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Conserved domains on  [gi|126723191|ref|NP_932349|]
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dehydrogenase/reductase SDR family member 4-like 2 isoform 1 precursor [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 24-210 1.09e-133

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 cd08936:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 256  Bit Score: 376.50  E-value: 1.09e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:cd08936    2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:cd08936   82 VNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYN 161

                        170       180
                 ....*....|....*....|....*..
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd08936  162 VSKTALLGLTKNLAPELAPRNIRVNCL 188
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 24-210 1.09e-133

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: 376.50  E-value: 1.09e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:cd08936    2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:cd08936   82 VNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYN 161

                        170       180
                 ....*....|....*....|....*..
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd08936  162 VSKTALLGLTKNLAPELAPRNIRVNCL 188
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 28-211 1.03e-66

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: 206.18  E-value: 1.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  28 DPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:COG1028   82 GRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160

                        170       180
                 ....*....|....*....|....
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:COG1028  161 AVVGLTRSLALELAPRGIRVNAVA 184
FabG-like PRK07231
SDR family oxidoreductase;
30-211 4.86e-66

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 204.29  E-value: 4.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK07231  82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAV 161

                        170       180
                 ....*....|....*....|..
gi 126723191 190 LGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK07231 162 ITLTKALAAELGPDKIRVNAVA 183
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 33-210 7.38e-55

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 173.95  E-value: 7.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191   33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  113 LVSNAAVNPFFGSLmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:pfam00106  81 LVNNAGITGLGPFS-ELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170
                  ....*....|....*...
gi 126723191  193 NNTLAIELAPRNIRVNCL 210
Cdd:pfam00106 160 TRSLALELAPHGIRVNAV 177
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 34-220 1.40e-12

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: 65.33  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191   34 VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQA-VATLQ----GEGLSVTGTVCHVGKAEDR-ERLVAMAVKLH 107
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTlAAELNarrpNSAVTCQADLSNSATLFSRcEAIIDACFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  108 GGIDILVSNAAVnpFFGSLM---DVTEEVWD-KTLDI--------NVKAPALMTKAVVPEMEKRGGG----SVVIVSSIA 171
Cdd:TIGR02685  83 GRCDVLVNNASA--FYPTPLlrgDAGEGVGDkKSLEVqvaelfgsNAIAPYFLIKAFAQRQAGTRAEqrstNLSIVNLCD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 126723191  172 AFS--PSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCLHLDLSRLASA 220
Cdd:TIGR02685 161 AMTdqPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPDA 211
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 33-182 2.29e-06

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: 46.32  E-value: 2.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191    33 KVALVTASTDGIGFAIARRLAQDRA-HVVVSSR---KQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126723191   109 GIDILVsNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVvpemEKRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:smart00822  81 PLTGVI-HAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELT----ADLPLDFFVLFSSIAGVLGSPGQANY 149
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 24-210 1.09e-133

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: 376.50  E-value: 1.09e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:cd08936    2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:cd08936   82 VNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYN 161

                        170       180
                 ....*....|....*....|....*..
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd08936  162 VSKTALLGLTKNLAPELAPRNIRVNCL 188
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 28-211 1.03e-66

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: 206.18  E-value: 1.03e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  28 DPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:COG1028   82 GRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160

                        170       180
                 ....*....|....*....|....
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:COG1028  161 AVVGLTRSLALELAPRGIRVNAVA 184
FabG-like PRK07231
SDR family oxidoreductase;
30-211 4.86e-66

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 204.29  E-value: 4.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK07231  82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAV 161

                        170       180
                 ....*....|....*....|..
gi 126723191 190 LGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK07231 162 ITLTKALAAELGPDKIRVNAVA 183
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 35-211 9.81e-60

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: 187.88  E-value: 9.81e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVAtLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDILV 114
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 115 SNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLNN 194
Cdd:cd05233   80 NNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                        170
                 ....*....|....*..
gi 126723191 195 TLAIELAPRNIRVNCLH 211
Cdd:cd05233  159 SLALELAPYGIRVNAVA 175
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 33-210 7.38e-55

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 173.95  E-value: 7.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191   33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  113 LVSNAAVNPFFGSLmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:pfam00106  81 LVNNAGITGLGPFS-ELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170
                  ....*....|....*...
gi 126723191  193 NNTLAIELAPRNIRVNCL 210
Cdd:pfam00106 160 TRSLALELAPHGIRVNAV 177
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
30-209 3.64e-54

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 173.81  E-value: 3.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK05653  83 LDILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGV 161

                        170       180
                 ....*....|....*....|
gi 126723191 190 LGLNNTLAIELAPRNIRVNC 209
Cdd:PRK05653 162 IGFTKALALELASRGITVNA 181
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
30-211 1.64e-53

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 172.36  E-value: 1.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:COG0300   83 IDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161

                        170       180
                 ....*....|....*....|..
gi 126723191 190 LGLNNTLAIELAPRNIRVNCLH 211
Cdd:COG0300  162 EGFSESLRAELAPTGVRVTAVC 183
PRK07035 PRK07035
SDR family oxidoreductase;
30-210 3.68e-53

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 171.74  E-value: 3.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVdQAVA-TLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGC-QAVAdAIVAAGGKAEALACHIGEMEQIDALFAHIRERHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK07035  85 RLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAA 164

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07035 165 VISMTKAFAKECAPFGIRVNAL 186
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 31-211 1.12e-52

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: 169.98  E-value: 1.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVtgtVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAV---PLDVTDEAAVEAAVAAAVAEFGRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:COG4221   81 DVLVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVR 159

                        170       180
                 ....*....|....*....|.
gi 126723191 191 GLNNTLAIELAPRNIRVNCLH 211
Cdd:COG4221  160 GLSESLRAELRPTGIRVTVIE 180
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-211 8.80e-52

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 168.12  E-value: 8.80e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRK-QQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSdEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK12825  83 GRIDILVNNAGIFED-KPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKA 161

                        170       180
                 ....*....|....*....|....
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVA 185
PRK12826 PRK12826
SDR family oxidoreductase;
27-211 6.96e-50

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 163.16  E-value: 6.96e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  27 RDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKL 106
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAA-FSPSPGFSPYNVS 185
Cdd:PRK12826  81 FGRLDILVANAGIFP-LTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGpRVGYPGLAHYAAS 159

                        170       180
                 ....*....|....*....|....*.
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK12826 160 KAGLVGFTRALALELAARNITVNSVH 185
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-209 1.55e-49

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 162.32  E-value: 1.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVAT-LQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEeIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK05565  83 KIDILVNNAGIS-NFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGA 161

                        170       180
                 ....*....|....*....|.
gi 126723191 189 LLGLNNTLAIELAPRNIRVNC 209
Cdd:PRK05565 162 VNAFTKALAKELAPSGIRVNA 182
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 30-210 2.61e-46

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 153.81  E-value: 2.61e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRK-QQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASsEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK05557  83 GVDILVNNAGIT-RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAV 183
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 32-210 6.15e-46

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: 153.20  E-value: 6.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAvNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLG 191
Cdd:cd05344   81 ILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159

                        170
                 ....*....|....*....
gi 126723191 192 LNNTLAIELAPRNIRVNCL 210
Cdd:cd05344  160 LVKTLSRELAPDGVTVNSV 178
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 22-211 3.78e-44

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 149.05  E-value: 3.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  22 SRMTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLqgEGLSVTGTVCHVGKAEDRERLVA 101
Cdd:PRK12829   1 SAIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 102 MAVKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAA-FSPSPGFS 180
Cdd:PRK12829  79 TAVERFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAgRLGYPGRT 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 126723191 181 PYNVSKTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK12829 159 PYAASKWAVVGLVKSLAIELGPLGIRVNAIL 189
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 39-211 9.68e-44

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: 146.81  E-value: 9.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191   39 ASTDGIGFAIARRLAQDRAHVVVS--SRKQQNVDQAVATLQGEGLsvtgTVCHVGKAEDRERLVAMAVKLHGGIDILVSN 116
Cdd:pfam13561   3 ANESGIGWAIARALAEEGAEVVLTdlNEALAKRVEELAEELGAAV----LPCDVTDEEQVEALVAAAVEKFGRLDILVNN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  117 AAV-NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLNNT 195
Cdd:pfam13561  79 AGFaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE--GGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRY 156

                         170
                  ....*....|....*.
gi 126723191  196 LAIELAPRNIRVNCLH 211
Cdd:pfam13561 157 LAVELGPRGIRVNAIS 172
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 30-210 2.67e-43

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: 146.38  E-value: 2.67e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTgtvCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQ---ADVTKRADVEAMVEAALSKFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:cd05345   80 LDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWV 159

                        170       180
                 ....*....|....*....|.
gi 126723191 190 LGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05345  160 VTATKAMAVELAPRNIRVNCL 180
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 30-227 3.26e-43

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 146.18  E-value: 3.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAA---VNPffgsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK12429  82 VDILVNNAGiqhVAP----IEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAK 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNCLhldlsrlasagCSGWTR 227
Cdd:PRK12429 158 HGLIGLTKVVALEGATHGVTVNAI-----------CPGYVD 187
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
22-213 4.08e-43

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 153.85  E-value: 4.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  22 SRMTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVA 101
Cdd:PRK08324 412 QRMPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFE 490

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 102 MAVKLHGGIDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFS 180
Cdd:PRK08324 491 EAALAFGGVDIVVSNAGIAI-SGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPNFG 569

                        170       180       190
                 ....*....|....*....|....*....|...
gi 126723191 181 PYNVSKTALLGLNNTLAIELAPRNIRVNCLHLD 213
Cdd:PRK08324 570 AYGAAKAAELHLVRQLALELGPDGIRVNGVNPD 602
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 33-209 5.89e-42

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: 142.30  E-value: 5.89e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAV--NPFFgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:cd05333   81 LVNNAGItrDNLL---MRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVI 157

                        170
                 ....*....|....*....
gi 126723191 191 GLNNTLAIELAPRNIRVNC 209
Cdd:cd05333  158 GFTKSLAKELASRGITVNA 176
PRK07326 PRK07326
SDR family oxidoreductase;
30-210 1.40e-40

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 138.99  E-value: 1.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAFGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK07326  83 LDVLIANAGVG-HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160

                        170       180
                 ....*....|....*....|.
gi 126723191 190 LGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTI 181
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 19-208 5.35e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 137.87  E-value: 5.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  19 MASSRMTRRD-PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnVDQAVATLQGEGLSvtGTVCHVGKAEDRE 97
Cdd:PRK06841   1 MTDTKQFDLAfDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSED-VAEVAAQLLGGNAK--GLVCDVSDSQSVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  98 RLVAMAVKLHGGIDILVSNAAVNPFFGSLmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSP 177
Cdd:PRK06841  78 AAVAAVISAFGRIDILVNSAGVALLAPAE-DVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALE 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 126723191 178 GFSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06841 157 RHVAYCASKAGVVGMTKVLALEWGPYGITVN 187
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 33-211 6.99e-40

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: 137.36  E-value: 6.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLqgeGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELL---NDNLEVLELDVTDEESIKAAVKEVIERFGRIDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:cd05374   78 LVNNAGYG-LFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEAL 156

                        170
                 ....*....|....*....
gi 126723191 193 NNTLAIELAPRNIRVNCLH 211
Cdd:cd05374  157 SESLRLELAPFGIKVTIIE 175
PRK07063 PRK07063
SDR family oxidoreductase;
30-210 1.31e-39

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 137.10  E-value: 1.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQ--GEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIArdVAGARVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFFGSLmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK07063  85 GPLDVLVNNAGINVFADPL-AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163

                        170       180
                 ....*....|....*....|...
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07063 164 GLLGLTRALGIEYAARNVRVNAI 186
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 30-210 4.66e-39

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 135.44  E-value: 4.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPS-PGFSPYNVSKTA 188
Cdd:PRK07478  84 LDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGfPGMAAYAASKAG 163

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07478 164 LIGLTQVLAAEYGAQGIRVNAL 185
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 30-210 4.28e-38

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: 132.87  E-value: 4.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV---NPFfgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:cd05347   83 IDILVNNAGIirrHPA----EEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASK 158

                        170       180
                 ....*....|....*....|....
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05347  159 GGVAGLTKALATEWARHGIQVNAI 182
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 30-208 2.52e-37

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 131.23  E-value: 2.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK07890  83 VDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAKGAL 161

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:PRK07890 162 LAASQSLATELGPQGIRVN 180
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 30-210 4.07e-37

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 130.45  E-value: 4.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpfFGS-LMDVTEEVWDKTLDINVKAPALMTKAVVPE-MEKRGGGSVVIVSSIAAFSPS-PGFSP---YN 183
Cdd:PRK08213  90 VDILVNNAGAT--WGApAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLGGNpPEVMDtiaYN 167

                        170       180
                 ....*....|....*....|....*..
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK08213 168 TSKGAVINFTRALAAEWGPHGIRVNAI 194
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 30-208 9.22e-37

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 129.32  E-value: 9.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK12939  85 LDGLVNNAGITN-SKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAV 163

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:PRK12939 164 IGMTRSLARELGGRGITVN 182
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 30-210 1.44e-36

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: 128.76  E-value: 1.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTgtvCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALR---VDVTDEQQVAALFERAVEEFGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:cd08944   78 LDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAI 157

                        170       180
                 ....*....|....*....|.
gi 126723191 190 LGLNNTLAIELAPRNIRVNCL 210
Cdd:cd08944  158 RNLTRTLAAELRHAGIRCNAL 178
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 30-207 5.62e-36

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


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 127.70  E-value: 5.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQavatLQGEGLSVTGTVCHV-----GKAEDRERLVAMAV 104
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEE----VKSECLELGAPSPHVvpldmSDLEDAEQVVEEAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 105 KLHGGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:cd05332   77 KLFGGLDILINNAGIS-MRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAA 155

                        170       180
                 ....*....|....*....|...
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRV 207
Cdd:cd05332  156 SKHALQGFFDSLRAELSEPNISV 178
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 35-210 5.77e-36

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: 127.08  E-value: 5.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSRKqqNVDQAVATLQG-EGLSVTGTVCH--VGKAEDRERLVAMAVKLHGGID 111
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRK--SKDAAAEVAAEiEELGGKAVVVRadVSQPQDVEEMFAAVKERFGRLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLG 191
Cdd:cd05359   79 VLVSNAAAGAF-RPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEA 157

                        170
                 ....*....|....*....
gi 126723191 192 LNNTLAIELAPRNIRVNCL 210
Cdd:cd05359  158 LVRYLAVELGPRGIRVNAV 176
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 33-210 5.98e-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: 126.98  E-value: 5.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGE----GLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEanasGQKVSYISADLSDYEEVEQAFAQAVEKGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:cd08939   82 PPDLVVNCAGIS-IPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFA 160

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd08939  161 LRGLAESLRQELKPYNIRVSVV 182
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-210 8.13e-36

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 126.73  E-value: 8.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK07666  85 IDILINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGV 163

                        170       180
                 ....*....|....*....|.
gi 126723191 190 LGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07666 164 LGLTESLMQEVRKHNIRVTAL 184
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
29-209 1.32e-35

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 126.37  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVS-SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAA--VNPffgSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK08063  81 GRLDVFVNNAAsgVLR---PAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVS 157

                        170       180
                 ....*....|....*....|....
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVNC 209
Cdd:PRK08063 158 KAALEALTRYLAVELAPKGIAVNA 181
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 33-211 1.34e-35

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 125.81  E-value: 1.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLA-QDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAkSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAafspSPGFSPYNVSKTALLG 191
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGL----GSLTSAYGVSKAALNA 156

                        170       180
                 ....*....|....*....|
gi 126723191 192 LNNTLAIELAPRNIRVNCLH 211
Cdd:cd05324  157 LTRILAKELKETGIKVNACC 176
PRK06172 PRK06172
SDR family oxidoreductase;
30-208 2.67e-35

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 125.63  E-value: 2.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK06172  85 LDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAV 164

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:PRK06172 165 IGLTKSAAIEYAKKGIRVN 183
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 30-210 2.81e-35

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: 125.39  E-value: 2.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGL-SVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGgRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPE-MEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:cd05369   81 KIDILINNAAGN-FLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGSILNISATYAYTGSPFQVHSAAAKA 159

                        170       180
                 ....*....|....*....|...
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05369  160 GVDALTRSLAVEWGPYGIRVNAI 182
PRK07774 PRK07774
SDR family oxidoreductase;
30-208 4.17e-35

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 125.24  E-value: 4.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVnpfFG-----SLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSpgfSPYNV 184
Cdd:PRK07774  84 IDYLVNNAAI---YGgmkldLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYS---NFYGL 157

                        170       180
                 ....*....|....*....|....
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK07774 158 AKVGLNGLTQQLARELGGMNIRVN 181
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 30-211 7.19e-35

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 124.14  E-value: 7.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTvcHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNRQFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK12828  83 LDALVNIAGAFVW-GTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161

                        170       180
                 ....*....|....*....|..
gi 126723191 190 LGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVL 183
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 30-209 9.94e-35

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 123.92  E-value: 9.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVS-SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:cd05362   81 GVDILVNNAGVMLK-KPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAA 157

                        170       180
                 ....*....|....*....|.
gi 126723191 189 LLGLNNTLAIELAPRNIRVNC 209
Cdd:cd05362  158 VEAFTRVLAKELGGRGITVNA 178
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 33-210 1.34e-34

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: 123.00  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGeglSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELE---GVLGLAGDVRDEADVRRAVDAMEEAFGGLDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:cd08929   78 LVNNAGVG-VMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGL 156

                        170
                 ....*....|....*...
gi 126723191 193 NNTLAIELAPRNIRVNCL 210
Cdd:cd08929  157 SEAAMLDLREANIRVVNV 174
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 32-227 1.68e-34

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: 123.71  E-value: 1.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAV--ATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVraGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:cd08940   82 VDILVNNAGIQ-HVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGV 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 126723191 190 LGLNNTLAIELAPRNIRVNCLhldlsrlasagCSGWTR 227
Cdd:cd08940  161 VGLTKVVALETAGTGVTCNAI-----------CPGWVL 187
PRK06138 PRK06138
SDR family oxidoreductase;
30-210 4.09e-34

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 122.57  E-value: 4.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQaVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAER-VAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK06138  82 LDVLVNNAGFG-CGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160

                        170       180
                 ....*....|....*....|.
gi 126723191 190 LGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAV 181
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 30-208 6.09e-34

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: 122.17  E-value: 6.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLV-AMAVKLHG 108
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMdTVASHFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:cd05329   84 KLNILVNNAGTN-IRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162

                        170       180
                 ....*....|....*....|
gi 126723191 189 LLGLNNTLAIELAPRNIRVN 208
Cdd:cd05329  163 LNQLTRSLACEWAKDNIRVN 182
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 30-210 1.19e-33

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: 121.41  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSrKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIAD-IDDDAGQAVAAELGDP-DISFVHCDVTVEADVRAAVDTAVARFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV-NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:cd05326   80 LDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHA 159

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05326  160 VLGLTRSAATELGEHGIRVNCV 181
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 30-208 1.77e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 121.32  E-value: 1.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV---NPffgsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK07097  88 IDILVNNAGIikrIP----MLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAK 163

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK07097 164 GGLKMLTKNIASEYGEANIQCN 185
PRK06181 PRK06181
SDR family oxidoreductase;
32-207 2.36e-33

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 120.85  E-value: 2.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVNPF--FGSLMDVteEVWDKTLDINVKAPALMTKAVVPEMEKRgGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK06181  81 ILVNNAGITMWsrFDELTDL--SVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHAL 157

                        170
                 ....*....|....*...
gi 126723191 190 LGLNNTLAIELAPRNIRV 207
Cdd:PRK06181 158 HGFFDSLRIELADDGVAV 175
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 30-210 3.34e-33

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: 120.18  E-value: 3.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnvDQAVATLQ------GEGLSVTGTVchvGKAEDRERLVAMA 103
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKE--DAAEEVVEeikavgGKAIAVQADV---SKEEDVVALFQSA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSlMDVTEEVWDKTLDINVKAPALMTKAVVPEMEK-RGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:cd05358   76 IKEFGTLDILVNNAGLQGDASS-HEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIPWPGHVNY 154

                        170       180
                 ....*....|....*....|....*...
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05358  155 AASKGGVKMMTKTLAQEYAPKGIRVNAI 182
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 30-211 2.38e-32

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: 117.87  E-value: 2.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlsvtgTVCH--VGKAEDRERLVAMAVKLH 107
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAA-----RFFHldVTDEDGWTAVVDTAREAF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:cd05341   78 GRLDVLVNNAGIL-TGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKG 156

                        170       180
                 ....*....|....*....|....*.
gi 126723191 188 ALLGLNNTLAIELAPR--NIRVNCLH 211
Cdd:cd05341  157 AVRGLTKSAALECATQgyGIRVNSVH 182
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
30-216 2.50e-32

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 118.36  E-value: 2.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAA-FSPSPGFSPYNVSKTA 188
Cdd:PRK08226  83 IDILVNNAGVCRL-GSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKAA 161

                        170       180
                 ....*....|....*....|....*...
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCLHLDLSR 216
Cdd:PRK08226 162 IVGLTKSLAVEYAQSGIRVNAICPGYVR 189
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 29-208 3.11e-32

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 117.54  E-value: 3.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVS-SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK12937   2 TLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK12937  82 GRIDVLVNNAGVMP-LGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKA 158

                        170       180
                 ....*....|....*....|.
gi 126723191 188 ALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVN 179
PRK06500 PRK06500
SDR family oxidoreductase;
24-210 3.77e-32

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 117.36  E-value: 3.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRrdpLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTgtvCHVGKAEDrERLVAMA 103
Cdd:PRK06500   1 MSR---LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIR---ADAGDVAA-QKALAQA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGG-IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK06500  74 LAEAFGrLDAVFINAGVAKF-APLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLAN--PASIVLNGSINAHIGMPNSSVY 150

                        170       180
                 ....*....|....*....|....*...
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK06500 151 AASKAALLSLAKTLSGELLPRGIRVNAV 178
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 32-208 4.22e-32

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: 117.64  E-value: 4.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:cd08945    3 SEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAvNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPE--MEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:cd08945   83 VLVNNAG-RSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGV 161

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:cd08945  162 VGFTKALGLELARTGITVN 180
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 33-213 4.60e-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: 117.11  E-value: 4.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGeGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQG-GPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKTALLG 191
Cdd:cd08943   81 VVSNAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNAAAYSAAKAAEAH 159

                        170       180
                 ....*....|....*....|..
gi 126723191 192 LNNTLAIELAPRNIRVNCLHLD 213
Cdd:cd08943  160 LARCLALEGGEDGIRVNTVNPD 181
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 29-208 6.73e-32

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 117.03  E-value: 6.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNvDQAVATLQGEGlsvtGTVCHVGKAEDR--ERLVAMAVKL 106
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADN-GAAVAASLGER----ARFIATDITDDAaiERAVATVVAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAA--VNPFFGSlmdvTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:PRK08265  78 FGRVDILVNLACtyLDDGLAS----SRADWLAALDVNLVSAAMLAQAAHPHL-ARGGGAIVNFTSISAKFAQTGRWLYPA 152

                        170       180
                 ....*....|....*....|....
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08265 153 SKAAIRQLTRSMAMDLAPDGIRVN 176
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 30-210 2.42e-31

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: 115.18  E-value: 2.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVD------------QAVATLQGEGLSVTGTVCHVGKAEDRE 97
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpgtieETAEEIEAAGGQALPIVVDVRDEDQVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  98 RLVAMAVKLHGGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSP 177
Cdd:cd05338   81 ALVEATVDQFGRLDILVNNAGAI-WLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 126723191 178 GFSPYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05338  160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSL 192
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 30-208 7.10e-31

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: 114.70  E-value: 7.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVS--SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:cd05355  104 GKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAYKGSPHLLDYAATKG 181

                        170       180
                 ....*....|....*....|.
gi 126723191 188 ALLGLNNTLAIELAPRNIRVN 208
Cdd:cd05355  182 AIVAFTRGLSLQLAEKGIRVN 202
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 30-208 1.47e-30

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: 113.27  E-value: 1.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLS---VTGTVCHVGKAEDRERLVAMAVKL 106
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSekkILLVVADLTEEEGQDRIISTTLAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGgSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:cd05364   81 FGRLDILVNNAGI-LAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKG-EIVNVSSVAGGRSFPGVLYYCISK 158

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:cd05364  159 AALDQFTRCTALELAPKGVRVN 180
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-207 1.53e-30

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 113.52  E-value: 1.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSS-RKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVNPFF-GSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGG------GSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:PRK12745  83 CLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNRGEYCI 162

                        170       180
                 ....*....|....*....|...
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK12745 163 SKAGLSMAAQLFAARLAEEGIGV 185
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 34-211 1.59e-30

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: 113.11  E-value: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDIL 113
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 114 VSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLN 193
Cdd:cd05339   81 INNAGV-VSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159

                        170       180
                 ....*....|....*....|.
gi 126723191 194 NTLAIELAP---RNIRVNCLH 211
Cdd:cd05339  160 ESLRLELKAygkPGIKTTLVC 180
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
30-208 1.90e-30

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 113.29  E-value: 1.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQqNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGT-NWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV---NPffgsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK06935  92 IDILVNNAGTirrAP----LLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASK 167

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06935 168 HGVAGLTKAFANELAAYNIQVN 189
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 31-210 2.09e-30

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: 112.56  E-value: 2.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSsrkqqNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAvklhGGI 110
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIAT-----DINEEKLKELERGPGITTRVLDVTDKEQVAALAKEE----GRI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAA-FSPSPGFSPYNVSKTAL 189
Cdd:cd05368   72 DVLFNCAGFVHH-GSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAV 150

                        170       180
                 ....*....|....*....|.
gi 126723191 190 LGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05368  151 IGLTKSVAADFAQQGIRCNAI 171
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 30-212 3.26e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 112.41  E-value: 3.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRA-HVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVsNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGG-GSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK06198  84 RLDALV-NAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKG 162

                        170       180
                 ....*....|....*....|....*
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCLHL 212
Cdd:PRK06198 163 ALATLTRNAAYALLRNRIRVNGLNI 187
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 33-226 3.29e-30

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: 111.69  E-value: 3.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVAtlqgEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSA----SGGDVEAVPYDARDPEDARALVDALRDRFGRIDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:cd08932   77 LVHNAGIGRP-TTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRAL 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 126723191 193 NNTLAIELAPRNIRVnclhldlsrlaSAGCSGWT 226
Cdd:cd08932  156 AHALRQEGWDHGVRV-----------SAVCPGFV 178
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 34-208 4.76e-30

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: 111.89  E-value: 4.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDIL 113
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 114 VSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLN 193
Cdd:cd05365   81 VNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160

                        170
                 ....*....|....*
gi 126723191 194 NTLAIELAPRNIRVN 208
Cdd:cd05365  161 RNLAFDLGPKGIRVN 175
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 30-208 7.79e-30

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 111.59  E-value: 7.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRkqqNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLER---SAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLD----INVKAPALMTKAVVPEMEKRGGgSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK06200  81 LDCFVGNAGIWDYNTSLVDIPAETLDTAFDeifnVNVKGYLLGAKAALPALKASGG-SMIFTLSNSSFYPGGGGPLYTAS 159

                        170       180
                 ....*....|....*....|...
gi 126723191 186 KTALLGLNNTLAIELAPRnIRVN 208
Cdd:PRK06200 160 KHAVVGLVRQLAYELAPK-IRVN 181
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 32-208 7.96e-30

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: 111.70  E-value: 7.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnvDQAVATLQGegLSVTGTVCH-----VGKAEDRERLVAMAVKL 106
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLE--EAAKSTIQE--ISEAGYNAVavgadVTDKDDVEALIDQAVEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVI-VSSIAAFSPSPGFSPYNVS 185
Cdd:cd05366   78 FGSFDVMVNNAGIAPI-TPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIInASSIAGVQGFPNLGAYSAS 156

                        170       180
                 ....*....|....*....|...
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVN 208
Cdd:cd05366  157 KFAVRGLTQTAAQELAPKGITVN 179
PRK07856 PRK07856
SDR family oxidoreductase;
30-210 1.04e-29

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 111.18  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQ-QNVDQAVATLQGeglsvtgtvCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRApETVDGRPAEFHA---------ADVRDPDQVAALVDAIVERHG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKR-GGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK07856  75 RLDVLVNNAGGSPY-ALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPGTAAYGAAKA 153

                        170       180
                 ....*....|....*....|...
gi 126723191 188 ALLGLNNTLAIELAPRnIRVNCL 210
Cdd:PRK07856 154 GLLNLTRSLAVEWAPK-VRVNAV 175
PRK06124 PRK06124
SDR family oxidoreductase;
24-208 3.28e-29

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 109.80  E-value: 3.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:PRK06124   3 ILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAV---NPffgsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFS 180
Cdd:PRK06124  83 DAEHGRLDILVNNVGArdrRP----LAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDA 158

                        170       180
                 ....*....|....*....|....*...
gi 126723191 181 PYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06124 159 VYPAAKQGLTGLMRALAAEFGPHGITSN 186
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 24-208 3.35e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 109.99  E-value: 3.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEdRERLvama 103
Cdd:PRK06523   1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVEFVAADLTTAEGCAAVARAV-LERL---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 vklhGGIDILVSNA-AVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPG-FSP 181
Cdd:PRK06523  76 ----GGVDILVHVLgGSSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPEsTTA 151

                        170       180
                 ....*....|....*....|....*..
gi 126723191 182 YNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06523 152 YAAAKAALSTYSKSLSKEVAPKGVRVN 178
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 30-208 3.94e-29

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 109.99  E-value: 3.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAA---VNPFfgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEK-RGGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK13394  85 VDILVSNAGiqiVNPI----ENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTA 160

                        170       180
                 ....*....|....*....|...
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKHNVRSH 183
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-208 4.61e-29

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 109.43  E-value: 4.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQ-QNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRaEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK06077  84 VADILVNNAGLG-LFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAA 160

                        170       180
                 ....*....|....*....|
gi 126723191 189 LLGLNNTLAIELAPRnIRVN 208
Cdd:PRK06077 161 VINLTKYLALELAPK-IRVN 179
PRK09242 PRK09242
SDR family oxidoreductase;
30-208 5.44e-29

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 109.45  E-value: 5.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATL--QGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeEFPEREVHGLAADVSDDEDRRAILDWVEDHW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK09242  87 DGLHILVNNAGGN-IRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKA 165

                        170       180
                 ....*....|....*....|.
gi 126723191 188 ALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK09242 166 ALLQMTRNLAVEWAEDGIRVN 186
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 34-207 8.25e-29

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: 108.70  E-value: 8.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQDRAHV-VVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIaINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPF-FGSLMDVTEEVWDKTLDINVKAPALMTKAVV------PEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:cd05337   83 LVNNAGIAVRpRGDLLDLTEDSFDRLIAINLRGPFFLTQAVArrmveqPDRFDGPHRSIIFVTSINAYLVSPNRGEYCIS 162

                        170       180
                 ....*....|....*....|..
gi 126723191 186 KTALLGLNNTLAIELAPRNIRV 207
Cdd:cd05337  163 KAGLSMATRLLAYRLADEGIAV 184
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
31-208 9.97e-29

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 108.66  E-value: 9.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK08643  81 NVVVNNAGVAP-TTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINATSQAGVVGNPELAVYSSTKFAV 159

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:PRK08643 160 RGLTQTAARDLASEGITVN 178
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 30-210 1.04e-28

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: 108.57  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGE-GLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFFGSLmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAF---SPSPGfSPYNVS 185
Cdd:cd05352   86 KIDILIANAGITVHKPAL-DYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTivnRPQPQ-AAYNAS 163

                        170       180
                 ....*....|....*....|....*
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05352  164 KAAVIHLAKSLAVEWAKYFIRVNSI 188
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 24-212 1.17e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 109.29  E-value: 1.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLqGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAEL-GGDDRVLTVVADVTDLAAMQAAAEEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGgSVVIVSSIAAFSPSPGFSPYN 183
Cdd:PRK05872  80 VERFGGIDVVVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRG-YVLQVSSLAAFAAAPGMAAYC 157

                        170       180
                 ....*....|....*....|....*....
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCLHL 212
Cdd:PRK05872 158 ASKAGVEAFANALRLEVAHHGVTVGSAYL 186
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 30-207 1.23e-28

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 108.56  E-value: 1.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVvssrkqqNVDQAVATLQGEGLsvTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVV-------NADIHGGDGQHENY--QFVPTDVSSAEEVNHTVAEIIEKFGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVN-PFFgsLMD---------VTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGF 179
Cdd:PRK06171  78 IDGLVNNAGINiPRL--LVDekdpagkyeLNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQ 155

                        170       180
                 ....*....|....*....|....*...
gi 126723191 180 SPYNVSKTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK06171 156 SCYAATKAALNSFTRSWAKELGKHNIRV 183
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 30-208 1.85e-28

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: 107.56  E-value: 1.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVAtlqgEGLSVTGTVCHVGKAEDRERlvamAVKLHGG 109
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVR----ECPGIEPVCVDLSDWDATEE----ALGSVGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV---NPFfgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:cd05351   77 VDLLVNNAAVailQPF----LEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCST 152

                        170       180
                 ....*....|....*....|...
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVN 208
Cdd:cd05351  153 KAALDMLTKVMALELGPHKIRVN 175
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 30-208 1.98e-28

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 108.01  E-value: 1.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNA---AVNPFfgslmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK06113  89 VDILVNNAgggGPKPF-----DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSK 163

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06113 164 AAASHLVRNMAFDLGEKNIRVN 185
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 30-221 2.40e-28

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: 107.44  E-value: 2.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVdQAVATLQGEglSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKV-AELRADFGD--AVVGVEGDVRSLADNERAVARCVERFGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLD----INVKAPALMTKAVVPEMEKrGGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:cd05348   79 LDCFIGNAGIWDYSTSLVDIPEEKLDEAFDelfhINVKGYILGAKAALPALYA-TEGSVIFTVSNAGFYPGGGGPLYTAS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 126723191 186 KTALLGLNNTLAIELAPRnIRVNC-----LHLDLSRLASAG 221
Cdd:cd05348  158 KHAVVGLVKQLAYELAPH-IRVNGvapggMVTDLRGPASLG 197
PRK05650 PRK05650
SDR family oxidoreductase;
36-210 3.78e-28

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 107.43  E-value: 3.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  36 LVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQ---GEGLSVTgtvCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLReagGDGFYQR---CDVRDYSQLTALAQACEEKWGGIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:PRK05650  81 IVNNAGVASG-GFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVAL 159

                        170
                 ....*....|....*...
gi 126723191 193 NNTLAIELAPRNIRVNCL 210
Cdd:PRK05650 160 SETLLVELADDEIGVHVV 177
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
30-208 4.30e-28

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 107.04  E-value: 4.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRkqqNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADI---KPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVnpF-FGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK07067  81 IDILFNNAAL--FdMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGrGGKIINMASQAGRRGEALVSHYCATKA 158

                        170       180
                 ....*....|....*....|.
gi 126723191 188 ALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK07067 159 AVISYTQSAALALIRHGINVN 179
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 30-207 5.09e-28

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: 105.85  E-value: 5.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVAtlqgEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKK----ELPNIHTIVLDVGDAESVEALAEALLSEYPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVN-PFfgSLMDVTE--EVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:cd05370   79 LDILINNAGIQrPI--DLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATK 156

                        170       180
                 ....*....|....*....|.
gi 126723191 187 TALLGLNNTLAIELAPRNIRV 207
Cdd:cd05370  157 AALHSYTLALRHQLKDTGVEV 177
PRK06398 PRK06398
aldose dehydrogenase; Validated
 30-208 5.17e-28

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 106.84  E-value: 5.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNvDQAVATLQgeglsvtgtvCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS-YNDVDYFK----------VDVSNKEQVIKGIDYVISKYGR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK06398  73 IDILVNNAGIESY-GAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRnIRVN 208
Cdd:PRK06398 152 LGLTRSIAVDYAPT-IRCV 169
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 33-211 6.06e-28

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 106.23  E-value: 6.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRkQQNVdQAVATLQG--EGLSVTGTVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDR-NENP-GAAAELQAinPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVN-PFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKR---GGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:cd05323   79 DILINNAGILdEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                        170       180
                 ....*....|....*....|....*.
gi 126723191 187 TALLGLNNTLAIELAPR-NIRVNCLH 211
Cdd:cd05323  159 HGVVGFTRSLADLLEYKtGVRVNAIC 184
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 31-210 1.07e-27

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: 105.88  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLS-VTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNrVIALELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPF--FGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSpSPGF-------- 179
Cdd:cd08930   81 IDILINNAYPSPKvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVI-APDFriyentqm 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 126723191 180 -SP--YNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd08930  160 ySPveYSVIKAGIIHLTKYLAKYYADTGIRVNAI 193
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 33-209 1.39e-27

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: 105.23  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGE-GLSVTGTVchvGKAEDRERLVAMAVKLHGGID 111
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAGErAIAIQADV---RDRDQVQAMIEEAKNHFGPVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVN-PFFG----SLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:cd05349   78 TIVNNALIDfPFDPdqrkTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAK 157

                        170       180
                 ....*....|....*....|...
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNC 209
Cdd:cd05349  158 AALLGFTRNMAKELGPYGITVNM 180
PRK07454 PRK07454
SDR family oxidoreductase;
33-207 2.57e-27

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 104.66  E-value: 2.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:PRK07454  87 LINNAGM-AYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165

                        170
                 ....*....|....*
gi 126723191 193 NNTLAIELAPRNIRV 207
Cdd:PRK07454 166 TKCLAEEERSHGIRV 180
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 30-208 5.13e-27

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 103.81  E-value: 5.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVvssrkqqNVDQAvaTLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVI-------GFDQA--FLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVsNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK08220  77 LDVLV-NAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAAL 155

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCN 174
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 29-211 5.48e-27

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 104.03  E-value: 5.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVV----SSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAV 104
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 105 KLHGGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEK-RGGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:PRK12827  83 EEFGRLDILVNNAGIATD-AAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYA 161

                        170       180
                 ....*....|....*....|....*...
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK12827 162 ASKAGLIGLTKTLANELAPRGITVNAVA 189
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 30-202 5.63e-27

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: 103.70  E-value: 5.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGeglsVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:COG3967    3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPG----LHTIVLDVADPASIAALAEQVTAEFPD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVnpffGSLMDVTEEVWD-----KTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:COG3967   79 LNVLINNAGI----MRAEDLLDEAEDladaeREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSA 154

                        170       180
                 ....*....|....*....|....*...
gi 126723191 185 SKTAL----LGLNNTLA------IELAP 202
Cdd:COG3967  155 TKAALhsytQSLRHQLKdtsvkvIELAP 182
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 33-208 8.72e-27

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: 103.13  E-value: 8.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRK-QQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVnpFF-GSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:cd05357   81 VLVNNASA--FYpTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALE 158

                        170
                 ....*....|....*...
gi 126723191 191 GLNNTLAIELAPrNIRVN 208
Cdd:cd05357  159 GLTRSAALELAP-NIRVN 175
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 35-208 1.02e-26

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: 102.93  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVvssrkqqNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDILV 114
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVI-------ALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 115 sNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLNN 194
Cdd:cd05331   74 -NCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152

                        170
                 ....*....|....
gi 126723191 195 TLAIELAPRNIRVN 208
Cdd:cd05331  153 CLGLELAPYGVRCN 166
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 30-207 1.36e-26

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: 102.62  E-value: 1.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:cd08934   81 LDILVNNAGIM-LLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGV 159

                        170
                 ....*....|....*...
gi 126723191 190 LGLNNTLAIELAPRNIRV 207
Cdd:cd08934  160 NAFSEGLRQEVTERGVRV 177
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 32-210 1.38e-26

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: 102.68  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCH--VGKAEDRERLVAMAVKLHgg 109
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAAdfSAGDDIYERIEKELEGLD-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFF-GSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:cd05356   79 IGILVNNVGISHSIpEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAF 158

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05356  159 LDFFSRALYEEYKSQGIDVQSL 180
PRK07831 PRK07831
SDR family oxidoreductase;
30-208 1.42e-26

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 103.19  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTD-GIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGE-GLS-VTGTVCHVGKAEDRERLVAMAVKL 106
Cdd:PRK07831  15 LAGKVVLVTAAAGtGIGSATARRALEEGARVVISDIHERRLGETADELAAElGLGrVEAVVCDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVI-VSSIAAFSPSPGFSPYNVS 185
Cdd:PRK07831  95 LGRLDVLVNNAGLGGQ-TPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVnNASVLGWRAQHGQAHYAAA 173

                        170       180
                 ....*....|....*....|...
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK07831 174 KAGVMALTRCSALEAAEYGVRIN 196
PRK09135 PRK09135
pteridine reductase; Provisional
 28-208 1.99e-26

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 102.31  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  28 DPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRK-QQNVDQAVATL-QGEGLSVTGTVCHVGKAEDRERLVAMAVK 105
Cdd:PRK09135   2 MTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELnALRPGSAAALQADLLDPDALPELVAACVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNAAVnpFFGS-LMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGgSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:PRK09135  82 AFGRLDALVNNASS--FYPTpLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRG-AIVNITDIHAERPLKGYPVYCA 158

                        170       180
                 ....*....|....*....|....
gi 126723191 185 SKTALLGLNNTLAIELAPrNIRVN 208
Cdd:PRK09135 159 AKAALEMLTRSLALELAP-EVRVN 181
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 30-208 2.11e-26

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 102.50  E-value: 2.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRK-QQNVDQAVATLQ---GEGLSVTGtvcHVGKAEDRERLVAMAVK 105
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKkagGEAIAVKG---DVTVESDVVNLIQTAVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNAAV-NPFfgSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:PRK08936  82 EFGTLDVMINNAGIeNAV--PSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSSVHEQIPWPLFVHYA 159

                        170       180
                 ....*....|....*....|....*
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08936 160 ASKGGVKLMTETLAMEYAPKGIRVN 184
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 28-210 2.20e-26

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 103.11  E-value: 2.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  28 DPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK05876   2 DGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPE-MEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK05876  82 GHVDVVFSNAGI-VVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRlLEQGTGGHVVFTASFAGLVPNAGLGAYGVAK 160

                        170       180
                 ....*....|....*....|....
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK05876 161 YGVVGLAETLAREVTADGIGVSVL 184
PRK07074 PRK07074
SDR family oxidoreductase;
31-208 2.78e-26

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 102.16  E-value: 2.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlsVTGTVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDAR--FVPVACDLTDAASLAAALANAAAERGPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNA----AVnpffgSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSI---AAFspspGFSPYN 183
Cdd:PRK07074  79 DVLVANAgaarAA-----SLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVngmAAL----GHPAYS 149

                        170       180
                 ....*....|....*....|....*
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK07074 150 AAKAGLIHYTKLLAVEYGRFGIRAN 174
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 24-210 8.62e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 100.96  E-value: 8.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRdpLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSsrkqqNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:PRK06057   1 LSQR--LAGRVAVITGGGSGIGLATARRLAAEGATVVVG-----DIDPEAGKAAADEVGGLFVPTDVTDEDAVNALFDTA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNP-FFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAF--SPSPGFS 180
Cdd:PRK06057  74 AETYGSVDIAFNNAGISPpEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVmgSATSQIS 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 126723191 181 pYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK06057 154 -YTASKGGVLAMSRELGVQFARQGIRVNAL 182
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 31-207 8.92e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 101.15  E-value: 8.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARrLAQDRAH-VVVSSRKQQNVDQAVATLQGEGLSVtgtVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQ-AALAAGHrVVGTVRSEAARADFEALHPDRALAR---LLDVTDFDAIDAVVADAEATFGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK06180  79 IDVLVNNAGYG-HEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFAL 157

                        170
                 ....*....|....*...
gi 126723191 190 LGLNNTLAIELAPRNIRV 207
Cdd:PRK06180 158 EGISESLAKEVAPFGIHV 175
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 24-211 9.72e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 100.56  E-value: 9.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTvchvgkaedRERLVAMA 103
Cdd:PRK07060   1 MNMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRLDVG---------DDAAIRAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEM-EKRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK07060  72 LAAAGAFDGLVNCAGIA-SLESALDMTAEGFDRVMAVNARGAALVARHVARAMiAAGRGGSIVNVSSQAALVGLPDHLAY 150

                        170       180
                 ....*....|....*....|....*....
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK07060 151 CASKAALDAITRVLCVELGPHGIRVNSVN 179
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 30-208 1.37e-25

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 100.70  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEG-LSVTGTVCHVGKAEDRERLVAmAVKLHG 108
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESnVDVSYIVADLTKREDLERTVK-ELKNIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAvNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK08339  85 EPDIFFFSTG-GPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRIS 163

                        170       180
                 ....*....|....*....|
gi 126723191 189 LLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08339 164 MAGLVRTLAKELGPKGITVN 183
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
32-210 1.55e-25

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 99.84  E-value: 1.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKqqNVDQAVATLQGEGLS---VTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDGYRVIATYFS--GNDCAKDWFEEYGFTedqVRLKELDVTDTEECAEALAEIEEEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK12824  80 PVDILVNNAGITRD-SVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAG 158

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK12824 159 MIGFTKALASEGARYGITVNCI 180
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 30-210 1.73e-25

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 100.08  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVS-SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINyNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK12935  84 KVDILVNNAGITRD-RTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK12935 163 MLGFTKSLALELAKTNVTVNAI 184
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 28-209 2.24e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 100.02  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  28 DPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSsrkqqNVDQAVATLQGEGLS-VTGTVCHVGKAEDRERLVAMAVKL 106
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGARVAIG-----DLDEALAKETAAELGlVVGGPLDVTDPASFAAFLDAVEAD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK07825  76 LGPIDVLVNNAGVMPV-GPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASK 154

                        170       180
                 ....*....|....*....|...
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNC 209
Cdd:PRK07825 155 HAVVGFTDAARLELRGTGVHVSV 177
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 30-208 2.42e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 99.83  E-value: 2.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV---NPFfgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK08085  87 IDVLINNAGIqrrHPF----TEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASK 162

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08085 163 GAVKMLTRGMCVELARHNIQVN 184
PRK07069 PRK07069
short chain dehydrogenase; Validated
 35-209 2.99e-25

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 99.40  E-value: 2.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVA----TLQGEGLSVTGTVcHVGKAEDRERLVAMAVKLHGGI 110
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAaeinAAHGEGVAFAAVQ-DVTDEAQWQALLAQAADAMGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:PRK07069  81 SVLVNNAGVGSF-GAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVA 159

                        170
                 ....*....|....*....
gi 126723191 191 GLNNTLAIELAPRNIRVNC 209
Cdd:PRK07069 160 SLTKSIALDCARRGLDVRC 178
PRK07201 PRK07201
SDR family oxidoreductase;
23-216 3.12e-25

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 103.11  E-value: 3.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  23 RMTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAM 102
Cdd:PRK07201 362 RRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKD 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 103 AVKLHGGIDILVSNA------AVNPFFGSLMDvteevWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPS 176
Cdd:PRK07201 442 ILAEHGHVDYLVNNAgrsirrSVENSTDRFHD-----YERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNA 516

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 126723191 177 PGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCLHLDLSR 216
Cdd:PRK07201 517 PRFSAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVR 556
PRK08264 PRK08264
SDR family oxidoreductase;
32-212 3.85e-25

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 98.81  E-value: 3.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARR-LAQDRAHVVVSSRKQQNVDQA---VATLQgegLSVTgtvchvgKAEDrerlVAMAVKLH 107
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQlLARGAAKVYAAARDPESVTDLgprVVPLQ---LDVT-------DPAS----VAAAAEAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK08264  72 SDVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKA 151

                        170       180
                 ....*....|....*....|....*
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCLHL 212
Cdd:PRK08264 152 AAWSLTQALRAELAPQGTRVLGVHP 176
PRK07814 PRK07814
SDR family oxidoreductase;
30-208 7.06e-25

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 98.70  E-value: 7.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAvNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEM-EKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK07814  88 LDIVVNNVG-GTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMlEHSGGGSVINISSTMGRLAGRGFAAYGTAKAA 166

                        170       180
                 ....*....|....*....|
gi 126723191 189 LLGLNNTLAIELAPRnIRVN 208
Cdd:PRK07814 167 LAHYTRLAALDLCPR-IRVN 185
PRK08589 PRK08589
SDR family oxidoreductase;
30-210 8.36e-25

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 98.70  E-value: 8.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEA-VSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRgGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK08589  83 VDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTSSFSGQAADLYRSGYNAAKGAV 161

                        170       180
                 ....*....|....*....|.
gi 126723191 190 LGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK08589 162 INFTKSIAIEYGRDGIRANAI 182
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-210 1.14e-24

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 97.84  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTAST--DGIGFAIARRLAQDRAHVVVSSRKQQNVDQAV------ATLQGEGLSVTGTVCH-----VGKAED 95
Cdd:PRK12748   2 PLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWgmhdkePVLLKEEIESYGVRCEhmeidLSQPYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  96 RERLVAMAVKLHGGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSP 175
Cdd:PRK12748  82 PNRVFYAVSERLGDPSILINNAAYSTH-TRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGP 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126723191 176 SPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK12748 161 MPDELAYAATKGAIEAFTKSLAPELAEKGITVNAV 195
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 34-212 1.19e-24

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 97.45  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDIL 113
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 114 VSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLN 193
Cdd:cd05360   82 VNNAGVA-VFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFT 160

                        170       180
                 ....*....|....*....|.
gi 126723191 194 NTLAIELAP--RNIRVNCLHL 212
Cdd:cd05360  161 ESLRAELAHdgAPISVTLVQP 181
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 32-210 2.00e-24

(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: 97.01  E-value: 2.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVV------------SSRKQQNVDQAVATLQGEGLSVTGTVchvgkaEDRERL 99
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgsgkSSSAADKVVDEIKAAGGKAVANYDSV------EDGEKI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 100 VAMAVKLHGGIDILVSNAavnpffGSLMDV-----TEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFS 174
Cdd:cd05353   79 VKTAIDAFGRVDILVNNA------GILRDRsfakmSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLY 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 126723191 175 PSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05353  153 GNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTI 188
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-210 2.32e-24

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 96.57  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVV-VSSRKQQNVDQAVATLQgegLSVTGtvchvgkaeDRERLVAMAVKlhg 108
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQVYgVDKQDKPDLSGNFHFLQ---LDLSD---------DLEPLFDWVPS--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 gIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK06550  68 -VDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHA 146

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK06550 147 LAGFTKQLALDYAKDGIQVFGI 168
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-208 2.61e-24

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 99.91  E-value: 2.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSsrkqqNVDQAVATLQGEGLSVTGTVCH--VGKAEDRERLVAMAVKL 106
Cdd:PRK08261 207 PLAGKVALVTGAARGIGAAIAEVLARDGAHVVCL-----DVPAAGEALAAVANRVGGTALAldITAPDAPARIAEHLAER 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAavnpffG-----SLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSP 181
Cdd:PRK08261 282 HGGLDIVVHNA------GitrdkTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTN 355

                        170       180
                 ....*....|....*....|....*..
gi 126723191 182 YNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08261 356 YAASKAGVIGLVQALAPLLAERGITIN 382
PRK06484 PRK06484
short chain dehydrogenase; Validated
 33-208 5.19e-24

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 99.54  E-value: 5.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRkqqNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADR---NVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAV-NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEM-EKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:PRK06484  83 LVNNAGVtDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMiEQGHGAAIVNVASGAGLVALPKRTAYSASKAAVI 162

                        170
                 ....*....|....*...
gi 126723191 191 GLNNTLAIELAPRNIRVN 208
Cdd:PRK06484 163 SLTRSLACEWAAKGIRVN 180
PRK05855 PRK05855
SDR family oxidoreductase;
27-207 5.49e-24

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 99.67  E-value: 5.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  27 RDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKL 106
Cdd:PRK05855 310 RGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAE 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK05855 390 HGVPDIVVNNAGIG-MAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGtGGHIVNVASAAAYAPSRSLPAYATS 468

                        170       180
                 ....*....|....*....|..
gi 126723191 186 KTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK05855 469 KAAVLMLSECLRAELAAAGIGV 490
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 30-210 5.65e-24

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: 96.04  E-value: 5.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEG-LSVTGTVCHVgkaEDRERLVAM--AVK- 105
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGyPTLFPYQCDL---SNEEQILSMfsAIRt 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNAAV---NPffgsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG--GGSVVIVSSIAAFS--PSPG 178
Cdd:cd05343   81 QHQGVDVCINNAGLarpEP----LLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGHRvpPVSV 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 126723191 179 FSPYNVSKTALLGLNNTLAIEL--APRNIRVNCL 210
Cdd:cd05343  157 FHFYAATKHAVTALTEGLRQELreAKTHIRATSI 190
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 30-216 5.81e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 96.41  E-value: 5.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAV---ATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKL 106
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAeeiEALKGAG-AVRYEPADVTDEDQVARAVDAATAW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK05875  84 HGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTK 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNCLHLDLSR 216
Cdd:PRK05875 164 SAVDHLMKLAADELGPSWVRVNSIRPGLIR 193
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 28-209 6.03e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 96.64  E-value: 6.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  28 DPLTNKVALVTASTDGIGFAIARRLAQDRAHV-VVSSRKQQNVDQAVATLQGEG---LSVTGTVCHVGKAEDrerLVAMA 103
Cdd:PRK06701  42 GKLKGKVALITGGDSGIGRAVAVLFAKEGADIaIVYLDEHEDANETKQRVEKEGvkcLLIPGDVSDEAFCKD---AVEET 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:PRK06701 119 VRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQ--GSAIINTGSITGYEGNETLIDYS 196

                        170       180
                 ....*....|....*....|....*.
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNC 209
Cdd:PRK06701 197 ATKGAIHAFTRSLAQSLVQKGIRVNA 222
PRK09072 PRK09072
SDR family oxidoreductase;
30-207 7.51e-24

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 95.78  E-value: 7.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTgTVCHVGKAEDRERLVAmAVKLHGG 109
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRW-VVADLTSEAGREAVLA-RAREMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK09072  81 INVLINNAGVNH-FALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFAL 159

                        170
                 ....*....|....*...
gi 126723191 190 LGLNNTLAIELAPRNIRV 207
Cdd:PRK09072 160 RGFSEALRRELADTGVRV 177
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 35-211 1.11e-23

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: 94.70  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDILV 114
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 115 SNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLNN 194
Cdd:cd05350   81 INAGVG-KGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAE 159

                        170
                 ....*....|....*..
gi 126723191 195 TLAIELAPRNIRVNCLH 211
Cdd:cd05350  160 SLRYDVKKRGIRVTVIN 176
PRK07062 PRK07062
SDR family oxidoreductase;
29-208 1.30e-23

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 95.11  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGE--GLSVTGTVCHVGKAEDRERLVAMAVKL 106
Cdd:PRK07062   5 QLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKfpGARLLAARCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 107 HGGIDILVSNAA---VNPFfgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:PRK07062  85 FGGVDMLVNNAGqgrVSTF----ADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATS 160

                        170       180
                 ....*....|....*....|....*
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK07062 161 AARAGLLNLVKSLATELAPKGVRVN 185
PRK06128 PRK06128
SDR family oxidoreductase;
30-208 2.57e-23

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 95.31  E-value: 2.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVS--SRKQQNVDQAVATLQGEG---LSVTGTVchvgkAEDR--ERLVAM 102
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNylPEEEQDAAEVVQLIQAEGrkaVALPGDL-----KDEAfcRQLVER 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 103 AVKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK06128 128 AVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPP--GASIINTGSIQSYQPSPTLLDY 205

                        170       180
                 ....*....|....*....|....*.
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06128 206 ASTKAAIVAFTKALAKQVAEKGIRVN 231
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 30-232 3.02e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 94.06  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK07523  88 IDILVNNAGMQ-FRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAV 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 126723191 190 LGLNNTLAIELAPRNIRVNCLH-------LDLSRLASAGCSGWTRKKRKA 232
Cdd:PRK07523 167 GNLTKGMATDWAKHGLQCNAIApgyfdtpLNAALVADPEFSAWLEKRTPA 216
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 33-207 3.18e-23

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: 93.88  E-value: 3.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQavatLQGEGLSVTGTVCHVGKAE--DRERLVAMAVKLHGG- 109
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQE----LADELGAKFPVKVLPLQLDvsDRESIEAALENLPEEf 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 --IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:cd05346   77 rdIDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKA 156

                        170       180
                 ....*....|....*....|
gi 126723191 188 ALLGLNNTLAIELAPRNIRV 207
Cdd:cd05346  157 AVRQFSLNLRKDLIGTGIRV 176
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 30-208 7.51e-23

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: 92.93  E-value: 7.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERSDR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGG----GSVVIVSSIAAF--SPSPGFSpYN 183
Cdd:cd08942   83 LDVLVNNAGAT-WGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIvvSGLENYS-YG 160

                        170       180
                 ....*....|....*....|....*
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:cd08942  161 ASKAAVHQLTRKLAKELAGEHITVN 185
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 30-208 1.01e-22

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: 92.91  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVN-------------PFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPS 176
Cdd:cd08935   83 VDILINGAGGNhpdattdpehyepETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPL 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 126723191 177 PGFSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:cd08935  163 TKVPAYSAAKAAVSNFTQWLAVEFATTGVRVN 194
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 31-207 1.02e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 93.04  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnvdqAVATLQGeglsVTGTVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPA----RAAPIPG----VELLELDVTDDASVQAAVDEVIARAGRI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFFGSLMDVTEEVwdKTL-DINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK06179  75 DVLVNNAGVGLAGAAEESSIAQA--QALfDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAV 152

                        170
                 ....*....|....*...
gi 126723191 190 LGLNNTLAIELAPRNIRV 207
Cdd:PRK06179 153 EGYSESLDHEVRQFGIRV 170
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 31-209 1.02e-22

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 92.70  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSEL-VHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAA----VNPFfgslmdvtEEVWDKTLDINVKA---PAL-MTKAVVPEMEKRGGGSVVIVSSIAafspSPGFS-- 180
Cdd:PRK12823  86 DVLINNVGgtiwAKPF--------EEYEEEQIEAEIRRslfPTLwCCRAVLPHMLAQGGGAIVNVSSIA----TRGINrv 153

                        170       180
                 ....*....|....*....|....*....
gi 126723191 181 PYNVSKTALLGLNNTLAIELAPRNIRVNC 209
Cdd:PRK12823 154 PYSAAKGGVNALTASLAFEYAEHGIRVNA 182
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 35-211 2.12e-22

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: 91.20  E-value: 2.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQD-RAHVVVSSRKQQNVDQAvatlqgEGLSVTGTVCHVGKA----EDRERLVAMAVKLH-G 108
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARgNNTVIATCRDPSAATEL------AALGASHSRLHILELdvtdEIAESAEAVAERLGdA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVS----SIAAFSPSPGFSpYNV 184
Cdd:cd05325   75 GLDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISsrvgSIGDNTSGGWYS-YRA 153

                        170       180
                 ....*....|....*....|....*..
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:cd05325  154 SKAALNMLTKSLAVELKRDGITVVSLH 180
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 30-210 3.95e-22

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 91.13  E-value: 3.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLqGEGLSVtgtvcHVGKAEDRERLVAMAVKLH-- 107
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAEL-GERVKI-----FPANLSDRDEVKALGQKAEad 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 -GGIDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK12936  78 lEGVDILVNNAGITKD-GLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASK 156

                        170       180
                 ....*....|....*....|....
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK12936 157 AGMIGFSKSLAQEIATRNVTVNCV 180
PRK12743 PRK12743
SDR family oxidoreductase;
31-208 1.23e-21

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 89.71  E-value: 1.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATlQGEGLSVTGTVCHVGKAEDRER---LVAMAVKLh 107
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAE-EVRSHGVRAEIRQLDLSDLPEGaqaLDKLIQRL- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSK 186
Cdd:PRK12743  79 GRIDVLVNNAGAM-TKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGqGGRIINITSVHEHTPLPGASAYTAAK 157

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK12743 158 HALGGLTKAMALELVEHGILVN 179
PRK08219 PRK08219
SDR family oxidoreductase;
33-211 1.84e-21

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 88.84  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRaHVVVSSRKQQNVDQAVATLQGeglsVTGTVCHVGKAEDrerlVAMAVKLHGGIDI 112
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPTH-TLLLGGRPAERLDELAAELPG----ATPFPVDLTDPEA----IAAAVEQLGRLDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:PRK08219  75 LVHNAGV-ADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPAL-RAAHGHVVFINSGAGLRANPGWGSYAASKFALRAL 152

                        170
                 ....*....|....*....
gi 126723191 193 NNTLAIELAPrNIRVNCLH 211
Cdd:PRK08219 153 ADALREEEPG-NVRVTSVH 170
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 32-210 2.12e-21

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: 88.79  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnvdQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEE---RGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRID 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAV-NPffGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:cd09761   78 VLVNNAARgSK--GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIK-NKGRIINIASTRAFQSEPDSEAYAASKGGLV 154

                        170       180
                 ....*....|....*....|
gi 126723191 191 GLNNTLAIELAPrNIRVNCL 210
Cdd:cd09761  155 ALTHALAMSLGP-DIRVNCI 173
PRK05866 PRK05866
SDR family oxidoreductase;
16-216 3.47e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 89.42  E-value: 3.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  16 SVRMASSRMTRRD-PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAE 94
Cdd:PRK05866  23 SPQLLINRPPRQPvDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  95 DRERLVAMAVKLHGGIDILVSNAAVN---PFFGSLmdvteEVW---DKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVS 168
Cdd:PRK05866 103 AVDALVADVEKRIGGVDILINNAGRSirrPLAESL-----DRWhdvERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVA 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 126723191 169 SIAAFS-PSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCLHLDLSR 216
Cdd:PRK05866 178 TWGVLSeASPLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVA 226
PRK08628 PRK08628
SDR family oxidoreductase;
30-210 3.50e-21

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 88.48  E-value: 3.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQN--VDQAVATLQGEGLSVTGTVChvgKAEDRERLVAMAVKLH 107
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDdeFAEELRALQPRAEFVQVDLT---DDAQCRDAVEQTVAKF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFFGslMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK08628  82 GRIDGLVNNAGVNDGVG--LEAGREAFVASLERNLIHYYVMAHYCLPHL-KASRGAIVNISSKTALTGQGGTSGYAAAKG 158

                        170       180
                 ....*....|....*....|...
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK08628 159 AQLALTREWAVALAKDGVRVNAV 181
PRK07985 PRK07985
SDR family oxidoreductase;
30-210 4.98e-21

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 88.90  E-value: 4.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVS--SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylPVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK07985 127 GGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPK--GASIITTSSIQAYQPSPHLLDYAATKA 204

                        170       180
                 ....*....|....*....|...
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07985 205 AILNYSRGLAKQVAEKGIRVNIV 227
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 34-207 5.01e-21

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: 87.82  E-value: 5.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQ-AVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAlLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFFGsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:cd05373   81 LVYNAGANVWFP-ILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRAL 159

                        170
                 ....*....|....*
gi 126723191 193 NNTLAIELAPRNIRV 207
Cdd:cd05373  160 AQSMARELGPKGIHV 174
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 34-210 6.43e-21

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: 87.63  E-value: 6.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQDRAHVVV--SSRKQQNVDQAVATlqgeglSVTGTVCHvgKAEDRERLVAMAVKLHGGID 111
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVChdASFADAAERQAFES------ENPGTKAL--SEQKPEELVDAVLQAGGAID 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLG 191
Cdd:cd05361   75 VLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVA 154

                        170
                 ....*....|....*....
gi 126723191 192 LNNTLAIELAPRNIRVNCL 210
Cdd:cd05361  155 LAESLAKELSRDNILVYAI 173
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 29-208 6.64e-21

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 87.84  E-value: 6.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEglSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADELGD--RAIALQADVTDREQVQAMFATATEHFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 -GIDILVSNAAVNPFFG-----SLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK08642  80 kPITTVVNNALADFSFDgdarkKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHDY 159

                        170       180
                 ....*....|....*....|....*.
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08642 160 TTAKAALLGLTRNLAAELGPYGITVN 185
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 29-200 9.81e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 88.83  E-value: 9.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK07109  85 PIDTWVNNAMVT-VFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHA 163

                        170
                 ....*....|..
gi 126723191 189 LLGLNNTLAIEL 200
Cdd:PRK07109 164 IRGFTDSLRCEL 175
PRK06914 PRK06914
SDR family oxidoreductase;
32-207 1.16e-20

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 87.77  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSR---KQQNVDQAVATLQGEG------LSVTgtvchvgkaeDRERLVAM 102
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRnpeKQENLLSQATQLNLQQnikvqqLDVT----------DQNSIHNF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 103 --AVKLHGGIDILVSNA--AVNPFfgsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPG 178
Cdd:PRK06914  73 qlVLKEIGRIDLLVNNAgyANGGF---VEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPG 149

                        170       180
                 ....*....|....*....|....*....
gi 126723191 179 FSPYNVSKTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK06914 150 LSPYVSSKYALEGFSESLRLELKPFGIDV 178
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 30-210 1.84e-20

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: 86.48  E-value: 1.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEG------LSVTGTVChvgKAEDRERLVAMA 103
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGgrqpqwFILDLLTC---TSENCQQLAQRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:cd05340   79 AVNYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 158

                        170       180
                 ....*....|....*....|....*..
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05340  159 VSKFATEGL*QVLADEYQQRNLRVNCI 185
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 30-208 2.27e-20

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 86.88  E-value: 2.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVsNAA---------------VNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFS 174
Cdd:PRK08277  88 CDILI-NGAggnhpkattdnefheLIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFT 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 126723191 175 PSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08277 167 PLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVN 200
PRK12742 PRK12742
SDR family oxidoreductase;
29-208 2.44e-20

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 85.96  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATlqgeglsVTGTVCHVGKAEDRERLVAmAVKLHG 108
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQ-------ETGATAVQTDSADRDAVID-VVRKSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK12742  75 ALDILVVNAGI-AVFGDALELDADDIDRLFKINIHAPYHASVEAARQM-PEGGRIIIIGSVNGDRMPVAGMAAYAASKSA 152

                        170       180
                 ....*....|....*....|
gi 126723191 189 LLGLNNTLAIELAPRNIRVN 208
Cdd:PRK12742 153 LQGMARGLARDFGPRGITIN 172
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 30-208 2.78e-20

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 86.16  E-value: 2.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:PRK07576  87 IDVLVSGAAGN-FPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLL-RRPGASIIQISAPQAFVPMPMQAHVCAAKAGV 164

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:PRK07576 165 DMLTRTLALEWGPEGIRVN 183
PRK06484 PRK06484
short chain dehydrogenase; Validated
 33-210 2.96e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 88.75  E-value: 2.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEdreRLVAMAVKLHGGIDI 112
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVE---SAFAQIQARWGRLDV 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:PRK06484 347 LVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTML 424

                        170
                 ....*....|....*...
gi 126723191 193 NNTLAIELAPRNIRVNCL 210
Cdd:PRK06484 425 SRSLACEWAPAGIRVNTV 442
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
30-210 3.62e-20

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 85.73  E-value: 3.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVvsSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIV--GVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK12481  84 IDILINNAGIIRR-QDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGnGGKIINIASMLSFQGGIRVPSYTASKSA 162

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK12481 163 VMGLTRALATELSQYNINVNAI 184
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 33-211 4.39e-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: 85.74  E-value: 4.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEG-----------LSVTGTVCHVGKA--EDRERL 99
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETgnakveviqldLSSLASVRQFAEEflARFPRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 100 vamavklhggiDILVSNAAV--NPFFgslmdVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAA----- 172
Cdd:cd05327   82 -----------DILINNAGImaPPRR-----LTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHragpi 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 126723191 173 ------FSPSPGFSP---YNVSKTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:cd05327  146 dfndldLENNKEYSPykaYGQSKLANILFTRELARRLEGTGVTVNALH 193
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 26-209 6.40e-20

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 84.92  E-value: 6.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  26 RRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQ-------------AVATLQGEGLSvtgtvchvgk 92
Cdd:PRK08945   6 KPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAvydeieaaggpqpAIIPLDLLTAT---------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  93 AEDRERLVAMAVKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAA 172
Cdd:PRK08945  76 PQNYQQLADTIEEQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVG 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 126723191 173 FSPSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNC 209
Cdd:PRK08945 156 RQGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNC 192
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 30-211 6.89e-20

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: 84.77  E-value: 6.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARR-LAQDRAHVVVSSRKQQNVDQAVATlqgEGLSVTGTVCHVgkaEDRERLVAMAVKLHG 108
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESlLAHGAKKVYAAVRDPGSAAHLVAK---YGDKVVPLRLDV---TDPESIKAAAAQAKD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 gIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:cd05354   75 -VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSA 153

                        170       180
                 ....*....|....*....|...
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCLH 211
Cdd:cd05354  154 AYSLTQGLRAELAAQGTLVLSVH 176
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 31-212 1.03e-19

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 84.70  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVS---SRKQQNVDQAVATLQGEGLSVtGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVAdinSEKAANVAQEINAEYGEGMAY-GFGADATSEQSVLALSRGVDEIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVnpffGSLMDVTE---EVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVI-VSSIAAFSPSPGFSPYN 183
Cdd:PRK12384  80 GRVDLLVYNAGI----AKAAFITDfqlGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIqINSKSGKVGSKHNSGYS 155

                        170       180
                 ....*....|....*....|....*....
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVNCLHL 212
Cdd:PRK12384 156 AAKFGGVGLTQSLALDLAEYGITVHSLML 184
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 30-207 1.81e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 83.94  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGE-GLSVTGTVCHVGKAEDRERLVAMAvklhG 108
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEAREQLAAEA----G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK06125  81 DIDILVNNAGAIP-GGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADYICGSAGNAA 159

                        170
                 ....*....|....*....
gi 126723191 189 LLGLNNTLAIELAPRNIRV 207
Cdd:PRK06125 160 LMAFTRALGGKSLDDGVRV 178
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 29-208 1.93e-19

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: 84.12  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRkqqnvDQAVATLQGEGLSvTGTVCHVGKAE-----DRERLVAMA 103
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDR-----SELVHEVLAEILA-AGDAAHVHTADletyaGAQGVVRAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVkAPALMT-KAVVPEMEKRGGGSVVIVSSIAafSPSPGFSPY 182
Cdd:cd08937   75 VERFGRVDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSL-FPTLWCcRAVLPHMLERQQGVIVNVSSIA--TRGIYRIPY 151

                        170       180
                 ....*....|....*....|....*.
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:cd08937  152 SAAKGGVNALTASLAFEHARDGIRVN 177
PRK06114 PRK06114
SDR family oxidoreductase;
30-210 2.00e-19

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 83.68  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQN----VDQAVATLQGEGLSVTGTVChvgKAEDRERLVAMAVK 105
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDglaeTAEHIEAAGRRAIQIAADVT---SKADLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNAAV---NPffgsLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGF--S 180
Cdd:PRK06114  83 ELGALTLAVNAAGIanaNP----AEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGLlqA 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 126723191 181 PYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK06114 159 HYNASKAGVIHLSKSLAMEWVGRGIRVNSI 188
PRK06182 PRK06182
short chain dehydrogenase; Validated
 33-207 2.83e-19

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 83.86  E-value: 2.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKqqnVD--QAVATLQGEGLSVTgtvchVGKAEDRERLVAMAVKLHGGI 110
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARR---VDkmEDLASLGVHPLSLD-----VTDEASIKAAVDTIIAEEGRI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:PRK06182  76 DVLVNNAGYGS-YGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALE 154

                        170
                 ....*....|....*..
gi 126723191 191 GLNNTLAIELAPRNIRV 207
Cdd:PRK06182 155 GFSDALRLEVAPFGIDV 171
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 33-207 5.37e-19

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 82.89  E-value: 5.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQD---RAHVVVSSRKQQNVDQAVATLqGEGLSVTGTVCHVGKAEDRErlVAMAVKLHGG 109
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASDpskRFKVYATMRDLKKKGRLWEAA-GALAGGTLETLQLDVCDSKS--VAAAVERVTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 --IDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:cd09806   78 rhVDVLVCNAGVG-LLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKF 156

                        170       180
                 ....*....|....*....|
gi 126723191 188 ALLGLNNTLAIELAPRNIRV 207
Cdd:cd09806  157 ALEGLCESLAVQLLPFNVHL 176
PRK07577 PRK07577
SDR family oxidoreductase;
30-208 8.34e-19

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 81.70  E-value: 8.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRkqqnvdQAVATLQGEGLSvtgtvCHVGKAEDRERLVAmAVKLHGG 109
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIAR------SAIDDFPGELFA-----CDLADIEQTAATLA-QINEIHP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSpSPGFSPYNVSKTAL 189
Cdd:PRK07577  69 VDAIVNNVGI-ALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFG-ALDRTSYSAAKSAL 146

                        170
                 ....*....|....*....
gi 126723191 190 LGLNNTLAIELAPRNIRVN 208
Cdd:PRK07577 147 VGCTRTWALELAEYGITVN 165
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 30-208 1.06e-18

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: 81.90  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSrkqQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIAD---INLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:cd05363   78 IDILVNNAALFD-LAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGrGGKIINMASQAGRRGEALVGVYCATKAA 156

                        170       180
                 ....*....|....*....|
gi 126723191 189 LLGLNNTLAIELAPRNIRVN 208
Cdd:cd05363  157 VISLTQSAGLNLIRHGINVN 176
PRK09134 PRK09134
SDR family oxidoreductase;
24-208 1.50e-18

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 81.51  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVV-SSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAM 102
Cdd:PRK09134   1 SPPMSMAAPRAALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 103 AVKLHGGIDILVSNAAVnpF-FGSLMDVTEEVWDKTLDINVKAPALMTKA---VVPEmEKRGggsvVIVSSI--AAFSPS 176
Cdd:PRK09134  81 ASAALGPITLLVNNASL--FeYDSAASFTRASWDRHMATNLRAPFVLAQAfarALPA-DARG----LVVNMIdqRVWNLN 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 126723191 177 PGFSPYNVSKTALLGLNNTLAIELAPRnIRVN 208
Cdd:PRK09134 154 PDFLSYTLSKAALWTATRTLAQALAPR-IRVN 184
PRK07832 PRK07832
SDR family oxidoreductase;
33-207 1.51e-18

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 81.63  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlsvtGTVcHVGKA---EDRERLVAMAVKLH-- 107
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALG----GTV-PEHRAldiSDYDAVAAFAADIHaa 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 -GGIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEM-EKRGGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK07832  76 hGSMDVVMNIAGIS-AWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvAAGRGGHLVNVSSAAGLVALPWHAAYSAS 154

                        170       180
                 ....*....|....*....|..
gi 126723191 186 KTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK07832 155 KFGLRGLSEVLRFDLARHGIGV 176
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-207 1.63e-18

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 81.16  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAavnpffGSLMD----------VTE----EVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVI-VSSIAAfS 174
Cdd:PRK08217  83 LNGLINNA------GILRDgllvkakdgkVTSkmslEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGVIInISSIAR-A 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 126723191 175 PSPGFSPYNVSKTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK08217 156 GNMGQTNYSASKAGVAAMTVTWAKELARYGIRV 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 31-207 2.21e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 81.24  E-value: 2.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIG--FAIARRLAQDRahVVVSSRKQQNVDQAVATLQGEGLSVTGTVChvgkaeDRE---RLVAMAVK 105
Cdd:PRK08263   2 MEKVWFITGASRGFGraWTEAALERGDR--VVATARDTATLADLAEKYGDRLLPLALDVT------DRAavfAAVETAVE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNAAvNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK08263  74 HFGRLDIVVNNAG-YGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHAS 152

                        170       180
                 ....*....|....*....|..
gi 126723191 186 KTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK08263 153 KWALEGMSEALAQEVAEFGIKV 174
PRK05867 PRK05867
SDR family oxidoreductase;
30-208 3.19e-18

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 80.46  E-value: 3.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAA--FSPSPGFSPYNVSK 186
Cdd:PRK05867  87 IDIAVCNAGIIT-VTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGqGGVIINTASMSGhiINVPQQVSHYCASK 165

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK05867 166 AAVIHLTKAMAVELAPHKIRVN 187
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 32-210 3.46e-18

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: 80.66  E-value: 3.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTV-CHVGKAEDRERLVAMAVKLHGGI 110
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVpCDVTKEEDIKTLISVTVERFGRI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGfSPYNVSKTALL 190
Cdd:cd08933   89 DCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQA-APYVATKGAIT 167

                        170       180
                 ....*....|....*....|
gi 126723191 191 GLNNTLAIELAPRNIRVNCL 210
Cdd:cd08933  168 AMTKALAVDESRYGVRVNCI 187
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 34-200 4.67e-18

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: 80.02  E-value: 4.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQ--DRAHVVVSSRKQQNVDQAVATLQGeGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKrgSPSVVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIRKLDGERD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGG-GSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:cd05367   80 LLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAARD 159

                        170
                 ....*....|
gi 126723191 191 GLNNTLAIEL 200
Cdd:cd05367  160 MFFRVLAAEE 169
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-208 5.45e-18

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 79.83  E-value: 5.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTAST--DGIGFAIARRLAQDRAHVVVS--SRKQQN----VDQAVATLQGEGLSVTGTVCH-----VGKAEDR 96
Cdd:PRK12859   4 LKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTywTAYDKEmpwgVDQDEQIQLQEELLKNGVKVSsmeldLTQNDAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  97 ERLVAMAVKLHGGIDILVSNAA--VNPFFGSLmdvTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFS 174
Cdd:PRK12859  84 KELLNKVTEQLGYPHILVNNAAysTNNDFSNL---TAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQG 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 126723191 175 PSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK12859 161 PMVGELAYAATKGAIDALTSSLAAEVAHLGITVN 194
PRK06194 PRK06194
hypothetical protein; Provisional
 30-209 9.60e-18

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 79.67  E-value: 9.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAVNPffGSLM-DVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGG------GSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK06194  84 VHLLFNNAGVGA--GGLVwENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASMAGLLAPPAMGIY 161

                        170       180
                 ....*....|....*....|....*..
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVNC 209
Cdd:PRK06194 162 NVSKHAVVSLTETLYQDLSLVTDQVGA 188
PRK06949 PRK06949
SDR family oxidoreductase;
24-210 1.17e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 79.04  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:PRK06949   1 MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGS--------VVIVSSIAAFSP 175
Cdd:PRK06949  81 ETEAGTIDILVNNSGVST-TQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLRV 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126723191 176 SPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK06949 160 LPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAI 194
PRK05693 PRK05693
SDR family oxidoreductase;
33-207 1.54e-17

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 79.06  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVdqavATLQGEGLsvTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDV----EALAAAGF--TAVQLDVNDGAALARLAEELEAEHGGLDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:PRK05693  76 LINNAGYGAM-GPLLDGGVEAMRRQFETNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHAL 153

                        170
                 ....*....|....*
gi 126723191 193 NNTLAIELAPRNIRV 207
Cdd:PRK05693 154 SDALRLELAPFGVQV 168
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 22-208 1.61e-17

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 80.73  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  22 SRMTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLS--VTGTVCHVGKAEDRERL 99
Cdd:COG3347  415 QRMPKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGAdaVDATDVDVTAEAAVAAA 494

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 100 VAMAVKLHGGIDILVSNAAVnpfFGSLMDVTE--EVWDKTLDINVKAPALMTKAVVPEM--EKRGGGSVVIVSSIAAFsP 175
Cdd:COG3347  495 FGFAGLDIGGSDIGVANAGI---ASSSPEEETrlSFWLNNFAHLSTGQFLVARAAFQGTggQGLGGSSVFAVSKNAAA-A 570

                        170       180       190
                 ....*....|....*....|....*....|...
gi 126723191 176 SPGFSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:COG3347  571 AYGAAAAATAKAAAQHLLRALAAEGGANGINAN 603
PLN02253 PLN02253
xanthoxin dehydrogenase
 30-210 2.77e-17

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 78.33  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRkQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDL-QDDLGQNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKFGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV-NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PLN02253  95 LDIMVNNAGLtGPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHA 174

                        170       180
                 ....*....|....*....|..
gi 126723191 189 LLGLNNTLAIELAPRNIRVNCL 210
Cdd:PLN02253 175 VLGLTRSVAAELGKHGIRVNCV 196
PRK08278 PRK08278
SDR family oxidoreductase;
29-210 5.29e-17

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 77.64  E-value: 5.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  29 PLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQ-------NVDQAVATLQ---GEGLSVtgtVCHVGKAEDRER 98
Cdd:PRK08278   3 SLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEphpklpgTIHTAAEEIEaagGQALPL---VGDVRDEDQVAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  99 LVAMAVKLHGGIDILVSNA-AVNpfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPS- 176
Cdd:PRK08278  80 AVAKAVERFGGIDICVNNAsAIN--LTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPKw 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 126723191 177 -PGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK08278 158 fAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNAL 192
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 32-208 5.42e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 77.03  E-value: 5.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQA---VATLQGEGLSVtgtVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAkleIEQFPGQVLTV---QMDVRNPEDVQKMVEQIDEKFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK07677  78 RIDALINNAAGN-FICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGiKGNIINMVATYAWDAGPGVIHSAAAKA 156

                        170       180
                 ....*....|....*....|..
gi 126723191 188 ALLGLNNTLAIELAPR-NIRVN 208
Cdd:PRK07677 157 GVLAMTRTLAVEWGRKyGIRVN 178
PRK08340 PRK08340
SDR family oxidoreductase;
36-206 6.59e-17

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 77.15  E-value: 6.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  36 LVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKLHGGIDILVS 115
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDALVW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 116 NAA---VNPFFgsLMDVTEEVWDKTLDINVKAPALMTKAVVPE-MEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLG 191
Cdd:PRK08340  83 NAGnvrCEPCM--LHEAGYSDWLEAALLHLVAPGYLTTLLIQAwLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQ 160

                        170
                 ....*....|....*
gi 126723191 192 LNNTLAIELAPRNIR 206
Cdd:PRK08340 161 LAKGVSRTYGGKGIR 175
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 31-208 7.47e-17

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: 76.94  E-value: 7.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQaVATLQGEGLSVTGTVChvgKAEDRERLVAMAVKLHGGI 110
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGET-VAKLGDNCRFVPVDVT---SEKDVKAALALAKAKFGRL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNP------FFGSLMDVTEEvWDKTLDINVKAPALMTKAVVPEMEK----RGG--GSVVIVSSIAAFSPSPG 178
Cdd:cd05371   77 DIVVNCAGIAVaaktynKKGQQPHSLEL-FQRVINVNLIGTFNVIRLAAGAMGKnepdQGGerGVIINTASVAAFEGQIG 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 126723191 179 FSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:cd05371  156 QAAYSASKGGIVGMTLPIARDLAPQGIRVV 185
PRK05993 PRK05993
SDR family oxidoreductase;
31-207 2.86e-16

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 75.45  E-value: 2.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNvdqaVATLQGEGLsvTGTVCHVGKAEDRERLVAMAVKLHGG- 109
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEED----VAALEAEGL--EAFQLDYAEPESIAALVAQVLELSGGr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV-NPffGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK05993  77 LDALFNNGAYgQP--GAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154

                        170
                 ....*....|....*....
gi 126723191 189 LLGLNNTLAIELAPRNIRV 207
Cdd:PRK05993 155 IEGLSLTLRMELQGSGIHV 173
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 30-210 5.19e-16

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 74.73  E-value: 5.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVS-SRKQQNVDQAVATLQ---GEGLSVTGTVCHVGKAEDRERLVAMAVK 105
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHyGNRKEEAEETVYEIQsngGSAFSIGANLESLHGVEALYSSLDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGG---IDILVSNAAVNPffGSLM-DVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSP 181
Cdd:PRK12747  82 NRTGstkFDILINNAGIGP--GAFIeETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIA 157

                        170       180
                 ....*....|....*....|....*....
gi 126723191 182 YNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK12747 158 YSMTKGAINTMTFTLAKQLGARGITVNAI 186
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-208 1.14e-15

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 73.66  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQnvDQAVATLQGEGLSVTgtvCHVGkaeDRERLVAMAVKLH-- 107
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAE--NEAKELREKGVFTIK---CDVG---NRDQVKKSKEVVEke 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 -GGIDILVSNAAV---NPFfgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAF-SPSPGFSPY 182
Cdd:PRK06463  77 fGRVDVLVNNAGImylMPF----EEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFY 152

                        170       180
                 ....*....|....*....|....*.
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06463 153 AITKAGIIILTRRLAFELGKYGIRVN 178
PRK07775 PRK07775
SDR family oxidoreductase;
24-211 1.42e-15

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 73.64  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNK-VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAM 102
Cdd:PRK07775   1 MPRFEPHPDRrPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 103 AVKLHGGIDILVSNAAvNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK07775  81 AEEALGEIEVLVSGAG-DTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAY 159

                        170       180
                 ....*....|....*....|....*....
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK07775 160 GAAKAGLEAMVTNLQMELEGTGVRASIVH 188
PRK12746 PRK12746
SDR family oxidoreductase;
30-210 1.44e-15

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 73.53  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVS-SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAM---AVK 105
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQlknELQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGG---IDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK12746  84 IRVGtseIDILVNNAGIGT-QGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAY 160

                        170       180
                 ....*....|....*....|....*...
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTI 188
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
30-208 1.48e-15

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 73.12  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVV-----SSRKQQNVDQAVATlqgeGLSVTGTVCHVGKAEDRERLVAMAV 104
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnSPRRVKWLEDQKAL----GFDFIASEGNVGDWDSTKAAFDKVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 105 KLHGGIDILVSNAAVNpffgslMDV-----TEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGF 179
Cdd:PRK12938  77 AEVGEIDVLVNNAGIT------RDVvfrkmTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQ 150

                        170       180
                 ....*....|....*....|....*....
gi 126723191 180 SPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK12938 151 TNYSTAKAGIHGFTMSLAQEVATKGVTVN 179
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 30-210 1.54e-15

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: 73.32  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQ--GEGLSVTGTVCHVGKAEDRERLVAMAVKLH 107
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLeiAPDAEVLLIKADVSDEAQVEAYVDATVEQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:cd05330   81 GRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH 160

                        170       180
                 ....*....|....*....|...
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05330  161 GVVGLTRNSAVEYGQYGIRINAI 183
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 30-208 3.47e-15

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 72.10  E-value: 3.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAvnpffGSLMDVTEEV--WDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSI-AAFSPSPGFSPYNVSK 186
Cdd:PRK05786  82 IDGLVVTVG-----GYVEDTVEEFsgLEEMLTNHIKIPLYAVNASLRFLKE--GSSIVLVSSMsGIYKASPDQLSYAVAK 154

                        170       180
                 ....*....|....*....|..
gi 126723191 187 TALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK05786 155 AGLAKAVEILASELLGRGIRVN 176
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
30-210 3.60e-15

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 72.21  E-value: 3.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVV-VSSRKQQNVDQAVATLQGEGLSVTGTVChvgKAEDRERLVAMAVKLHG 108
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVgINIVEPTETIEQVTALGRRFLSLTADLR---KIDGIPALLERAVAEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFFGSLmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK08993  85 HIDILVNNAGLIRREDAI-EFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGnGGKIINIASMLSFQGGIRVPSYTASKS 163

                        170       180
                 ....*....|....*....|...
gi 126723191 188 ALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK08993 164 GVMGVTRLMANEWAKHNINVNAI 186
PRK08267 PRK08267
SDR family oxidoreductase;
36-210 3.64e-15

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 72.28  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  36 LVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLsVTGTVCHVGKAEDRERLVAMAVKLHGGIDILVS 115
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNA-WTGALDVTDRAAWDAALADFAAATGGRLDVLFN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 116 NAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLNNT 195
Cdd:PRK08267  84 NAGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEA 162

                        170
                 ....*....|....*
gi 126723191 196 LAIELAPRNIRVNCL 210
Cdd:PRK08267 163 LDLEWRRHGIRVADV 177
PRK08703 PRK08703
SDR family oxidoreductase;
28-210 6.40e-15

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 71.50  E-value: 6.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  28 DPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNV----DQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMA 103
Cdd:PRK08703   2 ATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLekvyDAIVEAGHPEPFAIRFDLMSAEEKEFEQFAATIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLHGGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYN 183
Cdd:PRK08703  82 EATQGKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFG 161

                        170       180
                 ....*....|....*....|....*....
gi 126723191 184 VSKTALLGLNNTLAIE--LAPrNIRVNCL 210
Cdd:PRK08703 162 ASKAALNYLCKVAADEweRFG-NLRANVL 189
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 30-207 6.44e-15

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: 71.71  E-value: 6.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQN----VDQAVATLQGEGLSVtgtVCHVGKAEDRERLVA-MAV 104
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPqlpgTAEEIEARGGKCIPV---RCDHSDDDEVEALFErVAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 105 KLHGGIDILVSNA-AVN---------PFFgslmDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFS 174
Cdd:cd09763   78 EQQGRLDILVNNAyAAVqlilvgvakPFW----EEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLE 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 126723191 175 PSPGFsPYNVSKTALLGLNNTLAIELAPRNIRV 207
Cdd:cd09763  154 YLFNV-AYGVGKAAIDRMAADMAHELKPHGVAV 185
PRK09291 PRK09291
SDR family oxidoreductase;
31-207 6.58e-15

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 71.57  E-value: 6.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERlvamAVKLHggI 110
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQ----AAEWD--V 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALL 190
Cdd:PRK09291  75 DVLLNNAGIGEA-GAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALE 153

                        170
                 ....*....|....*..
gi 126723191 191 GLNNTLAIELAPRNIRV 207
Cdd:PRK09291 154 AIAEAMHAELKPFGIQV 170
PRK09730 PRK09730
SDR family oxidoreductase;
33-210 6.63e-15

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 71.42  E-value: 6.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSrkQQNVDQA---VATLQGEGLSVTGTVCHVGkaeDRERLVAM--AVKLH 107
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNY--QQNLHAAqevVNLITQAGGKAFVLQADIS---DENQVVAMftAIDQH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GG-IDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGS---VVIVSSIAAFSPSPG-FSPY 182
Cdd:PRK09730  77 DEpLAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGAPGeYVDY 156

                        170       180
                 ....*....|....*....|....*...
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK09730 157 AASKGAIDTLTTGLSLEVAAQGIRVNCV 184
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 33-210 1.20e-14

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: 70.69  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVT--ASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDrerLVAMAVKLH--- 107
Cdd:cd05372    2 KRILITgiANDRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEE---IKELFAEVKkdw 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILV---SNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:cd05372   79 GKLDGLVhsiAFAPKVQLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNP--GGSIVTLSYLGSERVVPGYNVMGV 156

                        170       180
                 ....*....|....*....|....*.
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:cd05372  157 AKAALESSVRYLAYELGRKGIRVNAI 182
PRK06482 PRK06482
SDR family oxidoreductase;
33-207 1.93e-14

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 70.53  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQaVATLQGEGLSVTgtVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK06482   3 KTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDD-LKARYGDRLWVL--QLDVTDSAAVRAVVDRAFAALGRIDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:PRK06482  80 VVSNAGYG-LFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGF 158

                        170
                 ....*....|....*
gi 126723191 193 NNTLAIELAPRNIRV 207
Cdd:PRK06482 159 VEAVAQEVAPFGIEF 173
PRK06123 PRK06123
SDR family oxidoreductase;
32-210 2.93e-14

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 69.81  E-value: 2.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRK-QQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRnRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKR---GGGSVVIVSSIAAFSPSPG-FSPYNVSK 186
Cdd:PRK06123  82 DALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGeYIDYAASK 161

                        170       180
                 ....*....|....*....|....
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK06123 162 GAIDTMTIGLAKEVAAEGIRVNAV 185
PRK05717 PRK05717
SDR family oxidoreductase;
33-210 7.27e-14

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 68.76  E-value: 7.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTgtvCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIA---MDVADEAQVAAGVAEVLGQFGRLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAV-NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSpSPGFSPYNVSKTALLG 191
Cdd:PRK05717  88 LVCNAAIaDPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQS-EPDTEAYAASKGGLLA 166

                        170
                 ....*....|....*....
gi 126723191 192 LNNTLAIELAPrNIRVNCL 210
Cdd:PRK05717 167 LTHALAISLGP-EIRVNAV 184
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 30-221 2.01e-13

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: 67.36  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVT--ASTDGIGFAIARRLAQDRAHVVVSS---RKQQNVDQAVATLQGEGLsvtgTVCHVGKAEDRERLVAMAV 104
Cdd:COG0623    3 LKGKRGLITgvANDRSIAWGIAKALHEEGAELAFTYqgeALKKRVEPLAEELGSALV----LPCDVTDDEQIDALFDEIK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 105 KLHGGIDILV---SNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAfspSPGFSP 181
Cdd:COG0623   79 EKWGKLDFLVhsiAFAPKEELGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLM--NEGGSIVTLTYLGA---ERVVPN 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 126723191 182 YN---VSKTALLGLNNTLAIELAPRNIRVNCLhldlsrlaSAG 221
Cdd:COG0623  154 YNvmgVAKAALEASVRYLAADLGPKGIRVNAI--------SAG 188
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 33-210 6.04e-13

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: 65.55  E-value: 6.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLsVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENV-VAGALDVTDRAAWAAALADFAAATGGRLDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:cd08931   80 LFNNAGVGRG-GPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGL 158

                        170
                 ....*....|....*...
gi 126723191 193 NNTLAIELAPRNIRVNCL 210
Cdd:cd08931  159 TEALDVEWARHGIRVADV 176
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 34-220 1.40e-12

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: 65.33  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191   34 VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQA-VATLQ----GEGLSVTGTVCHVGKAEDR-ERLVAMAVKLH 107
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTlAAELNarrpNSAVTCQADLSNSATLFSRcEAIIDACFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  108 GGIDILVSNAAVnpFFGSLM---DVTEEVWD-KTLDI--------NVKAPALMTKAVVPEMEKRGGG----SVVIVSSIA 171
Cdd:TIGR02685  83 GRCDVLVNNASA--FYPTPLlrgDAGEGVGDkKSLEVqvaelfgsNAIAPYFLIKAFAQRQAGTRAEqrstNLSIVNLCD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 126723191  172 AFS--PSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCLHLDLSRLASA 220
Cdd:TIGR02685 161 AMTdqPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPDA 211
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 34-207 4.93e-12

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 63.62  E-value: 4.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  34 VALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLqGEGLsvtgtvcHVGKAEDRER-----LVAMAVKLHG 108
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL-GDNL-------YIAQLDVRNRaaieeMLASLPAEWR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA 188
Cdd:PRK10538  74 NIDVLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAF 153

                        170
                 ....*....|....*....
gi 126723191 189 LLGLNNTLAIELAPRNIRV 207
Cdd:PRK10538 154 VRQFSLNLRTDLHGTAVRV 172
PRK07041 PRK07041
SDR family oxidoreductase;
36-208 5.11e-12

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 63.13  E-value: 5.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  36 LVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLqGEGLSVTGTVCHVGKAEDRERLVAMavklHGGIDILVS 115
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARAL-GGGAPVRTAALDITDEAAVDAFFAE----AGPFDHVVI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 116 NAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAV-VPEmekrgGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLNN 194
Cdd:PRK07041  76 TAADTP-GGPVRALPLAAAQAAMDSKFWGAYRVARAArIAP-----GGSLTFVSGFAAVRPSASGVLQGAINAALEALAR 149

                        170
                 ....*....|....
gi 126723191 195 TLAIELAPrnIRVN 208
Cdd:PRK07041 150 GLALELAP--VRVN 161
PRK12744 PRK12744
SDR family oxidoreductase;
30-208 6.66e-12

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 63.22  E-value: 6.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVV----SSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVK 105
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVsNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrGGGSVVIVSS-IAAFspSPGFSPYNV 184
Cdd:PRK12744  86 AFGRPDIAI-NTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLND-NGKIVTLVTSlLGAF--TPFYSAYAG 161

                        170       180
                 ....*....|....*....|....
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK12744 162 SKAPVEHFTRAASKEFGARGISVT 185
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 35-209 2.96e-11

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 61.81  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSR---KQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKlhgGID 111
Cdd:PLN02780  56 ALVTGPTDGIGKGFAFQLARKGLNLVLVARnpdKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIE---GLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 --ILVSNAAVN-PFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVV-IVSSIAAFSPS-PGFSPYNVSK 186
Cdd:PLN02780 133 vgVLINNVGVSyPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIInIGSGAAIVIPSdPLYAVYAATK 212

                        170       180
                 ....*....|....*....|...
gi 126723191 187 TALLGLNNTLAIELAPRNIRVNC 209
Cdd:PLN02780 213 AYIDQFSRCLYVEYKKSGIDVQC 235
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 21-208 3.07e-11

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 61.72  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  21 SSRMTRRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVV----SSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDr 96
Cdd:PRK07792   1 SPRTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVndvaSALDASDVLDEIRAAGAKAVAVAGDISQRATADE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  97 erLVAMAVKLhGGIDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVP---EMEKRGGGSV----VIVSS 169
Cdd:PRK07792  80 --LVATAVGL-GGLDIVVNNAGITR-DRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAywrAKAKAAGGPVygriVNTSS 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 126723191 170 IAAFSPSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK07792 156 EAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRAN 194
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 32-212 3.34e-11

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: 61.33  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGE-GLSVTGTVCHVGKAEDRERLVAMAVKLHGGI 110
Cdd:cd05322    2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIFKRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVNPFfGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRG-GGSVVIVSSIAAFSPSPGFSPYNVSKTAL 189
Cdd:cd05322   82 DLLVYSAGIAKS-AKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFGG 160

                        170       180
                 ....*....|....*....|...
gi 126723191 190 LGLNNTLAIELAPRNIRVNCLHL 212
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLML 183
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 30-210 4.55e-11

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: 60.54  E-value: 4.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQ----------NVDQAVATLQGEGLSVTGTVchvgKAEDRER- 98
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiyTAAEEIEAAGGKALPCIVDI----RDEDQVRa 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  99 LVAMAVKLHGGIDILVSNA-AVNpfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGggsvviVSSIAAFSPSP 177
Cdd:cd09762   77 AVEKAVEKFGGIDILVNNAsAIS--LTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSK------NPHILNLSPPL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 126723191 178 GFSP--------YNVSKTAL----LGlnntLAIELAPRNIRVNCL 210
Cdd:cd09762  149 NLNPkwfknhtaYTMAKYGMsmcvLG----MAEEFKPGGIAVNAL 189
PRK06947 PRK06947
SDR family oxidoreductase;
33-208 1.88e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 59.05  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVS-SRKQQNVDQAVATLQGEGlsvtGTVCHV-GKAEDRERLVAM---AVKLH 107
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRAAG----GRACVVaGDVANEADVIAMfdaVQSAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEK-RGG--GSVVIVSSIAAFSPSPG-FSPYN 183
Cdd:PRK06947  79 GRLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTdRGGrgGAIVNVSSIASRLGSPNeYVDYA 158

                        170       180
                 ....*....|....*....|....*
gi 126723191 184 VSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK06947 159 GSKGAVDTLTLGLAKELGPHGVRVN 183
PRK07806 PRK07806
SDR family oxidoreductase;
30-188 4.17e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 57.81  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSR-KQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK07806   4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVNPFFGslMDVteevwDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSS-----IAAFSPSPGFSPYN 183
Cdd:PRK07806  84 GLDALVLNASGGMESG--MDE-----DYAMRLNRDAQRNLARAALPLM--PAGSRVVFVTShqahfIPTVKTMPEYEPVA 154


                 ....*
gi 126723191 184 VSKTA 188
Cdd:PRK07806 155 RSKRA 159
PRK07024 PRK07024
SDR family oxidoreductase;
33-207 4.39e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 58.02  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTdGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlsvtgtVCHVGKAE--DRERLVAMA---VKLH 107
Cdd:PRK07024   4 KVFITGASS-GIGQALAREYARQGATLGLVARRTDALQAFAARLPKAA------RVSVYAADvrDADALAAAAadfIAAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 GGIDILVSNAAVnpffgSLMDVTEEVWD-----KTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:PRK07024  77 GLPDVVIANAGI-----SVGTLTEEREDlavfrEVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAY 151

                        170       180
                 ....*....|....*....|....*
gi 126723191 183 NVSKTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK07024 152 SASKAAAIKYLESLRVELRPAGVRV 176
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 33-231 4.77e-10

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: 58.06  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLaQDRAHVVVSsrkqqnvdqAVATLQGEGLSVTGTVC---------HVGKAEDRERlVAMA 103
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKL-DSLGFTVLA---------GCLTKNGPGAKELRRVCsdrlrtlqlDVTKPEQIKR-AAQW 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 104 VKLH---GGIDILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPeMEKRGGGSVVIVSSIAAFSPSPGFS 180
Cdd:cd09805   70 VKEHvgeKGLWGLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGG 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 126723191 181 PYNVSKTALLGLNNTLAIELAPRNIRVNCLHLDLSRLASAGCSG-WTRKKRK 231
Cdd:cd09805  149 AYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSElWEKQAKK 200
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 33-210 4.85e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 58.15  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVV-------------SSRKQQNVDQAVAtLQGEGLSVTGTVCHVGKAedrERL 99
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgsasgGSAAQAVVDEIVA-AGGEAVANGDDIADWDGA---ANL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 100 VAMAVKLHGGIDILVSNAAV--NPFFGSLmdvTEEVWDKTLDINVK---APALMTKAVVPEMEKRG---GGSVVIVSSIA 171
Cdd:PRK07791  83 VDAAVETFGGLDVLVNNAGIlrDRMIANM---SEEEWDAVIAVHLKghfATLRHAAAYWRAESKAGravDARIINTSSGA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 126723191 172 AFSPSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07791 160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAI 198
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 35-209 5.95e-10

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 56.82  E-value: 5.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSRKQqnVDQAVatlqgeglsvtgtvchvgKAEDRERLVAMAVKLhGGIDILV 114
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSS--GDYQV------------------DITDEASIKALFEKV-GHFDAIV 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 115 SNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLNN 194
Cdd:cd11731   60 STAGDAE-FAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVR 136

                        170
                 ....*....|....*
gi 126723191 195 TLAIELaPRNIRVNC 209
Cdd:cd11731  137 AAAIEL-PRGIRINA 150
PRK08017 PRK08017
SDR family oxidoreductase;
33-207 9.06e-10

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 57.02  E-value: 9.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVdqavATLQGEGLsvTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV----ARMNSLGF--TGILLDLDDPESVERAADEVIALTDNRLY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGL 192
Cdd:PRK08017  77 GLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAW 156

                        170
                 ....*....|....*
gi 126723191 193 NNTLAIELAPRNIRV 207
Cdd:PRK08017 157 SDALRMELRHSGIKV 171
PRK09186 PRK09186
flagellin modification protein A; Provisional
 30-210 1.15e-09

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 56.92  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVV----SSRKQQNVDQAVATLQGEGLSVTGtvCHVGKAEDRERLVAMAVK 105
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAadidKEALNELLESLGKEFKSKKLSLVE--LDITDQESLEEFLSKSAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNA-AVNPFFGSLM-DVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSpSPGFSPYN 183
Cdd:PRK09186  80 KYGKIDGAVNCAyPRNKDYGKKFfDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVV-APKFEIYE 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 126723191 184 -----------VSKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK09186 159 gtsmtspveyaAIKAGIIHLTKYLAKYFKDSNIRVNCV 196
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
30-224 2.50e-09

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 55.88  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVT--ASTDGIGFAIARRLAQDRAHVVVS------SRKQQNVDQAVATLQGEGLsvtgTVCHVGKAEDRERLVA 101
Cdd:PRK07370   4 LTGKKALVTgiANNRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVRELTEPLNPSLF----LPCDVQDDAQIEETFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 102 MAVKLHGGIDILV---SNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPG 178
Cdd:PRK07370  80 TIKQKWGKLDILVhclAFAGKEELIGDFSATSREGFARALEISAYSLAPLCKAAKPLMSE--GGSIVTLTYLGGVRAIPN 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 126723191 179 FSPYNVSKTALLGLNNTLAIELAPRNIRVNCLHLDLSR-LASAGCSG 224
Cdd:PRK07370 158 YNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRtLASSAVGG 204
PRK06139 PRK06139
SDR family oxidoreductase;
26-207 2.70e-09

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 56.27  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  26 RRDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVK 105
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNAAVNPfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK06139  81 FGGRIDVWVNNVGVGA-VGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSAS 159

                        170       180
                 ....*....|....*....|...
gi 126723191 186 KTALLGLNNTLAIELAP-RNIRV 207
Cdd:PRK06139 160 KFGLRGFSEALRGELADhPDIHV 182
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
33-199 1.16e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 53.92  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLS-VTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSNLTfHSLDLQDVHELETNFNEILSSIQEDNVSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 I-LVSNAA-VNPffgslMDVTEEVWDKTL----DINVKAPALMTKAVVPEMEKRGGG-SVVIVSSIAAFSPSPGFSPYNV 184
Cdd:PRK06924  82 IhLINNAGmVAP-----IKPIEKAESEELitnvHLNLLAPMILTSTFMKHTKDWKVDkRVINISSGAAKNPYFGWSAYCS 156

                        170
                 ....*....|....*
gi 126723191 185 SKTALLGLNNTLAIE 199
Cdd:PRK06924 157 SKAGLDMFTQTVATE 171
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 33-211 1.54e-08

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 53.76  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDR--ERLVAMAVKLHGGI 110
Cdd:cd09809    2 KVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRsvQRFAEAFKAKNSPL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 111 DILVSNAAVnpfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSS----------------IAAFS 174
Cdd:cd09809   82 HVLVCNAAV---FALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSeshrftdlpdscgnldFSLLS 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 126723191 175 PSP----GFSPYNVSKTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:cd09809  159 PPKkkywSMLAYNRAKLCNILFSNELHRRLSPRGITSNSLH 199
PRK08177 PRK08177
SDR family oxidoreductase;
33-211 1.70e-08

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 53.11  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVD--QAVATLQGEGLSVTgtvchvgkaeDRERLVAMAVKLHGG- 109
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTalQALPGVHIEKLDMN----------DPASLDQLLQRLQGQr 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNAAV-NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMeKRGGGSVVIVSSI---AAFSPSPGFSPYNVS 185
Cdd:PRK08177  72 FDLLFVNAGIsGPAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQV-RPGQGVLAFMSSQlgsVELPDGGEMPLYKAS 150

                        170       180
                 ....*....|....*....|....*.
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVNCLH 211
Cdd:PRK08177 151 KAALNSMTRSFVAELGEPTLTVLSMH 176
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
88-221 2.14e-08

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 53.21  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  88 CHVGKAEDRERLVAMAVKLHGGIDILVSNAAVNP---FFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSV 164
Cdd:PRK08415  62 LDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFAPkeaLEGSFLETSKEAFNIAMEISVYSLIELTRALLPLLND--GASV 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126723191 165 VIVSSIAAFSPSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVNCLHLD-LSRLASAG 221
Cdd:PRK08415 140 LTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGpIKTLAASG 197
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 33-208 5.27e-08

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 51.56  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVvssrkqqNVDQAVATLQGEGLSVTGTVCHVgkaEDRERLVAMAVKLHGGIDI 112
Cdd:cd05334    2 RVVLVYGGRGALGSAVVQAFKSRGWWVA-------SIDLAENEEADASIIVLDSDSFT---EQAKQVVASVARLSGKVDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVsNAAVNPFFGSLMDVTE-EVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLG 191
Cdd:cd05334   72 LI-CVAGGWAGGSAKSKSFvKNWDLMWKQNLWTSFIASHLATKHL--LSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQ 148

                        170
                 ....*....|....*....
gi 126723191 192 LNNTLAIEL--APRNIRVN 208
Cdd:cd05334  149 LTQSLAAENsgLPAGSTAN 167
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 25-211 6.47e-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: 6.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  25 TRRDPLTNKVaLVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVgkaeDRERLVAMAV 104
Cdd:cd08951    1 TRSPPPMKRI-FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSL----AETRKLADQV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 105 KLHGGIDILVSNAAVnpFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVP---------EMEKRGGGSvviVSSIAAFS- 174
Cdd:cd08951   76 NAIGRFDAVIHNAGI--LSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRpkrliylssGMHRGGNAS---LDDIDWFNr 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 126723191 175 PSPGFSPYNVSKTALLGLNNTLAIelAPRNIRVNCLH 211
Cdd:cd08951  151 GENDSPAYSDSKLHVLTLAAAVAR--RWKDVSSNAVH 185
PRK06196 PRK06196
oxidoreductase; Provisional
 30-211 7.11e-08

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 51.99  E-value: 7.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKqqnVDQAVATLQG-EGLSVTGTvcHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARR---PDVAREALAGiDGVEVVML--DLADLESVRAFAERFLDSGR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDILVSNAAVnpfFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIA-AFSP----SPGFS--- 180
Cdd:PRK06196  99 RIDILINNAGV---MACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGhRRSPirwdDPHFTrgy 175

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 126723191 181 ----PYNVSKTAllglNNTLAIEL----APRNIRVNCLH 211
Cdd:PRK06196 176 dkwlAYGQSKTA----NALFAVHLdklgKDQGVRAFSVH 210
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 31-121 1.80e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 50.40  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTAStDGIGFAIARRLAQDRaHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLhGGI 110
Cdd:PRK06940   1 MKEVVVVIGA-GGIGQAIARRVGAGK-KVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQTL-GPV 77

                         90
                 ....*....|.
gi 126723191 111 DILVSNAAVNP 121
Cdd:PRK06940  78 TGLVHTAGVSP 88
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 36-175 4.09e-07

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: 49.41  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  36 LVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVdqavatlqgeglsvtgtVCHVGKAEDRERLVA-MAVKLHGGIDILV 114
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLREADV-----------------IADLSTPEGRAAAIAdVLARCSGVLDGLV 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126723191 115 SNAAVNPFFGSlmdvteevwDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSP 175
Cdd:cd05328   66 NCAGVGGTTVA---------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGW 117
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 31-182 4.09e-07

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: 50.06  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQD-RAHVVVSSR-----KQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAV 104
Cdd:cd08953  204 PGGVYLVTGGAGGIGRALARALARRyGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVR 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126723191 105 KLHGGIDILVSNAAVnPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRgggsVVIVSSIAAFSPSPGFSPY 182
Cdd:cd08953  284 ERYGAIDGVIHAAGV-LRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDF----FVLFSSVSAFFGGAGQADY 356
PRK05854 PRK05854
SDR family oxidoreductase;
30-119 4.48e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 49.68  E-value: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVA-----------TLQGEGLSVTGTVCHVGK---AED 95
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAairtavpdaklSLRALDLSSLASVAALGEqlrAEG 91

                         90       100
                 ....*....|....*....|....
gi 126723191  96 RErlvamavklhggIDILVSNAAV 119
Cdd:PRK05854  92 RP------------IHLLINNAGV 103
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 33-182 2.29e-06

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: 46.32  E-value: 2.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191    33 KVALVTASTDGIGFAIARRLAQDRA-HVVVSSR---KQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHG 108
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126723191   109 GIDILVsNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVvpemEKRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:smart00822  81 PLTGVI-HAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELT----ADLPLDFFVLFSSIAGVLGSPGQANY 149
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
36-188 2.66e-06

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 47.28  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  36 LVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEglsvtgtvCHVGKAEDRERLVAMAvklhGGIDILVS 115
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVE--------FVRGDLRDPEALAAAL----AGVDAVVH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 116 NAAVnpffgslMDVTEEVWDKTLDINVKApalmTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGF----------SPYNVS 185
Cdd:COG0451   71 LAAP-------AGVGEEDPDETLEVNVEG----TLNLLEAARAAGVKRFVYASSSSVYGDGEGPidedtplrpvSPYGAS 139


                 ...
gi 126723191 186 KTA 188
Cdd:COG0451  140 KLA 142
PRK08416 PRK08416
enoyl-ACP reductase;
32-210 2.87e-06

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 47.07  E-value: 2.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVS--SRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGG 109
Cdd:PRK08416   8 GKTLVISGGTRGIGKAIVYEFAQSGVNIAFTynSNVEEANKIAEDLEQKYGIKAKAYPLNILEPETYKELFKKIDEDFDR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 110 IDILVSNA-----AVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:PRK08416  88 VDFFISNAiisgrAVVGGYTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNLVYIENYAGHGT 167

                        170       180
                 ....*....|....*....|....*.
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK08416 168 SKAAVETMVKYAATELGEKNIRVNAV 193
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 27-203 6.33e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 46.15  E-value: 6.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  27 RDPLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSR--KQQNVDQA-----------VATLQGEGLSVtgTVCHVgKA 93
Cdd:PRK08303   3 MKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRstRARRSEYDrpetieetaelVTAAGGRGIAV--QVDHL-VP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  94 EDRERLVAMAVKLHGGIDILvsnaaVNPFFG--SLMDVTEEVWDKTLD-------INVKAPALMTKAVVPEMEKRGGGSV 164
Cdd:PRK08303  80 EQVRALVERIDREQGRLDIL-----VNDIWGgeKLFEWGKPVWEHSLDkglrmlrLAIDTHLITSHFALPLLIRRPGGLV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 126723191 165 VIVSSIAAFSPSPGF--SP-YNVSKTALLGLNNTLAIELAPR 203
Cdd:PRK08303 155 VEITDGTAEYNATHYrlSVfYDLAKTSVNRLAFSLAHELAPH 196
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 20-192 7.23e-06

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 46.22  E-value: 7.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  20 ASSRMTRRDPLTNKVALVTASTDGIGFAIARRLAQDRA-HVVVSSRKQQN--VDQAVATLQGEGLSVTGTVCHVGKAEDR 96
Cdd:cd05274  138 AALELAAAPGGLDGTYLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAprAAARAALLRAGGARVSVVRCDVTDPAAL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  97 ERLVAmAVKLHGGIDILVsNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVvpemEKRGGGSVVIVSSIAAFSPS 176
Cdd:cd05274  218 AALLA-ELAAGGPLAGVI-HAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELT----PDLPLDFFVLFSSVAALLGG 291

                        170
                 ....*....|....*.
gi 126723191 177 PGFSPYNVSKTALLGL 192
Cdd:cd05274  292 AGQAAYAAANAFLDAL 307
PRK06953 PRK06953
SDR family oxidoreductase;
33-189 1.14e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 44.68  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVdQAVATLQGEGLSVTGTvchvgkaeDRERLVAMAVKLHG-GID 111
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAAL-AALQALGAEALALDVA--------DPASVAGLAWKLDGeALD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNAAV-NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVS---SIAAFSPSPGFSpYNVSKT 187
Cdd:PRK06953  73 AAVYVAGVyGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSrmgSIGDATGTTGWL-YRASKA 151


                 ..
gi 126723191 188 AL 189
Cdd:PRK06953 152 AL 153
PRK06720 PRK06720
hypothetical protein; Provisional
 16-119 4.15e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 42.65  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  16 SVRMASSRMTRRdpLTNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQ---QNVDQAVATLQGEGLSVTgtvCHVGK 92
Cdd:PRK06720   2 TVRLIEGVMKMK--LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQesgQATVEEITNLGGEALFVS---YDMEK 76

                         90       100
                 ....*....|....*....|....*..
gi 126723191  93 AEDRERLVAMAVKLHGGIDILVSNAAV 119
Cdd:PRK06720  77 QGDWQRVISITLNAFSRIDMLFQNAGL 103
PRK07023 PRK07023
SDR family oxidoreductase;
35-189 5.97e-05

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 42.69  E-value: 5.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSRkqqNVDQAVATLQGE-------GLSVTGTVCHVGKAEDRERLVAMAVKLh 107
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVAR---SRHPSLAAAAGErlaevelDLSDAAAAAAWLAGDLLAAFVDGASRV- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 108 ggidILVSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKT 187
Cdd:PRK07023  80 ----LLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKA 155


                 ..
gi 126723191 188 AL 189
Cdd:PRK07023 156 AL 157
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
30-221 6.15e-05

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 43.01  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  30 LTNKVALVTA--STDGIGFAIARrLAQDR-AHVVVSS--RKQQNVDQAVATLQGEG----LSVTgtvchvgkaeDRERLV 100
Cdd:PRK07889   5 LEGKRILVTGviTDSSIAFHVAR-VAQEQgAEVVLTGfgRALRLTERIAKRLPEPApvleLDVT----------NEEHLA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 101 AMAVKL---HGGIDILVSNAAVNP---FFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSsiaaFS 174
Cdd:PRK07889  74 SLADRVrehVDGLDGVVHSIGFAPqsaLGGNFLDAPWEDVATALHVSAYSLKSLAKALLPLMNE--GGSIVGLD----FD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 126723191 175 PSPGFSPYN---VSKTALLGLNNTLAIELAPRNIRVNclhldlsrLASAG 221
Cdd:PRK07889 148 ATVAWPAYDwmgVAKAALESTNRYLARDLGPRGIRVN--------LVAAG 189
PRK06101 PRK06101
SDR family oxidoreductase;
32-207 7.50e-05

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 42.55  E-value: 7.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQ------AVATLQgegLSVTgtvchvgkaeDRERLVAMAVK 105
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDElhtqsaNIFTLA---FDVT----------DHPGTKAALSQ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 106 LHGGIDILVSNAAVNPFFGS-LMDVTeeVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPYNV 184
Cdd:PRK06101  68 LPFIPELWIFNAGDCEYMDDgKVDAT--LMARVFNVNVLGVANCIEGIQPHLSC--GHRVVIVGSIASELALPRAEAYGA 143

                        170       180
                 ....*....|....*....|...
gi 126723191 185 SKTALLGLNNTLAIELAPRNIRV 207
Cdd:PRK06101 144 SKAAVAYFARTLQLDLRPKGIEV 166
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 35-205 1.06e-04

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: 41.74  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  35 ALVTASTDGIGFAIARRLAQDRAHVVVSSRKQqnvdQAVATLQGE--GLSVTGTVCHVGKAEdrerlvAMAVKLhGGIDI 112
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDA----GALAGLAAEvgALARPADVAAELEVW------ALAQEL-GPLDL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 113 LVSnaAVNPFFGS-LMDVTEEVWDKTLDINVKAPALMTKAVVPemEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLG 191
Cdd:cd11730   70 LVY--AAGAILGKpLARTKPAAWRRILDANLTGAALVLKHALA--LLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEA 145

                        170
                 ....*....|....
gi 126723191 192 LNNTLAIELAPRNI 205
Cdd:cd11730  146 YVEVARKEVRGLRL 159
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
88-208 1.97e-04

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 41.66  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  88 CHVGKAEDRERLVAMAVKLHGGIDILVSNAAV---NPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSV 164
Cdd:PRK08159  67 CDVTDEASIDAVFETLEKKWGKLDFVVHAIGFsdkDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLMTD--GGSI 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 126723191 165 VIVSSIAAFSPSPGFSPYNVSKTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08159 145 LTLTYYGAEKVMPHYNVMGVAKAALEASVKYLAVDLGPKNIRVN 188
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 36-208 2.91e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 40.69  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  36 LVTASTDGIGFAIARRLAQDRAHVVVSSRKQQ-NVDQavatlqgegLSVTGTVCHVGKAEDRERLVAMAVKLH---GGID 111
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYpAIDG---------LRQAGAQCIQADFSTNAGIMAFIDELKqhtDGLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 112 ILVSNA----AVNPffgslMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGsvviVSSIAAFSP------SPGFSP 181
Cdd:PRK06483  77 AIIHNAsdwlAEKP-----GAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHA----ASDIIHITDyvvekgSDKHIA 147

                        170       180
                 ....*....|....*....|....*..
gi 126723191 182 YNVSKTALLGLNNTLAIELAPrNIRVN 208
Cdd:PRK06483 148 YAASKAALDNMTLSFAAKLAP-EVKVN 173
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 36-182 3.41e-04

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: 40.24  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191   36 LVTASTDGIGFAIARRLAQDRA-HVVVSSRKQQ---NVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVAMAVKLHGGID 111
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSAAprpDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126723191  112 ILVsNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVvpemEKRGGGSVVIVSSIAAFSPSPGFSPY 182
Cdd:pfam08659  84 GVI-HAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEAT----PDEPLDFFVLFSSIAGLLGSPGQANY 149
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
24-210 3.94e-04

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 40.31  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  24 MTRRDPLTNKVALVT--ASTDGIGFAIARRLAQDRAHVVV---SSRKQQNVDQAVATLQGEGLsvtgTVCHVGKAEDRER 98
Cdd:PRK07533   2 MQPLLPLAGKRGLVVgiANEQSIAWGCARAFRALGAELAVtylNDKARPYVEPLAEELDAPIF----LPLDVREPGQLEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  99 LVAMAVKLHGGIDILVSNAAVNP---FFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMekRGGGSVVIVSSIAAFSP 175
Cdd:PRK07533  78 VFARIAEEWGRLDFLLHSIAFAPkedLHGRVVDCSREGFALAMDVSCHSFIRMARLAEPLM--TNGGSLLTMSYYGAEKV 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 126723191 176 SPGfspYNV---SKTALLGLNNTLAIELAPRNIRVNCL 210
Cdd:PRK07533 156 VEN---YNLmgpVKAALESSVRYLAAELGPKGIRVHAI 190
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
32-208 4.85e-04

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 40.10  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  32 NKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQ---QNVDQAVATLQGEGLSVTGtvCHVGKAEDRERLVAMAVKLHG 108
Cdd:PRK08594   9 TYVVMGVANKRSIAWGIARSLHNAGAKLVFTYAGErleKEVRELADTLEGQESLLLP--CDVTSDEEITACFETIKEEVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191 109 GIDIL---VSNAAVNPFFGSLMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKrgGGSVVIVSSIAAFSPSPGFSPYNVS 185
Cdd:PRK08594  87 VIHGVahcIAFANKEDLRGEFLETSRDGFLLAQNISAYSLTAVAREAKKLMTE--GGSIVTLTYLGGERVVQNYNVMGVA 164

                        170       180
                 ....*....|....*....|...
gi 126723191 186 KTALLGLNNTLAIELAPRNIRVN 208
Cdd:PRK08594 165 KASLEASVKYLANDLGKDGIRVN 187
PRK07102 PRK07102
SDR family oxidoreductase;
33-171 8.18e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 39.52  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  33 KVALVTASTDgIGFAIARRLAQDRAHVVVSSRKQQNVDQAVATLQGEGlsVTGTVCHVGKAEDRERLVAMAVKLHGGIDI 112
Cdd:PRK07102   3 KILIIGATSD-IARACARRYAAAGARLYLAARDVERLERLADDLRARG--AVAVSTHELDILDTASHAAFLDSLPALPDI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126723191 113 LVSnaavnpFFGSLMDVT--EEVWDKTL---DINVKAPALMTKAVVPEMEKRGGGSVVIVSSIA 171
Cdd:PRK07102  80 VLI------AVGTLGDQAacEADPALALrefRTNFEGPIALLTLLANRFEARGSGTIVGISSVA 137
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 34-207 8.33e-04

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 39.51  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191   34 VALVTASTDGIGFAIARRLAQ----DRAHVVVSSRKQQNVDQAVATLQGE--GLSVTGTVCHVGKAEDRERLVAmAVKLH 107
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLK-ALREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  108 GGID-----ILVSNAavnpffGSLMDVTE---EVWDKTL-----DINVKAPALMTKAVVPEMEKRGGGSVVIV--SSIAA 172
Cdd:TIGR01500  81 PRPKglqrlLLINNA------GTLGDVSKgfvDLSDSTQvqnywALNLTSMLCLTSSVLKAFKDSPGLNRTVVniSSLCA 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 126723191  173 FSPSPGFSPYNVSKTALLGLNNTLAIELAPRNIRV 207
Cdd:TIGR01500 155 IQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRV 189
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 31-119 9.16e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 39.62  E-value: 9.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126723191  31 TNKVALVTASTDGIGFAIARRLAQDRAHVVVSSRKQQNVDQAVA-----------TLQGEGLSVTGTVchvgkaedreRL 99
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAAritaatpgadvTLQELDLTSLASV----------RA 84

                         90       100
                 ....*....|....*....|.
gi 126723191 100 VAMAVKL-HGGIDILVSNAAV 119
Cdd:PRK06197  85 AADALRAaYPRIDLLINNAGV 105
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 33-76 5.80e-03

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic 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: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 36.98  E-value: 5.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 126723191  33 KVALVTASTDGIGFAIARRLAQ-----DRAHVVVSSRKQQNVDQAVATL 76
Cdd:cd08941    2 KVVLVTGANSGLGLAICERLLAeddenPELTLILACRNLQRAEAACRAL 50
 
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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