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Conserved domains on  [gi|562866750|ref|XP_006161513|]
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carbonyl reductase family member 4 [Tupaia chinensis]

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 ...
 3-233 3.94e-91

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: 268.26  E-value: 3.94e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE---EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEkvkEKILKQIPLGRLGTPEEVANAVAFLAsdDASYITGQVLHVNGGM 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; ...
 3-233 3.94e-91

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: 268.26  E-value: 3.94e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE---EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEkvkEKILKQIPLGRLGTPEEVANAVAFLAsdDASYITGQVLHVNGGM 239
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-233 7.51e-90

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 265.11  E-value: 7.51e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:COG1028    5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:COG1028   85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:COG1028  165 LTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGaeevrEALAARIPLGRLGTPEEVAAAVLFLAsdAASYITGQVLAVD 244


                 ...
gi 562866750 231 GGL 233
Cdd:COG1028  245 GGL 247
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 7-233 7.15e-89

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: 262.14  E-value: 7.15e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750    7 VFGGSRGIGRAVAQLMARKGYRLAIIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:TIGR01830   3 VTGASRGIGRAIALKLAKEGAKVIITYRSseegAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDILVN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:TIGR01830  83 NAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTKSL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 562866750  163 AKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK---NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:TIGR01830 163 AKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKilsQIPLGRFGQPEEVANAVAFLAsdEASYITGQVIHVDGGM 238
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-235 4.85e-88

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 260.48  E-value: 4.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE---EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK05653 164 FTKALALELASRGITVNAVAPGFIDTDMTEGLPEevkAEILKEIPLGRLGQPEEVANAVAFLAsdAASYITGQVIPVNGG 243


                 ...
gi 562866750 233 LQL 235
Cdd:PRK05653 244 MYM 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-233 1.49e-70

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: 215.76  E-value: 1.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   12 RGIGRAVAQLMARKGYRLAIIARNLEGAKAA---AGDLGGDhlAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGV-- 86
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVeelAEELGAA--VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFap 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   87 NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:pfam13561  84 KLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVEL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 562866750  167 ARKKIRVNVVAPGFIHTDMTKDLK-----EEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:pfam13561 162 GPRGIRVNAISPGPIKTLAASGIPgfdelLAAAEARAPLGRLGTPEEVANAAAFLAsdLASYITGQVLYVDGGY 235
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-150 1.41e-14

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 69.43  E-value: 1.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750     9 GGSRGIGRAVAQLMARKGYR-LAIIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750    82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRtmiqQQGGAIVNVGSIIGVRGNSGQSVYSA 150
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAA 151
 
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; ...
 3-233 3.94e-91

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: 268.26  E-value: 3.94e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE---EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEkvkEKILKQIPLGRLGTPEEVANAVAFLAsdDASYITGQVLHVNGGM 239
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-233 7.51e-90

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 265.11  E-value: 7.51e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:COG1028    5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:COG1028   85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:COG1028  165 LTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGaeevrEALAARIPLGRLGTPEEVAAAVLFLAsdAASYITGQVLAVD 244


                 ...
gi 562866750 231 GGL 233
Cdd:COG1028  245 GGL 247
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 7-233 7.15e-89

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: 262.14  E-value: 7.15e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750    7 VFGGSRGIGRAVAQLMARKGYRLAIIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:TIGR01830   3 VTGASRGIGRAIALKLAKEGAKVIITYRSseegAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDILVN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:TIGR01830  83 NAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTKSL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 562866750  163 AKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK---NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:TIGR01830 163 AKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKilsQIPLGRFGQPEEVANAVAFLAsdEASYITGQVIHVDGGM 238
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-235 4.85e-88

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 260.48  E-value: 4.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE---EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK05653 164 FTKALALELASRGITVNAVAPGFIDTDMTEGLPEevkAEILKEIPLGRLGQPEEVANAVAFLAsdAASYITGQVIPVNGG 243


                 ...
gi 562866750 233 LQL 235
Cdd:PRK05653 244 MYM 246
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-230 3.15e-83

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: 247.97  E-value: 3.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   5 CAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMTKDLKEEH----LKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:cd05233  161 ALELAPYGIRVNAVAPGLVDTPMLAKLGPEEaekeLAAAIPLGRLGTPEEVAEAVVFLAsdEASYITGQVIPVD 234
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-233 3.50e-83

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 248.18  E-value: 3.50e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK05557   4 EGKVALVTGASRGIGRAIAERLAAQGANVVInYASSEAGAEALVaeiGALGGKALAVQGDVSDAESVERAVDEAKAEFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK05557  84 VDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE---EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDG 231
Cdd:PRK05557 164 GFTKSLARELASRGITVNAVAPGFIETDMTDALPEdvkEAILAQIPLGRLGQPEEIASAVAFLAsdEAAYITGQTLHVNG 243


                 ..
gi 562866750 232 GL 233
Cdd:PRK05557 244 GM 245
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-233 1.49e-70

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: 215.76  E-value: 1.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   12 RGIGRAVAQLMARKGYRLAIIARNLEGAKAA---AGDLGGDhlAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGV-- 86
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVeelAEELGAA--VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFap 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   87 NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:pfam13561  84 KLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVEL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 562866750  167 ARKKIRVNVVAPGFIHTDMTKDLK-----EEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:pfam13561 162 GPRGIRVNAISPGPIKTLAASGIPgfdelLAAAEARAPLGRLGTPEEVANAAAFLAsdLASYITGQVLYVDGGY 235
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-235 3.23e-70

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 215.59  E-value: 3.23e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK08217   5 DKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNqekLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTK----TEDM-LSQ----LHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIiGVRGNSGQSVY 148
Cdd:PRK08217  85 GLINNAGILRDGLLVKAKdgkvTSKMsLEQfqsvIDVNLTGVFLCGREAAAKMIESgSKGVIINISSI-ARAGNMGQTNY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 149 SASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE---HLKKNIPLGRFGETVEVAHAVVFLLESPYITGH 225
Cdd:PRK08217 164 SASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEaleRLEKMIPVGRLGEPEEIAHTVRFIIENDYVTGR 243

                        250
                 ....*....|
gi 562866750 226 VLVVDGGLQL 235
Cdd:PRK08217 244 VLEIDGGLRL 253
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-232 8.57e-69

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 211.62  E-value: 8.57e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAII-ARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLeeiKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK05565  84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH---LKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDG 231
Cdd:PRK05565 164 AFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDkegLAEEIPLGRLGKPEEIAKVVLFLAsdDASYITGQIITVDG 243


                 .
gi 562866750 232 G 232
Cdd:PRK05565 244 G 244
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-233 2.05e-68

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 210.50  E-value: 2.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIAR-NLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEaveALGRRAQAVQADVTDKAALEAAVAAAVERFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK12825  85 IDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHL---KKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDG 231
Cdd:PRK12825 165 GLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAReakDAETPLGRSGTPEDIARAVAFLCsdASDYITGQVIEVTG 244


                 ..
gi 562866750 232 GL 233
Cdd:PRK12825 245 GV 246
PRK12826 PRK12826
SDR family oxidoreductase;
1-235 4.85e-66

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 204.77  E-value: 4.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVeaaGGKARARQVDVRDRAALKAAVAAGVEDFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVR-GNSGQSVYSASKGGLV 156
Cdd:PRK12826  85 DILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAASKAGLV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:PRK12826 165 GFTRALALELAARNITVNSVHPGGVDTPMAGNLGDaqwaEAIAAAIPLGRLGEPEDIAAAVLFLAsdEARYITGQTLPVD 244


                 ....*
gi 562866750 231 GGLQL 235
Cdd:PRK12826 245 GGATL 249
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 2-220 1.06e-64

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: 200.79  E-value: 1.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:COG4221    5 GKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:COG4221   85 NNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSES 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIPLGRFGETV---EVAHAVVFLLESP 220
Cdd:COG4221  165 LRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLtpeDVAEAVLFALTQP 226
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-220 2.08e-63

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 198.17  E-value: 2.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFGPI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:COG0300   84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKeehlkknIPLGRFGETVE-VAHAVVFLLESP 220
Cdd:COG0300  164 FSESLRAELAPTGVRVTAVCPGPVDTPFTARAG-------APAGRPLLSPEeVARAILRALERG 220
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-192 7.62e-61

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 189.36  E-value: 7.62e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750    3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 562866750  160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE 192
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTDMTKELRED 193
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-232 1.41e-60

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 198.53  E-value: 1.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVN--RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06484  86 NAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQgHGAAIVNVASGAGLVALPKRTAYSASKAAVISLT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHL------KKNIPLGRFGETVEVAHAVVFL--LESPYITGHVLVVDG 231
Cdd:PRK06484 166 RSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKldpsavRSRIPLGRLGRPEEIAEAVFFLasDQASYITGSTLVVDG 245


                 .
gi 562866750 232 G 232
Cdd:PRK06484 246 G 246
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 3-232 2.61e-58

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: 184.87  E-value: 2.61e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05347    6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIekeGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd05347   86 LVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH-----LKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:cd05347  166 KALATEWARHGIQVNAIAPGYFATEMTEAVVADPefnddILKRIPAGRWGQPEDLVGAAVFLAsdASDYVNGQIIFVDGG 245
FabG-like PRK07231
SDR family oxidoreductase;
2-233 5.59e-58

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 184.26  E-value: 5.59e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILagGRAIAVAADVSDEADVEAAVAAALERFGSVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVN-RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK07231  85 LVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-------KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK07231 165 TKALAAELGPDKIRVNAVAPVVVETGLLEAFmgeptpeNRAKFLATIPLGRLGTPEDIANAALFLAsdEASWITGVTLVV 244


                 ....
gi 562866750 230 DGGL 233
Cdd:PRK07231 245 DGGR 248
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-233 3.37e-56

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 179.58  E-value: 3.37e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYR-LAIIARNLEGAKAAAGDLGGDHL---AFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRvIATYFSGNDCAKDWFEEYGFTEDqvrLKELDVTDTEECAEALAEIEEEEGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK12824  81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK---NIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDG 231
Cdd:PRK12824 161 GFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSivnQIPMKRLGTPEEIAAAVAFLVSeaAGFITGETISING 240


                 ..
gi 562866750 232 GL 233
Cdd:PRK12824 241 GL 242
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 2-233 9.69e-56

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: 178.62  E-value: 9.69e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:cd05344   81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKN--------------IPLGRFGETVEVAHAVVFLL--ESPYI 222
Cdd:cd05344  161 VKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEKEgisveeaekevasqIPLGRVGKPEELAALIAFLAseKASYI 240

                        250
                 ....*....|.
gi 562866750 223 TGHVLVVDGGL 233
Cdd:cd05344  241 TGQAILVDGGL 251
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 2-232 5.41e-54

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 174.08  E-value: 5.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK06841  15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK06841  95 NSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGMTKV 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDL----KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK06841 175 LALEWGPYGITVNAISPTVVLTELGKKAwageKGERAKKLIPAGRFAYPEEIAAAALFLAsdAAAMITGENLVIDGG 251
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-232 1.30e-53

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: 172.90  E-value: 1.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:cd05352    8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYgvktKAYKCDVSSQESVEKTFKQIQKDFGKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRD-SLLVRTKtEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGN--SGQSVYSASKGG 154
Cdd:cd05352   88 DILIANAGITVHkPALDYTY-EQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNrpQPQAAYNASKAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPGFIHTDMT----KDLKeEHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLV 228
Cdd:cd05352  167 VIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTdfvdKELR-KKWESYIPLKRIALPEELVGAYLYLASdaSSYTTGSDLI 245


                 ....
gi 562866750 229 VDGG 232
Cdd:cd05352  246 IDGG 249
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 3-235 1.71e-53

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: 172.57  E-value: 1.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGyrlAIIARNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEEMEKHLG 75
Cdd:cd05358    4 KVALVTGASSGIGKAIAIRLATAG---ANVVVNYRSKEDAAEEVveeikavGGKAIAVQADVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQG-GAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:cd05358   81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIkGKIINMSSVHEKIPWPGHVNYAASKGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-----KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVL 227
Cdd:cd05358  161 VKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAwddpeQRADLLSLIPMGRIGEPEEIAAAAAWLAsdEASYVTGTTL 240


                 ....*...
gi 562866750 228 VVDGGLQL 235
Cdd:cd05358  241 FVDGGMTL 248
PRK06138 PRK06138
SDR family oxidoreductase;
2-233 2.90e-52

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 169.56  E-value: 2.90e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL--GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIaaGGRAFARQGDVGSAEAVEALVDFVAARWGRLDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06138  85 LVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASLT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTK---------DLKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLV 228
Cdd:PRK06138 165 RAMALDHATDGIRVNAVAPGTIDTPYFRrifarhadpEALREALRARHPMNRFGTAEEVAQAALFLAsdESSFATGTTLV 244


                 ....*
gi 562866750 229 VDGGL 233
Cdd:PRK06138 245 VDGGW 249
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 2-235 6.63e-52

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: 168.53  E-value: 6.63e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:cd05369    3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEIssatGGRAHPIQCDVRDPEAVEAAVDETLKEFGKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSllvrtKTEDmLSQ------LHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSA 150
Cdd:cd05369   83 DILINNAAGNFLA-----PAES-LSPngfktvIDIDLNGTFNTTKAVGKRLIEAKhGGSILNISATYAYTGSPFQVHSAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 151 SKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTD--MTK----DLKEEHLKKNIPLGRFGETVEVAHAVVFLLeSP---Y 221
Cdd:cd05369  157 AKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTegMERlapsGKSEKKMIERVPLGRLGTPEEIANLALFLL-SDaasY 235

                        250
                 ....*....|....
gi 562866750 222 ITGHVLVVDGGLQL 235
Cdd:cd05369  236 INGTTLVVDGGQWL 249
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-233 1.28e-51

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 175.04  E-value: 1.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVN 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSL-LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK06484 350 NAGIAEVFKpSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRS 427

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKE------EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:PRK06484 428 LACEWAPAGIRVNTVAPGYIETPAVLALKAsgradfDSIRRRIPLGRLGDPEEVAEAIAFLAspAASYVNGATLTVDGGW 507
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 3-233 6.70e-51

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 166.28  E-value: 6.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGARVVLSARkaeELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDsllvrTKTEDMLSQ-----LHTNLLGS-MLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSV----YS 149
Cdd:PRK08213  93 LVNNAGATWG-----APAEDHPVEawdkvMNLNVRGLfLLSQAVAKRSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 150 ASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL---KEEHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITG 224
Cdd:PRK08213 168 TSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTlerLGEDLLAHTPLGRLGDDEDLKGAALLLASdaSKHITG 247


                 ....*....
gi 562866750 225 HVLVVDGGL 233
Cdd:PRK08213 248 QILAVDGGV 256
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 3-235 1.25e-50

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: 165.32  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAA-------GVNRDSLLVRTkTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:cd05349   81 NNAlidfpfdPDQRKTFDTID-WEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPGFI----HTDMTKDLKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLV 228
Cdd:cd05349  160 LLGFTRNMAKELGPYGITVNMVSGGLLkvtdASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFAspWARAVTGQNLV 239


                 ....*..
gi 562866750 229 VDGGLQL 235
Cdd:cd05349  240 VDGGLVM 246
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 3-232 1.50e-50

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 165.14  E-value: 1.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaaGGRAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK12939  88 LVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMT 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH----LKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK12939 168 RSLARELGGRGITVNAIAPGLTATEATAYVPADErhayYLKGRALERLQVPDDVAGAVLFLLsdAARFVTGQLLPVNGG 246
PRK06172 PRK06172
SDR family oxidoreductase;
2-233 2.20e-50

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 164.92  E-value: 2.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNL---EGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQL-HTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK06172  87 YAFNNAGIEIEQGRLAEGSEAEFDAImGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTK------DLKEEHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVV 229
Cdd:PRK06172 167 LTKSAAIEYAKKGIRVNAVCPAVIDTDMFRrayeadPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSdgASFTTGHALMV 246


                 ....
gi 562866750 230 DGGL 233
Cdd:PRK06172 247 DGGA 250
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-235 4.03e-49

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 161.33  E-value: 4.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIiarNLEGAKAAA-------GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLG 75
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAenlvnelGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK12935  84 KVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK---NIPLGRFGETVEVAHAVVFLL-ESPYITGHVLVVDG 231
Cdd:PRK12935 164 LGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKivaKIPKKRFGQADEIAKGVVYLCrDGAYITGQQLNING 243


                 ....
gi 562866750 232 GLQL 235
Cdd:PRK12935 244 GLYM 247
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 2-232 4.69e-49

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: 161.01  E-value: 4.69e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:cd05341    5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:cd05341   85 NNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKS 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 162 LAKEVARKK--IRVNVVAPGFIHTDMT----KDLKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:cd05341  165 AALECATQGygIRVNSVHPGYIYTPMTdellIAQGEMGNYPNTPMGRAGEPDEIAYAVVYLAsdESSFVTGSELVVDGG 243
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 7-236 4.86e-49

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 161.24  E-value: 4.86e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGV 86
Cdd:PRK12936  11 VTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:PRK12936  91 TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLAQEI 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 562866750 167 ARKKIRVNVVAPGFIHTDMTKDLKE---EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGLQLM 236
Cdd:PRK12936 171 ATRNVTVNCVAPGFIESAMTGKLNDkqkEAIMGAIPMKRMGTGAEVASAVAYLAssEAAYVTGQTIHVNGGMAMI 245
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-235 1.06e-48

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: 160.62  E-value: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLE-GAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEIseaGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:cd05366   81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKFAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE--------------HLKKNIPLGRFGETVEVAHAVVFLL--ES 219
Cdd:cd05366  161 RGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEvgeiagkpegegfaEFSSSIPLGRLSEPEDVAGLVSFLAseDS 240

                        250
                 ....*....|....*.
gi 562866750 220 PYITGHVLVVDGGLQL 235
Cdd:cd05366  241 DYITGQTILVDGGMVY 256
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 3-232 3.22e-48

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: 158.98  E-value: 3.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAeieAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:cd05362   84 ILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH----LKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:cd05362  162 TRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEavegYAKMSPLGRLGEPEDIAPVVAFLAspDGRWVNGQVIRANGG 241
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-232 1.07e-46

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: 154.96  E-value: 1.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDLLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGV-NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:cd08944   84 NAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIP----------LGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:cd08944  164 LAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPggfhllihqlQGRLGRPEDVAAAVVFLLsdDASFITGQVLCV 243


                 ...
gi 562866750 230 DGG 232
Cdd:cd08944  244 DGG 246
PRK06124 PRK06124
SDR family oxidoreductase;
3-233 4.81e-46

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 153.72  E-value: 4.81e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALraaGGAAEALAFDIADEEAVAAAFARIDAEHGRLDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06124  92 LVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGLM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTD----MTKD-LKEEHLKKNIPLGRFGETVEVAHAVVFlLESP---YITGHVLVVDG 231
Cdd:PRK06124 172 RALAAEFGPHGITSNAIAPGYFATEtnaaMAADpAVGPWLAQRTPLGRWGRPEEIAGAAVF-LASPaasYVNGHVLAVDG 250


                 ..
gi 562866750 232 GL 233
Cdd:PRK06124 251 GY 252
PRK06123 PRK06123
SDR family oxidoreductase;
1-232 1.08e-45

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 152.63  E-value: 1.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAvvqAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVnrdsLLVRTKTEDMLSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGAIVNVGSIIGVRGNSGQSV- 147
Cdd:PRK06123  81 LDALVNNAGI----LEAQMRLEQMDAArltriFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGEYId 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 148 YSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPY 221
Cdd:PRK06123 157 YAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEpgrvDRVKAGIPMGRGGTAEEVARAILWLLsdEASY 236

                        250
                 ....*....|.
gi 562866750 222 ITGHVLVVDGG 232
Cdd:PRK06123 237 TTGTFIDVSGG 247
PRK07063 PRK07063
SDR family oxidoreductase;
3-236 1.70e-45

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 152.51  E-value: 1.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardvaGARVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVN--RDSLlvRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK07063  88 DVLVNNAGINvfADPL--AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKHGL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL----------KEEHLKKNiPLGRFGETVEVAHAVVFLL--ESPYIT 223
Cdd:PRK07063 166 LGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWwnaqpdpaaaRAETLALQ-PMKRIGRPEEVAMTAVFLAsdEAPFIN 244

                        250
                 ....*....|...
gi 562866750 224 GHVLVVDGGLQLM 236
Cdd:PRK07063 245 ATCITIDGGRSVL 257
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-235 2.13e-45

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 152.19  E-value: 2.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLskdGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNrDSLLVRTKTEDMLSQLH-TNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK08643  81 NVVVNNAGVA-PTTPIETITEEQFDKVYnINVGGVIWGIQAAQEAFKKLgHGGKIINATSQAGVVGNPELAVYSSTKFAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE--------------EHLKKNIPLGRFGETVEVAHAVVFLL--ES 219
Cdd:PRK08643 160 RGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHqvgenagkpdewgmEQFAKDITLGRLSEPEDVANCVSFLAgpDS 239

                        250
                 ....*....|....*.
gi 562866750 220 PYITGHVLVVDGGLQL 235
Cdd:PRK08643 240 DYITGQTIIVDGGMVF 255
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 1-236 2.33e-45

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: 151.67  E-value: 2.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGdlGGDHLAFS-CDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK--LGDNCRFVpVDVTSEKDVKAALALAKAKFGRLDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGV-------NRDSLLVRtKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQG------GAIVNVGSIIGVRGNSGQS 146
Cdd:cd05371   79 VVNCAGIavaaktyNKKGQQPH-SLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTASVAAFEGQIGQA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 147 VYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE---HLKKNIP-LGRFGETVEVAHAVVFLLESPYI 222
Cdd:cd05371  158 AYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKvrdFLAKQVPfPSRLGDPAEYAHLVQHIIENPYL 237

                        250
                 ....*....|....
gi 562866750 223 TGHVLVVDGGLQLM 236
Cdd:cd05371  238 NGEVIRLDGAIRMP 251
PRK09730 PRK09730
SDR family oxidoreductase;
3-232 2.73e-45

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 151.54  E-value: 2.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVnYQQNLHAAQEVVNLItqaGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVnrdsLLVRTKTEDMLSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGAIVNVGSIIGVRGNSGQSV-YS 149
Cdd:PRK09730  82 ALVNNAGI----LFTQCTVENLTAErinrvLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEYVdYA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 150 ASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYIT 223
Cdd:PRK09730 158 ASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEpgrvDRVKSNIPMQRGGQPEEVAQAIVWLLsdKASYVT 237


                 ....*....
gi 562866750 224 GHVLVVDGG 232
Cdd:PRK09730 238 GSFIDLAGG 246
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 2-232 4.26e-45

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 151.19  E-value: 4.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK12429   4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK12429  84 ILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHT--------DMTKDL-------KEEHLKKNIPLGRFGETVEVAHAVVFL--LESPY 221
Cdd:PRK12429 164 TKVVALEGATHGVTVNAICPGYVDTplvrkqipDLAKERgiseeevLEDVLLPLVPQKRFTTVEEIADYALFLasFAAKG 243

                        250
                 ....*....|.
gi 562866750 222 ITGHVLVVDGG 232
Cdd:PRK12429 244 VTGQAWVVDGG 254
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-236 4.95e-45

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 151.36  E-value: 4.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK12829  10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGaKVTATVADVADPAQVERVFDTAVERFGGLDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK12829  90 LVNNAGIAGPTGGIDEITPEQWEQtLAVNLNGQFYFARAAVPLLKASGhGGVIIALSSVAGRLGYPGRTPYAASKWAVVG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTK---------------DLKEEHLKKnIPLGRFGETVEVAHAVVFLL--ESP 220
Cdd:PRK12829 170 LVKSLAIELGPLGIRVNAILPGIVRGPRMRrviearaqqlgigldEMEQEYLEK-ISLGRMVEPEDIAATALFLAspAAR 248

                        250
                 ....*....|....*.
gi 562866750 221 YITGHVLVVDGGLQLM 236
Cdd:PRK12829 249 YITGQAISVDGNVEYL 264
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 2-236 5.20e-45

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: 151.02  E-value: 5.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKA------AAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLG 75
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEEtrqsclQAGVSEKKILLVVADLTEEEGQDRIISTTLAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGgAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:cd05364   83 RLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKG-EIVNVSSVAGGRSFPGVLYYCISKAAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKD--LKEEHLKK-------NIPLGRFGETVEVAHAVVFLLE--SPYITG 224
Cdd:cd05364  162 DQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRmgMPEEQYIKflsrakeTHPLGRPGTVDEVAEAIAFLASdaSSFITG 241

                        250
                 ....*....|..
gi 562866750 225 HVLVVDGGLQLM 236
Cdd:cd05364  242 QLLPVDGGRHLM 253
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 7-235 5.84e-45

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: 150.58  E-value: 5.84e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd05359    3 VTGGSRGIGKAIALRLAERGADVVInYRKSKDAAAEVAAEieeLGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 --AAGVNRDslLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05359   83 naAAGAFRP--LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTDMTK------DLKEEHLkKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:cd05359  161 YLAVELGPRGIRVNAVSPGVIDTDALAhfpnreDLLEAAA-ANTPAGRVGTPQDVADAVGFLCsdAARMITGQTLVVDGG 239


                 ...
gi 562866750 233 LQL 235
Cdd:cd05359  240 LSI 242
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-233 6.79e-45

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 150.64  E-value: 6.79e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIA----RNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKH 73
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIeaaGGKALGLAFDVRDFAATRAALDAGVEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  74 LGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQ-QQGGAIVNVGSIIGVRGNSGQSVYSASK 152
Cdd:PRK12827  85 FGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYAASK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDM-TKDLKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK12827 165 AGLIGLTKTLANELAPRGITVNAVAPGAINTPMaDNAAPTEHLLNPVPVQRLGEPDEVAALVAFLVsdAASYVTGQVIPV 244


                 ....
gi 562866750 230 DGGL 233
Cdd:PRK12827 245 DGGF 248
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 2-232 5.63e-44

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 149.41  E-value: 5.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdaneTKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK06701 126 DILVNNAAFQYPQQSLEDITAEQLDKtFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSATKGAIH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDM---TKDLKE-EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:PRK06701 204 AFTRSLAQSLVQKGIRVNAVAPGPIWTPLipsDFDEEKvSQFGSNTPMQRPGQPEELAPAYVFLAspDSSYITGQMLHVN 283


                 ..
gi 562866750 231 GG 232
Cdd:PRK06701 284 GG 285
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-233 1.75e-43

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 146.82  E-value: 1.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHL-GQVNFLVN 82
Cdd:cd05329   11 VTGGTKGIGYAIVEELAGLGAEVYTCARNqkeLDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgGKLNILVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd05329   91 NAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLTRSL 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMTKDL--KEEHLKKNI---PLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:cd05329  171 ACEWAKDNIRVNAVAPWVIATPLVEPViqQKENLDKVIertPLKRFGEPEEVAALVAFLCmpAASYITGQIIAVDGGL 248
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 2-232 1.83e-43

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 147.47  E-value: 1.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNlegakaaAGDLGGDHLAF-SCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK06171   9 GKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-------GGDGQHENYQFvPTDVSSAEEVNHTVAEIIEKFGRIDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHT---------NLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSAS 151
Cdd:PRK06171  82 VNNAGINIPRLLVDEKDPAGKYELNEaafdkmfniNQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCYAAT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGFIH-TDM----------------TKDLKEEHLKKN-IPLGRFGETVEVAHAV 213
Cdd:PRK06171 162 KAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLrtpeyeealaytrgitVEQLRAGYTKTStIPLGRSGKLSEVADLV 241

                        250       260
                 ....*....|....*....|.
gi 562866750 214 VFLL--ESPYITGHVLVVDGG 232
Cdd:PRK06171 242 CYLLsdRASYITGVTTNIAGG 262
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 2-233 3.07e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 146.41  E-value: 3.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGG--LFVPTDVTDEDAVNALFDTAAETYGSVDIAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVN--RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGN-SGQSVYSASKGGLVGF 158
Cdd:PRK06057  85 NNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSaTSQISYTASKGGVLAM 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK------NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:PRK06057 165 SRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDPERaarrlvHVPMGRFAEPEEIAAAVAFLAsdDASFITASTFLVD 244


                 ...
gi 562866750 231 GGL 233
Cdd:PRK06057 245 GGI 247
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 3-233 4.27e-43

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: 146.06  E-value: 4.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750    3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEInqaGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGFDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   80 LVNAAGVNR-DSLLvrTKTEDMLSQLHT-NLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:TIGR02415  81 MVNNAGVAPiTPIL--EITEEELKKVYNvNVKGVLFGIQAAARQFKKQGhGGKIINAASIAGHEGNPILSAYSSTKFAVR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLK--------------KNIPLGRFGETVEVAHAVVFLL--ESP 220
Cdd:TIGR02415 159 GLTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETSEiagkpigegfeefsSEIALGRPSEPEDVAGLVSFLAseDSD 238

                         250
                  ....*....|...
gi 562866750  221 YITGHVLVVDGGL 233
Cdd:TIGR02415 239 YITGQSILVDGGM 251
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-232 4.48e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 145.63  E-value: 4.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFscDVAKEHDVQNTFEEmekhLGQVNFLVN 82
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL--DVGDDAAIRAALAA----AGAFDGLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMI-QQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK07060  84 CAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIaAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITRV 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDL-----KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK07060 164 LCVELGPHGIRVNSVNPTVTLTPMAAEAwsdpqKSGPMLAAIPLGRFAEVDDVAAPILFLLsdAASMVSGVSLPVDGG 241
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 2-233 5.15e-43

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: 145.68  E-value: 5.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFvHCDVTVEADVRAAVDTAVARFGRLDIM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGV--NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:cd05326   84 FNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMT---KDLKEEHLKK-----NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLV 228
Cdd:cd05326  164 TRSAATELGEHGIRVNCVSPYGVATPLLtagFGVEDEAIEEavrgaANLKGTALRPEDIAAAVLYLAsdDSRYVSGQNLV 243


                 ....*
gi 562866750 229 VDGGL 233
Cdd:cd05326  244 VDGGL 248
PRK07035 PRK07035
SDR family oxidoreductase;
3-233 1.54e-42

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 144.39  E-value: 1.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIvaaGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVN-------RDSLLVRTKTEDMlsqlhtNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASK 152
Cdd:PRK07035  89 LVNNAAANpyfghilDTDLGAFQKTVDV------NIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGH 225
Cdd:PRK07035 163 AAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKndailKQALAHIPLRRHAEPSEMAGAVLYLASdaSSYTTGE 242


                 ....*...
gi 562866750 226 VLVVDGGL 233
Cdd:PRK07035 243 CLNVDGGY 250
PRK05867 PRK05867
SDR family oxidoreductase;
7-232 6.74e-42

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 142.87  E-value: 6.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA 83
Cdd:PRK05867  14 ITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIgtsGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVCN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  84 AGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSV--YSASKGGLVGFSR 160
Cdd:PRK05867  94 AGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVPQQVshYCASKAAVIHLTK 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH--LKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGG 232
Cdd:PRK05867 174 AMAVELAPHKIRVNSVSPGYILTELVEPYTEYQplWEPKIPLGRLGRPEELAGLYLYLASeaSSYMTGSDIVIDGG 249
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
3-235 8.02e-42

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 142.46  E-value: 8.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI--------IARNLEGAKAaagdLGGDHLAFSCDVAKEHDVQNTFEEMEKHL 74
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnsprRVKWLEDQKA----LGFDFIASEGNVGDWDSTKAAFDKVKAEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  75 GQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:PRK12938  80 GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK---NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK12938 160 IHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKivaTIPVRRLGSPDEIGSIVAWLAseESGFSTGADFSL 239


                 ....*.
gi 562866750 230 DGGLQL 235
Cdd:PRK12938 240 NGGLHM 245
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 1-232 1.02e-41

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: 142.47  E-value: 1.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELtnlyKNRVIALELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGV---NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGV--------RGNSGQ 145
Cdd:cd08930   81 IDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGViapdfriyENTQMY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 146 S--VYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKeEHLKKNIPLGRFGETVEVAHAVVFLL--ESPY 221
Cdd:cd08930  161 SpvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEFL-EKYTKKCPLKRMLNPEDLRGAIIFLLsdASSY 239

                        250
                 ....*....|.
gi 562866750 222 ITGHVLVVDGG 232
Cdd:cd08930  240 VTGQNLVIDGG 250
PRK06947 PRK06947
SDR family oxidoreductase;
1-232 2.31e-41

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 141.48  E-value: 2.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGInYARDAAAAEETADavrAAGGRACVVAGDVANEADVIAMFDAVQSAFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQL-HTNLLGSMLTCKAAMRTMIQQQGG---AIVNVGSIIGVRGNSGQSV-YSAS 151
Cdd:PRK06947  81 LDALVNNAGIVAPSMPLADMDAARLRRMfDTNVLGAYLCAREAARRLSTDRGGrggAIVNVSSIASRLGSPNEYVdYAGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDM----TKDLKEEHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGH 225
Cdd:PRK06947 161 KGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIhasgGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSdaASYVTGA 240


                 ....*..
gi 562866750 226 VLVVDGG 232
Cdd:PRK06947 241 LLDVGGG 247
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-232 1.06e-40

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 139.87  E-value: 1.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIA--RNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKAGADIIITThgTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDIL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK06935  96 VNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVAGLTK 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGG 232
Cdd:PRK06935 176 AFANELAAYNIQVNAIAPGYIKTANTAPIRAdknrnDEILKRIPAGRWGEPDDLMGAAVFLASraSDYVNGHILAVDGG 254
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 2-232 1.51e-40

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: 139.73  E-value: 1.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKA-----AAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd05355   26 GKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAeetkkLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:cd05355  106 LDILVNNAAYQHPQESIEDITTEQLEKtFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKGAI 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHT-----DMTKDLKEEHlKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLV 228
Cdd:cd05355  184 VAFTRGLSLQLAEKGIRVNAVAPGPIWTplipsSFPEEKVSEF-GSQVPMGRAGQPAEVAPAYVFLAsqDSSYVTGQVLH 262


                 ....
gi 562866750 229 VDGG 232
Cdd:cd05355  263 VNGG 266
PRK12743 PRK12743
SDR family oxidoreductase;
1-236 3.32e-40

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 138.63  E-value: 3.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAII-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEvrsHGVRAEIRQLDLSDLPEGAQALDKLIQRLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK12743  81 IDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTkDLKEEHLKK----NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK12743 161 GGLTKAMALELVEHGILVNAVAPGAIATPMN-GMDDSDVKPdsrpGIPLGRPGDTHEIASLVAWLCseGASYTTGQSLIV 239


                 ....*..
gi 562866750 230 DGGLQLM 236
Cdd:PRK12743 240 DGGFMLA 246
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 2-232 5.70e-40

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 138.49  E-value: 5.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK08277  10 GKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIkaaGGEALAVKADVLDKESLEQARQQILEDFGPCD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNR---------DSLLVRTKT------EDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNS 143
Cdd:PRK08277  90 ILINGAGGNHpkattdnefHELIEPTKTffdldeEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTPLT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 144 GQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL----------KEEHLKKNIPLGRFGETVEVAHAV 213
Cdd:PRK08277 170 KVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALlfnedgslteRANKILAHTPMGRFGKPEELLGTL 249

                        250       260
                 ....*....|....*....|..
gi 562866750 214 VFLLE---SPYITGHVLVVDGG 232
Cdd:PRK08277 250 LWLADekaSSFVTGVVLPVDGG 271
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-235 7.43e-40

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 137.24  E-value: 7.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFS-CDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGgIDLVDPQAARRAVDEVNRQFGRLDALV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK12828  88 NIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEA 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMtkdlkeehLKKNIPLGRFGETV---EVAHAVVFLL--ESPYITGHVLVVDGGLQL 235
Cdd:PRK12828 168 LAAELLDRGITVNAVLPSIIDTPP--------NRADMPDADFSRWVtpeQIAAVIAFLLsdEAQAITGASIPVDGGVAL 238
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 3-233 8.94e-40

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 137.18  E-value: 8.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIiarNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEEMEKHLG 75
Cdd:PRK12937   6 KVAIVTGASRGIGAAIARRLAADGFAVAV---NYAGSAAAADELvaeieaaGGRAIAVQADVADAAAVTRLFDAAETAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKAAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK12937 161 EGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSaeqiDQLAGLAPLERLGTPEEIAAAVAFLAgpDGAWVNGQVLRV 240


                 ....
gi 562866750 230 DGGL 233
Cdd:PRK12937 241 NGGF 244
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-232 1.01e-39

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: 137.14  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQ----NTFEEMekhlGQ 76
Cdd:cd05345    4 EGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEamveAALSKF----GR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGV---NRDSLLVRTKTEDMLSQLhtNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKG 153
Cdd:cd05345   80 LDILVNNAGIthrNKPMLEVDEEEFDRVFAV--NVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 154 GLVGFSRSLAKEVARKKIRVNVVAP-----GFIHTDMTKDLKE--EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITG 224
Cdd:cd05345  158 WVVTATKAMAVELAPRNIRVNCLCPvagetPLLSMFMGEDTPEnrAKFRATIPLGRLSTPDDIANAALYLAsdEASFITG 237


                 ....*...
gi 562866750 225 HVLVVDGG 232
Cdd:cd05345  238 VALEVDGG 245
PRK07074 PRK07074
SDR family oxidoreductase;
1-233 1.13e-39

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 137.21  E-value: 1.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH-LAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARfVPVACDLTDAASLAAALANAAAERGPVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGnSGQSVYSASKGGLVGFS 159
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAA-LGHPAYSAAKAGLIHYT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHT-------DMTKDLKEEhLKKNIPLGRFGETVEVAHAVVFlLESPY---ITGHVLVV 229
Cdd:PRK07074 160 KLLAVEYGRFGIRANAVAPGTVKTqawearvAANPQVFEE-LKKWYPLQDFATPDDVANAVLF-LASPAaraITGVCLPV 237


                 ....
gi 562866750 230 DGGL 233
Cdd:PRK07074 238 DGGL 241
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-232 1.99e-39

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 136.45  E-value: 1.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGV--FTIKCDVGNRDQVKKSKEVVEKEFGRVDVLV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGV-------NRDSllvrTKTEDMLSqlhTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVrGNS--GQSVYSASK 152
Cdd:PRK06463  85 NNAGImylmpfeEFDE----EKYNKMIK---INLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGI-GTAaeGTTFYAITK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMT---------KDLKEEHLKKNIpLGRFGETVEVAHAVVFLL--ESPY 221
Cdd:PRK06463 157 AGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsgksqeeaEKLRELFRNKTV-LKTTGKPEDIANIVLFLAsdDARY 235

                        250
                 ....*....|.
gi 562866750 222 ITGHVLVVDGG 232
Cdd:PRK06463 236 ITGQVIVADGG 246
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 3-232 2.21e-39

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: 136.28  E-value: 2.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLE-GAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpGAAAELQAINPKVKAtfVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVN--RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQ---GGAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:cd05323   81 LINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkGGVIVNIGSVAGLYPAPQFPVYSASKHG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 155 LVGFSRSLAKEVARKK-IRVNVVAPGFIHTDMTKDLKEEHLKKNIPLGrFGETVEVAHAVVFLLESPYITGHVLVVDGG 232
Cdd:cd05323  161 VVGFTRSLADLLEYKTgVRVNAICPGFTNTPLLPDLVAKEAEMLPSAP-TQSPEVVAKAIVYLIEDDEKNGAIWIVDGG 238
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 3-229 3.42e-39

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: 135.18  E-value: 3.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDlGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd08932   80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMtkdLKEEHLKKNIPLGRFGETVEVAHAVVFLLESPYITGHVLVV 229
Cdd:cd08932  160 RQEGWDHGVRVSAVCPGFVDTPM---AQGLTLVGAFPPEEMIQPKDIANLVRMVIELPENITSVAVL 223
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
2-232 4.77e-39

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 135.54  E-value: 4.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK07067   6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK07067  86 NNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTDM-----TKDLKEEHLK---------KNIPLGRFGETVEVAHAVVFLL--ESPYITG 224
Cdd:PRK07067 166 SAALALIRHGINVNAIAPGVVDTPMwdqvdALFARYENRPpgekkrlvgEAVPLGRMGVPDDLTGMALFLAsaDADYIVA 245


                 ....*...
gi 562866750 225 HVLVVDGG 232
Cdd:PRK07067 246 QTYNVDGG 253
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-233 8.28e-39

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 134.83  E-value: 8.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ-VN 78
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKpIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAA-------GVNRDSLLVRTkTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSiigvrgNSGQSV---- 147
Cdd:PRK08642  84 TVVNNAladfsfdGDARKKADDIT-WEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGT------NLFQNPvvpy 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 148 --YSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTD----MTKDLKEEHLKKNIPLGRFGETVEVAHAVVFLLeSPY 221
Cdd:PRK08642 157 hdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTdasaATPDEVFDLIAATTPLRKVTTPQEFADAVLFFA-SPW 235

                        250
                 ....*....|....*
gi 562866750 222 ---ITGHVLVVDGGL 233
Cdd:PRK08642 236 araVTGQNLVVDGGL 250
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 2-232 1.22e-38

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: 134.89  E-value: 1.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:cd08935    5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalGGRAIALAADVLDRASLERAREEIVAQFGTVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNR-------DSLLVRTKT-------EDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSG 144
Cdd:cd08935   85 ILINGAGGNHpdattdpEHYEPETEQnffdldeEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 145 QSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL----------KEEHLKKNIPLGRFGETVEVAHAVV 214
Cdd:cd08935  165 VPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLlinpdgsytdRSNKILGRTPMGRFGKPEELLGALL 244

                        250       260
                 ....*....|....*....|.
gi 562866750 215 FLLE---SPYITGHVLVVDGG 232
Cdd:cd08935  245 FLASekaSSFVTGVVIPVDGG 265
PRK09242 PRK09242
SDR family oxidoreductase;
2-233 1.24e-38

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 134.49  E-value: 1.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeefpEREVHGLAADVSDDEDRRAILDWVEDHWDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNrdsllVRTKTEDMLSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSAS 151
Cdd:PRK09242  89 LHILVNNAGGN-----IRKAAIDYTEDewrgiFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL--KEEHLKKNI---PLGRFGETVEVAHAVVFLL--ESPYITG 224
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlsDPDYYEQVIertPMRRVGEPEEVAAAVAFLCmpAASYITG 243


                 ....*....
gi 562866750 225 HVLVVDGGL 233
Cdd:PRK09242 244 QCIAVDGGF 252
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-230 2.52e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 133.98  E-value: 2.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYR-LAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELealGAKAVFVQADLSDVEDCRRVVAAADEAFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGV-NRDSLLvRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQG-GAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK06198  86 DALVNAAGLtDRGTIL-DTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKGAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-KEEHLK---------KNIPLGRFGETVEVAHAVVFLL--ESPYIT 223
Cdd:PRK06198 165 ATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIqREFHGApddwlekaaATQPFGRLLDPDEVARAVAFLLsdESGLMT 244


                 ....*..
gi 562866750 224 GHVLVVD 230
Cdd:PRK06198 245 GSVIDFD 251
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-190 2.97e-38

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 133.28  E-value: 2.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLG--GDHLAF-SCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEayGVKVVIaTADVSDYEEVTAAIEQLKNELGSIDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07666  88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLT 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLK 190
Cdd:PRK07666 168 ESLMQEVRKHNIRVTALTPSTVATDMAVDLG 198
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 3-220 3.34e-38

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: 132.63  E-value: 3.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd08929   81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMTKDLKEE--HLKKNiplgrfgetvEVAHAVVFLLESP 220
Cdd:cd08929  161 MLDLREANIRVVNVMPGSVDTGFAGSPEGQawKLAPE----------DVAQAVLFALEMP 210
PRK07326 PRK07326
SDR family oxidoreductase;
1-220 3.94e-38

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 132.83  E-value: 3.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNnkGNVLGLAADVRDEADVQRAVDAIVAAFGGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK07326  85 VLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNASKFGLVGF 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIplgrfgETVEVAHAVVFLLESP 220
Cdd:PRK07326 164 SEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDAWKI------QPEDIAQLVLDLLKMP 219
PRK07069 PRK07069
short chain dehydrogenase; Validated
 7-236 4.74e-38

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 132.91  E-value: 4.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYR--LAIIArNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKvfLTDIN-DAAGLDAFAAEINAAHgegvaFAAVQDVTDEAQWQALLAQAADAMGGLSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07069  83 LVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKK--IRVNVVAPGFIHTDMTKDLKE--------EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVL 227
Cdd:PRK07069 163 KSIALDCARRGldVRCNSIHPTFIRTGIVDPIFQrlgeeeatRKLARGVPLGRLGEPDDVAHAVLYLAsdESRFVTGAEL 242


                 ....*....
gi 562866750 228 VVDGGLQLM 236
Cdd:PRK07069 243 VIDGGICAM 251
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-237 1.07e-37

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 132.15  E-value: 1.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAII-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEieaLGRKALAVKANVGDVEKIKEMFAQIDEEFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVN--AAGVNRDSLLVRTKTEDMlsQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:PRK08063  83 LDVFVNnaASGVLRPAMELEESHWDW--TMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL--KEEHLK---KNIPLGRFGETVEVAHAVVFLL--ESPYITGHVL 227
Cdd:PRK08063 161 LEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFpnREELLEdarAKTPAGRMVEPEDVANAVLFLCspEADMIRGQTI 240

                        250
                 ....*....|
gi 562866750 228 VVDGGLQLMI 237
Cdd:PRK08063 241 IVDGGRSLLV 250
PRK06398 PRK06398
aldose dehydrogenase; Validated
 2-237 1.60e-37

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 131.88  E-value: 1.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGakaaagDLGGDHlaFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK06398   6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS------YNDVDY--FKVDVSNKEQVIKGIDYVISKYGRIDILV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK06398  78 NNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVArKKIRVNVVAPGFIHT---DMTKDLK----EEHLKKNI-------PLGRFGETVEVAHAVVFLL--ESPYITGH 225
Cdd:PRK06398 158 IAVDYA-PTIRCVAVCPGSIRTpllEWAAELEvgkdPEHVERKIrewgemhPMKRVGKPEEVAYVVAFLAsdLASFITGE 236

                        250
                 ....*....|..
gi 562866750 226 VLVVDGGLQLMI 237
Cdd:PRK06398 237 CVTVDGGLRALI 248
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-214 1.79e-37

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: 131.21  E-value: 1.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   4 VCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05339   81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 161 SLAKEVAR---KKIRVNVVAPGFIHTDMTKDLKeehlkknIPLGRFGETVE---VAHAVV 214
Cdd:cd05339  161 SLRLELKAygkPGIKTTLVCPYFINTGMFQGVK-------TPRPLLAPILEpeyVAEKIV 213
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-235 2.68e-37

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 131.46  E-value: 2.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA--GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK08226   7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADelCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIG-VRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08226  87 VNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKAAIVGLT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH-----------LKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHV 226
Cdd:PRK08226 167 KSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSnpedpesvlteMAKAIPLRRLADPLEVGELAAFLAsdESSYLTGTQ 246


                 ....*....
gi 562866750 227 LVVDGGLQL 235
Cdd:PRK08226 247 NVIDGGSTL 255
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 3-233 2.97e-37

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 131.34  E-value: 2.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA---IIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVfndINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07097  91 LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGLKMLT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKN-----------IPLGRFGETVEVAHAVVFLLE--SPYITGHV 226
Cdd:PRK07097 171 KNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGSrhpfdqfiiakTPAARWGDPEDLAGPAVFLASdaSNFVNGHI 250


                 ....*..
gi 562866750 227 LVVDGGL 233
Cdd:PRK07097 251 LYVDGGI 257
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-232 3.03e-37

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: 130.47  E-value: 3.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd05357    5 VTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDelnaLRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd05357   85 NASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562866750 163 AKEVArKKIRVNVVAPGFI--HTDMTKDLKEEHLKKnIPLGRFGETVEVAHAVVFLLESPYITGHVLVVDGG 232
Cdd:cd05357  165 ALELA-PNIRVNGIAPGLIllPEDMDAEYRENALRK-VPLKRRPSAEEIADAVIFLLDSNYITGQIIKVDGG 234
PRK07062 PRK07062
SDR family oxidoreductase;
2-233 4.06e-37

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 130.93  E-value: 4.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK07062   8 GRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFpgarlLAARCDVLDEADVAAFAAAVEARFGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK07062  88 VDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARAGLL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHT------------------DMTKDLKEehlKKNIPLGRFGETVEVAHAVVFLLE 218
Cdd:PRK07062 168 NLVKSLATELAPKGVRVNSILLGLVESgqwrrryearadpgqsweAWTAALAR---KKGIPLGRLGRPDEAARALFFLAS 244

                        250
                 ....*....|....*..
gi 562866750 219 --SPYITGHVLVVDGGL 233
Cdd:PRK07062 245 plSSYTTGSHIDVSGGF 261
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 3-228 4.48e-37

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: 130.43  E-value: 4.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd05374   81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMTK----------------DLKEEHLKKNIPLGRFGETVE-VAHAVVFLLESPYITGH 225
Cdd:cd05374  161 RLELAPFGIKVTIIEPGPVRTGFADnaagsaledpeispyaPERKEIKENAAGVGSNPGDPEkVADVIVKALTSESPPLR 240


                 ...
gi 562866750 226 VLV 228
Cdd:cd05374  241 YFL 243
PRK07856 PRK07856
SDR family oxidoreductase;
2-232 8.67e-37

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 129.67  E-value: 8.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNlegAKAAAGDLGGDHLAfsCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK07856   6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR---APETVDGRPAEFHA--ADVRDPDQVAALVDAIVERHGRLDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK07856  81 NNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLTR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 161 SLAKEVArKKIRVNVVAPGFIHTdmtkDLKEEH---------LKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK07856 161 SLAVEWA-PKVRVNAVVVGLVRT----EQSELHygdaegiaaVAATVPLGRLATPADIAWACLFLAsdLASYVSGANLEV 235


                 ...
gi 562866750 230 DGG 232
Cdd:PRK07856 236 HGG 238
PRK08589 PRK08589
SDR family oxidoreductase;
2-233 1.03e-36

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 129.90  E-value: 1.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAI--IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGAYVLAvdIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQqGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK08589  86 LFNNAGVDNAAGRIHEYPVDVFDKiMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTSSFSGQAADLYRSGYNAAKGAVINF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDL---KEEHLKKNI--------PLGRFGETVEVAHAVVFLL--ESPYITGH 225
Cdd:PRK08589 165 TKSIAIEYGRDGIRANAIAPGTIETPLVDKLtgtSEDEAGKTFrenqkwmtPLGRLGKPEEVAKLVVFLAsdDSSFITGE 244


                 ....*...
gi 562866750 226 VLVVDGGL 233
Cdd:PRK08589 245 TIRIDGGV 252
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 9-233 2.11e-36

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 128.72  E-value: 2.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAG 85
Cdd:PRK08085  16 GSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLrqeGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINNAG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  86 VNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKE 165
Cdd:PRK08085  96 IQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAVKMLTRGMCVE 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 562866750 166 VARKKIRVNVVAPGFIHTDMTKDLKEEH-----LKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGGL 233
Cdd:PRK08085 176 LARHNIQVNGIAPGYFKTEMTKALVEDEaftawLCKRTPAARWGDPQELIGAAVFLSSkaSDFVNGHLLFVDGGM 250
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 2-196 2.46e-36

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 128.14  E-value: 2.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLA-------FSCDVAKEHDVQNTFEEMEKHL 74
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANAsgqkvsyISADLSDYEEVEQAFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  75 GQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPGFIHTDMtkdLKEEHLKK 196
Cdd:cd08939  161 LRGLAESLRQELKPYNIRVSVVYPPDTDTPG---FEEENKTK 199
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-236 6.09e-36

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 127.84  E-value: 6.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEEMEKHLG 75
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYgegmaYGFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPG-FIHTDMTKDLKEEHLKK--------------NIPLGRFGETVEVAHAVVFLL-- 217
Cdd:PRK12384 161 GVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQSLLPQYAKKlgikpdeveqyyidKVPLKRGCDYQDVLNMLLFYAsp 240

                        250
                 ....*....|....*....
gi 562866750 218 ESPYITGHVLVVDGGlQLM 236
Cdd:PRK12384 241 KASYCTGQSINVTGG-QVM 258
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-232 6.20e-36

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 127.31  E-value: 6.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKaaagdlgGDHLA-FSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQE-------DYPFAtFVLDVSDAAAVAQVCQRLLAETGPLDVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSiigvrgNS------GQSVYSASKGGL 155
Cdd:PRK08220  82 NAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGS------NAahvpriGMAAYGASKAAL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-KEEHLKKN------------IPLGRFGETVEVAHAVVFLL--ESP 220
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLwVDEDGEQQviagfpeqfklgIPLGKIARPQEIANAVLFLAsdLAS 235

                        250
                 ....*....|..
gi 562866750 221 YITGHVLVVDGG 232
Cdd:PRK08220 236 HITLQDIVVDGG 247
PRK09135 PRK09135
pteridine reductase; Provisional
 1-235 7.53e-36

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 126.97  E-value: 7.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN-LEGAKAAAGDLG----GDHLAFSCDVAKEHDVQNTFEEMEKHLG 75
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNalrpGSAAALQADLLDPDALPELVAACVAAFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAgvnrdSLLVRTK----TEDMLSQLH-TNLLGSMLTCKAAMrTMIQQQGGAIVNVGSIIGVRGNSGQSVYSA 150
Cdd:PRK09135  85 RLDALVNNA-----SSFYPTPlgsiTEAQWDDLFaSNLKAPFFLSQAAA-PQLRKQRGAIVNITDIHAERPLKGYPVYCA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 151 SKGGLVGFSRSLAKEVArKKIRVNVVAPGFI----HTDMTKDLKEEHLKKNIPLGRFGETVEVAHAVVFLL-ESPYITGH 225
Cdd:PRK09135 159 AKAALEMLTRSLALELA-PEVRVNAVAPGAIlwpeDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLLaDASFITGQ 237

                        250
                 ....*....|
gi 562866750 226 VLVVDGGLQL 235
Cdd:PRK09135 238 ILAVDGGRSL 247
PRK06114 PRK06114
SDR family oxidoreductase;
2-232 7.95e-36

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 127.21  E-value: 7.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK06114   8 GQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEhieaAGRRAIQIAADVTSKADLRAAVARTEAELGAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSG--QSVYSASKGGL 155
Cdd:PRK06114  88 TLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllQAHYNASKAGV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK----NIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVV 229
Cdd:PRK06114 168 IHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKlfeeQTPMQRMAKVDEMVGPAVFLLSdaASFCTGVDLLV 247


                 ...
gi 562866750 230 DGG 232
Cdd:PRK06114 248 DGG 250
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-235 1.24e-35

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 126.61  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRpddeELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGV---NRDSLLvRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQG------GAIVNVGSIIGVRGNSGQSV 147
Cdd:PRK12745  81 IDCLVNNAGVgvkVRGDLL-DLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNRGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 148 YSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH----LKKNIPLGRFGETVEVAHAVVFLLES--PY 221
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYdaliAKGLVPMPRWGEPEDVARAVAALASGdlPY 239

                        250
                 ....*....|....
gi 562866750 222 ITGHVLVVDGGLQL 235
Cdd:PRK12745 240 STGQAIHVDGGLSI 253
PRK08628 PRK08628
SDR family oxidoreductase;
2-232 1.28e-35

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 126.61  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK08628   7 DKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEElrALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNrDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMrTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08628  87 LVNNAGVN-DGVGLEAGREAFVASLERNLIHYYVMAHYCL-PHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQLALT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDM------TKDLKEEHLK---KNIPLG-RFGETVEVAHAVVFLLE--SPYITGHVL 227
Cdd:PRK08628 165 REWAVALAKDGVRVNAVIPAEVMTPLyenwiaTFDDPEAKLAaitAKIPLGhRMTTAEEIADTAVFLLSerSSHTTGQWL 244


                 ....*
gi 562866750 228 VVDGG 232
Cdd:PRK08628 245 FVDGG 249
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-235 1.48e-35

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 126.37  E-value: 1.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK06077   6 DKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKkraeEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK06077  86 DILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAAVIN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVArKKIRVNVVAPGFIHTDMTKDL-------KEEHLKKNIPLGRFGETVEVAHAVVFLLESPYITGHVLVVD 230
Cdd:PRK06077 164 LTKYLALELA-PKIRVNAIAPGFVKTKLGESLfkvlgmsEKEFAEKFTLMGKILDPEEVAEFVAAILKIESITGQVFVLD 242


                 ....*
gi 562866750 231 GGLQL 235
Cdd:PRK06077 243 SGESL 247
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 2-236 2.63e-35

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 125.89  E-value: 2.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK08265   6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGRVDILV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKtEDMLSQLHTNLLGSMLTCKAAMRTMIQQqGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK08265  86 NLACTYLDDGLASSR-ADWLAALDVNLVSAAMLAQAAHPHLARG-GGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTRS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNI-------PLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK08265 164 MAMDLAPDGIRVNSVSPGWTWSRVMDELSGGDRAKADrvaapfhLLGRVGDPEEVAQVVAFLCsdAASFVTGADYAVDGG 243


                 ....
gi 562866750 233 LQLM 236
Cdd:PRK08265 244 YSAL 247
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 3-235 2.87e-35

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: 125.27  E-value: 2.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLaiIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEmekhLGQVNFLVN 82
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANV--IATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKE----EGRIDVLFN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIG-VRGNSGQSVYSASKGGLVGFSRS 161
Cdd:cd05368   77 CAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAVIGLTKS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDL------KEEHLK---KNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:cd05368  157 VAADFAQQGIRCNAICPGTVDTPSLEERiqaqpdPEEALKafaARQPLGRLATPEEVAALAVYLAsdESAYVTGTAVVID 236


                 ....*
gi 562866750 231 GGLQL 235
Cdd:cd05368  237 GGWSL 241
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 6-186 2.91e-35

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: 125.52  E-value: 2.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   6 AVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH---LAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd05350    2 LITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNpsvEVEILDVTDEERNQLVIAELEAELGGLDLVII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd05350   82 NAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAESL 161

                        170       180
                 ....*....|....*....|....
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMT 186
Cdd:cd05350  162 RYDVKKRGIRVTVINPGFIDTPLT 185
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 2-235 3.93e-35

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: 125.73  E-value: 3.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLG----GDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNragpGSCKFVPCDVTKEEDIKTLISVTVERFGRI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNR-DSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGaIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:cd08933   89 DCLVNNAGWHPpHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGN-IINLSSLVGSIGQKQAAPYVATKGAIT 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-----------KEEHLKKniPLGRFGETVEVAHAVVFLL-ESPYITG 224
Cdd:cd08933  168 AMTKALAVDESRYGVRVNCISPGNIWTPLWEELaaqtpdtlatiKEGELAQ--LLGRMGTEAESGLAALFLAaEATFCTG 245

                        250
                 ....*....|.
gi 562866750 225 HVLVVDGGLQL 235
Cdd:cd08933  246 IDLLLSGGAEL 256
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 4-220 4.20e-35

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: 124.80  E-value: 4.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   4 VCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVrelGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562866750 161 SLAKEVARKK--IRVNVVAPGFIHTDMTKDLKEEHLKKNIPLGRFGETVEVAHAVVFLLESP 220
Cdd:cd05360  162 SLRAELAHDGapISVTLVQPTAMNTPFFGHARSYMGKKPKPPPPIYQPERVAEAIVRAAEHP 223
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 7-235 4.78e-35

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: 124.89  E-value: 4.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRlaIIARNLEGAKAAAGdlgGDHL-AFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAG 85
Cdd:cd05331    3 VTGAAQGIGRAVARHLLQAGAT--VIALDLPFVLLLEY---GDPLrLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  86 VNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKE 165
Cdd:cd05331   78 VLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 166 VARKKIRVNVVAPGFIHTDMTKDL-------------KEEHLKKNIPLGRFGETVEVAHAVVFLLeSP---YITGHVLVV 229
Cdd:cd05331  158 LAPYGVRCNVVSPGSTDTAMQRTLwhdedgaaqviagVPEQFRLGIPLGKIAQPADIANAVLFLA-SDqagHITMHDLVV 236


                 ....*.
gi 562866750 230 DGGLQL 235
Cdd:cd05331  237 DGGATL 242
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 2-232 4.91e-35

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: 125.33  E-value: 4.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd05330    3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapDAEVLLIKADVSDEAQVEAYVDATVEQFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVN-RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:cd05330   83 IDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMT----KDLKEEHLKK-------NIPLGRFGETVEVAHAVVFLL--ESPYI 222
Cdd:cd05330  163 VGLTRNSAVEYGQYGIRINAIAPGAILTPMVegslKQLGPENPEEageefvsVNPMKRFGEPEEVAAVVAFLLsdDAGYV 242

                        250
                 ....*....|
gi 562866750 223 TGHVLVVDGG 232
Cdd:cd05330  243 NAAVVPIDGG 252
PRK07774 PRK07774
SDR family oxidoreductase;
2-232 5.43e-35

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 124.86  E-value: 5.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadGGTAIAVQVDVSDPDSAKAMADATVSAFGGID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRD---SLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNvGSIIGVRGNSGqsVYSASKGGL 155
Cdd:PRK07774  86 YLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVN-QSSTAAWLYSN--FYGLAKVGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLK----KNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK07774 163 NGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVadmvKGIPLSRMGTPEDLVGMCLFLLsdEASWITGQIFNV 242


                 ...
gi 562866750 230 DGG 232
Cdd:PRK07774 243 DGG 245
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 2-232 9.33e-35

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 124.56  E-value: 9.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEilAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVN-AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIiGVRGNSgQSVYSASKGGLVGF 158
Cdd:cd08937   84 LINnVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSI-ATRGIY-RIPYSAAKGGVNAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKN----------------IPLGRFGETVEVAHAVVFLL--ESP 220
Cdd:cd08937  162 TASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEqekvwyqrivdqtldsSLMGRYGTIDEQVRAILFLAsdEAS 241

                        250
                 ....*....|..
gi 562866750 221 YITGHVLVVDGG 232
Cdd:cd08937  242 YITGTVLPVGGG 253
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 2-232 1.27e-34

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 124.30  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK07890   5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARtaeRLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVN-AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQqGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK07890  85 ALVNnAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES-GGSIVMINSMVLRHSQPKYGAYKMAKGALLA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTK------------DLKE--EHLKKNIPLGRFGETVEVAHAVVFLLeSPY-- 221
Cdd:PRK07890 164 ASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfrhqagkygvTVEQiyAETAANSDLKRLPTDDEVASAVLFLA-SDLar 242

                        250
                 ....*....|..
gi 562866750 222 -ITGHVLVVDGG 232
Cdd:PRK07890 243 aITGQTLDVNCG 254
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 2-235 1.56e-34

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 124.07  E-value: 1.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIAR-NLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIkkaGGEAIAVKGDVTVESDVVNLIQTAVKEFGTL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK08936  87 DVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAASKGGVK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKN-----IPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK08936 167 LMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRAdvesmIPMGYIGKPEEIAAVAAWLAssEASYVTGITLFA 246


                 ....*.
gi 562866750 230 DGGLQL 235
Cdd:PRK08936 247 DGGMTL 252
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 7-232 3.33e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 123.09  E-value: 3.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNlegakaAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGV 86
Cdd:PRK06523  14 VTGGTKGIGAATVARLLEAGARVVTTARS------RPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDILVHVLGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSL--LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIigvrgnsgQSV---------YSASKGGL 155
Cdd:PRK06523  88 SSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSI--------QRRlplpesttaYAAAKAAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE----------EHLKKN-------IPLGRFGETVEVAHAVVFLLe 218
Cdd:PRK06523 160 STYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAErlaeaagtdyEGAKQIimdslggIPLGRPAEPEEVAELIAFLA- 238

                        250
                 ....*....|....*..
gi 562866750 219 SP---YITGHVLVVDGG 232
Cdd:PRK06523 239 SDraaSITGTEYVIDGG 255
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 4-235 5.76e-34

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: 122.57  E-value: 5.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   4 VCAVFGGSRGIGRAVAQLMARKGYRLAIIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVnrdSLLVRTK----TEDMLSQL-HTNLLGSMLTCKAAMRTMIQQQG------GAIVNVGSI--IGVRGNSGQs 146
Cdd:cd05337   83 LVNNAGI---AVRPRGDlldlTEDSFDRLiAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSInaYLVSPNRGE- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 147 vYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKK----NIPLGRFGETVEVAHAVVFLLES--P 220
Cdd:cd05337  159 -YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELiaagLVPIRRWGQPEDIAKAVRTLASGllP 237

                        250
                 ....*....|....*
gi 562866750 221 YITGHVLVVDGGLQL 235
Cdd:cd05337  238 YSTGQPINIDGGLSM 252
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 2-183 6.11e-34

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 124.26  E-value: 6.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK07109   8 RQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIraaGGEALAVVADVADAEAVQAAADRAEEELGPID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK07109  88 TWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGF 167

                        170       180
                 ....*....|....*....|....*..
gi 562866750 159 SRSLAKEV--ARKKIRVNVVAPGFIHT 183
Cdd:PRK07109 168 TDSLRCELlhDGSPVSVTMVQPPAVNT 194
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-220 6.20e-34

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: 121.88  E-value: 6.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd08934    4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDEQQVDAAVERTVEALGRLDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd08934   84 LVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFS 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDM--------TKDLKEEHLKKNIPLgrfgETVEVAHAVVFLLESP 220
Cdd:cd08934  164 EGLRQEVTERGVRVVVIEPGTVDTELrdhithtiTKEAYEERISTIRKL----QAEDIAAAVRYAVTAP 228
PRK07577 PRK07577
SDR family oxidoreductase;
2-232 7.11e-34

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 121.76  E-value: 7.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNlegakaAAGDLGGDHLAfsCDVAKEHDVQNTFEEMEKHlGQVNFLV 81
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGELFA--CDLADIEQTAATLAQINEI-HPVDAIV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGS--IIGVRGnsgQSVYSASKGGLVGFS 159
Cdd:PRK07577  74 NNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSraIFGALD---RTSYSAAKSALVGCT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLK------EEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDG 231
Cdd:PRK07577 151 RTWALELAEYGITVNAVAPGPIETELFRQTRpvgseeEKRVLASIPMRRLGTPEEVAAAIAFLLsdDAGFITGQVLGVDG 230


                 .
gi 562866750 232 G 232
Cdd:PRK07577 231 G 231
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 2-220 7.32e-34

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 122.74  E-value: 7.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK07825   5 GKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVV-GGPLDVTDPASFAAFLDAVEADLGPIDVLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK07825  84 NNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGFTDA 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIplgrfgETVEVAHAVVFLLESP 220
Cdd:PRK07825 164 ARLELRGTGVHVSVVLPSFVNTELIAGTGGAKGFKNV------EPEDVAAAIVGTVAKP 216
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 2-232 1.12e-33

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: 121.57  E-value: 1.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:cd05363    3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDILV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:cd05363   83 NNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTDMTKDL--------------KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITG 224
Cdd:cd05363  163 SAGLNLIRHGINVNAIAPGVVDGEHWDGVdakfaryenrprgeKKRLVGEAVPFGRMGRAEDLTGMAIFLAstDADYIVA 242


                 ....*...
gi 562866750 225 HVLVVDGG 232
Cdd:cd05363  243 QTYNVDGG 250
PRK09072 PRK09072
SDR family oxidoreductase;
9-185 1.45e-33

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 121.59  E-value: 1.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEG--AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHlGQVNFLVNAAGV 86
Cdd:PRK09072  12 GASGGIGQALAEALAAAGARLLLVGRNAEKleALAARLPYPGRHRWVVADLTSEAGREAVLARAREM-GGINVLINNAGV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:PRK09072  91 NHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSEALRREL 170

                        170
                 ....*....|....*....
gi 562866750 167 ARKKIRVNVVAPGFIHTDM 185
Cdd:PRK09072 171 ADTGVRVLYLAPRATRTAM 189
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 2-232 4.34e-33

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: 119.88  E-value: 4.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEgakaaagDLggDHLAFSC--------DVAkehDVQNTFEEMEKH 73
Cdd:cd05351    7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQA-------DL--DSLVRECpgiepvcvDLS---DWDATEEALGSV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  74 lGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASK 152
Cdd:cd05351   75 -GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-----KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGH 225
Cdd:cd05351  154 AALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNwsdpeKAKKMLNRIPLGKFAEVEDVVNAILFLLsdKSSMTTGS 233


                 ....*..
gi 562866750 226 VLVVDGG 232
Cdd:cd05351  234 TLPVDGG 240
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 2-232 5.71e-33

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: 119.89  E-value: 5.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd08942    6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSayGECIAIPADLSSEEGIEALVARVAERSDRLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGV----NRDSLLVrtKTEDMLSQLHTNllgSMLTCKAAMRTMIQQQGGA-----IVNVGSIIGVRGNSGQS-VYS 149
Cdd:cd08942   86 LVNNAGAtwgaPLEAFPE--SGWDKVMDINVK---SVFFLTQALLPLLRAAATAenparVINIGSIAGIVVSGLENySYG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 150 ASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNIPLGRFGETVEVAHAVVFLLES--PYI 222
Cdd:cd08942  161 ASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNdpaalEAEEKSIPLGRWGRPEDMAGLAIMLASRagAYL 240

                        250
                 ....*....|
gi 562866750 223 TGHVLVVDGG 232
Cdd:cd08942  241 TGAVIPVDGG 250
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 3-189 6.48e-33

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 119.42  E-value: 6.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN-----------LEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTF 67
Cdd:cd05338    4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTasegdngsaksLPGtieeTAEEIEAAGGQALPIVVDVRDEDQVRALV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  68 EEMEKHLGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSV 147
Cdd:cd05338   84 EATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDVA 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 562866750 148 YSASKGGLVGFSRSLAKEVARKKIRVNVVAPG-FIHTDMTKDL 189
Cdd:cd05338  164 YAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIETPAATEL 206
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 2-232 8.77e-33

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: 119.57  E-value: 8.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFS---CDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:cd08936   10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTgtvCHVGKAEDRERLVATAVNLHGGVD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:cd08936   90 ILVSNAAVNPFFGNILDSTEEVWDKiLDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-----KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVD 230
Cdd:cd08936  170 LTKNLAPELAPRNIRVNCLAPGLIKTSFSSALwmdkaVEESMKETLRIRRLGQPEDCAGIVSFLCseDASYITGETVVVG 249


                 ..
gi 562866750 231 GG 232
Cdd:cd08936  250 GG 251
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-231 9.36e-33

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 123.02  E-value: 9.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRlaIIARNLEGAKAA----AGDLGGDHLAfsCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAH--VVCLDVPAAGEAlaavANRVGGTALA--LDITAPDAPARIAEHLAERHGGLD 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK08261 287 IVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGL 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTkdlkeehlkKNIPL-----GRF-------GETVEVAHAVVFLL--ESPYITG 224
Cdd:PRK08261 367 VQALAPLLAERGITINAVAPGFIETQMT---------AAIPFatreaGRRmnslqqgGLPVDVAETIAWLAspASGGVTG 437


                 ....*..
gi 562866750 225 HVLVVDG 231
Cdd:PRK08261 438 NVVRVCG 444
PRK06500 PRK06500
SDR family oxidoreductase;
1-232 1.13e-32

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 118.91  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK06500   5 QGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNrDSLLVRTKTEDMLSQL-HTNLLGSMLTCKAAMRtmIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06500  85 FINAGVA-KFAPLEDWDEAMFDRSfNTNVKGPYFLIQALLP--LLANPASIVLNGSINAHIGMPNSSVYAASKAALLSLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDM-------TKDLKE--EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLV 228
Cdd:PRK06500 162 KTLSGELLPRGIRVNAVSPGPVQTPLygklglpEATLDAvaAQIQALVPLGRFGTPEEIAKAVLYLAsdESAFIVGSEII 241


                 ....
gi 562866750 229 VDGG 232
Cdd:PRK06500 242 VDGG 245
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-236 1.43e-32

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: 118.72  E-value: 1.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA----GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVAdeinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDgIQGRIIQINSKSGKVGSKHNSGYSAAKFGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPG-FIHTDMTKDL----------KEEHLKK----NIPLGRFGETVEVAHAVVFLL--E 218
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSLlpqyakklgiKESEVEQyyidKVPLKRGCDYQDVLNMLLFYAspK 240

                        250
                 ....*....|....*...
gi 562866750 219 SPYITGHVLVVDGGlQLM 236
Cdd:cd05322  241 ASYCTGQSINITGG-QVM 257
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-232 1.64e-32

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 118.84  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVAdeiNKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQ-QQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK13394  88 LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHT--------DMTKDL---KEEHLKK----NIPLGRFGETVEVAHAVVFLLESP--Y 221
Cdd:PRK13394 168 ARVLAKEGAKHNVRSHVVCPGFVRTplvdkqipEQAKELgisEEEVVKKvmlgKTVDGVFTTVEDVAQTVLFLSSFPsaA 247

                        250
                 ....*....|.
gi 562866750 222 ITGHVLVVDGG 232
Cdd:PRK13394 248 LTGQSFVVSHG 258
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-233 2.65e-32

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 123.80  E-value: 2.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGG--DHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGpdRALGVACDVTDEAAVQAAFEEAALAFGGVDIV 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08324 503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLV 582

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTD-----------------MTKDLKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESP 220
Cdd:PRK08324 583 RQLALELGPDGIRVNGVNPDAVVRGsgiwtgewiearaaaygLSEEELEEFYRARNLLKREVTPEDVAEAVVFLAsgLLS 662

                        250
                 ....*....|...
gi 562866750 221 YITGHVLVVDGGL 233
Cdd:PRK08324 663 KTTGAIITVDGGN 675
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 4-232 8.54e-32

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 116.51  E-value: 8.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   4 VCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAiqqAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAG---VNRDSLLVrtKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:cd05365   81 VNNAGgggPKPFDMPM--TEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTK----DLKEEHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDG 231
Cdd:cd05365  159 MTRNLAFDLGPKGIRVNAVAPGAVKTDALAsvltPEIERAMLKHTPLGRLGEPEDIANAALFLCSpaSAWVSGQVLTVSG 238


                 .
gi 562866750 232 G 232
Cdd:cd05365  239 G 239
PRK06181 PRK06181
SDR family oxidoreductase;
2-187 9.13e-32

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 117.00  E-value: 9.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNetrLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQL-HTNLLGSMLTCKAAMRTMIQQQGgAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK06181  81 ILVNNAGITMWSRFDELTDLSVFERVmRVNYLGAVYCTHAALPHLKASRG-QIVVVSSLAGLTGVPTRSGYAASKHALHG 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTK 187
Cdd:PRK06181 160 FFDSLRIELADDGVAVTVVCPGFVATDIRK 189
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 3-232 9.94e-32

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 116.34  E-value: 9.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGD--LGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAaqGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd08943   82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAP-----GFIHTDM--------TKDLKEEHLKKNIPLGRFGETVEVAHAVVFLLESPY--ITG 224
Cdd:cd08943  162 RCLALEGGEDGIRVNTVNPdavfrGSKIWEGvwraarakAYGLLEEEYRTRNLLKREVLPEDVAEAVVAMASEDFgkTTG 241


                 ....*...
gi 562866750 225 HVLVVDGG 232
Cdd:cd08943  242 AIVTVDGG 249
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 2-232 1.13e-31

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 116.48  E-value: 1.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLvRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK06113  91 ILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTD-----MTKDLkEEHLKKNIPLGRFGETVEVAHAVVFLLeSP---YITGHVLVVD 230
Cdd:PRK06113 170 VRNMAFDLGEKNIRVNGIAPGAILTDalksvITPEI-EQKMLQHTPIRRLGQPQDIANAALFLC-SPaasWVSGQILTVS 247


                 ..
gi 562866750 231 GG 232
Cdd:PRK06113 248 GG 249
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 2-187 7.01e-31

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: 113.85  E-value: 7.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntFEEMEKHLGQ- 76
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYgvetKTIAADFSAGDDI---YERIEKELEGl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 -VNFLVNAAGVNRD--SLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKG 153
Cdd:cd05356   78 dIGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 562866750 154 GLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTK 187
Cdd:cd05356  158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 3-233 7.24e-31

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: 114.21  E-value: 7.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:cd09761   82 NAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSEAYAASKGGLVALTHAL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 562866750 163 AKEVARkKIRVNVVAPGFIHTDMTKDLKEEHLKK----NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:cd09761  161 AMSLGP-DIRVNCISPGWINTTEQQEFTAAPLTQedhaQHPAGRVGTPKDIANLVLFLCqqDAGFITGETFIVDGGM 236
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 2-232 8.98e-31

(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: 113.96  E-value: 8.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAI----IARNLEGAKAAAGDL--------GGDHLAFSCDVAkehDVQNTFEE 69
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKGSGKSSSAADKvvdeikaaGGKAVANYDSVE---DGEKIVKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  70 MEKHLGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYS 149
Cdd:cd05353   82 AIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 150 ASKGGLVGFSRSLAKEVARKKIRVNVVAPGfIHTDMTKDLKEEHLKKNIplgrfgETVEVAHAVVFLL-ESPYITGHVLV 228
Cdd:cd05353  162 AAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRMTETVMPEDLFDAL------KPEYVAPLVLYLChESCEVTGGLFE 234


                 ....
gi 562866750 229 VDGG 232
Cdd:cd05353  235 VGAG 238
PRK07831 PRK07831
SDR family oxidoreductase;
13-229 1.48e-30

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 113.59  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  13 GIGRAVAQLMARKGYRLAII---ARNL-EGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGVN 87
Cdd:PRK07831  29 GIGSATARRALEEGARVVISdihERRLgETADELAAELGLGRVeAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  88 RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMI-QQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:PRK07831 109 GQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRaRGHGGVIVNNASVLGWRAQHGQAHYAAAKAGVMALTRCSALEA 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 167 ARKKIRVNVVAPGF-IHTDMTK----DLKEEhLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVV 229
Cdd:PRK07831 189 AEYGVRINAVAPSIaMHPFLAKvtsaELLDE-LAAREAFGRAAEPWEVANVIAFLASdySSYLTGEVVSV 257
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 9-184 1.71e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 113.86  E-value: 1.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGVNR 88
Cdd:PRK06180  11 GVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  89 DSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVAR 168
Cdd:PRK06180  91 EGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAP 170

                        170
                 ....*....|....*.
gi 562866750 169 KKIRVNVVAPGFIHTD 184
Cdd:PRK06180 171 FGIHVTAVEPGSFRTD 186
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 2-232 1.92e-30

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 113.50  E-value: 1.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN--LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNrdsllVRTK------TEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSII--GVRgnsgQSVYSAS 151
Cdd:PRK12823  88 LINNVGGT-----IWAKpfeeyeEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIAtrGIN----RVPYSAA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGFI-------------HTDMTKDLKEEHLKKNI---PLGRFGETVEVAHAVVF 215
Cdd:PRK12823 159 KGGVNALTASLAFEYAEHGIRVNAVAPGGTeapprrvprnaapQSEQEKAWYQQIVDQTLdssLMKRYGTIDEQVAAILF 238

                        250
                 ....*....|....*....
gi 562866750 216 LL--ESPYITGHVLVVDGG 232
Cdd:PRK12823 239 LAsdEASYITGTVLPVGGG 257
PRK06128 PRK06128
SDR family oxidoreductase;
9-235 4.04e-30

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 113.42  E-value: 4.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA-----GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA 83
Cdd:PRK06128  62 GADSGIGRATAIAFAREGADIALNYLPEEEQDAAEvvqliQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLDILVNI 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  84 AG--VNRDSLLVRTkTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK06128 142 AGkqTAVKDIADIT-TEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTGSIQSYQPSPTLLDYASTKAAIVAFTKA 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDM-----TKDLKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGLQ 234
Cdd:PRK06128 219 LAKQVAEKGIRVNAVAPGPVWTPLqpsggQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLAsqESSYVTGEVFGVTGGLL 298


                 .
gi 562866750 235 L 235
Cdd:PRK06128 299 L 299
PRK07814 PRK07814
SDR family oxidoreductase;
2-234 6.14e-30

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 112.18  E-value: 6.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEqirAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQG-GAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK07814  90 IVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGgGSVINISSTMGRLAGRGFAAYGTAKAALAH 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVArKKIRVNVVAPGFIHTD-----MTKDLKEEHLKKNIPLGRFGETVEVAHAVVFlLESP---YITGHVLVV 229
Cdd:PRK07814 170 YTRLAALDLC-PRIRVNAIAPGSILTSalevvAANDELRAPMEKATPLRRLGDPEDIAAAAVY-LASPagsYLTGKTLEV 247


                 ....*
gi 562866750 230 DGGLQ 234
Cdd:PRK07814 248 DGGLT 252
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 1-192 6.22e-30

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: 111.91  E-value: 6.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL--GGDHLAFSC--DVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd05332    2 QGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECleLGAPSPHVVplDMSDLEDAEQVVEEALKLFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:cd05332   82 LDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQ 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMT-KDLKEE 192
Cdd:cd05332  162 GFFDSLRAELSEPNISVTVVCPGLIDTNIAmNALSGD 198
PRK07454 PRK07454
SDR family oxidoreductase;
9-183 6.73e-30

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 111.59  E-value: 6.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAG 85
Cdd:PRK07454  13 GASSGIGKATALAFAKAGWDLALVARSqdaLEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  86 VNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKE 165
Cdd:PRK07454  93 MAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCLAEE 172

                        170
                 ....*....|....*...
gi 562866750 166 VARKKIRVNVVAPGFIHT 183
Cdd:PRK07454 173 ERSHGIRVCTITLGAVNT 190
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 3-233 9.49e-30

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: 111.48  E-value: 9.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRT--MIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:cd08945   84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE--------------EHLKKNIPLGRFGETVEVAHAVVFLL--ESPY 221
Cdd:cd08945  164 FTKALGLELARTGITVNAVCPGFVETPMAASVREhyadiwevsteeafDRITARVPLGRYVTPEEVAGMVAYLIgdGAAA 243

                        250
                 ....*....|..
gi 562866750 222 ITGHVLVVDGGL 233
Cdd:cd08945  244 VTAQALNVCGGL 255
PRK07041 PRK07041
SDR family oxidoreductase;
7-232 4.11e-29

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 108.97  E-value: 4.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH--LAFSCDVAKEHDVQNTFEEMekhlGQVNFLVNAA 84
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGApvRTAALDITDEAAVDAFFAEA----GPFDHVVITA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  85 GVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAmrtmIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAK 164
Cdd:PRK07041  78 ADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLAL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 562866750 165 EVArkKIRVNVVAPGFIHTD----MTKDLKEEHL---KKNIPLGRFGETVEVAHAVVFLLESPYITGHVLVVDGG 232
Cdd:PRK07041 154 ELA--PVRVNTVSPGLVDTPlwskLAGDAREAMFaaaAERLPARRVGQPEDVANAILFLAANGFTTGSTVLVDGG 226
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 2-232 4.80e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 109.63  E-value: 4.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRqaeLDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVR-GNSGQSVYSASKGGLV 156
Cdd:PRK07478  86 IAFNNAGTLGEMGPVAEMSLEGWREtLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTaGFPGMAAYAASKAGLI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL-----KEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVV 229
Cdd:PRK07478 166 GLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMgdtpeALAFVAGLHALKRMAQPEEIAQAALFLAsdAASFVTGTALLV 245


                 ...
gi 562866750 230 DGG 232
Cdd:PRK07478 246 DGG 248
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 4-184 5.90e-29

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: 109.01  E-value: 5.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   4 VCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKA----AAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAllvdIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALA 160

                        170       180
                 ....*....|....*....|....*.
gi 562866750 160 RSLAKEVARKKIRV-NVVAPGFIHTD 184
Cdd:cd05373  161 QSMARELGPKGIHVaHVIIDGGIDTD 186
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 7-233 6.28e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 109.47  E-value: 6.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH-----LAFscDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK07523  15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGlsahaLAF--DVTDHDAVRAAIDAFEAEIGPIDILV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK07523  93 NNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVGNLTKG 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH-----LKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGGL 233
Cdd:PRK07523 173 MATDWAKHGLQCNAIAPGYFDTPLNAALVADPefsawLEKRTPAGRWGKVEELVGACVFLASdaSSFVNGHVLYVDGGI 251
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 1-232 1.62e-28

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: 108.30  E-value: 1.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGyrlAIIARNLEGAKA--------AAGDLGGDHLAFSCDVAKEHDVQNTFEEMEK 72
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAG---ANIVLNGFGDAAeieavragLAAKHGVKVLYHGADLSKPAAIEDMVAYAQR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  73 HLGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASK 152
Cdd:cd08940   78 QFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTK---------------DLKEEHLKKNIPLGRFGETVEVAHAVVFLL 217
Cdd:cd08940  158 HGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEkqisalaqkngvpqeQAARELLLEKQPSKQFVTPEQLGDTAVFLA 237

                        250
                 ....*....|....*..
gi 562866750 218 --ESPYITGHVLVVDGG 232
Cdd:cd08940  238 sdAASQITGTAVSVDGG 254
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-232 2.01e-28

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 107.36  E-value: 2.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRlaIIARNLEGAKAAAGDLGgdhlafscdvAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQ--VYGVDKQDKPDLSGNFH----------FLQLDLSDDLEPLFDWVPSVDIL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK06550  72 CNTAGILDDYKPLLDTSLEEWQHiFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMT-KDLKEEHLKKNI----PLGRFGETVEVAHAVVFlLESP---YITGHVLVVDG 231
Cdd:PRK06550 152 KQLALDYAKDGIQVFGIAPGAVKTPMTaADFEPGGLADWVaretPIKRWAEPEEVAELTLF-LASGkadYMQGTIVPIDG 230


                 .
gi 562866750 232 G 232
Cdd:PRK06550 231 G 231
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 3-235 2.28e-28

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 108.12  E-value: 2.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07576  10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVaqlQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07576  90 LVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLL-RRPGASIIQISAPQAFVPMPMQAHVCAAKAGVDMLT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIhtDMTKDLK--------EEHLKKNIPLGRFGETVEVAHAVVFlLESP---YITGHVLV 228
Cdd:PRK07576 169 RTLALEWGPEGIRVNSIVPGPI--AGTEGMArlapspelQAAVAQSVPLKRNGTKQDIANAALF-LASDmasYITGVVLP 245


                 ....*..
gi 562866750 229 VDGGLQL 235
Cdd:PRK07576 246 VDGGWSL 252
PRK05650 PRK05650
SDR family oxidoreductase;
9-185 8.85e-28

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 106.66  E-value: 8.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAG 85
Cdd:PRK05650   7 GAASGLGRAIALRWAREGWRLALADVNEEGGEETLkllREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  86 VNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKE 165
Cdd:PRK05650  87 VASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLLVE 166

                        170       180
                 ....*....|....*....|
gi 562866750 166 VARKKIRVNVVAPGFIHTDM 185
Cdd:PRK05650 167 LADDEIGVHVVCPSFFQTNL 186
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-184 1.03e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 106.66  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK08263  82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSE 161

                        170       180
                 ....*....|....*....|....
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTD 184
Cdd:PRK08263 162 ALAQEVAEFGIKVTLVEPGGYSTD 185
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-232 1.51e-27

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 106.06  E-value: 1.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVcfFHCDVTVEDDVSRAVDFTVDKFGTLDIM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVN--RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PLN02253  99 VNNAGLTgpPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHAVLGL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMT------KDLKEEHLK-------KNIPLGRFGETV-EVAHAVVFLL--ESPYI 222
Cdd:PLN02253 179 TRSVAAELGKHGIRVNCVSPYAVPTALAlahlpeDERTEDALAgfrafagKNANLKGVELTVdDVANAVLFLAsdEARYI 258

                        250
                 ....*....|
gi 562866750 223 TGHVLVVDGG 232
Cdd:PLN02253 259 SGLNLMIDGG 268
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 2-220 9.38e-27

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: 103.36  E-value: 9.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECqsagYPTLFPYQCDLSNEEQILSMFSAIRTQHQGV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ--QGGAIVNVGSIIGVRGNSGQ--SVYSASKG 153
Cdd:cd05343   86 DVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERnvDDGHIININSMSGHRVPPVSvfHFYAATKH 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562866750 154 GLVGFSRSLAKEV--ARKKIRVNVVAPGFIHTDMTKDL---KEEHLKKNIPLGRFGETVEVAHAVVFLLESP 220
Cdd:cd05343  166 AVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLhdnDPEKAAATYESIPCLKPEDVANAVLYVLSTP 237
PRK08267 PRK08267
SDR family oxidoreductase;
6-193 1.96e-26

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 102.71  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   6 AVF--GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEE-MEKHLGQVNFLV 81
Cdd:PRK08267   3 SIFitGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAwTGALDVTDRAAWDAALADfAAATGGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK08267  83 NNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEA 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKEEH 193
Cdd:PRK08267 163 LDLEWRRHGIRVADVMPLFVDTAMLDGTSNEV 194
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 3-187 2.28e-26

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: 101.93  E-value: 2.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKG-YRLAIIARNLEGAKAAAGDLGGDHL---AFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAEGLsvrFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGvrgnSGQSVYSASKGGLVG 157
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREQAREtMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLG----SLTSAYGVSKAALNA 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTK 187
Cdd:cd05324  157 LTRILAKELKETGIKVNACCPGWVKTDMGG 186
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 3-185 5.11e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 101.90  E-value: 5.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDhlafsCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGVELLE-----LDVTDDASVQAAVDEVIARAGRIDVLVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNrdslLVRTKTEDMLSQLH----TNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK06179  80 NAGVG----LAGAAEESSIAQAQalfdTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGY 155

                        170       180
                 ....*....|....*....|....*..
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDM 185
Cdd:PRK06179 156 SESLDHEVRQFGIRVSLVEPAYTKTNF 182
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-203 6.10e-26

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: 101.01  E-value: 6.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGVNR 88
Cdd:COG3967   12 GGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLH-TIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIMR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  89 DSLLVRTKT--EDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:COG3967   91 AEDLLDEAEdlADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSLRHQL 170

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 562866750 167 ARKKIRVNVVAPGFIHTDMTKDLKEEHLKknIPLGRF 203
Cdd:COG3967  171 KDTSVKVIELAPPAVDTDLTGGQGGDPRA--MPLDEF 205
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 2-233 8.89e-26

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: 100.89  E-value: 8.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:cd05348    4 GEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCFI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQL-----HTNLLGSMLTCKAAMRTMIQQQGGAIVNVgSIIGVRGNSGQSVYSASKGGLV 156
Cdd:cd05348   84 GNAGIWDYSTSLVDIPEEKLDEAfdelfHINVKGYILGAKAALPALYATEGSVIFTV-SNAGFYPGGGGPLYTASKHAVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVArKKIRVNVVAPGFIHTDMTKDLKEEHLKKNI-------------PLGRFGETVEVAHAVVFLL---ESP 220
Cdd:cd05348  163 GLVKQLAYELA-PHIRVNGVAPGGMVTDLRGPASLGQGETSIstpplddmlksilPLGFAPEPEDYTGAYVFLAsrgDNR 241

                        250
                 ....*....|...
gi 562866750 221 YITGHVLVVDGGL 233
Cdd:cd05348  242 PATGTVINYDGGM 254
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-232 1.40e-25

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 100.36  E-value: 1.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGyrLAIIARNLEGA---KAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK12481   9 KVAIITGCNTGLGQGMAIGLAKAG--ADIVGVGVAEApetQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQ-GGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK12481  87 LINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGnGGKIINIASMLSFQGGIRVPSYTASKSAVMGL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLK-----KNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDG 231
Cdd:PRK12481 167 TRALATELSQYNINVNAIAPGYMATDNTAALRADTARneailERIPASRWGTPDDLAGPAIFLSSsaSDYVTGYTLAVDG 246


                 .
gi 562866750 232 G 232
Cdd:PRK12481 247 G 247
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 6-213 3.93e-25

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: 98.68  E-value: 3.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   6 AVF--GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEEM-EKHLGQVNFLV 81
Cdd:cd08931    2 AIFitGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVvAGALDVTDRAAWAAALADFaAATGGRLDALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:cd08931   82 NNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTKDLKEE-HLKKNipLGRFGETVEVAHAV 213
Cdd:cd08931  162 LDVEWARHGIRVADVWPWFVDTPILTKGETGaAPKKG--LGRVLPVSDVAKVV 212
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 3-232 4.19e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 98.98  E-value: 4.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTkekLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNrdsLLVRtkTEDML-----SQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGqSVYSAS-K 152
Cdd:PRK07677  82 LINNAAGN---FICP--AEDLSvngwnSVIDIVLNGTFYCSQAVGKYWIEKgIKGNIINMVATYAWDAGPG-VIHSAAaK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARK-KIRVNVVAPGFIHTDMTKD---LKEEHLKK---NIPLGRFGETVEVAHAVVFLL--ESPYIT 223
Cdd:PRK07677 156 AGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERTGGADklwESEEAAKRtiqSVPLGRLGTPEEIAGLAYFLLsdEAAYIN 235


                 ....*....
gi 562866750 224 GHVLVVDGG 232
Cdd:PRK07677 236 GTCITMDGG 244
PRK06914 PRK06914
SDR family oxidoreductase;
1-223 6.56e-25

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 99.33  E-value: 6.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAK-----AAAGDLGGDHLAFSCDVAKEHDVQNtFEEMEKHLG 75
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQEnllsqATQLNLQQNIKVQQLDVTDQNSIHN-FQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDM---TKDLKEEHLKKNIP---------------LGRFGETVEVAHAVVFLL 217
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIwevGKQLAENQSETTSPykeymkkiqkhinsgSDTFGNPIDVANLIVEIA 240


                 ....*.
gi 562866750 218 ESPYIT 223
Cdd:PRK06914 241 ESKRPK 246
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 9-184 6.95e-25

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: 98.51  E-value: 6.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAA 84
Cdd:cd05346    7 GASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFpvkvLPLQLDVSDRESIEAALENLPEEFRDIDILVNNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  85 GVNRDSLLV-RTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLA 163
Cdd:cd05346   87 GLALGLDPAqEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNLR 166

                        170       180
                 ....*....|....*....|.
gi 562866750 164 KEVARKKIRVNVVAPGFIHTD 184
Cdd:cd05346  167 KDLIGTGIRVTNIEPGLVETE 187
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-232 2.23e-24

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 97.25  E-value: 2.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGyrLAIIARNL---EGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAG--CDIVGINIvepTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHIDI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK08993  89 LVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIRVPSYTASKSGVMGV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 159 SRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLK-----KNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDG 231
Cdd:PRK08993 169 TRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRsaeilDRIPAGRWGLPSDLMGPVVFLASsaSDYINGYTIAVDG 248


                 .
gi 562866750 232 G 232
Cdd:PRK08993 249 G 249
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 3-236 5.89e-24

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: 96.11  E-value: 5.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFG--GSRGIGRAVAQLMARKGYRLAIIARN--LEG-AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:cd05372    2 KRILITGiaNDRSIAWGIAKALHEAGAELAFTYQPeaLRKrVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNA-AGVNRDSL---LVRTKTEDMLSQLHTNL--LGSMltCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSAS 151
Cdd:cd05372   82 DGLVHSiAFAPKVQLkgpFLDTSRKGFLKALDISAysLVSL--AKAALPIM--NPGGSIVTLSYLGSERVVPGYNVMGVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGFIHT-------DMTKDLkeEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYI 222
Cdd:cd05372  158 KAALESSVRYLAYELGRKGIRVNAISAGPIKTlaasgitGFDKML--EYSEQRAPLGRNVTAEEVGNTAAFLLsdLSSGI 235

                        250
                 ....*....|....
gi 562866750 223 TGHVLVVDGGLQLM 236
Cdd:cd05372  236 TGEIIYVDGGYHIM 249
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-232 7.44e-24

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 96.01  E-value: 7.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSR--GIGRAVAQLMARKGYRL---------------------AIIARNLE--GAKAAAGDLggdhlafscDV 57
Cdd:PRK12859   7 KVAVVTGVSRldGIGAAICKELAEAGADIfftywtaydkempwgvdqdeqIQLQEELLknGVKVSSMEL---------DL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  58 AKEHDVQNTFEEMEKHLGQVNFLVNAA--GVNRDsllVRTKTEDMLSQLH-TNLLGSMLTCKAAMRTMIQQQGGAIVNVG 134
Cdd:PRK12859  78 TQNDAPKELLNKVTEQLGYPHILVNNAaySTNND---FSNLTAEELDKHYmVNVRATTLLSSQFARGFDKKSGGRIINMT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 135 SIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTD-MTKDLKeEHLKKNIPLGRFGETVEVAHAV 213
Cdd:PRK12859 155 SGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTEEIK-QGLLPMFPFGRIGEPKDAARLI 233

                        250       260
                 ....*....|....*....|.
gi 562866750 214 VFLL--ESPYITGHVLVVDGG 232
Cdd:PRK12859 234 KFLAseEAEWITGQIIHSEGG 254
PRK05855 PRK05855
SDR family oxidoreductase;
2-187 1.38e-23

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 98.51  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAeliRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK05855 395 IVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSLPAYATSKAAVLM 474

                        170       180       190
                 ....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDMTK 187
Cdd:PRK05855 475 LSECLRAELAAAGIGVTAICPGFVDTNIVA 504
PRK08251 PRK08251
SDR family oxidoreductase;
9-186 1.84e-23

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 94.62  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA 83
Cdd:PRK08251   9 GASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpgikvAVAALDVNDHDQVFEVFAEFRDELGGLDRVIVN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  84 AGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSG-QSVYSASKGGLVGFSRSL 162
Cdd:PRK08251  89 AGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGvKAAYAASKAGVASLGEGL 168

                        170       180
                 ....*....|....*....|....
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMT 186
Cdd:PRK08251 169 RAELAKTPIKVSTIEPGYIRSEMN 192
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 2-235 2.13e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 95.25  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK05875   7 DRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIealkgAGAVRYEPADVTDEDQVARAVDAATAWHGR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRD-SLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK05875  87 LHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLV 228
Cdd:PRK05875 167 DHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITEspelsADYRACTPLPRVGEVEDVANLAMFLLsdAASWITGQVIN 246


                 ....*..
gi 562866750 229 VDGGLQL 235
Cdd:PRK05875 247 VDGGHML 253
PRK07775 PRK07775
SDR family oxidoreductase;
7-220 2.69e-23

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 94.82  E-value: 2.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA 83
Cdd:PRK07775  15 VAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIradGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  84 AGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLA 163
Cdd:PRK07775  95 AGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQ 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 164 KEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKkniPL------------GRFGETVEVAHAVVFLLESP 220
Cdd:PRK07775 175 MELEGTGVRASIVHPGPTLTGMGWSLPAEVIG---PMledwakwgqarhDYFLRASDLARAITFVAETP 240
PRK07201 PRK07201
SDR family oxidoreductase;
3-171 2.92e-23

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 97.71  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNgeaLDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGvnRDsllVRTKTEDMLSQLH-------TNLLGSMLTCKAAMRTMIQQQGGAIVNVGSiIGVRGNSGQ-SVYSAS 151
Cdd:PRK07201 452 LVNNAG--RS---IRRSVENSTDRFHdyertmaVNYFGAVRLILGLLPHMRERRFGHVVNVSS-IGVQTNAPRfSAYVAS 525

                        170       180
                 ....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKI 171
Cdd:PRK07201 526 KAALDAFSDVAASETLSDGI 545
PRK09186 PRK09186
flagellin modification protein A; Provisional
 2-235 3.20e-23

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 94.29  E-value: 3.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGD-----HLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK09186   4 GKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEfkskkLSLVELDITDQESLEEFLSKSAEKYGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAA---GVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGV--------RGNSGQ 145
Cdd:PRK09186  84 IDGAVNCAyprNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVvapkfeiyEGTSMT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 146 SV--YSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIPLGRFgETVEVAHAVVFLL--ESPY 221
Cdd:PRK09186 164 SPveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFLNAYKKCCNGKGML-DPDDICGTLVFLLsdQSKY 242

                        250
                 ....*....|....
gi 562866750 222 ITGHVLVVDGGLQL 235
Cdd:PRK09186 243 ITGQNIIVDDGFSL 256
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 4-227 1.13e-22

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 92.35  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   4 VCAVFGGSRGIGRAVAQLMARKGY--RLAIIARNLEGAKAAAGDL-GGDHLAF-SCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEELrPGLRVTTvKADLSDAAGVEQLLEAIRKLDGERDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRD-SLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQG-GAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:cd05367   81 LINNAGSLGPvSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEvaRKKIRVNVVAPGFIHTDMTKDLKEEHlKKNIPLGRF------GETVE---VAHAVVFLLESP-YITGHVL 227
Cdd:cd05367  161 FFRVLAAE--EPDVRVLSYAPGVVDTDMQREIRETS-ADPETRSRFrslkekGELLDpeqSAEKLANLLEKDkFESGAHV 237
PRK08264 PRK08264
SDR family oxidoreductase;
2-189 1.19e-22

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 92.26  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRA-VAQLMARKGYRLAIIARNLEGAKaaagDLGGDHLAFSCDVAKEHDVQNTFEemekHLGQVNFL 80
Cdd:PRK08264   6 GKVVLVTGANRGIGRAfVEQLLARGAAKVYAAARDPESVT----DLGPRVVPLQLDVTDPASVAAAAE----AASDVTIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNR-DSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08264  78 VNNAGIFRtGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSLT 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDL 189
Cdd:PRK08264 158 QALRAELAPQGTRVLGVHPGPIDTDMAAGL 187
PRK09134 PRK09134
SDR family oxidoreductase;
7-236 2.16e-22

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 91.91  E-value: 2.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:PRK09134  14 VTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAaeiRALGRRAVALQADLADEAEVRALVARASAALGPITLLVN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGV-NRDSllVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVgsiigvrgnSGQSV---------YSAS 151
Cdd:PRK09134  94 NASLfEYDS--AASFTRASWDRhMATNLRAPFVLAQAFARALPADARGLVVNM---------IDQRVwnlnpdflsYTLS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVArKKIRVNVVAPGFihTDMTKDLKEEHLKKNI---PLGRFGETVEVAHAVVFLLESPYITGHVLV 228
Cdd:PRK09134 163 KAALWTATRTLAQALA-PRIRVNAIGPGP--TLPSGRQSPEDFARQHaatPLGRGSTPEEIAAAVRYLLDAPSVTGQMIA 239


                 ....*...
gi 562866750 229 VDGGLQLM 236
Cdd:PRK09134 240 VDGGQHLA 247
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 7-236 3.17e-22

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: 91.24  E-value: 3.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFG--GSRGIGRAVAQLMARKGYRLAIIARN--LEG-AKAAAGDLGGDhLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:COG0623   10 ITGvaNDRSIAWGIAKALHEEGAELAFTYQGeaLKKrVEPLAEELGSA-LVLPCDVTDDEQIDALFDEIKEKWGKLDFLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NA-AGVNRDSL---LVRTKTEDMLSQLHTNL--LGSMltCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:COG0623   89 HSiAFAPKEELggrFLDTSREGFLLAMDISAysLVAL--AKAAEPLM--NEGGSIVTLTYLGAERVVPNYNVMGVAKAAL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHT-------DMTKDLKeeHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHV 226
Cdd:COG0623  165 EASVRYLAADLGPKGIRVNAISAGPIKTlaasgipGFDKLLD--YAEERAPLGRNVTIEEVGNAAAFLLsdLASGITGEI 242

                        250
                 ....*....|
gi 562866750 227 LVVDGGLQLM 236
Cdd:COG0623  243 IYVDGGYHIM 252
PRK07832 PRK07832
SDR family oxidoreductase;
3-187 4.40e-22

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 91.64  E-value: 4.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGD---LGG---DHLAFscDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADaraLGGtvpEHRAL--DISDYDAVAAFAADIHAAHGS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK07832  79 MDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAgRGGHLVNVSSAAGLVALPWHAAYSASKFGL 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTK 187
Cdd:PRK07832 159 RGLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 2-235 6.06e-22

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 90.78  E-value: 6.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:PRK06200   6 GQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVNRDSLLVRTKTEDMLSQL-----HTNLLGSMLTCKAAMRTMIQQQGGAIVNVgSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK06200  86 GNAGIWDYNTSLVDIPAETLDTAfdeifNVNVKGYLLGAKAALPALKASGGSMIFTL-SNSSFYPGGGGPLYTASKHAVV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 157 GFSRSLAKEVArKKIRVNVVAPGFIHTDM----TKDLKEEHLKKN----------IPLGRFGETVEVAHAVVFLL---ES 219
Cdd:PRK06200 165 GLVRQLAYELA-PKIRVNGVAPGGTVTDLrgpaSLGQGETSISDSpgladmiaaiTPLQFAPQPEDHTGPYVLLAsrrNS 243

                        250
                 ....*....|....*.
gi 562866750 220 PYITGHVLVVDGGLQL 235
Cdd:PRK06200 244 RALTGVVINADGGLGI 259
PRK05717 PRK05717
SDR family oxidoreductase;
3-233 7.44e-22

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 90.72  E-value: 7.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV- 81
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVc 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAGVN-RDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMrTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK05717  91 NAAIADpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCA-PYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLALTH 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 161 SLAKEVArKKIRVNVVAPGFIHTDMTKDLKEEHLKK----NIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:PRK05717 170 ALAISLG-PEIRVNAVSPGWIDARDPSQRRAEPLSEadhaQHPAGRVGTVEDVAAMVAWLLsrQAGFVTGQEFVVDGGM 247
PRK07024 PRK07024
SDR family oxidoreductase;
7-187 9.02e-22

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 90.37  E-value: 9.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VF--GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGD--HLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:PRK07024   5 VFitGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAarVSVYAADVRDADALAAAAADFIAAHGLPDVVIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK07024  85 NAGISVGTLTEEREDLAVFREvMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLES 164

                        170       180
                 ....*....|....*....|....*.
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTDMTK 187
Cdd:PRK07024 165 LRVELRPAGVRVVTIAPGYIRTPMTA 190
PRK08219 PRK08219
SDR family oxidoreductase;
1-220 1.74e-21

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 88.84  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARkGYRLAIIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEemekHLGQVNFL 80
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELPGAT-PFPVDLTDPEAIAAAVE----QLGRLDVL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSM-LTckAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08219  76 VHNAGVADLGPVAESTVDEWRATLEVNVVAPAeLT--RLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 562866750 160 RSLAKEvARKKIRVNVVAPGFIHTDMTKDLKeEHLKKNIPLGRFGETVEVAHAVVFLLESP 220
Cdd:PRK08219 154 DALREE-EPGNVRVTSVHPGRTDTDMQRGLV-AQEGGEYDPERYLRPETVAKAVRFAVDAP 212
PRK06949 PRK06949
SDR family oxidoreductase;
3-233 1.88e-21

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 89.44  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIeaeGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGA--------IVNVGSIIGVRGNSGQSVYSAS 151
Cdd:PRK06949  90 LVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLRVLPQIGLYCMS 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE----EHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGH 225
Cdd:PRK06949 170 KAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWEteqgQKLVSMLPRKRVGKPEDLDGLLLLLAadESQFINGA 249


                 ....*...
gi 562866750 226 VLVVDGGL 233
Cdd:PRK06949 250 IISADDGF 257
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 7-230 1.92e-21

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: 88.02  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNlegakaaagdlGGDHLafsCDVAKEHDVQNTFEEmekhLGQVNFLVNAAGV 86
Cdd:cd11731    3 VIGATGTIGLAVAQLLSAHGHEVITAGRS-----------SGDYQ---VDITDEASIKALFEK----VGHFDAIVSTAGD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:cd11731   65 AEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIEL 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 562866750 167 ARkKIRVNVVAPGFIHT--DMTKDLKEEHLKkniplgrfGETVEVAHAVVFLLESPYiTGHVLVVD 230
Cdd:cd11731  143 PR-GIRINAVSPGVVEEslEAYGDFFPGFEP--------VPAEDVAKAYVRSVEGAF-TGQVLHVD 198
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 2-192 2.84e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 89.64  E-value: 2.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAF--SCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLtvVADVTDLAAMQAAAEEAVERFGGIDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK05872  89 VVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALI-ERRGYVLQVSSLAAFAAAPGMAAYCASKAGVEAFA 167

                        170       180       190
                 ....*....|....*....|....*....|...
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE 192
Cdd:PRK05872 168 NALRLEVAHHGVTVGSAYLSWIDTDLVRDADAD 200
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 9-234 7.02e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 88.18  E-value: 7.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntfEEMEKHLGQVNFLVNAA 84
Cdd:PRK06125  14 GASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHgvdvAVHALDLSSPEAR----EQLAAEAGDIDILVNNA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  85 GVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVgsiIGVRGNSGQSVY---SASKGGLVGFSRS 161
Cdd:PRK06125  90 GAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV---IGAAGENPDADYicgSAGNAALMAFTRA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHTD-MTKDLKE------------EHLKKNIPLGRFGETVEVAHAVVFlLESP---YITGH 225
Cdd:PRK06125 167 LGGKSLDDGVRVVGVNPGPVATDrMLTLLKGraraelgdesrwQELLAGLPLGRPATPEEVADLVAF-LASPrsgYTSGT 245


                 ....*....
gi 562866750 226 VLVVDGGLQ 234
Cdd:PRK06125 246 VVTVDGGIS 254
PRK07985 PRK07985
SDR family oxidoreductase;
2-235 8.00e-21

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 88.51  E-value: 8.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAII-----ARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK07985  49 DRKALVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLH-TNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK07985 129 LDIMALVAGKQVAIPDIADLTSEQFQKTFaINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSPHLLDYAATKAAI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDM------TKDlKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVL 227
Cdd:PRK07985 207 LNYSRGLAKQVAEKGIRVNIVAPGPIWTALqisggqTQD-KIPQFGQQTPMKRAGQPAELAPVYVYLAsqESSYVTAEVH 285


                 ....*...
gi 562866750 228 VVDGGLQL 235
Cdd:PRK07985 286 GVCGGEHL 293
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-235 1.21e-20

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 87.12  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLAFScDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNenkLKRMKKTLSKYGNIHYVVG-DVSSTESARNVIEKAAKVLNAIDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 L-VNAAGVNRDSLLVRTKTEDMLSQlhtNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGV-RGNSGQSVYSASKGGLVG 157
Cdd:PRK05786  85 LvVTVGGYVEDTVEEFSGLEEMLTN---HIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIyKASPDQLSYAVAKAGLAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHTDmtkDLKEEHLKKNIPLGRFGETVE-VAHAVVFLL--ESPYITGHVLVVDGGLQ 234
Cdd:PRK05786 160 AVEILASELLGRGIRVNGIAPTTISGD---FEPERNWKKLRKLGDDMAPPEdFAKVIIWLLtdEADWVDGVVIPVDGGAR 236


                 .
gi 562866750 235 L 235
Cdd:PRK05786 237 L 237
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-229 1.42e-20

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 87.12  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHL-GQV 77
Cdd:cd09763    4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTilpqLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQqGRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAA-GVNRDSLLVRTKT---------EDMLSqlhTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRgNSGQSV 147
Cdd:cd09763   84 DILVNNAyAAVQLILVGVAKPfweepptiwDDINN---VGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLE-YLFNVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 148 YSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKdlkeEHLKKNIPL--------GRFGETVE-VAHAVVFLLE 218
Cdd:cd09763  160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVL----EMPEDDEGSwhakerdaFLNGETTEySGRCVVALAA 235

                        250
                 ....*....|....
gi 562866750 219 SP---YITGHVLVV 229
Cdd:cd09763  236 DPdlmELSGRVLIT 249
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-234 2.23e-20

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 86.67  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSR--GIGRAVAQLMARKGYR------------LAIIARNLEGA--KAAAGDLGGDHLAFSCDVAKEHDVQ 64
Cdd:PRK12748   4 MKKIALVTGASRlnGIGAAVCRRLAAKGIDifftywspydktMPWGMHDKEPVllKEEIESYGVRCEHMEIDLSQPYAPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  65 NTFEEMEKHLGQVNFLVNAAGVNRDSLLVrTKTEDMLSQLHT-NLLGSMLTCKAAMRTMIQQQGGAIVNVgsiigvrgNS 143
Cdd:PRK12748  84 RVFYAVSERLGDPSILINNAAYSTHTRLE-ELTAEQLDKHYAvNVRATMLLSSAFAKQYDGKAGGRIINL--------TS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 144 GQSV--------YSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTD-MTKDLKeEHLKKNIPLGRFGETVEVAHAVV 214
Cdd:PRK12748 155 GQSLgpmpdelaYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGwITEELK-HHLVPKFPQGRVGEPVDAARLIA 233

                        250       260
                 ....*....|....*....|..
gi 562866750 215 FLL--ESPYITGHVLVVDGGLQ 234
Cdd:PRK12748 234 FLVseEAKWITGQVIHSEGGFS 255
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-232 2.66e-20

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 87.04  E-value: 2.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI--IARNLEGAKAAAG----------DLGGDHLAFSCDVAKEHDVQNTFEEM 70
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARVVVndIGVGLDGSASGGSaaqavvdeivAAGGEAVANGDDIADWDGAANLVDAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  71 EKHLGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCK-AAMRTMIQQQGG-----AIVNVGSIIGVRGNSG 144
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRhAAAYWRAESKAGravdaRIINTSSGAGLQGSVG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 145 QSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGfIHTDMTKDLKEEHLKKnIPLGRFG--ETVEVAHAVVFL--LESP 220
Cdd:PRK07791 167 QGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-ARTRMTETVFAEMMAK-PEEGEFDamAPENVSPLVVWLgsAESR 244

                        250
                 ....*....|..
gi 562866750 221 YITGHVLVVDGG 232
Cdd:PRK07791 245 DVTGKVFEVEGG 256
PRK06139 PRK06139
SDR family oxidoreductase;
2-220 2.79e-20

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 87.47  E-value: 2.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK06139   7 GAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEecrALGAEVLVVPTDVTDADQVKALATQAASFGGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK06139  87 VWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGF 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 562866750 159 SRSLAKEVARK-KIRVNVVAPGFIHTDMTKDLKEEHLKKNIPLGRFGETVEVAHAVVFLLESP 220
Cdd:PRK06139 167 SEALRGELADHpDIHVCDVYPAFMDTPGFRHGANYTGRRLTPPPPVYDPRRVAKAVVRLADRP 229
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 2-224 2.86e-20

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: 86.51  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL----GGDHLAFS-CDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIkketGNAKVEVIqLDLSSLASVRQFAEEFLARFPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNrdsLLVRTKTEDML-SQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGN------------- 142
Cdd:cd05327   81 LDILINNAGIM---APPRRLTKDGFeLQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPidfndldlennke 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 143 -SGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIpLGRFG-ETVEV-AHAVVFLLES 219
Cdd:cd05327  158 ySPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYKL-LRPFLkKSPEQgAQTALYAATS 236


                 ....*
gi 562866750 220 PYITG 224
Cdd:cd05327  237 PELEG 241
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 4-235 5.93e-20

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: 85.75  E-value: 5.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750    4 VCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAA----------------AGDLGGDHLAFSCdvaKEHDVQNTF 67
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTlaaelnarrpnsavtcQADLSNSATLFSR---CEAIIDACF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   68 eemeKHLGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHT------NLLGSMLTCKAAM-RTMIQQQGG----------AI 130
Cdd:TIGR02685  80 ----RAFGRCDVLVNNASAFYPTPLLRGDAGEGVGDKKSlevqvaELFGSNAIAPYFLiKAFAQRQAGtraeqrstnlSI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  131 VNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGF--IHTDMTKDLKEEHLKKnIPLGRFGETVE 208
Cdd:TIGR02685 156 VNLCDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLslLPDAMPFEVQEDYRRK-VPLGQREASAE 234

                         250       260       270
                  ....*....|....*....|....*....|
gi 562866750  209 -VAHAVVFLL--ESPYITGHVLVVDGGLQL 235
Cdd:TIGR02685 235 qIADVVIFLVspKAKYITGTCIKVDGGLSL 264
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-188 9.19e-20

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: 84.27  E-value: 9.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRA-VAQLMARKGYRLAIIARNLEGAKAAAGdLGGDHLAFSC---DVAKEhdVQNTFEEMEKHLGQ--VNFL 80
Cdd:cd05325    3 ITGASRGIGLElVRQLLARGNNTVIATCRDPSAATELAA-LGASHSRLHIlelDVTDE--IAESAEAVAERLGDagLDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKT-EDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSI---IGVRGNSGQSVYSASKGGLV 156
Cdd:cd05325   80 INNAGILHSYGPASEVDsEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRvgsIGDNTSGGWYSYRASKAALN 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKD 188
Cdd:cd05325  160 MLTKSLAVELKRDGITVVSLHPGWVRTDMGGP 191
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 80-220 1.65e-19

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 82.56  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd02266   35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMTKDLK---EEHLKKNIPLGRFGETVEVAHAVVFLLESP 220
Cdd:cd02266  115 QQWASEGWGNGLPATAVACGTWAGSGMAKGPvapEEILGNRRHGVRTMPPEEVARALLNALDRP 178
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-232 2.22e-19

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 84.83  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI--IARNLEGAKAAA--GDLGGDHLAFSCDVAkEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGATVVVndVASALDASDVLDeiRAAGAKAVAVAGDIS-QRATADELVATAVGLGGLD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAM---RTMIQQQGGA----IVNVGSIIGVRGNSGQSVYSAS 151
Cdd:PRK07792  92 IVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGGPvygrIVNTSSEAGLVGPVGQANYGAA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGfIHTDMTKDLkeehlkkniplgrFGETVEVA----------HAV--VFLLES 219
Cdd:PRK07792 172 KAGITALTLSAARALGRYGVRANAICPR-ARTAMTADV-------------FGDAPDVEaggidplspeHVVplVQFLAS 237

                        250
                 ....*....|....*.
gi 562866750 220 PY---ITGHVLVVDGG 232
Cdd:PRK07792 238 PAaaeVNGQVFIVYGP 253
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 2-186 2.86e-19

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 83.23  E-value: 2.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQ-LMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKehdvQNTFEEMEKHLGQVNFL 80
Cdd:cd05354    3 DKTVLVTGANRGIGKAFVEsLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTD----PESIKAAAAQAKDVDVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNR-DSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:cd05354   79 INNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLT 158

                        170       180
                 ....*....|....*....|....*..
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMT 186
Cdd:cd05354  159 QGLRAELAAQGTLVLSVHPGPIDTRMA 185
PRK12746 PRK12746
SDR family oxidoreductase;
3-235 3.37e-19

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 83.54  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHL---- 74
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIesnGGKAFLIEADLNSIDGVKKLVEQLKNELqirv 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  75 --GQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQqgGAIVNVGSIIGVRGNSGQSVYSASK 152
Cdd:PRK12746  87 gtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLGFTGSIAYGLSK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIP-----LGRFGETVEVAHAVVFLL--ESPYITGH 225
Cdd:PRK12746 165 GALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFAtnssvFGRIGQVEDIADAVAFLAssDSRWVTGQ 244

                        250
                 ....*....|
gi 562866750 226 VLVVDGGLQL 235
Cdd:PRK12746 245 IIDVSGGFCL 254
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 7-185 4.07e-19

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: 82.18  E-value: 4.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEEmekhLGQVNFLVNAAGV 86
Cdd:cd11730    3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA--LARPADVAAELEVWALAQE----LGPLDLLVYAAGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIqqQGGAIVNVGS---IIGVRGNSGqsvYSASKGGLVGFSRSLA 163
Cdd:cd11730   77 ILGKPLARTKPAAWRRILDANLTGAALVLKHALALLA--AGARLVFLGAypeLVMLPGLSA---YAAAKAALEAYVEVAR 151

                        170       180
                 ....*....|....*....|..
gi 562866750 164 KEVarKKIRVNVVAPGFIHTDM 185
Cdd:cd11730  152 KEV--RGLRLTLVRPPAVDTGL 171
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 7-200 1.35e-18

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: 81.20  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGV 86
Cdd:cd05370   10 ITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIH-TIVLDVGDAESVEALAEALLSEYPNLDILINNAGI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSLL--VRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAK 164
Cdd:cd05370   89 QRPIDLrdPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHSYTLALRH 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 562866750 165 EVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNIPL 200
Cdd:cd05370  169 QLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKM 204
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-219 2.61e-18

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 80.88  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIAR--NLEGAKAAaGDLGGDHLAFSCDVAKEHDVQNTFEEM-----EKHLGQVNF 79
Cdd:PRK06924   6 ITGTSQGLGEAIANQLLEKGTHVISISRteNKELTKLA-EQYNSNLTFHSLDLQDVHELETNFNEIlssiqEDNVSSIHL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAM-RTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGF 158
Cdd:PRK06924  85 INNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMkHTKDWKVDKRVINISSGAAKNPYFGWSAYCSSKAGLDMF 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562866750 159 SRSLAKEVARKKIRVNVVA--PGFIHTDMTKDLKEEHLKKNIPLGRFGETVE---------VAHAVVFLLES 219
Cdd:PRK06924 165 TQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQIRSSSKEDFTNLDRFITLKEegkllspeyVAKALRNLLET 236
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 6-233 2.76e-18

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: 81.00  E-value: 2.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   6 AVFGGSRGIGRAVAQLMARKGYRLAIIarnlegakaaagDLGGDHlaFSCDVAKEHDVQNTFEEM-EKHLGQVNFLVNAA 84
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGI------------DLREAD--VIADLSTPEGRAAAIADVlARCSGVLDGLVNCA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  85 GVNrdsllVRTKTEDMLSqlhTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGV------------------------- 139
Cdd:cd05328   69 GVG-----GTTVAGLVLK---VNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalaagtearavala 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 140 --RGNSGQSVYSASKGGLVGFSRSLAKE-VARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNI------PLGRFGETVEVA 210
Cdd:cd05328  141 ehAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGGESvdafvtPMGRRAEPDEIA 220

                        250       260
                 ....*....|....*....|....*.
gi 562866750 211 HAVVFLLeSP---YITGHVLVVDGGL 233
Cdd:cd05328  221 PVIAFLA-SDaasWINGANLFVDGGL 245
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 60-232 5.47e-18

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 79.93  E-value: 5.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  60 EHDVQNTFEEMEKHLGQVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNL-LGSMLTCKAAMRTMIQQQGGAIVNVGSIIG 138
Cdd:cd05361   56 EQKPEELVDAVLQAGGAIDVLVSNDYIPRPMNPIDGTSEADIRQAFEALsIFPFALLQAAIAQMKKAGGGSIIFITSAVP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 139 VRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDM---TKDLKE-----EHLKKNIPLGRFGETVEVA 210
Cdd:cd05361  136 KKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTyfpTSDWENnpelrERVKRDVPLGRLGRPDEMG 215

                        170       180
                 ....*....|....*....|....
gi 562866750 211 HAVVFLL--ESPYITGHVLVVDGG 232
Cdd:cd05361  216 ALVAFLAsrRADPITGQFFAFAGG 239
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-232 2.05e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 78.58  E-value: 2.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAI-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFE----EMEKHL 74
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIqsnGGSAFSIGANLESLHGVEALYSsldnELQNRT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  75 GQVNF--LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASK 152
Cdd:PRK12747  85 GSTKFdiLINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAYSMTK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 153 GGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEEHLKKNI-----PLGRFGETVEVAHAVVFLL--ESPYITGH 225
Cdd:PRK12747 163 GAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYattisAFNRLGEVEDIADTAAFLAspDSRWVTGQ 242


                 ....*..
gi 562866750 226 VLVVDGG 232
Cdd:PRK12747 243 LIDVSGG 249
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 11-232 2.82e-17

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 78.36  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  11 SRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGG----DHLAFSCDVAKEHDVQNTFEEMeKHLGQVNFLVNAAGV 86
Cdd:PRK08339  17 SKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSesnvDVSYIVADLTKREDLERTVKEL-KNIGEPDIFFFSTGG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:PRK08339  96 PKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKEL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 167 ARKKIRVNVVAPGFIHTDMTKDLKEEHLK--------------KNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVD 230
Cdd:PRK08339 176 GPKGITVNGIMPGIIRTDRVIQLAQDRAKregksveealqeyaKPIPLGRLGEPEEIGYLVAFLASdlGSYINGAMIPVD 255


                 ..
gi 562866750 231 GG 232
Cdd:PRK08339 256 GG 257
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 3-185 3.64e-17

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 78.28  E-value: 3.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHL-----AFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLnheviVRHLDLASLKSIRAFAAEFLAEEDRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRdslLVRTKTEDML-SQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRG-------NSGQS--- 146
Cdd:cd09807   82 DVLINNAGVMR---CPYSKTEDGFeMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGkinfddlNSEKSynt 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 562866750 147 --VYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDM 185
Cdd:cd09807  159 gfAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK05866 PRK05866
SDR family oxidoreductase;
9-185 3.77e-17

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 78.24  E-value: 3.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAG 85
Cdd:PRK05866  47 GASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRItraGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  86 VNrdsllVRTKTEDMLSQLH-------TNLLGSMLTCKAAMRTMIQQQGGAIVNVGSiIGVRGNSGQ--SVYSASKGGLV 156
Cdd:PRK05866 127 RS-----IRRPLAESLDRWHdvertmvLNYYAPLRLIRGLAPGMLERGDGHIINVAT-WGVLSEASPlfSVYNASKAALS 200

                        170       180
                 ....*....|....*....|....*....
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDM 185
Cdd:PRK05866 201 AVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-221 6.44e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 77.31  E-value: 6.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAgDLGGDHLAFscDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA-SLGVHPLSL--DVTDEASIKAAVDTIIAEEGRIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:PRK06182  81 NAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDAL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMTkDLKEEHLKKNIPLGRFGETvevAHAVVFLLESPY 221
Cdd:PRK06182 161 RLEVAPFGIDVVVIEPGGIKTEWG-DIAADHLLKTSGNGAYAEQ---AQAVAASMRSTY 215
PRK08416 PRK08416
enoyl-ACP reductase;
3-232 8.22e-17

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 77.12  E-value: 8.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAII-ARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK08416   9 KTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDLeqkyGIKAKAYPLNILEPETYKELFKKIDEDFDRV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSL------LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSiigvrgnSGQSVY--- 148
Cdd:PRK08416  89 DFFISNAIISGRAVvggytkFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSS-------TGNLVYien 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 149 ----SASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTK------DLKEEHLKKNiPLGRFGETVEVAHAVVFLL- 217
Cdd:PRK08416 162 yaghGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKaftnyeEVKAKTEELS-PLNRMGQPEDLAGACLFLCs 240

                        250
                 ....*....|....*.
gi 562866750 218 -ESPYITGHVLVVDGG 232
Cdd:PRK08416 241 eKASWLTGQTIVVDGG 256
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 3-192 4.11e-16

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: 75.19  E-value: 4.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMAR---KGYRLAIIARNL---EGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEEMEKhlG 75
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLkkkGRLWEAAGALAGGTLETlQLDVCDSKSVAAAVERVTE--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:cd09806   79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFAL 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE 192
Cdd:cd09806  159 EGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGS 195
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
11-232 6.81e-16

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 74.62  E-value: 6.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  11 SRGIGRAVAQLMARKGYRLA---IIARNLEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAG-V 86
Cdd:PRK08690  17 ERSIAYGIAKACREQGAELAftyVVDKLEERVRKMAAELDSE-LVFRCDVASDDEINQVFADLGKHWDGLDGLVHSIGfA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSL---LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLA 163
Cdd:PRK08690  96 PKEALsgdFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTA 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562866750 164 KEVARKKIRVNVVAPGFIHT-------DMTKDLKeeHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGG 232
Cdd:PRK08690 176 ACLGKEGIRCNGISAGPIKTlaasgiaDFGKLLG--HVAAHNPLRRNVTIEEVGNTAAFLLSdlSSGITGEITYVDGG 251
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 7-188 1.31e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 73.84  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA 83
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLraeGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFSN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  84 AGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ-QGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:PRK05876  91 AGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQgTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAETL 170

                        170       180
                 ....*....|....*....|....*.
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMTKD 188
Cdd:PRK05876 171 AREVTADGIGVSVLCPMVVETNLVAN 196
PRK06482 PRK06482
SDR family oxidoreductase;
1-189 3.57e-15

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 72.84  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLegakAAAGDLG---GDHL-AFSCDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVRRP----DALDDLKaryGDRLwVLQLDVTDSAAVRAVVDRAFAALGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIE 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 562866750 157 GFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDL 189
Cdd:PRK06482 157 GFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGL 189
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-192 3.77e-15

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: 72.25  E-value: 3.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750    4 VCAVFGGSRGIGRAVAQLMAR----KGYRLAIIARNLEGAKAAAGDLGGDHLA-----FSCDVAKEHDVQNTFEEMEKHL 74
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGlrvvrVSLDLGAEAGLEQLLKALRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   75 GQVNF----LVNAAGvnrdSLLVRTKTEDMLSQL-------HTNLLGSMLTCKAAMRTMIQQQGG--AIVNVGSIIGVRG 141
Cdd:TIGR01500  82 RPKGLqrllLINNAG----TLGDVSKGFVDLSDStqvqnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNISSLCAIQP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 562866750  142 NSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE 192
Cdd:TIGR01500 158 FKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREE 208
PRK05693 PRK05693
SDR family oxidoreductase;
3-192 4.26e-15

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 72.52  E-value: 4.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLE--GAKAAAGdlggdHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFL 80
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEdvEALAAAG-----FTAVQLDVNDGAALARLAEELEAEHGGLDVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLgSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK05693  77 INNAGYGAMGPLLDGGVEAMRRQFETNVF-AVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSD 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTDMTKDLKEE 192
Cdd:PRK05693 156 ALRLELAPFGVQVMEVQPGAIASQFASNASRE 187
PRK06194 PRK06194
hypothetical protein; Provisional
 3-183 4.31e-15

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 72.74  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA---IIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNF 79
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKLVladVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  80 LVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQ------QGGAIVNVGSIIGVRGNSGQSVYSASKG 153
Cdd:PRK06194  87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAMGIYNVSKH 166

                        170       180       190
                 ....*....|....*....|....*....|..
gi 562866750 154 GLVGFSRSLAK--EVARKKIRVNVVAPGFIHT 183
Cdd:PRK06194 167 AVVSLTETLYQdlSLVTDQVGASVLCPYFVPT 198
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-150 1.41e-14

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 69.43  E-value: 1.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750     9 GGSRGIGRAVAQLMARKGYR-LAIIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750    82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRtmiqQQGGAIVNVGSIIGVRGNSGQSVYSA 150
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAA 151
PRK07102 PRK07102
SDR family oxidoreductase;
7-190 2.27e-14

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 69.95  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFScdvakEHDVQNT--FEEMEKHL-GQVNFL 80
Cdd:PRK07102   6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLrarGAVAVSTH-----ELDILDTasHAAFLDSLpALPDIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK07102  81 LIAVGTLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFLS 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHTDMTKDLK 190
Cdd:PRK07102 161 GLRNRLFKSGVHVLTVKPGFVRTPMTAGLK 190
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
12-236 4.11e-14

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 69.37  E-value: 4.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  12 RGIGRAVAQLMARKGYRLAII---ARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA-AGV 86
Cdd:PRK08594  19 RSIAWGIARSLHNAGAKLVFTyagERLEKEVRELADTLEGqESLLLPCDVTSDEEITACFETIKEEVGVIHGVAHCiAFA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSL---LVRTKTEDMLsqLHTNLLGSMLT--CKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRS 161
Cdd:PRK08594  99 NKEDLrgeFLETSRDGFL--LAQNISAYSLTavAREAKKLM--TEGGSIVTLTYLGGERVVQNYNVMGVAKASLEASVKY 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHT-------DMTKDLKEehLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGG 232
Cdd:PRK08594 175 LANDLGKDGIRVNAISAGPIRTlsakgvgGFNSILKE--IEERAPLRRTTTQEEVGDTAAFLFSdlSRGVTGENIHVDSG 252


                 ....
gi 562866750 233 LQLM 236
Cdd:PRK08594 253 YHII 256
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 9-235 6.83e-14

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 68.42  E-value: 6.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV-NAAGVN 87
Cdd:PRK06483   9 GAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAGA--QCIQADFSTNAGIMAFIDELKQHTDGLRAIIhNASDWL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  88 RDSLlvRTKTEDMLS---QLHTN---LLGsmLTCKAAMRTmiQQQGGA-IVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK06483  87 AEKP--GAPLADVLArmmQIHVNapyLLN--LALEDLLRG--HGHAASdIIHITDYVVEKGSDKHIAYAASKAALDNMTL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 161 SLAKEVArKKIRVNVVAPGFI----HTDmtKDLKEEHLKKNIpLGRFGETVEVAHAVVFLLESPYITGHVLVVDGGLQL 235
Cdd:PRK06483 161 SFAAKLA-PEVKVNSIAPALIlfneGDD--AAYRQKALAKSL-LKIEPGEEEIIDLVDYLLTSCYVTGRSLPVDGGRHL 235
PRK12742 PRK12742
SDR family oxidoreductase;
7-232 9.69e-14

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 68.25  E-value: 9.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAII-ARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEEMekhlGQVNFLVNAAG 85
Cdd:PRK12742  11 VLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDAAERLAQETGAT--AVQTDSADRDAVIDVVRKS----GALDILVVNAG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  86 VNR--DSLLVRTKTEDMLsqLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGN-SGQSVYSASKGGLVGFSRSL 162
Cdd:PRK12742  85 IAVfgDALELDADDIDRL--FKINIHAPYHASVEAARQM--PEGGRIIIIGSVNGDRMPvAGMAAYAASKSALQGMARGL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 562866750 163 AKEVARKKIRVNVVAPGFIHTDMTKD--LKEEHLKKNIPLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK12742 161 ARDFGPRGITINVVQPGPIDTDANPAngPMKDMMHSFMAIKRHGRPEEVAGMVAWLAgpEASFVTGAMHTIDGA 234
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-150 4.10e-13

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 65.28  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750    9 GGSRGIGRAVAQLMARKGYR-LAIIARNLEGAKAAAG------DLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:pfam08659   7 GGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQAliaeleARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRGVI 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750   82 NAAGVNRDSLLVRTKTEDMLSQLHTNLLGSmltcKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSA 150
Cdd:pfam08659  87 HAAGVLRDALLENMTDEDWRRVLAPKVTGT----WNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAA 151
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 3-185 6.88e-13

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: 65.42  E-value: 6.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNlEGAKAAAGDLGGDHlafSCDVAKEHDVqntFEEMEKHLGQVNFLVN 82
Cdd:cd05334    2 RVVLVYGGRGALGSAVVQAFKSRGWWVASIDLA-ENEEADASIIVLDS---DSFTEQAKQV---VASVARLSGKVDALIC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAG------VNRDSLLVRTKTedMLSQlhtNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLV 156
Cdd:cd05334   75 VAGgwaggsAKSKSFVKNWDL--MWKQ---NLWTSFIASHLATKHL--LSGGLLVLTGAKAALEPTPGMIGYGAAKAAVH 147

                        170       180       190
                 ....*....|....*....|....*....|.
gi 562866750 157 GFSRSLAKE--VARKKIRVNVVAPGFIHTDM 185
Cdd:cd05334  148 QLTQSLAAEnsGLPAGSTANAILPVTLDTPA 178
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 2-185 9.78e-13

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: 65.29  E-value: 9.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAK------AAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLG 75
Cdd:cd05340    4 DRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRqvadhiNEEGGRQPQWFILDLLTCTSENCQQLAQRIAVNYP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVNRDSL-LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGG 154
Cdd:cd05340   84 RLDGVLHNAGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFA 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 562866750 155 LVGFSRSLAKEVARKKIRVNVVAPGFIHTDM 185
Cdd:cd05340  164 TEGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 7-150 1.63e-12

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 66.24  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARK-GYRLAIIAR--------NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:cd08953  210 VTGGAGGIGRALARALARRyGARLVLLGRsplppeeeWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAI 289

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSmltckAAMRTMIQQQG-GAIVNVGSIIGVRGNSGQSVYSA 150
Cdd:cd08953  290 DGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGL-----LNLAQALADEPlDFFVLFSSVSAFFGGAGQADYAA 358
PRK12744 PRK12744
SDR family oxidoreductase;
2-232 2.55e-12

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 64.38  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAG-------DLGGDHLAFSCDVAKEHDVQNTFEEMEKHL 74
Cdd:PRK12744   8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEetvaavkAAGAKAVAFQADLTTAAAVEKLFDDAKAAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  75 GQVNFLVNAAG-VNRDSLLVRTKTE-DMLSQLhtNLLGSMLTCKAAMRTMiqQQGGAIVN-VGSIIGVRgNSGQSVYSAS 151
Cdd:PRK12744  88 GRPDIAINTVGkVLKKPIVEISEAEyDEMFAV--NSKSAFFFIKEAGRHL--NDNGKIVTlVTSLLGAF-TPFYSAYAGS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPG-----FIHTDMTKDLKEEHlKKNIPLGRFGET-----VEVAHAVVFLL-ESP 220
Cdd:PRK12744 163 KAPVEHFTRAASKEFGARGISVTAVGPGpmdtpFFYPQEGAEAVAYH-KTAAALSPFSKTgltdiEDIVPFIRFLVtDGW 241

                        250
                 ....*....|..
gi 562866750 221 YITGHVLVVDGG 232
Cdd:PRK12744 242 WITGQTILINGG 253
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
55-236 3.42e-12

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 63.96  E-value: 3.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  55 CDVAKEHDVQNTFEEMEKHLGQVNFLVNA-AGVNRDSL---LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAI 130
Cdd:PRK07370  66 CDVQDDAQIEETFETIKQKWGKLDILVHClAFAGKEELigdFSATSREGFARALEISAYSLAPLCKAAKPLM--SEGGSI 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 131 VNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHT----------DMTkdlkeEHLKKNIPL 200
Cdd:PRK07370 144 VTLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTlassavggilDMI-----HHVEEKAPL 218

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 562866750 201 GRFGETVEVAHAVVFLLE--SPYITGHVLVVDGGLQLM 236
Cdd:PRK07370 219 RRTVTQTEVGNTAAFLLSdlASGITGQTIYVDAGYCIM 256
PRK09291 PRK09291
SDR family oxidoreductase;
1-183 4.78e-12

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 63.86  E-value: 4.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRL---AIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEmekhlgQV 77
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNViagVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQAAEW------DV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVG 157
Cdd:PRK09291  75 DVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEA 154

                        170       180
                 ....*....|....*....|....*.
gi 562866750 158 FSRSLAKEVARKKIRVNVVAPGFIHT 183
Cdd:PRK09291 155 IAEAMHAELKPFGIQVATVNPGPYLT 180
PRK07023 PRK07023
SDR family oxidoreductase;
7-185 2.15e-11

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 61.57  E-value: 2.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGA-KAAAGDLGGDHLAFSCDVAK-----EHDVQNTFEEMEKHLgqvnFL 80
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSlAAAAGERLAEVELDLSDAAAaaawlAGDLLAAFVDGASRV----LL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK07023  82 INNAGTVEPIGPLATLDAAAIARaVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALDHHA 161

                        170       180
                 ....*....|....*....|....*.
gi 562866750 160 RSLAKEvARKKIRVNVVAPGFIHTDM 185
Cdd:PRK07023 162 RAVALD-ANRALRIVSLAPGVVDTGM 186
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 5-196 3.07e-11

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: 61.52  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   5 CAVF--GGSRGIGRAVAQLMARKGYRL--AIIARNLEGAK----AAAGDLGGDHLafscDVAKEHDVQNTFEEMEKHLGQ 76
Cdd:cd09805    1 KAVLitGCDSGFGNLLAKKLDSLGFTVlaGCLTKNGPGAKelrrVCSDRLRTLQL----DVTKPEQIKRAAQWVKEHVGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  77 VNF--LVNAAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAaMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKG 153
Cdd:cd09805   77 KGLwgLVNNAGILGFGGDEELLPMDDYRKcMEVNLFGTVEVTKA-FLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 562866750 154 GLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTkdLKEEHLKK 196
Cdd:cd09805  156 AVEAFSDSLRRELQPWGVKVSIIEPGNFKTGIT--GNSELWEK 196
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
75-233 5.78e-11

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 60.40  E-value: 5.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  75 GQVNFLVNAAGVnrdsllvrTKTEDMLSQLHTNLLGsmltckaaMRTMIQQ------QGGAIVNVGSIIGV--------- 139
Cdd:PRK12428  47 GRIDALFNIAGV--------PGTAPVELVARVNFLG--------LRHLTEAllprmaPGGAIVNVASLAGAewpqrlelh 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 140 ------------------RGNSGQSVYSASKGGLVGFSRSLAKEVARKK-IRVNVVAPGFIHTDMTKDLK----EEHLKK 196
Cdd:PRK12428 111 kalaatasfdegaawlaaHPVALATGYQLSKEALILWTMRQAQPWFGARgIRVNCVAPGPVFTPILGDFRsmlgQERVDS 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 562866750 197 NI-PLGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGGL 233
Cdd:PRK12428 191 DAkRMGRPATADEQAAVLVFLCsdAARWINGVNLPVDGGL 230
PRK08340 PRK08340
SDR family oxidoreductase;
7-233 7.96e-11

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 60.20  E-value: 7.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLV-NA 83
Cdd:PRK08340   5 VTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKeyGEVYAVKADLSDKDDLKNLVKEAWELLGGIDALVwNA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  84 AGVNRDSLLVRTKT-EDML--SQLHTNLLGsMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSR 160
Cdd:PRK08340  85 GNVRCEPCMLHEAGySDWLeaALLHLVAPG-YLTTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQLAK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 161 SLAKEVARKKIRVNVVAPGFIHT------------DMTKDLKEEHLKKNI---PLGRFGETVEVAHAVVFLL--ESPYIT 223
Cdd:PRK08340 164 GVSRTYGGKGIRAYTVLLGSFDTpgarenlariaeERGVSFEETWEREVLertPLKRTGRWEELGSLIAFLLseNAEYML 243

                        250
                 ....*....|
gi 562866750 224 GHVLVVDGGL 233
Cdd:PRK08340 244 GSTIVFDGAM 253
PRK08278 PRK08278
SDR family oxidoreductase;
9-178 1.53e-10

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 59.53  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIAR------NLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVN 78
Cdd:PRK08278  13 GASRGIGLAIALRAARDGANIVIAAKtaephpKLPGtihtAAEEIEAAGGQALPLVGDVRDEDQVAAAVAKAVERFGGID 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAgvnrdSLLVRTKTE-------DMLSQLhtNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGV--RGNSGQSVYS 149
Cdd:PRK08278  93 ICVNNA-----SAINLTGTEdtpmkrfDLMQQI--NVRGTFLVSQACLPHLKKSENPHILTLSPPLNLdpKWFAPHTAYT 165

                        170       180
                 ....*....|....*....|....*....
gi 562866750 150 ASKGGLVGFSRSLAKEVARKKIRVNVVAP 178
Cdd:PRK08278 166 MAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-187 2.34e-10

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 59.49  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH---------LAFSCDVakEHDVQNTFEEMEKHlgQV 77
Cdd:PLN02780  58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYsktqiktvvVDFSGDI--DEGVKRIKETIEGL--DV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRD-SLLVRTKTEDMLSQL-HTNLLGSMLTCKAAMRTMIQQQGGAIVNVGS--IIGVRGNSGQSVYSASKG 153
Cdd:PLN02780 134 GVLINNVGVSYPyARFFHEVDEELLKNLiKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSgaAIVIPSDPLYAVYAATKA 213

                        170       180       190
                 ....*....|....*....|....*....|....
gi 562866750 154 GLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTK 187
Cdd:PLN02780 214 YIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMAS 247
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 5-185 4.53e-10

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 57.84  E-value: 4.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   5 CAVF--GGSRGIGRAVAQLMARKGYRLAIIARNLEG----------AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEK 72
Cdd:cd09762    4 KTLFitGASRGIGKAIALKAARDGANVVIAAKTAEPhpklpgtiytAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  73 HLGQVNFLV-NAAGVN-RDSLLVRTKTEDMLSQLhtNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGN--SGQSVY 148
Cdd:cd09762   84 KFGGIDILVnNASAISlTGTLDTPMKRYDLMMGV--NTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKwfKNHTAY 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 562866750 149 SASKGGLVGFSRSLAKEVARKKIRVNVVAP-GFIHTDM 185
Cdd:cd09762  162 TMAKYGMSMCVLGMAEEFKPGGIAVNALWPrTAIATAA 199
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 2-185 7.68e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 57.19  E-value: 7.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN---LEGAKAAAGDLGGDHLA-FSCDV--AKEHDVQNTFEEMEKHLG 75
Cdd:PRK08945  12 DRIILVTGAGDGIGREAALTYARHGATVILLGRTeekLEAVYDEIEAAGGPQPAiIPLDLltATPQNYQQLADTIEEQFG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  76 QVNFLVNAAGVnrdsLLVRT----KTEDMLSQ-LHTNLLGS-MLTcKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYS 149
Cdd:PRK08945  92 RLDGVLHNAGL----LGELGpmeqQDPEVWQDvMQVNVNATfMLT-QALLPLLLKSPAASLVFTSSSVGRQGRANWGAYA 166

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 562866750 150 ASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDM 185
Cdd:PRK08945 167 VSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK07984 PRK07984
enoyl-ACP reductase FabI;
12-235 8.76e-10

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 57.22  E-value: 8.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  12 RGIGRAVAQLMARKGYRLAIIARN--LEG-AKAAAGDLGGDhLAFSCDVAKEHDVQNTFEEMEK----HLGQVNFLVNAA 84
Cdd:PRK07984  18 LSIAYGIAQAMHREGAELAFTYQNdkLKGrVEEFAAQLGSD-IVLPCDVAEDASIDAMFAELGKvwpkFDGFVHSIGFAP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  85 GVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAK 164
Cdd:PRK07984  97 GDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSML-NPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMAN 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562866750 165 EVARKKIRVNVVAPGFIHT---DMTKDLKE--EHLKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGGLQL 235
Cdd:PRK07984 176 AMGPEGVRVNAISAGPIRTlaaSGIKDFRKmlAHCEAVTPIRRTVTIEDVGNSAAFLCSdlSAGISGEVVHVDGGFSI 253
PRK08703 PRK08703
SDR family oxidoreductase;
2-183 1.13e-09

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 56.86  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKA------AAGdlGGDHLAFSCDVAKEHDvqNTFEEM----- 70
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKvydaivEAG--HPEPFAIRFDLMSAEE--KEFEQFaatia 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  71 EKHLGQVNFLVNAAG-VNRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYS 149
Cdd:PRK08703  82 EATQGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFG 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 562866750 150 ASKGGLVGFSRSLAKEVAR-KKIRVNVVAPGFIHT 183
Cdd:PRK08703 162 ASKAALNYLCKVAADEWERfGNLRANVLVPGPINS 196
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 7-181 1.31e-09

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 56.69  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGV 86
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 nrdSLLV----RTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSL 162
Cdd:PRK10538  85 ---ALGLepahKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNL 161

                        170
                 ....*....|....*....
gi 562866750 163 AKEVARKKIRVNVVAPGFI 181
Cdd:PRK10538 162 RTDLHGTAVRVTDIEPGLV 180
PRK08017 PRK08017
SDR family oxidoreductase;
1-186 3.20e-09

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 55.48  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAkAAAGDLGGDHLAFSCDVAKEHDvQNTFEEMEKHLGQVNFL 80
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV-ARMNSLGFTGILLDLDDPESVE-RAADEVIALTDNRLYGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRDSLLVRTKTEDMLSQLHTNLLGS-MLTCkAAMRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFS 159
Cdd:PRK08017  79 FNNAGFGVYGPLSTISRQQMEQQFSTNFFGThQLTM-LLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWS 157

                        170       180
                 ....*....|....*....|....*..
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDMT 186
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRTRFT 184
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
14-236 3.54e-09

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 55.40  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  14 IGRAVAQLMARKGYRLAIIARN--LEG-AKAAAGDLGGDHLAfSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA-AGVNRD 89
Cdd:PRK06603  22 ISWAIAQLAKKHGAELWFTYQSevLEKrVKPLAEEIGCNFVS-ELDVTNPKSISNLFDDIKEKWGSFDFLLHGmAFADKN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  90 SL---LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEV 166
Cdd:PRK06603 101 ELkgrYVDTSLENFHNSLHISCYSLLELSRSAEALM--HDGGSIVTLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDM 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 562866750 167 ARKKIRVNVVAPGFIHT-------DMTKDLKEEhlKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGGLQLM 236
Cdd:PRK06603 179 GENNIRVNAISAGPIKTlassaigDFSTMLKSH--AATAPLKRNTTQEDVGGAAVYLFSelSKGVTGEIHYVDCGYNIM 255
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
12-236 3.92e-09

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 55.52  E-value: 3.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  12 RGIGRAVAQLMARKGYRLAIIARNLEGAKAA---AGDLGGDHLaFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNA-AGVN 87
Cdd:PRK08415  17 KSIAYGIAKACFEQGAELAFTYLNEALKKRVepiAQELGSDYV-YELDVSKPEHFKSLAESLKKDLGKIDFIVHSvAFAP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  88 RDSL---LVRTKTEDMLSQLHTNLLgSMLTCKAAMRTMIqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAK 164
Cdd:PRK08415  96 KEALegsFLETSKEAFNIAMEISVY-SLIELTRALLPLL-NDGASVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 165 EVARKKIRVNVVAPGFIHT-------DMTKDLKEEhlKKNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGGLQL 235
Cdd:PRK08415 174 DLGKKGIRVNAISAGPIKTlaasgigDFRMILKWN--EINAPLKKNVSIEEVGNSGMYLLSdlSSGVTGEIHYVDAGYNI 251


                 .
gi 562866750 236 M 236
Cdd:PRK08415 252 M 252
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
43-232 6.02e-09

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 54.76  E-value: 6.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  43 AGDLGGDhLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGV-NRDSL---LVRTKTEDMLSQLHTNLLGSMLTCKAA 118
Cdd:PRK08159  56 AAELGAF-VAGHCDVTDEASIDAVFETLEKKWGKLDFVVHAIGFsDKDELtgrYVDTSRDNFTMTMDISVYSFTAVAQRA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 119 MRTMiqQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHT-------DMTKDLKE 191
Cdd:PRK08159 135 EKLM--TDGGSILTLTYYGAEKVMPHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTlaasgigDFRYILKW 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 562866750 192 EHLkkNIPLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGG 232
Cdd:PRK08159 213 NEY--NAPLRRTVTIEEVGDSALYLLSdlSRGVTGEVHHVDSG 253
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 1-232 1.99e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 53.48  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGgSRGIGRAVAQLMArKGYRLAIIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEEMEKhLGQV 77
Cdd:PRK06940   1 MKEVVVVIG-AGGIGQAIARRVG-AGKKVLLADYNEENLEAAAKTLreaGFDVSTQEVDVSSRESVKALAATAQT-LGPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRdsllVRTKTEDMLSqlhTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVR----------------- 140
Cdd:PRK06940  78 TGLVHTAGVSP----SQASPEAILK---VDLYGTALVLEEFGKVI--APGGAGVVIASQSGHRlpaltaeqeralattpt 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 141 --------------GNSGQSvYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKD-LKEEH--LKKNI----P 199
Cdd:PRK06940 149 eellslpflqpdaiEDSLHA-YQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDeLNGPRgdGYRNMfaksP 227

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 562866750 200 LGRFGETVEVAHAVVFLL--ESPYITGHVLVVDGG 232
Cdd:PRK06940 228 AGRPGTPDEIAALAEFLMgpRGSFITGSDFLVDGG 262
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-150 3.29e-08

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 53.16  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYR-LAIIARN-----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKhLGQVNFLVN 82
Cdd:cd05274  157 GGLGGLGLLVARWLAARGARhLVLLSRRgpaprAAARAALLRAGGARVSVVRCDVTDPAALAALLAELAA-GGPLAGVIH 235

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQLHTNLLGSMLTCkaamRTMIQQQGGAIVNVGSIIGVRGNSGQSVYSA 150
Cdd:cd05274  236 AAGVLRDALLAELTPAAFAAVLAAKVAGALNLH----ELTPDLPLDFFVLFSSVAALLGGAGQAAYAA 299
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-185 7.57e-08

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 51.72  E-value: 7.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKhLGQVNFLVNAAGVNR 88
Cdd:cd08951   14 GSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHNAGILS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  89 DSlLVRTKTEDMLSQLHTNLLGS-MLTCKAA-------MRTMIQQQGGAIVNvGSIIGVRGNSGQSVYSASKgglvGFSR 160
Cdd:cd08951   93 GP-NRKTPDTGIPAMVAVNVLAPyVLTALIRrpkrliyLSSGMHRGGNASLD-DIDWFNRGENDSPAYSDSK----LHVL 166

                        170       180
                 ....*....|....*....|....*..
gi 562866750 161 SLAKEVAR--KKIRVNVVAPGFIHTDM 185
Cdd:cd08951  167 TLAAAVARrwKDVSSNAVHPGWVPTKM 193
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
55-236 1.37e-07

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 50.88  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  55 CDVAKEHDVQNTFEEMEKHLGQVNFLVNA-AGVNRDSL---LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAI 130
Cdd:PRK06079  62 CDVASDESIERAFATIKERVGKIDGIVHAiAYAKKEELggnVTDTSRDGYALAQDISAYSLIAVAKYARPLL--NPGASI 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 131 VNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE--EHLKKNIPLGRFGETV- 207
Cdd:PRK06079 140 VTLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGIKGhkDLLKESDSRTVDGVGVt 219

                        170       180       190
                 ....*....|....*....|....*....|...
gi 562866750 208 --EVAHAVVFLLE--SPYITGHVLVVDGGLQLM 236
Cdd:PRK06079 220 ieEVGNTAAFLLSdlSTGVTGDIIYVDKGVHLI 252
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
122-191 2.36e-07

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 50.09  E-value: 2.36e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 122 MIQQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE 191
Cdd:PRK07904 133 MRAQGFGQIIAMSSVAGERVRRSNFVYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSAHAKE 202
PRK08862 PRK08862
SDR family oxidoreductase;
10-183 3.24e-07

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 49.34  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  10 GSRgIGRAVAQLMARKGYRLAIIARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV-NFLVNAAG 85
Cdd:PRK08862  14 GSV-LGRTISCHFARLGATLILCDQDQSALKDtyeQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNRApDVLVNNWT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  86 VNRDSLLVRTKTEDMLSQLHTNLLGSMLT----CKAAMRTmiQQQGGAIVNVGSIIGVRGNSGqsvYSASKGGLVGFSRS 161
Cdd:PRK08862  93 SSPLPSLFDEQPSESFIQQLSSLASTLFTygqvAAERMRK--RNKKGVIVNVISHDDHQDLTG---VESSNALVSGFTHS 167

                        170       180
                 ....*....|....*....|..
gi 562866750 162 LAKEVARKKIRVNVVAPGFIHT 183
Cdd:PRK08862 168 WAKELTPFNIRVGGVVPSIFSA 189
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 149-236 4.89e-07

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 49.39  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 149 SASKGGLVGFSRSLAKEVARK-KIRVNVVAPGFIHTDMTK-----DLKEEHLKKNIPLGRFGETVEVAHAVVFLLeSPY- 221
Cdd:PLN02730 194 SSAKAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKaigfiDDMIEYSYANAPLQKELTADEVGNAAAFLA-SPLa 272

                         90
                 ....*....|....*..
gi 562866750 222 --ITGHVLVVDGGLQLM 236
Cdd:PLN02730 273 saITGATIYVDNGLNAM 289
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-229 6.76e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.82  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLafscdvakEHDVQNtFEEMEKHLGQVNFLVNAAGV 86
Cdd:COG0451    4 VTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFV--------RGDLRD-PEALAAALAGVDAVVHLAAP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 nrdsllVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMIQQqggaIVNVGSiIGVRGNSG-----------QSVYSASKggl 155
Cdd:COG0451   75 ------AGVGEEDPDETLEVNVEGTLNLLEAARAAGVKR----FVYASS-SSVYGDGEgpidedtplrpVSPYGASK--- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIH--------TDMTKDLKEehlKKNIPLGRFGETV-------EVAHAVVFLLESP 220
Cdd:COG0451  141 LAAELLARAYARRYGLPVTILRPGNVYgpgdrgvlPRLIRRALA---GEPVPVFGDGDQRrdfihvdDVARAIVLALEAP 217


                 ....*....
gi 562866750 221 YITGHVLVV 229
Cdd:COG0451  218 AAPGGVYNV 226
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
48-236 7.41e-07

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 48.97  E-value: 7.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  48 GDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVNAAGVNRDSLL----VRTKTEDMLSQLHTNLLGSMLTCKAAMRTMi 123
Cdd:PRK06505  57 GSDFVLPCDVEDIASVDAVFEALEKKWGKLDFVVHAIGFSDKNELkgryADTTRENFSRTMVISCFSFTEIAKRAAKLM- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 124 qQQGGAIVNVGSIIGVRGNSGQSVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNI 198
Cdd:PRK06505 136 -PDGGSMLTLTYGGSTRVMPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGIGDaraifSYQQRNS 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 562866750 199 PLGRFGETVEVAHAVVFLLE--SPYITGHVLVVDGGLQLM 236
Cdd:PRK06505 215 PLRRTVTIDEVGGSALYLLSdlSSGVTGEIHFVDSGYNIV 254
PRK05993 PRK05993
SDR family oxidoreductase;
1-198 1.96e-06

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 47.71  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAaagdLGGDHL-AFSCDVAKEHDVQNTFEE-MEKHLGQVN 78
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA----LEAEGLeAFQLDYAEPESIAALVAQvLELSGGRLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  79 FLVNAAGVNRDSLLVRTKTEDMLSQLHTNLLG-SMLTCKA--AMRTmiqQQGGAIVNVGSIIGV-----RGnsgqsVYSA 150
Cdd:PRK05993  79 ALFNNGAYGQPGAVEDLPTEALRAQFEANFFGwHDLTRRVipVMRK---QGQGRIVQCSSILGLvpmkyRG-----AYNA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 562866750 151 SKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKD-LKeeHLKKNI 198
Cdd:PRK05993 151 SKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRFRANaLA--AFKRWI 197
PRK06101 PRK06101
SDR family oxidoreductase;
9-186 2.33e-06

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 47.17  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   9 GGSRGIGRAVAQLMARKGYRLAIIARNlegaKAAAGDLGgdhlAFSCDVAK-EHDVQNtFEEMEKHLGQVNF-----LVN 82
Cdd:PRK06101   8 GATSGIGKQLALDYAKQGWQVIACGRN----QSVLDELH----TQSANIFTlAFDVTD-HPGTKAALSQLPFipelwIFN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AA-------GVNRDSLLVRTktedmlsqLHTNLLGsMLTCKAAMRTMIQQqGGAIVNVGSIIGVRGNSGQSVYSASKGGL 155
Cdd:PRK06101  79 AGdceymddGKVDATLMARV--------FNVNVLG-VANCIEGIQPHLSC-GHRVVIVGSIASELALPRAEAYGASKAAV 148

                        170       180       190
                 ....*....|....*....|....*....|.
gi 562866750 156 VGFSRSLAKEVARKKIRVNVVAPGFIHTDMT 186
Cdd:PRK06101 149 AYFARTLQLDLRPKGIEVVTVFPGFVATPLT 179
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
151-236 3.15e-06

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 46.86  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 151 SKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTK-----DLKEEHLKKNIPLG-RFGETVEVAHAVVFLLES--PYI 222
Cdd:PRK07889 161 AKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKaipgfELLEEGWDERAPLGwDVKDPTPVARAVVALLSDwfPAT 240

                         90
                 ....*....|....
gi 562866750 223 TGHVLVVDGGLQLM 236
Cdd:PRK07889 241 TGEIVHVDGGAHAM 254
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
55-236 1.01e-05

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 45.31  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  55 CDVAKEHDVQNTFEEMEKHLGQVNFLVNA-AGVNRDSL---LVRTKTEDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAI 130
Cdd:PRK07533  67 LDVREPGQLEAVFARIAEEWGRLDFLLHSiAFAPKEDLhgrVVDCSREGFALAMDVSCHSFIRMARLAEPLM--TNGGSL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750 131 VNVgSIIG---VRGNSGqsVYSASKGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLKE-----EHLKKNIPLGR 202
Cdd:PRK07533 145 LTM-SYYGaekVVENYN--LMGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDfdallEDAAERAPLRR 221

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 562866750 203 FGETVEVAHAVVFLLeSPY---ITGHVLVVDGGLQLM 236
Cdd:PRK07533 222 LVDIDDVGAVAAFLA-SDAarrLTGNTLYIDGGYHIV 257
PRK05599 PRK05599
SDR family oxidoreductase;
7-190 1.13e-05

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 45.26  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMArKGYRLAIIARNLEGAKAAAGDL------GGDHLAFSCDVAKEHdvQNTFEEMEKHLGQVNFL 80
Cdd:PRK05599   5 ILGGTSDIAGEIATLLC-HGEDVVLAARRPEAAQGLASDLrqrgatSVHVLSFDAQDLDTH--RELVKQTQELAGEISLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  81 VNAAGVNRD--------SLLVRTKTEDMLSQLhtnllgSMLTCKA-AMRTmiQQQGGAIVNVGSIIGVRGNSGQSVYSAS 151
Cdd:PRK05599  82 VVAFGILGDqeraetdeAHAVEIATVDYTAQV------SMLTVLAdELRA--QTAPAAIVAFSSIAGWRARRANYVYGST 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 562866750 152 KGGLVGFSRSLAKEVARKKIRVNVVAPGFIHTDMTKDLK 190
Cdd:PRK05599 154 KAGLDAFCQGLADSLHGSHVRLIIARPGFVIGSMTTGMK 192
PRK05884 PRK05884
SDR family oxidoreductase;
7-179 1.39e-05

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 44.80  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEEMEKHLgqvNFLVNAAGV 86
Cdd:PRK05884   5 VTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVD--AIVCDNTDPASLEEARGLFPHHL---DTIVNVPAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 NRDSLLVRTKT-----EDMLSQLHTNLLGSMLTCKAAMRTMiqQQGGAIVNVGSIIGVRGnsgqSVYSASKGGLVGFSRS 161
Cdd:PRK05884  80 SWDAGDPRTYSladtaNAWRNALDATVLSAVLTVQSVGDHL--RSGGSIISVVPENPPAG----SAEAAIKAALSNWTAG 153

                        170
                 ....*....|....*...
gi 562866750 162 LAKEVARKKIRVNVVAPG 179
Cdd:PRK05884 154 QAAVFGTRGITINAVACG 171
PRK07806 PRK07806
SDR family oxidoreductase;
2-85 2.01e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 44.33  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGL 85


                 ....*....
gi 562866750  78 NFLV-NAAG 85
Cdd:PRK07806  86 DALVlNASG 94
PRK06953 PRK06953
SDR family oxidoreductase;
7-185 2.40e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 43.91  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAkAAAGDLGGDhlAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVnaAGV 86
Cdd:PRK06953   6 IVGASRGIGREFVRQYRADGWRVIATARDAAAL-AALQALGAE--ALALDVADPASVAGLAWKLDGEALDAAVYV--AGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  87 --NRDSLLVRTKTEDMLSQLHTNLLGSMLTCKAAMrTMIQQQGGAIVNV----GSIIGVRGNSGQsVYSASKGGLVGFSR 160
Cdd:PRK06953  81 ygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILL-PLVEAAGGVLAVLssrmGSIGDATGTTGW-LYRASKAALNDALR 158

                        170       180
                 ....*....|....*....|....*
gi 562866750 161 SLAKEvARKKIRVNvVAPGFIHTDM 185
Cdd:PRK06953 159 AASLQ-ARHATCIA-LHPGWVRTDM 181
PRK08177 PRK08177
SDR family oxidoreductase;
7-185 1.00e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 42.32  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAkAAAGDLGGDHLAfscdvAKEHDVQNTFEEMEKHLGQVNF---LVNA 83
Cdd:PRK08177   6 IIGASRGLGLGLVDRLLERGWQVTATVRGPQQD-TALQALPGVHIE-----KLDMNDPASLDQLLQRLQGQRFdllFVNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  84 AGVNRDSLLVRTKTEDMLSQLH-TNLLgSMLTCKAAMRTMIQQQGGAIVNVGSIIG--VRGNSGQS-VYSASKGGLVGFS 159
Cdd:PRK08177  80 GISGPAHQSAADATAAEIGQLFlTNAI-APIRLARRLLGQVRPGQGVLAFMSSQLGsvELPDGGEMpLYKASKAALNSMT 158

                        170       180
                 ....*....|....*....|....*.
gi 562866750 160 RSLAKEVARKKIRVNVVAPGFIHTDM 185
Cdd:PRK08177 159 RSFVAELGEPTLTVLSMHPGWVKTDM 184
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 7-183 1.18e-04

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 42.20  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL---GGDHLAFS--CDVAKEHDVQNTFEEMEKHLGQVNFLV 81
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIeteSGNQNIFLhiVDMSDPKQVWEFVEEFKEEGKKLHVLI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  82 NAAG--VNRdsllvRTKTEDMLSQ-LHTNLLGSMLTCKAAM---------RTMIQQQGGAIV---NVGSIIGVRGN-SGQ 145
Cdd:cd09808   86 NNAGcmVNK-----RELTEDGLEKnFATNTLGTYILTTHLIpvlekeedpRVITVSSGGMLVqklNTNNLQSERTAfDGT 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 562866750 146 SVYSASKGGLVGFSRSLAKevARKKIRVNVVAPGFIHT 183
Cdd:cd09808  161 MVYAQNKRQQVIMTEQWAK--KHPEIHFSVMHPGWADT 196
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 7-162 1.36e-04

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 42.12  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   7 VFGGSRGIGRAVAQLMARKGYRLAIIA-RNLEGAKAAAGDLG---GDHLAFSCDVAKEHDVQNTFEEMEKHLGQVNFLVN 82
Cdd:cd09810    6 ITGASSGLGLAAAKALARRGEWHVVMAcRDFLKAEQAAQEVGmpkDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDALVC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  83 AAGVNRDSLLVRTKTEDMLSQ-LHTNLLGSMLTCKAAMRTMIQQQGGA--IVNVGSIIGVRGNSGQSV-YSASKGGLVGF 158
Cdd:cd09810   86 NAAVYLPTAKEPRFTADGFELtVGVNHLGHFLLTNLLLEDLQRSENASprIVIVGSITHNPNTLAGNVpPRATLGDLEGL 165


                 ....
gi 562866750 159 SRSL 162
Cdd:cd09810  166 AGGL 169
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-136 5.26e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 40.39  E-value: 5.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEEMEKHLGQV 77
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItaatpGADVTLQELDLTSLASVRAAADALRAAYPRI 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750  78 NFLVNAAGVNRDSllvRTKTEDMLS-QLHTNLLGSMLTCKAAMRTMIQQQGGAIVNVGSI 136
Cdd:PRK06197  97 DLLINNAGVMYTP---KQTTADGFElQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSG 153
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 10-85 8.77e-04

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 37.95  E-value: 8.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562866750   10 GSRGIGRAVAQLMARKG--YRLAIIARNLEGAKAAAGDLGGDHLafscdVAKEHDVQNTFEEMEKHLGQVNFLVNAAG 85
Cdd:pfam03435   5 GAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALAAKLGGVRF-----IAVAVDADNYEAVLAALLKEGDLVVNLSP 77
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 3-90 1.21e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 39.15  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562866750   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAA--AGDLGGdHLAFSCDVAKEHDVqntfeemEKHLGQVNFL 80
Cdd:cd05271    1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLlvMGDLGQ-VLFVEFDLRDDESI-------RKALEGSDVV 72

                         90
                 ....*....|
gi 562866750  81 VNAAGVNRDS 90
Cdd:cd05271   73 INLVGRLYET 82
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 2-43 2.21e-03

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 37.76  E-value: 2.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 562866750   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAA 43
Cdd:cd01078   28 GKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAA 69
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
6-50 4.75e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 37.51  E-value: 4.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 562866750   6 AVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDH 50
Cdd:COG5322  155 AVVGATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNP 199
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
6-46 6.40e-03

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 36.76  E-value: 6.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 562866750   6 AVFGGSRGIGRAVAQLMARKGYRLAIIARN-------LEGAKAAAGDL 46
Cdd:COG2910    3 AVIGATGRVGSLIVREALARGHEVTALVRNpeklpdeHPGLTVVVGDV 50
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 6-63 7.11e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 37.27  E-value: 7.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 562866750   6 AVFGGSRGIGRAVAQLMARKGYRLAIIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDV 63
Cdd:PRK08655   4 SIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANDNIDAAKDADI 61
 
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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