  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQG-GSIVNVGHRREMLLHkrsivglkgnSGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:cd05358   111 VNLTGQFLCAREAIKRFRKSKIkGKIINMSSVHEKIPW----------PGHVNYAASKGGVKMMTKTLAQEYAPKGIRVN 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  86 VVAPGFVHTDMTKDL-----KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:cd05358   181 AIAPGAINTPINAEAwddpeQRADLLSLIPMGRIGEPEEIAAAAAWLAsdEASYVTGTTLFVDGGMTL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-131 1.22e-28

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 105.34  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:COG0300   109 VFEVNVFGPVRLTRALLPLMRARGRGRIVNVS----------SVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVR 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEEHLKKNIPlgrfgeTIEVAHAVVFLLESP 131
Cdd:COG0300   179 VTAVCPGPVDTPFTARAGAPAGRPLLS------PEEVARAILRALERG 220
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 3-147 1.61e-28

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 105.00  E-value: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:PRK12936  106 SVLEVNLTATFRLTRELTHPMMRRRYGRIINI----------TSVVGVTGNPGQANYCASKAGMIGFSKSLAQEIATRNV 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  83 RVNVVAPGFVHTDMTKDLKE---EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQLI 147
Cdd:PRK12936  176 TVNCVAPGFIESAMTGKLNDkqkEAIMGAIPMKRMGTGAEVASAVAYLAssEAAYVTGQTIHVNGGMAMI 245
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 8-143 5.63e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 103.58  E-value: 5.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNvghrremLLHKRSIVGLKGNSGqsvYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK06841  120 NLKGSFLMAQAVGRHMIAAGGGKIVN-------LASQAGVVALERHVA---YCASKAGVVGMTKVLALEWGPYGITVNAI 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  88 APGFVHTDMTKDL----KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK06841  190 SPTVVLTELGKKAwageKGERAKKLIPAGRFAYPEEIAAAALFLAsdAAAMITGENLVIDGG 251
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 7-144 1.73e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 102.50  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN-SGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:PRK06057  111 VNLTSVYLCCKAALPHMVRQGKGSIINTA----------SFVAVMGSaTSQISYTASKGGVLAMSRELGVQFARQGIRVN 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  86 VVAPGFVHTDMTKDLKEEHLKK------NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK06057  181 ALCPGPVNTPLLQELFAKDPERaarrlvHVPMGRFAEPEEIAAAVAFLAsdDASFITASTFLVDGGI 247
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 7-143 6.42e-27

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: 100.87  E-value: 6.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN--SGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05352   116 VNLNGVFNCAQAAAKIFKKQGKGSLIITA----------SMSGTIVNrpQPQAAYNASKAAVIHLAKSLAVEWAKYFIRV 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  85 NVVAPGFVHTDMT----KDLKeEHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:cd05352   186 NSISPGYIDTDLTdfvdKELR-KKWESYIPLKRIALPEELVGAYLYLASdaSSYTTGSDLIIDGG 249
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 7-143 8.84e-27

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: 100.26  E-value: 8.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd08944   108 INLRGTFLCCRHAAPRMIARGGGSIVNLS----------SIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNA 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  87 VAPGFVHTDMTKDLKEEHLKKNIP----------LGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd08944   178 LAPGLIDTPLLLAKLAGFEGALGPggfhllihqlQGRLGRPEDVAAAVVFLLsdDASFITGQVLCVDGG 246
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-143 1.02e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 101.26  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK06701  153 FKTNIYSYFHMTKAALPHL--KQGSAIINTG----------SITGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKGIRV 220

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  85 NVVAPGFVHTDM---TKDLKE-EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK06701  221 NAVAPGPIWTPLipsDFDEEKvSQFGSNTPMQRPGQPEELAPAYVFLAspDSSYITGQMLHVNGG 285
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-144 1.15e-26

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: 100.04  E-value: 1.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05344   106 FDLKLLSVIRIVRAVLPGMKERGWGRIVNIS----------SLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTV 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKKN--------------IPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd05344   176 NSVLPGYIDTERVRRLLEARAEKEgisveeaekevasqIPLGRVGKPEELAALIAFLAseKASYITGQAILVDGGL 251
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 8-146 1.23e-26

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: 100.14  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05366   111 NVFGVLFGIQAAARQFKKLGhGGKIINAS----------SIAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNA 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  87 VAPGFVHTDMTKDLKEE--------------HLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:cd05366   181 YAPGIVKTEMWDYIDEEvgeiagkpegegfaEFSSSIPLGRLSEPEDVAGLVSFLAseDSDYITGQTILVDGGMVY 256
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 7-143 1.48e-26

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: 100.44  E-value: 1.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05355   136 TNIFSMFYLTKAALPHL--KKGSSIINTT----------SVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNA 203

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  87 VAPGFVHT-----DMTKDLKEEHlKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05355   204 VAPGPIWTplipsSFPEEKVSEF-GSQVPMGRAGQPAEVAPAYVFLAsqDSSYVTGQVLHVNGG 266
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 5-146 1.84e-26

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: 99.67  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVA 78
Cdd:cd05371   109 INVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTA----------SVAAFEGQIGQAAYSASKGGIVGMTLPIARDLA 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  79 RKKIRVNVVAPGFVHTDMTKDLKEE---HLKKNIP-LGRFGETIEVAHAVVFLLESPYITGHVLVVDGGLQL 146
Cdd:cd05371   179 PQGIRVVTIAPGLFDTPLLAGLPEKvrdFLAKQVPfPSRLGDPAEYAHLVQHIIENPYLNGEVIRLDGAIRM 250
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 7-146 2.02e-26

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: 99.58  E-value: 2.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:cd05369   111 IDLNGTFNTTKAVGKRLIEAKhGGSILNIS----------ATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVN 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  86 VVAPGFVHTD--MTK----DLKEEHLKKNIPLGRFGETIEVAHAVVFLLeSP---YITGHVLVVDGGLQL 146
Cdd:cd05369   181 AIAPGPIPTTegMERlapsGKSEKKMIERVPLGRLGTPEEIANLALFLL-SDaasYINGTTLVVDGGQWL 249
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-144 4.37e-26

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: 98.67  E-value: 4.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05329   114 TNFEAAYHLSRLAHPLLKASGNGNIVFIS----------SVAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIRVNA 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  87 VAPGFVHTDMTKDL--KEEHLKKNI---PLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd05329   184 VAPWVIATPLVEPViqQKENLDKVIertPLKRFGEPEEVAALVAFLCmpAASYITGQIIAVDGGL 248
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 5-143 4.40e-26

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: 98.56  E-value: 4.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL--------KGNSGQS--VYSASKGGLVGFSRALA 74
Cdd:cd08930   111 LNVNLGGAFLCSQAFIKLFKKQGKGSIINIA----------SIYGViapdfriyENTQMYSpvEYSVIKAGIIHLTKYLA 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599489  75 KEVARKKIRVNVVAPGFVHTDMTKDLKeEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd08930   181 KYYADTGIRVNAISPGGILNNQPSEFL-EKYTKKCPLKRMLNPEDLRGAIIFLLsdASSYVTGQNLVIDGG 250
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 7-143 5.47e-26

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: 98.12  E-value: 5.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05362   111 VNTKGAFFVLQEAAKRL--RDGGRIINIS----------SSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNA 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  87 VAPGFVHTDMTKDLKEEH----LKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05362   179 VAPGPVDTDMFYAGKTEEavegYAKMSPLGRLGEPEDIAPVVAFLAspDGRWVNGQVIRANGG 241
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 8-146 1.79e-25

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 96.79  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK12828  113 NVKTTLNASKAALPALTASGGGRIVNIG----------AGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAV 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  88 APGFVHTDMtkdlkeehLKKNIPLGRFGETI---EVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK12828  183 LPSIIDTPP--------NRADMPDADFSRWVtpeQIAAVIAFLLsdEAQAITGASIPVDGGVAL 238
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 5-144 2.17e-25

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: 96.76  E-value: 2.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05326   109 LDVNVYGAFLGTKHAARVMIPAKKGSIVSVA----------SVAGVVGGLGPHAYTASKHAVLGLTRSAATELGEHGIRV 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  85 NVVAPGFVHTDMT---KDLKEEHLKK-----NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd05326   179 NCVSPYGVATPLLtagFGVEDEAIEEavrgaANLKGTALRPEDIAAAVLYLAsdDSRYVSGQNLVVDGGL 248
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 5-146 2.38e-25

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: 96.65  E-value: 2.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05359   104 MNTNLKALVHCAQQAAKLMRERGGGRIVAIS----------SLGSIRALPNYLAVGTAKAALEALVRYLAVELGPRGIRV 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  85 NVVAPGFVHTDMTK------DLKEEHLkKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:cd05359   174 NAVSPGVIDTDALAhfpnreDLLEAAA-ANTPAGRVGTPQDVADAVGFLCsdAARMITGQTLVVDGGLSI 242
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 8-143 4.54e-25

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 96.23  E-value: 4.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK06171  117 NQKGVFLMSQAVARQMVKQHDGVIVNMS----------SEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGV 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  88 APGFVH-TDM----------------TKDLKEEHLKKN-IPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK06171  187 APGILEaTGLrtpeyeealaytrgitVEQLRAGYTKTStIPLGRSGKLSEVADLVCYLLsdRASYITGVTTNIAGG 262
PRK09135 PRK09135
pteridine reductase; Provisional
 7-148 5.67e-25

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 95.77  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMrTMIQQQGGSIVNvghrremllhkrsIVGLKGN---SGQSVYSASKGGLVGFSRALAKEVArKKIR 83
Cdd:PRK09135  115 SNLKAPFFLSQAAA-PQLRKQRGAIVN-------------ITDIHAErplKGYPVYCAAKAALEMLTRSLALELA-PEVR 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  84 VNVVAPGFV----HTDMTKDLKEEHLKKNIPLGRFGETIEVAHAVVFLL-ESPYITGHVLVVDGGLQLIL 148
Cdd:PRK09135  180 VNAVAPGAIlwpeDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLLaDASFITGQILAVDGGRSLTL 249
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 3-146 6.04e-25

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: 95.60  E-value: 6.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:cd05349   107 QQLEGAVKGALNLLQAVLPDFKERGSGRVINIG----------TNLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGI 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  83 RVNVVAPGFV----HTDMTKDLKEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:cd05349   177 TVNMVSGGLLkvtdASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFAspWARAVTGQNLVVDGGLVM 246
PRK12743 PRK12743
SDR family oxidoreductase;
5-146 6.23e-25

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 95.87  E-value: 6.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGHRREmllHKRSIvglkgnsGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK12743  108 FTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHE---HTPLP-------GASAYTAAKHALGGLTKAMALELVEHGIL 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  84 VNVVAPGFVHTDMTkDLKEEHLKK----NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK12743  178 VNAVAPGAIATPMN-GMDDSDVKPdsrpGIPLGRPGDTHEIASLVAWLCseGASYTTGQSLIVDGGFML 245
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
18-143 9.81e-25

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 95.19  E-value: 9.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  18 AAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMT 97
Cdd:PRK06935  132 AVAKVMAKQGSGKIINIA----------SMLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANT 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  98 KDLKE-----EHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK06935  202 APIRAdknrnDEILKRIPAGRWGEPDDLMGAAVFLASraSDYVNGHILAVDGG 254
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 8-146 1.56e-24

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 94.69  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK12935  115 NLSSVFNTTSAVLPYITEAEEGRIISIS----------SIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAI 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  88 APGFVHTDMTKDLKEEHLKK---NIPLGRFGETIEVAHAVVFLL-ESPYITGHVLVVDGGLQL 146
Cdd:PRK12935  185 CPGFIDTEMVAEVPEEVRQKivaKIPKKRFGQADEIAKGVVYLCrDGAYITGQQLNINGGLYM 247
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 8-143 2.15e-24

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 94.18  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK12429  112 MLDGAFLTTKAALPIMKAQGGGRIINMA----------SVHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAI 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  88 APGFVHT--------DMTKDL-------KEEHLKKNIPLGRFGETIEVAHAVVFL--LESPYITGHVLVVDGG 143
Cdd:PRK12429  182 CPGYVDTplvrkqipDLAKERgiseeevLEDVLLPLVPQKRFTTVEEIADYALFLasFAAKGVTGQAWVVDGG 254
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
7-146 3.29e-24

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 93.54  E-value: 3.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK12938  111 TNLTSLFNVTKQVIDGMVERGWGRIINIS----------SVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNT 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  87 VAPGFVHTDMTKDLKEEHLKK---NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK12938  181 VSPGYIGTDMVKAIRPDVLEKivaTIPVRRLGSPDEIGSIVAWLAseESGFSTGADFSLNGGLHM 245
PRK09730 PRK09730
SDR family oxidoreductase;
5-143 3.31e-24

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 93.76  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGhrremllhkrSIVGLKGNSGQSV-YSASKGGLVGFSRALAKEVARK 80
Cdd:PRK09730  108 LSTNVTGYFLCCREAVKRMALKhggSGGAIVNVS----------SAASRLGAPGEYVdYAASKGAIDTLTTGLSLEVAAQ 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  81 KIRVNVVAPGFVHTDMTKDLKE----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK09730  178 GIRVNCVRPGFIYTEMHASGGEpgrvDRVKSNIPMQRGGQPEEVAQAIVWLLsdKASYVTGSFIDLAGG 246
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
4-146 4.15e-24

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 93.71  E-value: 4.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVG-LKGNSGQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:PRK08226  109 HIDINIKGVWNVTKAVLPEMIARKDGRIVMMS----------SVTGdMVADPGETAYALTKAAIVGLTKSLAVEYAQSGI 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  83 RVNVVAPGFVHTDMTKDLKEEH-----------LKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK08226  179 RVNAICPGYVRTPMAESIARQSnpedpesvlteMAKAIPLRRLADPLEVGELAAFLAsdESSYLTGTQNVIDGGSTL 255
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-144 8.88e-24

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 95.69  E-value: 8.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK06484  375 NLSGAFACARAAARLM--SQGGVIVNLG----------SIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTV 442

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  88 APGFVHTDMTKDLKE------EHLKKNIPLGRFGETIEVAHAVVFlLESP---YITGHVLVVDGGL 144
Cdd:PRK06484  443 APGYIETPAVLALKAsgradfDSIRRRIPLGRLGDPEEVAEAIAF-LASPaasYVNGATLTVDGGW 507
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 7-145 9.06e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 92.81  E-value: 9.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:PRK12829  117 VNLNGQFYFARAAVPLLKASGhGGVIIALS----------SVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVN 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  86 VVAPGFVHTDMTK---------------DLKEEHLKKnIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQ 145
Cdd:PRK12829  187 AILPGIVRGPRMRrviearaqqlgigldEMEQEYLEK-ISLGRMVEPEDIAATALFLAspAARYITGQAISVDGNVE 262
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 8-143 1.97e-23

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: 91.76  E-value: 1.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05351   107 NVRAVIHVSQIVARGMIARGvPGSIVNVS----------SQASQRALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNS 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  87 VAPGFVHTDMTKDL-----KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05351   177 VNPTVVMTDMGRDNwsdpeKAKKMLNRIPLGKFAEVEDVVNAILFLLsdKSSMTTGSTLPVDGG 240
PRK07069 PRK07069
short chain dehydrogenase; Validated
 13-144 2.23e-23

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 91.70  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  13 MLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKK--IRVNVVAPG 90
Cdd:PRK07069  115 FLGCKHALPYLRASQPASIVNIS----------SVAAFKAEPDYTAYNASKAAVASLTKSIALDCARRGldVRCNSIHPT 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  91 FVHTDMTKDLKE--------EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK07069  185 FIRTGIVDPIFQrlgeeeatRKLARGVPLGRLGEPDDVAHAVLYLAsdESRFVTGAELVIDGGI 248
PRK07074 PRK07074
SDR family oxidoreductase;
5-144 4.26e-23

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 90.98  E-value: 4.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGnSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK07074  105 NALNLEAAYLCVEAVLEGMLKRSRGAVVNIG----------SVNGMAA-LGHPAYSAAKAGLIHYTKLLAVEYGRFGIRA 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  85 NVVAPGFVHT-------DMTKDLKEEhLKKNIPLGRFGETIEVAHAVVFlLESPY---ITGHVLVVDGGL 144
Cdd:PRK07074  174 NAVAPGTVKTqawearvAANPQVFEE-LKKWYPLQDFATPDDVANAVLF-LASPAaraITGVCLPVDGGL 241
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 8-146 4.72e-23

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: 90.61  E-value: 4.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVG-LKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05368   101 NVRSMYLMIKAVLPKMLARKDGSIINMS----------SVASsIKGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNA 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599489  87 VAPGFVHTDMTKDL------KEEHLK---KNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:cd05368   171 ICPGTVDTPSLEERiqaqpdPEEALKafaARQPLGRLATPEEVAALAVYLAsdESAYVTGTAVVIDGGWSL 241
PRK07063 PRK07063
SDR family oxidoreductase;
8-144 4.88e-23

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 90.88  E-value: 4.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremlLHKRSIVglkgnSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK07063  117 DLDGAWNGCRAVLPGMVERGRGSIVNIAS-----THAFKII-----PGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAI 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  88 APGFVHTDMTKDL----------KEEHLKKNiPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK07063  187 APGYIETQLTEDWwnaqpdpaaaRAETLALQ-PMKRIGRPEEVAMTAVFLAsdEAPFINATCITIDGGR 254
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-143 6.34e-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: 90.03  E-value: 6.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVArKKIRVNV 86
Cdd:cd05357   108 INLKAPYLLIQAFARRLAGSRNGSIINII----------DAMTDRPLTGYFAYCMSKAALEGLTRSAALELA-PNIRVNG 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  87 VAPGFV--HTDMTKDLKEEHLKKnIPLGRFGETIEVAHAVVFLLESPYITGHVLVVDGG 143
Cdd:cd05357   177 IAPGLIllPEDMDAEYRENALRK-VPLKRRPSAEEIADAVIFLLDSNYITGQIIKVDGG 234
PRK06123 PRK06123
SDR family oxidoreductase;
5-143 6.43e-23

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 90.22  E-value: 6.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGhrremllhkrSIVGLKGNSGQSV-YSASKGGLVGFSRALAKEVARK 80
Cdd:PRK06123  109 FATNVVGSFLCAREAVKRMSTRhggRGGAIVNVS----------SMAARLGSPGEYIdYAASKGAIDTMTIGLAKEVAAE 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  81 KIRVNVVAPGFVHTDMTKDLKE----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK06123  179 GIRVNAVRPGVIYTEIHASGGEpgrvDRVKAGIPMGRGGTAEEVARAILWLLsdEASYTTGTFIDVSGG 247
PRK06114 PRK06114
SDR family oxidoreductase;
8-143 7.71e-23

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 90.23  E-value: 7.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG--QSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:PRK06114  117 NLTGVFLSCQAEARAMLENGGGSIVNIA----------SMSGIIVNRGllQAHYNASKAGVIHLSKSLAMEWVGRGIRVN 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  86 VVAPGFVHTDMTKDLKEEHLKK----NIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK06114  187 SISPGYTATPMNTRPEMVHQTKlfeeQTPMQRMAKVDEMVGPAVFLLSdaASFCTGVDLLVDGG 250
PRK07035 PRK07035
SDR family oxidoreductase;
8-144 7.75e-23

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 90.08  E-value: 7.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK07035  117 NIRGYFFMSVEAGKLMKEQGGGSIVNVA----------SVNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNAL 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  88 APGFVHTDMTKDLKE-----EHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGL 144
Cdd:PRK07035  187 LPGLTDTKFASALFKndailKQALAHIPLRRHAEPSEMAGAVLYLASdaSSYTTGECLNVDGGY 250
PRK07856 PRK07856
SDR family oxidoreductase;
8-143 7.78e-23

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 89.99  E-value: 7.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVArKKIRVNV 86
Cdd:PRK07856  106 NLLAPLLVAQAANAVMQQQpGGGSIVNIG----------SVSGRRPSPGTAAYGAAKAGLLNLTRSLAVEWA-PKVRVNA 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  87 VAPGFVHTDmtkdLKEEH---------LKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK07856  175 VVVGLVRTE----QSELHygdaegiaaVAATVPLGRLATPADIAWACLFLAsdLASYVSGANLEVHGG 238
PRK06500 PRK06500
SDR family oxidoreductase;
52-143 9.15e-23

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 90.02  E-value: 9.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  52 GNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDM-------TKDLKE--EHLKKNIPLGRFGETIEVAH 122
Cdd:PRK06500  143 GMPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLygklglpEATLDAvaAQIQALVPLGRFGTPEEIAK 222

                          90       100
                  ....*....|....*....|...
gi 2462599489 123 AVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK06500  223 AVLYLAsdESAFIVGSEIIVDGG 245
PRK05867 PRK05867
SDR family oxidoreductase;
7-143 1.49e-22

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 89.71  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSV--YSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK05867  116 TNVTGVFLTAQAAAKAMVKQgQGGVIINTA----------SMSGHIINVPQQVshYCASKAAVIHLTKAMAVELAPHKIR 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEEH--LKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK05867  186 VNSVSPGYILTELVEPYTEYQplWEPKIPLGRLGRPEELAGLYLYLASeaSSYMTGSDIVIDGG 249
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 8-144 1.78e-22

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: 89.43  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:TIGR02415 108 NVKGVLFGIQAAARQFKKQGhGGKIINAA----------SIAGHEGNPILSAYSSTKFAVRGLTQTAAQELAPKGITVNA 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  87 VAPGFVHTDMTKDLKEEHLK--------------KNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:TIGR02415 178 YCPGIVKTPMWEEIDEETSEiagkpigegfeefsSEIALGRPSEPEDVAGLVSFLAseDSDYITGQSILVDGGM 251
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 5-144 1.89e-22

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 89.03  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVghrremllhKRSIVGLKGNSGqSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK12937  111 IATNLRGAFVVLREAARHL--GQGGRIINL---------STSVIALPLPGY-GPYAASKAAVEGLVHVLANELRGRGITV 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  85 NVVAPGFVHTDMTKDLKE----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK12937  179 NAVAPGPVATELFFNGKSaeqiDQLAGLAPLERLGTPEEIAAAVAFLAgpDGAWVNGQVLRVNGGF 244
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 3-143 4.17e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 88.42  E-value: 4.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGH-RREMLLHKRSIVglkgnsgqsvYSASKGGLVGFSRALAKEVARKK 81
Cdd:PRK06523  105 DELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSiQRRLPLPESTTA----------YAAAKAALSTYSKSLSKEVAPKG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  82 IRVNVVAPGFVHTDMTKDLKE----------EHLKKN-------IPLGRFGETIEVAHAVVFLLeSP---YITGHVLVVD 141
Cdd:PRK06523  175 VRVNTVSPGWIETEAAVALAErlaeaagtdyEGAKQIimdslggIPLGRPAEPEEVAELIAFLA-SDraaSITGTEYVID 253


                  ..
gi 2462599489 142 GG 143
Cdd:PRK06523  254 GG 255
PRK08589 PRK08589
SDR family oxidoreductase;
8-144 4.29e-22

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 88.68  E-value: 4.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQqGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK08589  114 DMRGTFLMTKMLLPLMMEQ-GGSIINTS----------SFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAI 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  88 APGFVHTDMTKDL---KEEHLKKNI--------PLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK08589  183 APGTIETPLVDKLtgtSEDEAGKTFrenqkwmtPLGRLGKPEEVAKLVVFLAsdDSSFITGETIRIDGGV 252
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-147 3.37e-21

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 85.93  E-value: 3.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVArKKIR 83
Cdd:PRK06077  111 HISTDFKSVIYCSQELAKEM--REGGAIVNIA----------SVAGIRPAYGLSIYGAMKAAVINLTKYLALELA-PKIR 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599489  84 VNVVAPGFVHTDMTKDL-------KEEHLKKNIPLGRFGETIEVAHAVVFLLESPYITGHVLVVDGGLQLI 147
Cdd:PRK06077  178 VNAIAPGFVKTKLGESLfkvlgmsEKEFAEKFTLMGKILDPEEVAEFVAAILKIESITGQVFVLDSGESLK 248
PRK09242 PRK09242
SDR family oxidoreductase;
5-144 5.19e-21

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 85.57  E-value: 5.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK09242  116 FETNLFSAFELSRYAHPLLKQHASSAIVNIG----------SVSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGIRV 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDL--KEEHLKKNI---PLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK09242  186 NAVAPWYIRTPLTSGPlsDPDYYEQVIertPMRRVGEPEEVAAAVAFLCmpAASYITGQCIAVDGGF 252
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-143 5.63e-21

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: 85.29  E-value: 5.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd08936   116 LDVNVKATALMTKAVVPEMEKRGGGSVVIVS----------SVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRV 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  85 NVVAPGFVHTDMTKDL-----KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd08936   186 NCLAPGLIKTSFSSALwmdkaVEESMKETLRIRRLGQPEDCAGIVSFLCseDASYITGETVVVGGG 251
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-146 6.15e-21

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: 85.21  E-value: 6.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:cd05331    99 NVTGVFNLLQAVAPHMKDRRTGAIVTVA----------SNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVV 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  88 APGFVHTDMTKDL-------------KEEHLKKNIPLGRFGETIEVAHAVVFLLeSP---YITGHVLVVDGGLQL 146
Cdd:cd05331   169 SPGSTDTAMQRTLwhdedgaaqviagVPEQFRLGIPLGKIAQPADIANAVLFLA-SDqagHITMHDLVVDGGATL 242
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 3-143 6.24e-21

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: 85.27  E-value: 6.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNsgQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:cd08937   107 AEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVS----------SIATRGIY--RIPYSAAKGGVNALTASLAFEHARDGI 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  83 RVNVVAPGFVHTDMTKDLKEEHLKKN----------------IPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd08937   175 RVNAVAPGGTEAPPRKIPRNAAPMSEqekvwyqrivdqtldsSLMGRYGTIDEQVRAILFLAsdEASYITGTVLPVGGG 253
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-143 6.40e-21

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: 85.59  E-value: 6.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd08935   126 LNLNGSFLPSQVFGKDMLEQKGGSIINIS----------SMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNA 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  87 VAPGFVHTDMTKDL----------KEEHLKKNIPLGRFGETIEVAHAVVFLLE---SPYITGHVLVVDGG 143
Cdd:cd08935   196 IAPGFFVTPQNRKLlinpdgsytdRSNKILGRTPMGRFGKPEELLGALLFLASekaSSFVTGVVIPVDGG 265
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 8-143 6.86e-21

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 84.94  E-value: 6.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVG----H--RREMllhkrsivglkgnsgqSVYSASKGGLVGFSRALAKEVARKK 81
Cdd:PRK08220  107 NAGGAFNLFRAVMPQFRRQRSGAIVTVGsnaaHvpRIGM----------------AAYGASKAALTSLAKCVGLELAPYG 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  82 IRVNVVAPGFVHTDMTKDL-KEEHLKKN------------IPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK08220  171 VRCNVVSPGSTDTDMQRTLwVDEDGEQQviagfpeqfklgIPLGKIARPQEIANAVLFLAsdLASHITLQDIVVDGG 247
PRK07577 PRK07577
SDR family oxidoreductase;
17-143 1.29e-20

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 84.01  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  17 KAAMRTMIQQQGGSIVNVGhrremllhKRSIVGLKGnsgQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDM 96
Cdd:PRK07577  108 QAFLEGMKLREQGRIVNIC--------SRAIFGALD---RTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  97 TKDLK------EEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK07577  177 FRQTRpvgseeEKRVLASIPMRRLGTPEEVAAAIAFLLsdDAGFITGQVLGVDGG 231
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 5-147 1.54e-20

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: 84.00  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGgSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05364   111 MNLNLRAVIYLTKLAVPHLIKTKG-EIVNVS----------SVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRV 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  85 NVVAPGFVHTDMTKD--LKEEHLKK-------NIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGLQLI 147
Cdd:cd05364   180 NSVSPGVIVTGFHRRmgMPEEQYIKflsrakeTHPLGRPGTVDEVAEAIAFLASdaSSFITGQLLPVDGGRHLM 253
PRK07774 PRK07774
SDR family oxidoreductase;
8-143 1.68e-20

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 84.03  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNvghrremllhkRSIVGLKGNSGqsVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK07774  117 NLDGALVCTRAVYKHMAKRGGGAIVN-----------QSSTAAWLYSN--FYGLAKVGLNGLTQQLARELGGMNIRVNAI 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  88 APGFVHTDMTKDLKEEHLK----KNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK07774  184 APGPIDTEATRTVTPKEFVadmvKGIPLSRMGTPEDLVGMCLFLLsdEASWITGQIFNVDGG 245
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 8-143 2.64e-20

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: 83.59  E-value: 2.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:cd05345   111 NVKSIYLSAQALVPHMEEQGGGVIINIA----------STAGLRPRPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCL 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  88 AP-----GFVHTDMTKDLKE--EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05345   181 CPvagetPLLSMFMGEDTPEnrAKFRATIPLGRLSTPDDIANAALYLAsdEASFITGVALEVDGG 245
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-143 2.86e-20

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 83.09  E-value: 2.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK06550   96 FDTNLTSTFLLTRAYLPQMLERKSGIIINMC----------SIASFVAGGGGAAYTASKHALAGFTKQLALDYAKDGIQV 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMT-KDLKEEHLKKNI----PLGRFGETIEVAHAVVFlLESP---YITGHVLVVDGG 143
Cdd:PRK06550  166 FGIAPGAVKTPMTaADFEPGGLADWVaretPIKRWAEPEEVAELTLF-LASGkadYMQGTIVPIDGG 231
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 8-143 4.76e-20

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 83.41  E-value: 4.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK08277  133 NLLGTLLPTQVFAKDMVGRKGGNIINIS----------SMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAI 202

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  88 APGFVHTDMTKDL----------KEEHLKKNIPLGRFGETIEVAHAVVFLLE---SPYITGHVLVVDGG 143
Cdd:PRK08277  203 APGFFLTEQNRALlfnedgslteRANKILAHTPMGRFGKPEELLGTLLWLADekaSSFVTGVVLPVDGG 271
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 7-143 5.15e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 82.70  E-value: 5.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQqGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK07890  113 LNVLGTLRLTQAFTPALAES-GGSIVMIN----------SMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNS 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  87 VAPGFVHTDMTK------------DLKE--EHLKKNIPLGRFGETIEVAHAVVFLLeSPY---ITGHVLVVDGG 143
Cdd:PRK07890  182 VAPGYIWGDPLKgyfrhqagkygvTVEQiyAETAANSDLKRLPTDDEVASAVLFLA-SDLaraITGQTLDVNCG 254
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 7-144 1.20e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 81.72  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLlhkrsivglkGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK08085  116 VNQTAVFLVSQAVARYMVKRQAGKIINICSMQSEL----------GRDTITPYAASKGAVKMLTRGMCVELARHNIQVNG 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  87 VAPGFVHTDMTKDLKEEH-----LKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGL 144
Cdd:PRK08085  186 IAPGYFKTEMTKALVEDEaftawLCKRTPAARWGDPQELIGAAVFLSSkaSDFVNGHLLFVDGGM 250
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
27-146 1.42e-19

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 81.70  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  27 QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKE---- 102
Cdd:PRK08643  130 HGGKIINAT----------SQAGVVGNPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHqvge 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489 103 ----------EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK08643  200 nagkpdewgmEQFAKDITLGRLSEPEDVANCVSFLAgpDSDYITGQTIIVDGGMVF 255
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 8-143 3.29e-19

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: 80.64  E-value: 3.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:cd05330   114 NLRGVFYGLEKVLKVMREQGSGMIVNTA----------SVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAI 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  88 APGFVHTDMT----KDLKEEHLKK-------NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05330   184 APGAILTPMVegslKQLGPENPEEageefvsVNPMKRFGEPEEVAAVVAFLLsdDAGYVNAAVVPIDGG 252
PRK06947 PRK06947
SDR family oxidoreductase;
7-143 5.80e-19

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 79.85  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGG---SIVNVGhrremllhkrSIVGLKGNSGQSV-YSASKGGLVGFSRALAKEVARKKI 82
Cdd:PRK06947  111 TNVLGAYLCAREAARRLSTDRGGrggAIVNVS----------SIASRLGSPNEYVdYAGSKGAVDTLTLGLAKELGPHGV 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  83 RVNVVAPGFVHTDM----TKDLKEEHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK06947  181 RVNAVRPGLIETEIhasgGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSdaASYVTGALLDVGGG 247
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-144 6.86e-19

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 79.75  E-value: 6.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRremlLHKRSIVGLKGnsgqsvYSASKGGLVGFSRALAKEVARKKI 82
Cdd:PRK08642  113 QQLEGSVKGALNTIQAALPGMREQGFGRIINIGTN----LFQNPVVPYHD------YTTAKAALLGLTRNLAAELGPYGI 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  83 RVNVVAPGFVHTD----MTKDLKEEHLKKNIPLGRFGETIEVAHAVVFLLeSPY---ITGHVLVVDGGL 144
Cdd:PRK08642  183 TVNMVSGGLLRTTdasaATPDEVFDLIAATTPLRKVTTPQEFADAVLFFA-SPWaraVTGQNLVVDGGL 250
PRK08628 PRK08628
SDR family oxidoreductase;
2-143 9.17e-19

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 79.62  E-value: 9.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   2 VSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKK 81
Cdd:PRK08628  107 VASLERNLIHYYVMAHYCL-PHLKASRGAIVNIS----------SKTALTGQGGTSGYAAAKGAQLALTREWAVALAKDG 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  82 IRVNVVAPGFVHTDM------TKDLKEEHLK---KNIPLG-RFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK08628  176 VRVNAVIPAEVMTPLyenwiaTFDDPEAKLAaitAKIPLGhRMTTAEEIADTAVFLLSerSSHTTGQWLFVDGG 249
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-101 1.08e-18

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 78.96  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK07666  112 IQVNLMGVYYATRAVLPSMIERQSGDIINIS----------STAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRV 181

                          90
                  ....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLK 101
Cdd:PRK07666  182 TALTPSTVATDMAVDLG 198
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
14-143 1.19e-18

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 79.18  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  14 LTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVH 93
Cdd:PRK12481  121 LSQAVAKQFVKQGNGGKIINIA----------SMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMA 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  94 TDMTKDLKEEHLK-----KNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK12481  191 TDNTAALRADTARneailERIPASRWGTPDDLAGPAIFLSSsaSDYVTGYTLAVDGG 247
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 5-143 1.28e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 79.20  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVN----VGHRremllhkrsiVGLKGNSgqsVYSASKGGLVGFSRALAKEVARK 80
Cdd:PRK07478  112 LATNLTSAFLGAKHQIPAMLARGGGSLIFtstfVGHT----------AGFPGMA---AYAASKAGLIGLTQVLAAEYGAQ 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  81 KIRVNVVAPGFVHTDMTKDL-----KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK07478  179 GIRVNALLPGGTDTPMGRAMgdtpeALAFVAGLHALKRMAQPEEIAQAALFLAsdAASFVTGTALLVDGG 248
PRK06128 PRK06128
SDR family oxidoreductase;
5-146 1.32e-18

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 79.90  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK06128  163 FKTNVYAMFWLCKAAIPHL--PPGASIINTG----------SIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRV 230

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  85 NVVAPGFVHTDM-----TKDLKEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK06128  231 NAVAPGPVWTPLqpsggQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLAsqESSYVTGEVFGVTGGLLL 299
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-148 1.40e-18

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 79.11  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLLHKRSivglkgnsgqSVYSASKGGLVGFSRALAKEVArKKIRV 84
Cdd:PRK06398  100 INVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNA----------AAYVTSKHAVLGLTRSIAVDYA-PTIRC 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  85 NVVAPGFVHT---DMTKDLK----EEHLKKNI-------PLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQLIL 148
Cdd:PRK06398  169 VAVCPGSIRTpllEWAAELEvgkdPEHVERKIrewgemhPMKRVGKPEEVAYVVAFLAsdLASFITGECVTVDGGLRALI 248
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 7-143 3.12e-18

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: 77.73  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQ---GGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKK-I 82
Cdd:cd05323   109 VNLTGVINTTYLALHYMDKNKggkGGVIVNIG----------SVAGLYPAPQFPVYSASKHGVVGFTRSLADLLEYKTgV 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599489  83 RVNVVAPGFVHTDMTKDLKEEHLKKNIPLGrFGETIEVAHAVVFLLESPYITGHVLVVDGG 143
Cdd:cd05323   179 RVNAICPGFTNTPLLPDLVAKEAEMLPSAP-TQSPEVVAKAIVYLIEDDEKNGAIWIVDGG 238
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 1-143 3.48e-18

(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: 77.75  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   1 MVSQLHtnLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARK 80
Cdd:cd05353   114 LVMRVH--LKGSFKVTRAAWPYMRKQKFGRIINTS----------SAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKY 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  81 KIRVNVVAPGfVHTDMTKDLKEEHLKKNI-PLGrfgetieVAHAVVFLL-ESPYITGHVLVVDGG 143
Cdd:cd05353   182 NITCNTIAPA-AGSRMTETVMPEDLFDALkPEY-------VAPLVLYLChESCEVTGGLFEVGAG 238
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 4-139 6.58e-18

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: 76.89  E-value: 6.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:cd05374   101 LFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVS----------SVAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIK 170

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  84 VNVVAPGFVHTDMTK----------------DLKEEHLKKNIPLGRFGETIE-VAHAVVFLLESPYITGHVLV 139
Cdd:cd05374   171 VTIIEPGPVRTGFADnaagsaledpeispyaPERKEIKENAAGVGSNPGDPEkVADVIVKALTSESPPLRYFL 243
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 28-142 9.25e-18

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 78.34  E-value: 9.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  28 GGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTkdlkeehlkK 107
Cdd:PRK08261  335 GGRIVGVS----------SISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT---------A 395

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462599489 108 NIPL-----GRF-------GETIEVAHAVVFLL--ESPYITGHVLVVDG 142
Cdd:PRK08261  396 AIPFatreaGRRmnslqqgGLPVDVAETIAWLAspASGGVTGNVVRVCG 444
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 30-143 9.49e-18

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: 76.75  E-value: 9.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  30 SIVNVGhrremllhkrSIVGLKGNSGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKE-----E 103
Cdd:cd08942   139 RVINIG----------SIAGIVVSGLENYsYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNdpaalE 208

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462599489 104 HLKKNIPLGRFGETIEVAHAVVFlLESP---YITGHVLVVDGG 143
Cdd:cd08942   209 AEEKSIPLGRWGRPEDMAGLAIM-LASRagaYLTGAVIPVDGG 250
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 8-143 9.99e-18

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 76.86  E-value: 9.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQ-QQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK13394  115 HVDGAFLTTKAALKHMYKdDRGGVVIYMG----------SVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHV 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  87 VAPGFVHT--------DMTKDL---KEEHLKK----NIPLGRFGETIEVAHAVVFLLESP--YITGHVLVVDGG 143
Cdd:PRK13394  185 VCPGFVRTplvdkqipEQAKELgisEEEVVKKvmlgKTVDGVFTTVEDVAQTVLFLSSFPsaALTGQSFVVSHG 258
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-143 1.52e-17

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 76.36  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLkGNS--GQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:PRK06463  107 IKINLNGAIYTTYEFLPLLKLSKNGAIVNIA----------SNAGI-GTAaeGTTFYAITKAGIIILTRRLAFELGKYGI 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  83 RVNVVAPGFVHTDMT---------KDLKEEHLKKNIpLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK06463  176 RVNAVAPGWVETDMTlsgksqeeaEKLRELFRNKTV-LKTTGKPEDIANIVLFLAsdDARYITGQVIVADGG 246
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
17-143 1.55e-17

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 76.07  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  17 KAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTD 95
Cdd:PRK08993  125 QAAAKHFIAQgNGGKIINIA----------SMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  96 MTKDLK--EEHLKK---NIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK08993  195 NTQQLRadEQRSAEildRIPAGRWGLPSDLMGPVVFLASsaSDYINGYTIAVDGG 249
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-146 1.68e-17

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 76.30  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGHRREML-----LHkrsivglkgnsgqsvYSASKGGLVGFSRALAKEVARK 80
Cdd:PRK08936  115 TNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIpwplfVH---------------YAASKGGVKLMTETLAMEYAPK 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  81 KIRVNVVAPGFVHTDMTKDLKEEHLKKN-----IPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK08936  180 GIRVNNIGPGAINTPINAEKFADPKQRAdvesmIPMGYIGKPEEIAAVAAWLAssEASYVTGITLFADGGMTL 252
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 3-140 2.58e-17

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: 75.09  E-value: 2.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:cd08932    99 AHFSINVIAPAELTRALLPALREAGSGRVVFLN----------SLSGKRVLAGNAGYSASKFALRALAHALRQEGWDHGV 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  83 RVNVVAPGFVHTDMtkdLKEEHLKKNIPLGRFGETIEVAHAVVFLLESPYITGHVLVV 140
Cdd:cd08932   169 RVSAVCPGFVDTPM---AQGLTLVGAFPPEEMIQPKDIANLVRMVIELPENITSVAVL 223
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 7-141 4.57e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 75.04  E-value: 4.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQG-GSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:PRK06198  114 VNVRAPFFLMQEAIKLMRRRKAeGTIVNIG----------SMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVN 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  86 VVAPGFVHTDMTKDL-KEEHLK---------KNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVD 141
Cdd:PRK06198  184 GLNIGWMATEGEDRIqREFHGApddwlekaaATQPFGRLLDPDEVARAVAFLLsdESGLMTGSVIDFD 251
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-146 5.59e-17

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: 74.81  E-value: 5.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQG------GSIVNVGhrremllhKRSIVGLKGNSGQsvYSASKGGLVGFSRALAKEVARK 80
Cdd:cd05337   111 INLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVT--------SINAYLVSPNRGE--YCISKAGLSMATRLLAYRLADE 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  81 KIRVNVVAPGFVHTDMTKDLKEEHLKK----NIPLGRFGETIEVAHAVVFLLES--PYITGHVLVVDGGLQL 146
Cdd:cd05337   181 GIAVHEIRPGLIHTDMTAPVKEKYDELiaagLVPIRRWGQPEDIAKAVRTLASGllPYSTGQPINIDGGLSM 252
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-144 5.70e-17

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 74.88  E-value: 5.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRT--MIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd08945   110 TNLTGVFRVTKEVLKAggMLERGTGRIINIA----------STGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITV 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  85 NVVAPGFVHTDMTKDLKE--------------EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd08945   180 NAVCPGFVETPMAASVREhyadiwevsteeafDRITARVPLGRYVTPEEVAGMVAYLIgdGAAAVTAQALNVCGGL 255
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 8-143 5.70e-17

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: 74.79  E-value: 5.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:cd08940   112 NLSAVFHTTRLALPHMKKQGWGRIINIA----------SVHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAI 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  88 APGFVHTDMTK----DL-----------KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd08940   182 CPGWVLTPLVEkqisALaqkngvpqeqaARELLLEKQPSKQFVTPEQLGDTAVFLAsdAASQITGTAVSVDGG 254
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-143 7.97e-17

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 74.44  E-value: 7.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  13 MLTCKAAmRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFV 92
Cdd:PRK12859  133 LLSSQFA-RGFDKKSGGRIINM----------TSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPT 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  93 HTD-MTKDLKeEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK12859  202 DTGwMTEEIK-QGLLPMFPFGRIGEPKDAARLIKFLAseEAEWITGQIIHSEGG 254
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
8-143 8.13e-17

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 74.29  E-value: 8.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK07067  111 NVKGLFFLMQAVARHMVEQgRGGKIINMA----------SQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNA 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  87 VAPGFVHTDM-----TKDLKEEHLK---------KNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK07067  181 IAPGVVDTPMwdqvdALFARYENRPpgekkrlvgEAVPLGRMGVPDDLTGMALFLAsaDADYIVAQTYNVDGG 253
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 16-143 8.95e-17

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 74.21  E-value: 8.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  16 CKAAMRTMIQQQGGSIVNVGHrremlLHKRSIvglkgnsgQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAPGFV-- 92
Cdd:PRK12823  124 CRAVLPHMLAQGGGAIVNVSS-----IATRGI--------NRVpYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTea 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  93 -----------HTDMTKDLKEEHLKKNI---PLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK12823  191 pprrvprnaapQSEQEKAWYQQIVDQTLdssLMKRYGTIDEQVAAILFLAsdEASYITGTVLPVGGG 257
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 12-143 9.40e-17

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: 73.76  E-value: 9.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  12 SMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGF 91
Cdd:cd05361   108 PFALLQAAIAQMKKAGGGSIIFI----------TSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNF 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  92 VHTDM---TKDLKE-----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05361   178 FNSPTyfpTSDWENnpelrERVKRDVPLGRLGRPDEMGALVAFLAsrRADPITGQFFAFAGG 239
PRK07041 PRK07041
SDR family oxidoreductase;
55-143 1.55e-16

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 73.15  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  55 GQSVYSASKGGLVGFSRALAKEVArkKIRVNVVAPGFVHTD----MTKDLKEEHL---KKNIPLGRFGETIEVAHAVVFL 127
Cdd:PRK07041  133 SGVLQGAINAALEALARGLALELA--PVRVNTVSPGLVDTPlwskLAGDAREAMFaaaAERLPARRVGQPEDVANAILFL 210

                          90
                  ....*....|....*.
gi 2462599489 128 LESPYITGHVLVVDGG 143
Cdd:PRK07041  211 AANGFTTGSTVLVDGG 226
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-145 1.70e-16

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 73.57  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrsivglkgNSGQSV--------YSASKGGLVGFSRALAKEVAR 79
Cdd:PRK12748  126 NVRATMLLSSAFAKQYDGKAGGRIINL------------------TSGQSLgpmpdelaYAATKGAIEAFTKSLAPELAE 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  80 KKIRVNVVAPGFVHTD-MTKDLKeEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQ 145
Cdd:PRK12748  188 KGITVNAVNPGPTDTGwITEELK-HHLVPKFPQGRVGEPVDAARLIAFLVseEAKWITGQVIHSEGGFS 255
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-144 1.96e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 73.56  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK07097  117 IDLNAPFIVSKAVIPSMIKKGHGKIINIC----------SMMSELGRETVSAYAAAKGGLKMLTKNIASEYGEANIQCNG 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599489  87 VAPGFVHTDMTKDLKEEHLKKN-----------IPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGL 144
Cdd:PRK07097  187 IGPGYIATPQTAPLRELQADGSrhpfdqfiiakTPAARWGDPEDLAGPAVFLASdaSNFVNGHILYVDGGI 257
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 7-131 3.58e-16

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 72.57  E-value: 3.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd08934   110 TNLLGLMYTTHAALPHHLLRNKGTIVNIS----------SVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVV 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  87 VAPGFVHTDM--------TKDLKEEHLKKNIPLgrfgETIEVAHAVVFLLESP 131
Cdd:cd08934   180 IEPGTVDTELrdhithtiTKEAYEERISTIRKL----QAEDIAAAVRYAVTAP 228
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-131 4.00e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 72.67  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:PRK07825  104 RILDVNVYGVILGSKLAAPRMVPRGRGHVVNVA----------SLAGKIPVPGMATYCASKHAVVGFTDAARLELRGTGV 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462599489  83 RVNVVAPGFVHTDMTKDLKEEHLKKNIplgrfgETIEVAHAVVFLLESP 131
Cdd:PRK07825  174 HVSVVLPSFVNTELIAGTGGAKGFKNV------EPEDVAAAIVGTVAKP 216
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 55-147 4.13e-16

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: 72.65  E-value: 4.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  55 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGF--VHTDMTKDLKEEHLKKnIPLGRFGETIE-VAHAVVFLL--E 129
Cdd:TIGR02685 169 GFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLslLPDAMPFEVQEDYRRK-VPLGQREASAEqIADVVIFLVspK 247

                          90
                  ....*....|....*...
gi 2462599489 130 SPYITGHVLVVDGGLQLI 147
Cdd:TIGR02685 248 AKYITGTCIKVDGGLSLT 265
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 5-146 9.20e-16

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: 71.41  E-value: 9.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGgSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd08933   116 LNLNLISYFLASKYALPHLRKSQG-NIINLS----------SLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRV 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  85 NVVAPGFVHTDMTKDL-----------KEEHLKKniPLGRFGETIEVAHAVVFLL-ESPYITGHVLVVDGGLQL 146
Cdd:cd08933   185 NCISPGNIWTPLWEELaaqtpdtlatiKEGELAQ--LLGRMGTEAESGLAALFLAaEATFCTGIDLLLSGGAEL 256
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 8-143 1.07e-15

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: 71.06  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:cd05365   108 NLFSAFRLSQLCAPHMQKAGGGAILNIS----------SMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAV 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  88 APGFVHTDMTK----DLKEEHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:cd05365   178 APGAVKTDALAsvltPEIERAMLKHTPLGRLGEPEDIANAALFLCSpaSAWVSGQVLTVSGG 239
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 5-143 1.20e-15

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 71.19  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK08265  107 LDVNLVSAAMLAQAAHPHLARG-GGAIVNFT----------SISAKFAQTGRWLYPASKAAIRQLTRSMAMDLAPDGIRV 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKKNI-------PLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK08265  176 NSVSPGWTWSRVMDELSGGDRAKADrvaapfhLLGRVGDPEEVAQVVAFLCsdAASFVTGADYAVDGG 243
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 5-144 1.26e-15

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 70.99  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVG-------HRREMLLHK----------RSIVGLKGNSGQSVYSASKGGLV 67
Cdd:cd05328    80 LKVNYFGLRALMEALLPRLRKGHGPAAVVVSsiagagwAQDKLELAKalaagtearaVALAEHAGQPGYLAYAGSKEALT 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  68 GFSRALAKE-VARKKIRVNVVAPGFVHTDMTKDLKEEHLKKNI------PLGRFGETIEVAHAVVFLLeSP---YITGHV 137
Cdd:cd05328   160 VWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGGESvdafvtPMGRRAEPDEIAPVIAFLA-SDaasWINGAN 238


                  ....*..
gi 2462599489 138 LVVDGGL 144
Cdd:cd05328   239 LFVDGGL 245
PRK07814 PRK07814
SDR family oxidoreductase;
18-145 1.28e-15

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 71.35  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  18 AAMRTMIQQQG-GSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVArKKIRVNVVAPGFVHTD- 95
Cdd:PRK07814  128 AAVPLMLEHSGgGSVINIS----------STMGRLAGRGFAAYGTAKAALAHYTRLAALDLC-PRIRVNAIAPGSILTSa 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  96 ----MTKDLKEEHLKKNIPLGRFGETIEVAHAVVFlLESP---YITGHVLVVDGGLQ 145
Cdd:PRK07814  197 levvAANDELRAPMEKATPLRRLGDPEDIAAAAVY-LASPagsYLTGKTLEVDGGLT 252
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 5-143 2.93e-15

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 70.06  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGHrremllhKRSIVGLKGNSGqsvYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK12384  109 LQVNLVGYFLCAREFSRLMIRDGiQGRIIQINS-------KSGKVGSKHNSG---YSAAKFGGVGLTQSLALDLAEYGIT 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  84 VNVVAPG-FVHTDMTKDLKEEHLKK--------------NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK12384  179 VHSLMLGnLLKSPMFQSLLPQYAKKlgikpdeveqyyidKVPLKRGCDYQDVLNMLLFYAspKASYCTGQSINVTGG 255
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 16-143 5.05e-15

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 69.49  E-value: 5.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  16 CKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTD 95
Cdd:PRK06113  126 SQLVAPEMEKNGGGVILTIT----------SMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  96 -----MTKDLkEEHLKKNIPLGRFGETIEVAHAVVFLLeSP---YITGHVLVVDGG 143
Cdd:PRK06113  196 alksvITPEI-EQKMLQHTPIRRLGQPQDIANAALFLC-SPaasWVSGQILTVSGG 249
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-144 7.72e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 69.03  E-value: 7.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLlhkrsivglkGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK07523  115 LRTNISSVFYVGQAVARHMIARGAGKIINIASVQSAL----------ARPGIAPYTATKGAVGNLTKGMATDWAKHGLQC 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEH-----LKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGL 144
Cdd:PRK07523  185 NAIAPGYFDTPLNAALVADPefsawLEKRTPAGRWGKVEELVGACVFLASdaSSFVNGHVLYVDGGI 251
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-144 8.99e-15

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: 68.76  E-value: 8.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGHRRemllhkrsivGLKGNSGQSVYSASKGGLVGFSRALAKEVARkKIRV 84
Cdd:cd09761   103 LSVNLTGPYELSRYCRDELIKN-KGRIINIASTR----------AFQSEPDSEAYAASKGGLVALTHALAMSLGP-DIRV 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKK----NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:cd09761   171 NCISPGWINTTEQQEFTAAPLTQedhaQHPAGRVGTPKDIANLVLFLCqqDAGFITGETFIVDGGM 236
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 3-95 1.18e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 68.53  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKI 82
Cdd:PRK08263  103 AQIDTNFFGALWVTQAVLPYLREQRSGHIIQIS----------SIGGISAFPMSGIYHASKWALEGMSEALAQEVAEFGI 172

                          90
                  ....*....|...
gi 2462599489  83 RVNVVAPGFVHTD 95
Cdd:PRK08263  173 KVTLVEPGGYSTD 185
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 8-143 1.32e-14

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: 68.41  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05363   108 NVSGTLFMMQAVARAMIAQgRGGKIINMA----------SQAGRRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNA 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  87 VAPGFVHTDMTKDL--------------KEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05363   178 IAPGVVDGEHWDGVdakfaryenrprgeKKRLVGEAVPFGRMGRAEDLTGMAIFLAstDADYIVAQTYNVDGG 250
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 5-131 1.87e-14

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 66.77  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd02266    59 IRANVVGTRRLLEAARELMKAKRLGRFILIS----------SVAGLFGAPGLGGYAASKAALDGLAQQWASEGWGNGLPA 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462599489  85 NVVAPGFVHTDMTKDLK---EEHLKKNIPLGRFGETIEVAHAVVFLLESP 131
Cdd:cd02266   129 TAVACGTWAGSGMAKGPvapEEILGNRRHGVRTMPPEEVARALLNALDRP 178
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 8-146 2.67e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 67.91  E-value: 2.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK05875  118 NVNGTMYVLKHAARELVRGGGGSFVGIS----------SIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSI 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  88 APGFVHTDMTKDLKE-----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK05875  188 RPGLIRTDLVAPITEspelsADYRACTPLPRVGEVEDVANLAMFLLsdAASWITGQVINVDGGHML 253
PRK07831 PRK07831
SDR family oxidoreductase;
9-140 2.93e-14

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 67.37  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   9 LLGSMLTCKAAMRTMI-QQQGGSIVNvghrremllhKRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK07831  129 LTGTFRATRAALRYMRaRGHGGVIVN----------NASVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAV 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  88 APGF-VHTDMTK----DLKEEhLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVV 140
Cdd:PRK07831  199 APSIaMHPFLAKvtsaELLDE-LAAREAFGRAAEPWEVANVIAFLASdySSYLTGEVVSV 257
PRK07985 PRK07985
SDR family oxidoreductase;
59-146 4.32e-14

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 67.33  E-value: 4.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  59 YSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDM------TKDlKEEHLKKNIPLGRFGETIEVAHAVVFLL--ES 130
Cdd:PRK07985  199 YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALqisggqTQD-KIPQFGQQTPMKRAGQPAELAPVYVYLAsqES 277

                          90
                  ....*....|....*.
gi 2462599489 131 PYITGHVLVVDGGLQL 146
Cdd:PRK07985  278 SYVTAEVHGVCGGEHL 293
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 5-97 4.62e-14

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: 66.58  E-value: 4.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05350   103 IDTNLLGAAAILEAALPQFRAKGRGHLVLIS----------SVAALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRV 172

                          90
                  ....*....|...
gi 2462599489  85 NVVAPGFVHTDMT 97
Cdd:cd05350   173 TVINPGFIDTPLT 185
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 6-144 4.74e-14

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: 66.99  E-value: 4.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   6 HTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVArKKIRVN 85
Cdd:cd05348   112 HINVKGYILGAKAALPALYATEGSVIFTV-----------SNAGFYPGGGGPLYTASKHAVVGLVKQLAYELA-PHIRVN 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  86 VVAPGFVHTDMTKDLKEEHLKKNI-------------PLGRFGETIEVAHAVVFLL---ESPYITGHVLVVDGGL 144
Cdd:cd05348   180 GVAPGGMVTDLRGPASLGQGETSIstpplddmlksilPLGFAPEPEDYTGAYVFLAsrgDNRPATGTVINYDGGM 254
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
8-144 5.52e-14

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 67.95  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQ-GGSIVNVGHrremllhKRSIVGLKGNSGqsvYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK08324  529 NATGHFLVAREAVRIMKAQGlGGSIVFIAS-------KNAVNPGPNFGA---YGAAKAAELHLVRQLALELGPDGIRVNG 598

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  87 VAPGFVHTD-----------------MTKDLKEEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK08324  599 VNPDAVVRGsgiwtgewiearaaaygLSEEELEEFYRARNLLKREVTPEDVAEAVVFLAsgLLSKTTGAIITVDGGN 675
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 6-125 5.60e-14

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: 66.50  E-value: 5.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   6 HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVAR---KKI 82
Cdd:cd05339   105 EVNTLAHFWTTKAFLPDMLERNHGHIVTIA----------SVAGLISPAGLADYCASKAAAVGFHESLRLELKAygkPGI 174

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462599489  83 RVNVVAPGFVHTDMTKDLKeehlkknIPLGRFGETIE---VAHAVV 125
Cdd:cd05339   175 KTTLVCPYFINTGMFQGVK-------TPRPLLAPILEpeyVAEKIV 213
PRK09072 PRK09072
SDR family oxidoreductase;
4-96 6.18e-14

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 66.50  E-value: 6.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK09072  107 LLALNLTAPMQLTRALLPLLRAQPSAMVVNVG----------STFGSIGYPGYASYCASKFALRGFSEALRRELADTGVR 176

                          90
                  ....*....|...
gi 2462599489  84 VNVVAPGFVHTDM 96
Cdd:PRK09072  177 VLYLAPRATRTAM 189
PLN02253 PLN02253
xanthoxin dehydrogenase
 8-143 8.14e-14

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 66.39  E-value: 8.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PLN02253  127 NVKGVFLGMKHAARIMIPLKKGSIVSLC----------SVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCV 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  88 APGFVHTDMT-KDLKEEHLKKNIPLGRFG--------ETIE-----VAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PLN02253  197 SPYAVPTALAlAHLPEDERTEDALAGFRAfagknanlKGVEltvddVANAVLFLAsdEARYISGLNLMIDGG 268
PRK07062 PRK07062
SDR family oxidoreductase;
4-144 1.34e-13

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 65.83  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK07062  114 ELELKYFSVINPTRAFLPLLRASAAASIVCVN----------SLLALQPEPHMVATSAARAGLLNLVKSLATELAPKGVR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  84 VNVVAPGFVHT------------------DMTKDLKEehlKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK07062  184 VNSILLGLVESgqwrrryearadpgqsweAWTAALAR---KKGIPLGRLGRPDEAARALFFLASplSSYTTGSHIDVSGG 260


                  .
gi 2462599489 144 L 144
Cdd:PRK07062  261 F 261
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 55-146 1.71e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 65.36  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  55 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVhtDMTKDLK--------EEHLKKNIPLGRFGETIEVAHAVVF 126
Cdd:PRK07576  153 MQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPI--AGTEGMArlapspelQAAVAQSVPLKRNGTKQDIANAALF 230

                          90       100
                  ....*....|....*....|...
gi 2462599489 127 lLESP---YITGHVLVVDGGLQL 146
Cdd:PRK07576  231 -LASDmasYITGVVLPVDGGWSL 252
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 7-98 1.92e-13

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: 64.57  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGlkgnSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05324   109 TNFFGTVDVTQALLPLLKKSPAGRIVNVS----------SGLG----SLTSAYGVSKAALNALTRILAKELKETGIKVNA 174

                          90
                  ....*....|..
gi 2462599489  87 VAPGFVHTDMTK 98
Cdd:cd05324   175 CCPGWVKTDMGG 186
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 6-146 5.95e-13

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 63.82  E-value: 5.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   6 HTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVArKKIRVN 85
Cdd:PRK06200  114 NVNVKGYLLGAKAALPALKASGGSMIFTL-----------SNSSFYPGGGGPLYTASKHAVVGLVRQLAYELA-PKIRVN 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599489  86 VVAPGFVHTDM----TKDLKEEHLKKN----------IPLGRFGETIEVAHAVVFLL---ESPYITGHVLVVDGGLQL 146
Cdd:PRK06200  182 GVAPGGTVTDLrgpaSLGQGETSISDSpgladmiaaiTPLQFAPQPEDHTGPYVLLAsrrNSRALTGVVINADGGLGI 259
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-148 6.24e-13

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 63.58  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNV---GHRRemLLHKRSIVGlkgnsgqsvysASKGGLVGFSRALAKEVARKK 81
Cdd:PRK08063  110 MNINAKALLFCAQEAAKLMEKVGGGKIISLsslGSIR--YLENYTTVG-----------VSKAALEALTRYLAVELAPKG 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  82 IRVNVVAPGFVHTDMTKDL--KEEHLK---KNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQLIL 148
Cdd:PRK08063  177 IAVNAVSGGAVDTDALKHFpnREELLEdarAKTPAGRMVEPEDVANAVLFLCspEADMIRGQTIIVDGGRSLLV 250
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-98 7.63e-13

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: 63.39  E-value: 7.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd05356   108 INVNVMATLKMTRLILPGMVKRKKGAIVNIS----------SFAGLIPTPLLATYSASKAFLDFFSRALYEEYKSQGIDV 177

                          90
                  ....*....|....
gi 2462599489  85 NVVAPGFVHTDMTK 98
Cdd:cd05356   178 QSLLPYLVATKMSK 191
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 5-143 7.80e-13

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: 63.64  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGHrremllhKRSIVGLKGNSGqsvYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:cd05322   108 LQVNLVGYFLCAREFSKLMIRDGiQGRIIQINS-------KSGKVGSKHNSG---YSAAKFGGVGLTQSLALDLAEHGIT 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  84 VNVVAPG-FVHTDMTKDL----------KEEHLKK----NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:cd05322   178 VNSLMLGnLLKSPMFQSLlpqyakklgiKESEVEQyyidKVPLKRGCDYQDVLNMLLFYAspKASYCTGQSINITGG 254
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-98 1.04e-12

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: 63.04  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd08939   112 VNYFGSLNVAHAVLPLMKEQRPGHIVFVS----------SQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSV 181

                          90
                  ....*....|....*...
gi 2462599489  87 VAP------GFVHTDMTK 98
Cdd:cd08939   182 VYPpdtdtpGFEEENKTK 199
PRK05717 PRK05717
SDR family oxidoreductase;
5-144 1.81e-12

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 62.60  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGHRREMllhkrsivglKGNSGQSVYSASKGGLVGFSRALAKEVArKKIRV 84
Cdd:PRK05717  114 LAVNLTGPMLLAKHCA-PYLRAHNGAIVNLASTRAR----------QSEPDTEAYAASKGGLLALTHALAISLG-PEIRV 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKK----NIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK05717  182 NAVSPGWIDARDPSQRRAEPLSEadhaQHPAGRVGTVEDVAAMVAWLLsrQAGFVTGQEFVVDGGM 247
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-146 2.39e-12

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 62.29  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGhrremllhKRSIVGLKGNSGQsvYSASKGGLVGFSRALAKEVA 78
Cdd:PRK12745  110 LAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVS--------SVNAIMVSPNRGE--YCISKAGLSMAAQLFAARLA 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599489  79 RKKIRVNVVAPGFVHTDMTKDLKEEH----LKKNIPLGRFGETIEVAHAVVFLLES--PYITGHVLVVDGGLQL 146
Cdd:PRK12745  180 EEGIGVYEVRPGLIKTDMTAPVTAKYdaliAKGLVPMPRWGEPEDVARAVAALASGdlPYSTGQAIHVDGGLSI 253
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 71-143 4.10e-12

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: 61.58  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  71 RALAKEVARKKIRVNVVAPGFVHT-------DMTKDLKeeHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVD 141
Cdd:COG0623   169 RYLAADLGPKGIRVNAISAGPIKTlaasgipGFDKLLD--YAEERAPLGRNVTIEEVGNAAAFLLsdLASGITGEIIYVD 246


                  ..
gi 2462599489 142 GG 143
Cdd:COG0623   247 GG 248
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 5-131 9.15e-12

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: 60.21  E-value: 9.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:cd08929   102 LDTNLTGAFYCIHKAAPALLRRGGGTIVNVG----------SLAGKNAFKGGAAYNASKFGLLGLSEAAMLDLREANIRV 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462599489  85 NVVAPGFVHTDMTKDLKEE--HLKKNiplgrfgetiEVAHAVVFLLESP 131
Cdd:cd08929   172 VNVMPGSVDTGFAGSPEGQawKLAPE----------DVAQAVLFALEMP 210
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-95 1.05e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 60.70  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   1 MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARK 80
Cdd:PRK06180  102 MRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNI----------TSMGGLITMPGIGYYCGSKFALEGISESLAKEVAPF 171

                          90
                  ....*....|....*
gi 2462599489  81 KIRVNVVAPGFVHTD 95
Cdd:PRK06180  172 GIHVTAVEPGSFRTD 186
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 7-95 1.08e-11

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: 60.37  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05346   109 TNVKGLLNVTRLILPIMIARNQGHIINLG----------SIAGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTN 178


                  ....*....
gi 2462599489  87 VAPGFVHTD 95
Cdd:cd05346   179 IEPGLVETE 187
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 9-145 1.26e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 60.06  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   9 LLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrsiVGLKGNSGQSVY---SASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:PRK06125  113 VFGYIDLTRLAYPRMKARGSGVIVNV-------------IGAAGENPDADYicgSAGNAALMAFTRALGGKSLDDGVRVV 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  86 VVAPGFVHTD-MTKDLKE------------EHLKKNIPLGRFGETIEVAHAVVFlLESP---YITGHVLVVDGGLQ 145
Cdd:PRK06125  180 GVNPGPVATDrMLTLLKGraraelgdesrwQELLAGLPLGRPATPEEVADLVAF-LASPrsgYTSGTVVTVDGGIS 254
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
27-144 2.03e-11

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 59.63  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  27 QGGSIVNV------GHRREMLLHKrSIVGLKG-NSGQSV-----------YSASKGGLV--GFSRALAKEVARKkIRVNV 86
Cdd:PRK12428   88 PGGAIVNVaslagaEWPQRLELHK-ALAATASfDEGAAWlaahpvalatgYQLSKEALIlwTMRQAQPWFGARG-IRVNC 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  87 VAPGFVHTDMTKDLK----EEHLKKNI-PLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK12428  166 VAPGPVFTPILGDFRsmlgQERVDSDAkRMGRPATADEQAAVLVFLCsdAARWINGVNLPVDGGL 230
PRK09134 PRK09134
SDR family oxidoreductase;
59-146 2.21e-11

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 59.56  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  59 YSASKGGLVGFSRALAKEVArKKIRVNVVAPG--FVHTDMT-KDLKEEHlkKNIPLGRFGETIEVAHAVVFLLESPYITG 135
Cdd:PRK09134  159 YTLSKAALWTATRTLAQALA-PRIRVNAIGPGptLPSGRQSpEDFARQH--AATPLGRGSTPEEIAAAVRYLLDAPSVTG 235

                          90
                  ....*....|.
gi 2462599489 136 HVLVVDGGLQL 146
Cdd:PRK09134  236 QMIAVDGGQHL 246
PRK06482 PRK06482
SDR family oxidoreductase;
4-100 3.56e-11

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 58.97  E-value: 3.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK06482  103 QIDTNLIGSIQVIRAALPHLRRQGGGRIVQVS----------SEGGQIAYPGFSLYHATKWGIEGFVEAVAQEVAPFGIE 172

                          90
                  ....*....|....*..
gi 2462599489  84 VNVVAPGFVHTDMTKDL 100
Cdd:PRK06482  173 FTIVEPGPARTNFGAGL 189
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 7-103 3.61e-11

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: 58.75  E-value: 3.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05332   111 VNYFGPVALTKAALPHLIERSQGSIVVVS----------SIAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTV 180

                          90
                  ....*....|....*...
gi 2462599489  87 VAPGFVHTDMT-KDLKEE 103
Cdd:cd05332   181 VCPGLIDTNIAmNALSGD 198
PRK07326 PRK07326
SDR family oxidoreductase;
5-131 4.07e-11

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 58.48  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMiQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK07326  110 IDTNLTGAFYTIKAAVPAL-KRGGGYIINIS----------SLAGTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKV 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462599489  85 NVVAPGFVHTdmtkdlkeeHLKKNIPLGRFGETI---EVAHAVVFLLESP 131
Cdd:PRK07326  179 STIMPGSVAT---------HFNGHTPSEKDAWKIqpeDIAQLVLDLLKMP 219
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 8-143 4.56e-11

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: 58.56  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQ-GGSIVNVGHrremllhKRSIVGLKGNSGqsvYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd08943   108 NLTGHFLVSREAFRIMKSQGiGGNIVFNAS-------KNAVAPGPNAAA---YSAAKAAEAHLARCLALEGGEDGIRVNT 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  87 VAP-----GFVHTDM--------TKDLKEEHLKKNIPLGRFGETIEVAHAVVFLLESPY--ITGHVLVVDGG 143
Cdd:cd08943   178 VNPdavfrGSKIWEGvwraarakAYGLLEEEYRTRNLLKREVLPEDVAEAVVAMASEDFgkTTGAIVTVDGG 249
PRK08264 PRK08264
SDR family oxidoreductase;
4-100 6.31e-11

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 57.98  E-value: 6.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK08264  101 EMETNYFGPLAMARAFAPVLAANGGGAIVNV----------LSVLSWVNFPNLGTYSASKAAAWSLTQALRAELAPQGTR 170

                          90
                  ....*....|....*..
gi 2462599489  84 VNVVAPGFVHTDMTKDL 100
Cdd:PRK08264  171 VLGVHPGPIDTDMAAGL 187
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 58-143 6.81e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 58.15  E-value: 6.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  58 VYSAS-KGGLVGFSRALAKEVARK-KIRVNVVAPGFVHTDMTKD---LKEEHLKK---NIPLGRFGETIEVAHAVVFLL- 128
Cdd:PRK07677  149 IHSAAaKAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERTGGADklwESEEAAKRtiqSVPLGRLGTPEEIAGLAYFLLs 228

                          90
                  ....*....|....*.
gi 2462599489 129 -ESPYITGHVLVVDGG 143
Cdd:PRK07677  229 dEAAYINGTCITMDGG 244
PRK05650 PRK05650
SDR family oxidoreductase;
4-109 8.67e-11

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 58.13  E-value: 8.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK05650  104 QIAINLMGVVKGCKAFLPLFKRQKSGRIVNIA----------SMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIG 173

                          90       100
                  ....*....|....*....|....*...
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEE--HLKKNI 109
Cdd:PRK05650  174 VHVVCPSFFQTNLLDSFRGPnpAMKAQV 201
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 7-131 1.64e-10

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: 57.01  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKK--IRV 84
Cdd:cd05360   107 VNYLGHVYGTLAALPHLRRRGGGALINVG----------SLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHDGapISV 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLKEEHLKKNIPLGRFGETIEVAHAVVFLLESP 131
Cdd:cd05360   177 TLVQPTAMNTPFFGHARSYMGKKPKPPPPIYQPERVAEAIVRAAEHP 223
PRK09186 PRK09186
flagellin modification protein A; Provisional
 5-146 2.26e-10

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 56.92  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL--------KGNSGQSV--YSASKGGLVGFSRALA 74
Cdd:PRK09186  114 LSLHLGSSFLFSQQFAKYFKKQGGGNLVNIS----------SIYGVvapkfeiyEGTSMTSPveYAAIKAGIIHLTKYLA 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  75 KEVARKKIRVNVVAPGFVhtdmtKDLK-EEHLKK------NIPLgrfGETIEVAHAVVFLL--ESPYITGHVLVVDGGLQ 145
Cdd:PRK09186  184 KYFKDSNIRVNCVSPGGI-----LDNQpEAFLNAykkccnGKGM---LDPDDICGTLVFLLsdQSKYITGQNIIVDDGFS 255


                  .
gi 2462599489 146 L 146
Cdd:PRK09186  256 L 256
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 66-143 2.66e-10

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 56.79  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  66 LVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKEEHLK--------------KNIPLGRFGETIEVAHAVVFLLE-- 129
Cdd:PRK08339  164 MAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKregksveealqeyaKPIPLGRLGEPEEIGYLVAFLASdl 243

                          90
                  ....*....|....
gi 2462599489 130 SPYITGHVLVVDGG 143
Cdd:PRK08339  244 GSYINGAMIPVDGG 257
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 71-144 3.02e-10

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 56.44  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  71 RALAKEVARKKIRVNVVAPGFVHT-------DMTKDLkeEHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVD 141
Cdd:cd05372   166 RYLAYELGRKGIRVNAISAGPIKTlaasgitGFDKML--EYSEQRAPLGRNVTAEEVGNTAAFLLsdLSSGITGEIIYVD 243


                  ...
gi 2462599489 142 GGL 144
Cdd:cd05372   244 GGY 246
PRK08416 PRK08416
enoyl-ACP reductase;
46-143 3.24e-10

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 56.32  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  46 SIVGLKgNSGQSVY-------SASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTK------DLKEEHLKKNiPLG 112
Cdd:PRK08416  146 SIISLS-STGNLVYienyaghGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKaftnyeEVKAKTEELS-PLN 223

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462599489 113 RFGETIEVAHAVVFLL--ESPYITGHVLVVDGG 143
Cdd:PRK08416  224 RMGQPEDLAGACLFLCseKASWLTGQTIVVDGG 256
PRK08251 PRK08251
SDR family oxidoreductase;
7-97 4.38e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 55.71  E-value: 4.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG-QSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:PRK08251  111 TNFVAALAQCEAAMEIFREQGSGHLVLIS----------SVSAVRGLPGvKAAYAASKAGVASLGEGLRAELAKTPIKVS 180

                          90
                  ....*....|..
gi 2462599489  86 VVAPGFVHTDMT 97
Cdd:PRK08251  181 TIEPGYIRSEMN 192
PRK06914 PRK06914
SDR family oxidoreductase;
4-134 5.90e-10

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 55.80  E-value: 5.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK06914  108 QFETNVFGAISVTQAVLPYMRKQKSGKIINIS----------SISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGID 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599489  84 VNVVAPGFVHTDM---TKDLKEEHLKKNIP---------------LGRFGETIEVAHAVVFLLESPYIT 134
Cdd:PRK06914  178 VALIEPGSYNTNIwevGKQLAENQSETTSPykeymkkiqkhinsgSDTFGNPIDVANLIVEIAESKRPK 246
PRK08219 PRK08219
SDR family oxidoreductase;
49-131 7.11e-10

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 54.94  E-value: 7.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  49 GLKGNSGQSVYSASKGGLVGFSRALAKEvARKKIRVNVVAPGFVHTDMTKDLKeEHLKKNIPLGRFGETIEVAHAVVFLL 128
Cdd:PRK08219  132 GLRANPGWGSYAASKFALRALADALREE-EPGNVRVTSVHPGRTDTDMQRGLV-AQEGGEYDPERYLRPETVAKAVRFAV 209


                  ...
gi 2462599489 129 ESP 131
Cdd:PRK08219  210 DAP 212
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 9-141 7.82e-10

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: 54.51  E-value: 7.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   9 LLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKkIRVNVVA 88
Cdd:cd11731    86 LLGQINLVRHGLPYL--NDGGSITLTS----------GILAQRPIPGGAAAATVNGALEGFVRAAAIELPRG-IRINAVS 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  89 PGFVHT--DMTKDLKEEHLKkniplgrfGETIEVAHAVVFLLESPYiTGHVLVVD 141
Cdd:cd11731   153 PGVVEEslEAYGDFFPGFEP--------VPAEDVAKAYVRSVEGAF-TGQVLHVD 198
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 51-146 1.04e-09

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 54.55  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  51 KGNSGQSVYSASKGGLVGFSRALAKEVArKKIRVNVVAPGFV----HTDmtKDLKEEHLKKNIpLGRFGETIEVAHAVVF 126
Cdd:PRK06483  140 KGSDKHIAYAASKAALDNMTLSFAAKLA-PEVKVNSIAPALIlfneGDD--AAYRQKALAKSL-LKIEPGEEEIIDLVDY 215

                          90       100
                  ....*....|....*....|
gi 2462599489 127 LLESPYITGHVLVVDGGLQL 146
Cdd:PRK06483  216 LLTSCYVTGRSLPVDGGRHL 235
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 49-143 1.05e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 55.06  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  49 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGfVHTDMTKDLKEEHLKKnIPLGRFG--ETIEVAHAVVF 126
Cdd:PRK07791  160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-ARTRMTETVFAEMMAK-PEEGEFDamAPENVSPLVVW 237

                          90
                  ....*....|....*....
gi 2462599489 127 L--LESPYITGHVLVVDGG 143
Cdd:PRK07791  238 LgsAESRDVTGKVFEVEGG 256
PRK12746 PRK12746
SDR family oxidoreductase;
52-146 1.11e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 55.04  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  52 GNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKEEHLKKNIP-----LGRFGETIEVAHAVVF 126
Cdd:PRK12746  153 GFTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFAtnssvFGRIGQVEDIADAVAF 232

                          90       100
                  ....*....|....*....|..
gi 2462599489 127 LL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK12746  233 LAssDSRWVTGQIIDVSGGFCL 254
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-146 1.13e-09

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 54.77  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGL-KGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK05786  107 LTNHIKIPLYAVNASLRFL--KEGSSIVLVS----------SMSGIyKASPDQLSYAVAKAGLAKAVEILASELLGRGIR 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  84 VNVVAPGFvhtdMTKDLK-EEHLKKNIPLGRFGETIE-VAHAVVFLL--ESPYITGHVLVVDGGLQL 146
Cdd:PRK05786  175 VNGIAPTT----ISGDFEpERNWKKLRKLGDDMAPPEdFAKVIIWLLtdEADWVDGVVIPVDGGARL 237
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 7-96 3.57e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 53.37  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK06179  103 TNVFGILRMTRAVLPHMRAQGSGRIINIS----------SVLGFLPAPYMALYAASKHAVEGYSESLDHEVRQFGIRVSL 172

                          90
                  ....*....|
gi 2462599489  87 VAPGFVHTDM 96
Cdd:PRK06179  173 VEPAYTKTNF 182
PRK07832 PRK07832
SDR family oxidoreductase;
8-98 6.76e-09

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 52.74  E-value: 6.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK07832  109 NLMGPIHVIETFVPPMVAAgRGGHLVNVS----------SAAGLVALPWHAAYSASKFGLRGLSEVLRFDLARHGIGVSV 178

                          90
                  ....*....|..
gi 2462599489  87 VAPGFVHTDMTK 98
Cdd:PRK07832  179 VVPGAVKTPLVN 190
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 4-124 6.77e-09

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: 52.45  E-value: 6.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:cd08931   103 MVDINVKGVLNGAYAALPYLKATPGARVINTA----------SSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIR 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEE-HLKKNipLGRFGETIEVAHAV 124
Cdd:cd08931   173 VADVWPWFVDTPILTKGETGaAPKKG--LGRVLPVSDVAKVV 212
PRK07454 PRK07454
SDR family oxidoreductase;
8-94 7.04e-09

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 52.27  E-value: 7.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK07454  114 NLTSVFQCCSAVLPGMRARGGGLIINVS----------SIAARNAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRVCTI 183


                  ....*..
gi 2462599489  88 APGFVHT 94
Cdd:PRK07454  184 TLGAVNT 190
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 4-97 7.79e-09

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: 52.41  E-value: 7.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:cd05354   102 EMDVNVFGLLRLAQAFAPVLKANGGGAIVNL----------NSVASLKNFPAMGTYSASKSAAYSLTQGLRAELAAQGTL 171

                          90
                  ....*....|....
gi 2462599489  84 VNVVAPGFVHTDMT 97
Cdd:cd05354   172 VLSVHPGPIDTRMA 185
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 59-143 9.53e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 52.38  E-value: 9.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  59 YSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKEEHLKKNI-----PLGRFGETIEVAHAVVFLL--ESP 131
Cdd:PRK12747  158 YSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYattisAFNRLGEVEDIADTAAFLAspDSR 237

                          90
                  ....*....|..
gi 2462599489 132 YITGHVLVVDGG 143
Cdd:PRK12747  238 WVTGQLIDVSGG 249
PRK06181 PRK06181
SDR family oxidoreductase;
8-98 1.11e-08

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 51.90  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGgSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK06181  110 NYLGAVYCTHAALPHLKASRG-QIVVVS----------SLAGLTGVPTRSGYAASKHALHGFFDSLRIELADDGVAVTVV 178

                          90
                  ....*....|.
gi 2462599489  88 APGFVHTDMTK 98
Cdd:PRK06181  179 CPGFVATDIRK 189
PRK08267 PRK08267
SDR family oxidoreductase;
4-104 1.29e-08

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 51.86  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK08267  104 VIDINVKGVLNGAHAALPYLKATPGARVINTS----------SASAIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIR 173

                          90       100
                  ....*....|....*....|.
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEEH 104
Cdd:PRK08267  174 VADVMPLFVDTAMLDGTSNEV 194
PRK12742 PRK12742
SDR family oxidoreductase;
55-143 1.35e-08

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 51.68  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  55 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKD--LKEEHLKKNIPLGRFGETIEVAHAVVFLL--ES 130
Cdd:PRK12742  142 GMAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANPAngPMKDMMHSFMAIKRHGRPEEVAGMVAWLAgpEA 221

                          90
                  ....*....|...
gi 2462599489 131 PYITGHVLVVDGG 143
Cdd:PRK12742  222 SFVTGAMHTIDGA 234
PRK06949 PRK06949
SDR family oxidoreductase;
7-144 2.27e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 51.30  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGS--------IVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVA 78
Cdd:PRK06949  116 TNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIA----------SVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWG 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  79 RKKIRVNVVAPGFVHTDMTKDLKE----EHLKKNIPLGRFGETIEVAHAVVFLL--ESPYITGHVLVVDGGL 144
Cdd:PRK06949  186 RHGINVNAICPGYIDTEINHHHWEteqgQKLVSMLPRKRVGKPEDLDGLLLLLAadESQFINGAIISADDGF 257
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 5-138 4.61e-08

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: 50.36  E-value: 4.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEvaRKKIR 83
Cdd:cd05367   106 FDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVS----------SGAAVNPFKGWGLYCSSKAARDMFFRVLAAE--EPDVR 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEEHlKKNIPLGRF------GETIE---VAHAVVFLLESP-YITGHVL 138
Cdd:cd05367   174 VLSYAPGVVDTDMQREIRETS-ADPETRSRFrslkekGELLDpeqSAEKLANLLEKDkFESGAHV 237
PRK07024 PRK07024
SDR family oxidoreductase;
7-98 5.76e-08

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 49.93  E-value: 5.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK07024  109 TNYFGMVATFQPFIAPMRAARRGTLVGIA----------SVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVT 178

                          90
                  ....*....|..
gi 2462599489  87 VAPGFVHTDMTK 98
Cdd:PRK07024  179 IAPGYIRTPMTA 190
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 24-144 8.18e-08

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 49.77  E-value: 8.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  24 IQQQGGSIVNVGHrremLLHKRSIVGLKGNsgqsvYSASKGGLVGFSRALAKEVARK-KIRVNVVAPGFVHTDMTK---- 98
Cdd:PLN02730  167 IMNPGGASISLTY----IASERIIPGYGGG-----MSSAKAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKaigf 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462599489  99 -DLKEEHLKKNIPLGRFGETIEVAHAVVFLLeSPY---ITGHVLVVDGGL 144
Cdd:PLN02730  238 iDDMIEYSYANAPLQKELTADEVGNAAAFLA-SPLasaITGATIYVDNGL 286
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 1-103 1.77e-07

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: 48.61  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   1 MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARK 80
Cdd:cd09806   103 MASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTS----------SVGGLQGLPFNDVYCASKFALEGLCESLAVQLLPF 172

                          90       100
                  ....*....|....*....|...
gi 2462599489  81 KIRVNVVAPGFVHTDMTKDLKEE 103
Cdd:cd09806   173 NVHLSLIECGPVHTAFMEKVLGS 195
PRK05855 PRK05855
SDR family oxidoreductase;
5-98 2.27e-07

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 48.82  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK05855  420 LDVNLWGVIHGCRLFGRQMVERgTGGHIVNVA----------SAAAYAPSRSLPAYATSKAAVLMLSECLRAELAAAGIG 489

                          90
                  ....*....|....*
gi 2462599489  84 VNVVAPGFVHTDMTK 98
Cdd:PRK05855  490 VTAICPGFVDTNIVA 504
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-143 3.98e-07

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 47.85  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   9 LLGSMLTCKAAM---RTMIQQQGGS----IVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKK 81
Cdd:PRK07792  121 LRGHFLLTRNAAaywRAKAKAAGGPvygrIVNTS----------SEAGLVGPVGQANYGAAKAGITALTLSAARALGRYG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599489  82 IRVNVVAPGfVHTDMTKDLkeehlkkniplgrFGETIEVA----------HAV--VFLLESPY---ITGHVLVVDGG 143
Cdd:PRK07792  191 VRANAICPR-ARTAMTADV-------------FGDAPDVEaggidplspeHVVplVQFLASPAaaeVNGQVFIVYGP 253
PRK06139 PRK06139
SDR family oxidoreductase;
5-131 4.38e-07

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 47.79  E-value: 4.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNvghrreMLlhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARK-KIR 83
Cdd:PRK06139  112 IQTNLIGYMRDAHAALPIFKKQGHGIFIN------MI----SLGGFAAQPYAAAYSASKFGLRGFSEALRGELADHpDIH 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEEHLKKNIPLGRFGETIEVAHAVVFLLESP 131
Cdd:PRK06139  182 VCDVYPAFMDTPGFRHGANYTGRRLTPPPPVYDPRRVAKAVVRLADRP 229
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 1-99 9.17e-07

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: 46.52  E-value: 9.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   1 MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREmllhkrSIvGLKGNSGQSVYSASKGGLVGFSRALAKEVARK 80
Cdd:cd05325   100 LLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVG------SI-GDNTSGGWYSYRASKAALNMLTKSLAVELKRD 172

                          90
                  ....*....|....*....
gi 2462599489  81 KIRVNVVAPGFVHTDMTKD 99
Cdd:cd05325   173 GITVVSLHPGWVRTDMGGP 191
PRK07775 PRK07775
SDR family oxidoreductase;
2-131 1.14e-06

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 46.29  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   2 VSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKK 81
Cdd:PRK07775  112 ESQVQIHLVGANRLATAVLPGMIERRRGDLIFVG----------SDVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTG 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599489  82 IRVNVVAPGFVHTDMTKDLKEEHLKkniPL------------GRFGETIEVAHAVVFLLESP 131
Cdd:PRK07775  182 VRASIVHPGPTLTGMGWSLPAEVIG---PMledwakwgqarhDYFLRASDLARAITFVAETP 240
PRK07023 PRK07023
SDR family oxidoreductase;
37-96 1.26e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 46.16  E-value: 1.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  37 RRemLLHKRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEvARKKIRVNVVAPGFVHTDM 96
Cdd:PRK07023  130 RR--ILHISSGAARNAYAGWSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGM 186
PRK07102 PRK07102
SDR family oxidoreductase;
5-101 1.60e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 45.69  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV 84
Cdd:PRK07102  104 FRTNFEGPIALLTLLANRFEARGSGTIVGIS----------SVAGDRGRASNYVYGSAKAALTAFLSGLRNRLFKSGVHV 173

                          90
                  ....*....|....*..
gi 2462599489  85 NVVAPGFVHTDMTKDLK 101
Cdd:PRK07102  174 LTVKPGFVRTPMTAGLK 190
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
16-143 2.46e-06

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 45.48  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  16 CKAAMRTMiqQQGGSIVNVGHrremllhkrsIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHT- 94
Cdd:PRK07370  130 CKAAKPLM--SEGGSIVTLTY----------LGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTl 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  95 ---------DMTkdlkeEHLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGG 143
Cdd:PRK07370  198 assavggilDMI-----HHVEEKAPLRRTVTQTEVGNTAAFLLSdlASGITGQTIYVDAG 252
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 8-103 2.58e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 45.35  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIqqqggsivnvgHRREMLLHKRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PRK05872  116 NLLGVFHTVRATLPALI-----------ERRGYVLQVSSLAAFAAAPGMAAYCASKAGVEAFANALRLEVAHHGVTVGSA 184

                          90
                  ....*....|....*.
gi 2462599489  88 APGFVHTDMTKDLKEE 103
Cdd:PRK05872  185 YLSWIDTDLVRDADAD 200
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
46-143 2.94e-06

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 45.32  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  46 SIVGLKGNSGQS--VYS---ASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTK-----DLKEEHLKKNIPLG-RF 114
Cdd:PRK07889  140 SIVGLDFDATVAwpAYDwmgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKaipgfELLEEGWDERAPLGwDV 219

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462599489 115 GETIEVAHAVVFLLES--PYITGHVLVVDGG 143
Cdd:PRK07889  220 KDPTPVARAVVALLSDwfPATTGEIVHVDGG 250
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
58-102 3.07e-06

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 45.08  E-value: 3.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462599489  58 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKE 102
Cdd:PRK07904  158 VYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSAHAKE 202
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 7-94 3.67e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 44.91  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIVgLkgnsgQSVYSASKGGLVGFSRALAKEV--ARKKIRV 84
Cdd:PRK07109  115 VTYLGVVHGTLAALRHMRPRDRGAIIQVGS----ALAYRSIP-L-----QSAYCAAKHAIRGFTDSLRCELlhDGSPVSV 184

                          90
                  ....*....|
gi 2462599489  85 NVVAPGFVHT 94
Cdd:PRK07109  185 TMVQPPAVNT 194
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
63-147 5.78e-06

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 44.16  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  63 KGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKE-----EHLKKNIPLGRFGETIEVAHAVVFLLeSPY---IT 134
Cdd:PRK07533  166 KAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDfdallEDAAERAPLRRLVDIDDVGAVAAFLA-SDAarrLT 244

                          90
                  ....*....|...
gi 2462599489 135 GHVLVVDGGLQLI 147
Cdd:PRK07533  245 GNTLYIDGGYHIV 257
PRK12744 PRK12744
SDR family oxidoreductase;
57-143 6.09e-06

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 44.35  E-value: 6.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  57 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPG-----FVHTDMTKDLKEEHlKKNIPLGRFGET----IE-VAHAVVF 126
Cdd:PRK12744  157 SAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGpmdtpFFYPQEGAEAVAYH-KTAAALSPFSKTgltdIEdIVPFIRF 235

                          90
                  ....*....|....*...
gi 2462599489 127 LL-ESPYITGHVLVVDGG 143
Cdd:PRK12744  236 LVtDGWWITGQTILINGG 253
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
55-130 1.03e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 43.52  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  55 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVA--PGFVHTDMTKDLKEEHLKKNIPLGRFGETIE---------VAHA 123
Cdd:PRK06924  150 GWSAYCSSKAGLDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQIRSSSKEDFTNLDRFITLKEegkllspeyVAKA 229


                  ....*..
gi 2462599489 124 VVFLLES 130
Cdd:PRK06924  230 LRNLLET 236
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 59-143 2.92e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 42.31  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  59 YSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKD-LKEEH--LKKNI----PLGRFGETIEVAHAVVFLL--E 129
Cdd:PRK06940  169 YQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDeLNGPRgdGYRNMfaksPAGRPGTPDEIAALAEFLMgpR 248

                          90
                  ....*....|....
gi 2462599489 130 SPYITGHVLVVDGG 143
Cdd:PRK06940  249 GSFITGSDFLVDGG 262
PRK08017 PRK08017
SDR family oxidoreductase;
1-97 4.16e-05

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 42.00  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   1 MVSQLHTNLLGS-MLTCkAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVAR 79
Cdd:PRK08017   98 MEQQFSTNFFGThQLTM-LLLPAMLPHGEGRIVMTS----------SVMGLISTPGRGAYAASKYALEAWSDALRMELRH 166

                          90
                  ....*....|....*...
gi 2462599489  80 KKIRVNVVAPGFVHTDMT 97
Cdd:PRK08017  167 SGIKVSLIEPGPIRTRFT 184
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 6-114 6.27e-05

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: 41.30  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   6 HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:COG3967   109 TTNLLGPIRLTAAFLPHLKAQPEAAIVNVS----------SGLAFVPLAVTPTYSATKAALHSYTQSLRHQLKDTSVKVI 178

                          90       100
                  ....*....|....*....|....*....
gi 2462599489  86 VVAPGFVHTDMTKDLKEEHLKknIPLGRF 114
Cdd:COG3967   179 ELAPPAVDTDLTGGQGGDPRA--MPLDEF 205
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 5-96 8.81e-05

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: 40.58  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQqqGGSIVNVGHRREMllhkrsiVGLKGNSGqsvYSASKGGLVGFSRALAKEVarKKIRV 84
Cdd:cd11730    94 LDANLTGAALVLKHALALLAA--GARLVFLGAYPEL-------VMLPGLSA---YAAAKAALEAYVEVARKEV--RGLRL 159

                          90
                  ....*....|..
gi 2462599489  85 NVVAPGFVHTDM 96
Cdd:cd11730   160 TLVRPPAVDTGL 171
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 3-135 1.38e-04

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: 40.29  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   3 SQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVG---HRR-----EMLLHKRSivglKGNSGQSVYSASKGGLVGFSRALA 74
Cdd:cd05327   104 LQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSsiaHRAgpidfNDLDLENN----KEYSPYKAYGQSKLANILFTRELA 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599489  75 KEVARKKIRVNVVAPGFVHTDMTKDLKEEHLKKNIpLGRFGE--TIEVAHAVVFLLESPYITG 135
Cdd:cd05327   180 RRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYKL-LRPFLKksPEQGAQTALYAATSPELEG 241
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 8-107 1.46e-04

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: 40.34  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAaMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:cd09805   110 NLFGTVEVTKA-FLPLLRRAKGRVVNVS----------SMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSII 178

                          90       100
                  ....*....|....*....|
gi 2462599489  88 APGFVHTDMTkdLKEEHLKK 107
Cdd:cd09805   179 EPGNFKTGIT--GNSELWEK 196
PRK06182 PRK06182
short chain dehydrogenase; Validated
 4-132 2.33e-04

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 39.56  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   4 QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:PRK06182  101 QFEVNLFGAARLTQLVLPHMRAQRSGRIINIS----------SMGGKIYTPLGAWYHATKFALEGFSDALRLEVAPFGID 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462599489  84 VNVVAPGFVHTDMTkDLKEEHLKKNIPLGRFGETievAHAVVFLLESPY 132
Cdd:PRK06182  171 VVVIEPGGIKTEWG-DIAADHLLKTSGNGAYAEQ---AQAVAASMRSTY 215
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 6-96 3.53e-04

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: 39.10  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   6 HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVN 85
Cdd:cd05340   114 QVNVNATFMLTQALLPLLLKSDAGSLVFTS----------SSVGRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVN 183

                          90
                  ....*....|.
gi 2462599489  86 VVAPGFVHTDM 96
Cdd:cd05340   184 CINPGGTRTAM 194
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 6-103 4.73e-04

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 38.74  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   6 HTNLLGSMLTCKAAMRTMIQQQGG--SIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIR 83
Cdd:TIGR01500 119 ALNLTSMLCLTSSVLKAFKDSPGLnrTVVNIS----------SLCAIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVR 188

                          90       100
                  ....*....|....*....|
gi 2462599489  84 VNVVAPGFVHTDMTKDLKEE 103
Cdd:TIGR01500 189 VLNYAPGVLDTDMQQQVREE 208
PRK06101 PRK06101
SDR family oxidoreductase;
59-97 6.39e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 38.31  E-value: 6.39e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462599489  59 YSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMT 97
Cdd:PRK06101  141 YGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLT 179
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 13-96 8.06e-04

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 37.93  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  13 MLTcKAAMRTMIQQQGGSIVnvghrremllHKRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFV 92
Cdd:PRK08945  130 MLT-QALLPLLLKSPAASLV----------FTSSSVGRQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGT 198


                  ....
gi 2462599489  93 HTDM 96
Cdd:PRK08945  199 RTAM 202
PRK09291 PRK09291
SDR family oxidoreductase;
7-94 8.14e-04

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 38.06  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:PRK09291  103 TNVFGPLELTQGFVRKMVARGKGKVVFTS----------SMAGLITGPFTGAYCASKHALEAIAEAMHAELKPFGIQVAT 172


                  ....*...
gi 2462599489  87 VAPGFVHT 94
Cdd:PRK09291  173 VNPGPYLT 180
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 8-95 9.06e-04

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: 37.75  E-value: 9.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRV-NV 86
Cdd:cd05373   108 AAFGGFLAAREAAKRMLARGRGTIIFTG----------ATASLRGRAGFAAFAGAKFALRALAQSMARELGPKGIHVaHV 177


                  ....*....
gi 2462599489  87 VAPGFVHTD 95
Cdd:cd05373   178 IIDGGIDTD 186
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 8-96 1.76e-03

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: 36.92  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKE--VARKKIRVN 85
Cdd:cd05334   100 NLWTSFIASHLATKHL--LSGGLLVLTG----------AKAALEPTPGMIGYGAAKAAVHQLTQSLAAEnsGLPAGSTAN 167

                          90
                  ....*....|.
gi 2462599489  86 VVAPGFVHTDM 96
Cdd:cd05334   168 AILPVTLDTPA 178
PRK05599 PRK05599
SDR family oxidoreductase;
46-101 1.78e-03

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 37.17  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462599489  46 SIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLK 101
Cdd:PRK05599  137 SIAGWRARRANYVYGSTKAGLDAFCQGLADSLHGSHVRLIIARPGFVIGSMTTGMK 192
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
38-147 2.00e-03

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 37.01  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  38 REMLLHKRSIVGL------KGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHTDMTKDLKE--EHLKKNI 109
Cdd:PRK06079  130 RPLLNPGASIVTLtyfgseRAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGIKGhkDLLKESD 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462599489 110 PLGRFGETI---EVAHAVVFLLE--SPYITGHVLVVDGGLQLI 147
Cdd:PRK06079  210 SRTVDGVGVtieEVGNTAAFLLSdlSTGVTGDIIYVDKGVHLI 252
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 8-98 2.26e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 36.77  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   8 NLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLLHKRSIVglkgnsgqSVYSASKGGLVGFSRALAKEVARKKIRVNVV 87
Cdd:PLN02780  165 NVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDPLY--------AVYAATKAYIDQFSRCLYVEYKKSGIDVQCQ 236

                          90
                  ....*....|.
gi 2462599489  88 APGFVHTDMTK 98
Cdd:PLN02780  237 VPLYVATKMAS 247
PRK07984 PRK07984
enoyl-ACP reductase FabI;
57-146 3.23e-03

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 36.42  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  57 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHT---DMTKDLKE--EHLKKNIPLGRFGETIEVAHAVVFLLE-- 129
Cdd:PRK07984  157 NVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTlaaSGIKDFRKmlAHCEAVTPIRRTVTIEDVGNSAAFLCSdl 236

                          90
                  ....*....|....*..
gi 2462599489 130 SPYITGHVLVVDGGLQL 146
Cdd:PRK07984  237 SAGISGEVVHVDGGFSI 253
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
17-147 3.72e-03

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 36.24  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  17 KAAMRTMiqQQGGSIVNVGHrremllhkrsIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPGFVHT-- 94
Cdd:PRK08594  131 REAKKLM--TEGGSIVTLTY----------LGGERVVQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTls 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489  95 -----DMTKDLKEehLKKNIPLGRFGETIEVAHAVVFLLE--SPYITGHVLVVDGGLQLI 147
Cdd:PRK08594  199 akgvgGFNSILKE--IEERAPLRRTTTQEEVGDTAAFLFSdlSRGVTGENIHVDSGYHII 256
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 7-111 3.79e-03

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: 36.13  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   7 TNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNV 86
Cdd:cd05370   110 TNLIGPIRLIKAFLPHLKKQPEATIVNVS----------SGLAFVPMAANPVYCATKAALHSYTLALRHQLKDTGVEVVE 179

                          90       100
                  ....*....|....*....|....*
gi 2462599489  87 VAPGFVHTDMTKDLKEEHLKKNIPL 111
Cdd:cd05370   180 IVPPAVDTELHEERRNPDGGTPRKM 204
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-131 3.94e-03

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: 35.95  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599489   5 LHTNLLGSMLTCKAAMRTMIQQ--QGGSIVNV----GHRremllhkrsivgLKGNSGQSVYSASKGGLVGFSRALAKEV- 77
Cdd:cd05343   112 FDVNVLALSICTREAYQSMKERnvDDGHIINInsmsGHR------------VPPVSVFHFYAATKHAVTALTEGLRQELr 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599489  78 -ARKKIRVNVVAPGFVHTDMTKDL------KEEHLKKNIPLGRFGetiEVAHAVVFLLESP 131
Cdd:cd05343   180 eAKTHIRATSISPGLVETEFAFKLhdndpeKAAATYESIPCLKPE---DVANAVLYVLSTP 237
 
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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