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Conserved domains on  [gi|42570969|ref|NP_973558|]
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senescence-associated gene 13 [Arabidopsis thaliana]

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 ...
 12-204 2.37e-112

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 cd05329:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 251  Bit Score: 321.71  E-value: 2.37e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  12 RWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  92 YQGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPL 193
 
Name Accession Description Interval E-value
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 12-204 2.37e-112

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: 321.71  E-value: 2.37e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  12 RWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  92 YQGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPL 193
PRK09242 PRK09242
SDR family oxidoreductase;
11-205 2.28e-76

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 230.79  E-value: 2.28e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   11 SRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK--GFQVTTSVCDVSSRDQRVKLMETV 88
Cdd:PRK09242   3 HRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEfpEREVHGLAADVSDDEDRRAILDWV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   89 SSLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYG 168
Cdd:PRK09242  83 EDHW-DGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYG 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK09242 162 MTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLT 198
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 14-210 1.04e-62

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: 195.77  E-value: 1.04e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:COG1028  82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42570969 174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:COG1028 162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLG 198
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 19-211 1.10e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 188.59  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERL-GRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 42570969   179 RNLACEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTDMTKELRED 193
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
 17-204 2.37e-35

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 125.56  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:TIGR01963   1 GKTALVTGAASGIGLAIARALAAAGANVVVNDFGEEGAEAAAKVAGDAGGSVIYLPADVTKEDEIADMIAAAAAEF-GGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:TIGR01963  80 DILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAKHGLIG 159

                         170       180
                  ....*....|....*....|....*...
gi 42570969   177 LARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:TIGR01963 160 LTKVLALEVAEHGITVNAICPGYVRTPL 187
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 19-179 1.41e-14

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 69.05  E-value: 1.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969     19 TALVTGGSKGIGEAVVEELAMLGA-KVHTCAR---DETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE-G 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969     95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPL-LKAsgsgsIVLISSAAGVvhvnVGSI----YGA 169
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLpLDF-----FVLFSSIAGV----LGSPgqanYAA 151

                          170
                   ....*....|
gi 42570969    170 TKGAMNQLAR 179
Cdd:smart00822 152 ANAFLDALAE 161
 
Name Accession Description Interval E-value
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 12-204 2.37e-112

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: 321.71  E-value: 2.37e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  12 RWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  92 YQGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPL 193
PRK09242 PRK09242
SDR family oxidoreductase;
11-205 2.28e-76

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 230.79  E-value: 2.28e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   11 SRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK--GFQVTTSVCDVSSRDQRVKLMETV 88
Cdd:PRK09242   3 HRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEfpEREVHGLAADVSDDEDRRAILDWV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   89 SSLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYG 168
Cdd:PRK09242  83 EDHW-DGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYG 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK09242 162 MTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLT 198
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 14-210 1.04e-62

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: 195.77  E-value: 1.04e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:COG1028  82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42570969 174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:COG1028 162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLG 198
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 20-212 1.13e-62

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: 195.20  E-value: 1.13e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQErLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNIL 99
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAE-LAAIEALGGNAVAVQADVSDEEDVEALVEEALEEF-GRLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLAR 179
Cdd:cd05233  79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 180 NLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd05233 159 SLALELAPYGIRVNAVAPGLVDTPMLAKLGPEE 191
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 19-211 1.10e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 188.59  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERL-GRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 42570969   179 RNLACEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTDMTKELRED 193
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
14-211 4.81e-56

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 178.91  E-value: 4.81e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARF- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:COG0300  81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42570969 174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:COG0300 161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAP 198
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 14-211 2.80e-53

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: 171.13  E-value: 2.80e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDEtqlqERLREWQAK-GFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRA----ERLEALAAElGGRALAVPLDVTDEAAVEAAVAAAVAEF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:COG4221  78 -GRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKA 156

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42570969 173 AMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:COG4221 157 AVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDG 195
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
14-203 1.69e-51

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 166.87  E-value: 1.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHvNVG-SIYGATKG 172
Cdd:PRK05653  81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTG-NPGqTNYSAAKA 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK05653 160 GVIGFTKALALELASRGITVNAVAPGFIDTD 190
PRK12826 PRK12826
SDR family oxidoreductase;
14-208 1.96e-46

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 153.92  E-value: 1.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQ-RVKLMETVSSLy 92
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAAlKAAVAAGVEDF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSI-YGATK 171
Cdd:PRK12826  82 -GRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPGLAhYAASK 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNL 197
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 15-202 1.90e-45

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 151.53  E-value: 1.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKV--HTcARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVviAY-DINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK05565  82 -GKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKG 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK05565 161 AVNAFTKALAKELAPSGIRVNAVAPGAIDT 190
FabG-like PRK07231
SDR family oxidoreductase;
15-205 5.00e-45

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 150.37  E-value: 5.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERF-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTS-IFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK07231  81 SVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLL 192
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 14-212 6.29e-44

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: 147.86  E-value: 6.29e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK-GFQVTTSVCDVSSRDQRVKLMETVSSlY 92
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQK-D 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  93 QGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVhVNVG---SIYGA 169
Cdd:cd05352  84 FGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTI-VNRPqpqAAYNA 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42570969 170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd05352 163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKEL 205
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 27-208 5.15e-43

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: 144.88  E-value: 5.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    27 KGIGEAVVEELAMLGAKVHTCARDETqLQERLREWqAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNILVNNVGTS 106
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEA-LAKRVEEL-AEELGAAVLPCDVTDEEQVEALVAAAVEKF-GRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   107 --IFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSgsIVLISSAAGVVHVNVGSIYGATKGAMNQLARNLACE 184
Cdd:pfam13561  83 pkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGS--IVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160

                         170       180
                  ....*....|....*....|....
gi 42570969   185 WASDNIRTNSVCPWYITTPLSNDV 208
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGI 184
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 14-212 3.30e-42

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 143.03  E-value: 3.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVViNYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHvNVG-SIYGATK 171
Cdd:PRK05557  82 -GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMG-NPGqANYAASK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:PRK05557 160 AGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDV 200
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 14-203 4.12e-42

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 143.09  E-value: 4.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVvHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHvNVG-SIYGATK 171
Cdd:PRK12825  83 -GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPG-WPGrSNYAAAK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK12825 161 AGLVGLTKALARELAEYGITVNMVAPGDIDTD 192
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 14-203 1.28e-40

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 139.42  E-value: 1.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREwqAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAAR--LPGAKVTATVADVADPAQVERVFDTAVERF- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGtsIFKPTT---EYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSG-SIVLISSAAGVVHVNVGSIYGA 169
Cdd:PRK12829  85 GGLDVLVNNAG--IAGPTGgidEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGRTPYAA 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK12829 163 SKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGP 196
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 14-222 2.27e-40

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: 138.26  E-value: 2.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDF- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSaagvVHVNVGSI----YGA 169
Cdd:cd05347  81 GKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICS----LLSELGGPpvpaYAA 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42570969 170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVR--PKF--IFLLRTMKNK 222
Cdd:cd05347 157 SKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVadPEFndDILKRIPAGR 213
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 19-211 2.98e-38

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: 132.67  E-value: 2.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSlYQGKLNI 98
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEA-EFGPVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKAsGSGSIVLISSAAGVVHvNVGSI-YGATKGAMNQ 176
Cdd:cd05333  81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQaVIRAMIKR-RSGRIINISSVVGLIG-NPGQAnYAASKAGVIG 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 42570969 177 LARNLACEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:cd05333 159 FTKSLAKELASRGITVNAVAPGFIDTDMTDALPEK 193
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 17-203 3.07e-37

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: 130.47  E-value: 3.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAF-GRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:cd05344  80 DILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159

                       170       180
                ....*....|....*....|....*..
gi 42570969 177 LARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:cd05344 160 LVKTLSRELAPDGVTVNSVLPGYIDTE 186
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 17-203 1.50e-36

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 128.14  E-value: 1.50e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK----GFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEanasGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:cd08939  81 -GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKF 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 42570969 173 AMNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:cd08939 160 ALRGLAESLRQELKPYNIRVSVVYPPDTDTP 190
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 14-211 4.60e-36

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: 127.11  E-value: 4.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDE---TQLQERLREwQAKGFQVttsvcDVSSRDQRVKLMETVSS 90
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDeegQAAAAELGD-AARFFHL-----DVTDEDGWTAVVDTARE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  91 LYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:cd05341  76 AF-GRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNAS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42570969 171 KGAMNQLARNLA--CEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:cd05341 155 KGAVRGLTKSAAleCATQGYGIRVNSVHPGYIYTPMTDELLIA 197
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 15-205 8.64e-36

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 126.98  E-value: 8.64e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERF-G 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLISSAAGVV---HVNVGSI-YGA 169
Cdd:PRK08213  89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQaVAKRSMIPRGYGRIINVASVAGLGgnpPEVMDTIaYNT 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK08213 169 SKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMT 204
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
 17-204 2.37e-35

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 125.56  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:TIGR01963   1 GKTALVTGAASGIGLAIARALAAAGANVVVNDFGEEGAEAAAKVAGDAGGSVIYLPADVTKEDEIADMIAAAAAEF-GGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:TIGR01963  80 DILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAKHGLIG 159

                         170       180
                  ....*....|....*....|....*...
gi 42570969   177 LARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:TIGR01963 160 LTKVLALEVAEHGITVNAICPGYVRTPL 187
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 20-202 7.94e-35

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: 124.00  E-value: 7.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVViNYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERF-GRLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:cd05359  80 LVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALV 159

                       170       180
                ....*....|....*....|....
gi 42570969 179 RNLACEWASDNIRTNSVCPWYITT 202
Cdd:cd05359 160 RYLAVELGPRGIRVNAVSPGVIDT 183
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 15-204 1.39e-34

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 123.84  E-value: 1.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETF-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:PRK12429  81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  175 NQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK12429 161 IGLTKVVALEGATHGVTVNAICPGYVDTPL 190
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
14-197 1.84e-34

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 129.58  E-value: 1.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQrVKLMETVSSLYQ 93
Cdd:PRK08324 419 PLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAA-VQAAFEEAALAF 496

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS-GSIVLISSAAGVV-HVNVGSiYGATK 171
Cdd:PRK08324 497 GGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNpGPNFGA-YGAAK 575

                        170       180
                 ....*....|....*....|....*.
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK08324 576 AAELHLVRQLALELGPDGIRVNGVNP 601
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 20-212 5.77e-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: 121.08  E-value: 5.77e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVttsVCDVSSRDQRVKLMETVSSLYqGKLNIL 99
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGL---AGDVRDEADVRRAVDAMEEAF-GGLDAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLAR 179
Cdd:cd08929  79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSE 158

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 180 NLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd08929 159 AAMLDLREANIRVVNVMPGSVDTGFAGSPEGQA 191
PRK07326 PRK07326
SDR family oxidoreductase;
14-210 5.90e-34

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 121.66  E-value: 5.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK07326  81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGAAYNASKFG 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK07326 160 LVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPS 196
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 14-209 1.72e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 120.94  E-value: 1.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVhtCARDETQ--LQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATI--VFNDINQelVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGtsIFK--PTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGA 169
Cdd:PRK07097  85 V-GVIDILVNNAG--IIKriPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:PRK07097 162 AKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLR 201
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 19-212 1.99e-33

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: 120.41  E-value: 1.99e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAkgfQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLND---NLEVLELDVTDEESIKAAVKEVIERF-GRIDV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:cd05374  78 LVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALS 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 42570969 179 RNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd05374 158 ESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSA 191
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 15-209 4.41e-33

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: 119.57  E-value: 4.41e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLME-TVSSLyq 93
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVErTVEAL-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:cd08934  79 GRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFG 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42570969 174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:cd08934 159 VNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHIT 194
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 20-202 1.08e-32

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


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 118.44  E-value: 1.08e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLME-TVSSLyqGKLNI 98
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKaTVSQF--GGITI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKP-TTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQL 177
Cdd:cd05365  80 LVNNAGGGGPKPfDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHM 159

                       170       180
                ....*....|....*....|....*
gi 42570969 178 ARNLACEWASDNIRTNSVCPWYITT 202
Cdd:cd05365 160 TRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK06124 PRK06124
SDR family oxidoreductase;
11-202 1.57e-32

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 118.28  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   11 SRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSS 90
Cdd:PRK06124   5 QRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 LYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:PRK06124  85 EH-GRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAA 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  171 KGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK06124 164 KQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 15-206 1.77e-32

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: 118.28  E-value: 1.77e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGF---QVTTSVCDVSS-RDQRVKLMETVSS 90
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVsekKILLVVADLTEeEGQDRIISTTLAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  91 LyqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASgSGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:cd05364  81 F--GRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT-KGEIVNVSSVAGGRSFPGVLYYCIS 157

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42570969 171 KGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSN 206
Cdd:cd05364 158 KAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 13-210 4.07e-32

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 117.13  E-value: 4.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHT----CARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETV 88
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   89 SSlYQGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLISSAAGVVHVNVGSIY 167
Cdd:PRK12827  82 VE-EFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQaALPPMIRARRGGRIVNIASVAGVRGNRGQVNY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAP 203
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 14-209 6.91e-32

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 116.61  E-value: 6.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK12939   4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAAL- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIV-LISSAAGVVHVNVGSiYGATKG 172
Cdd:PRK12939  83 GGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVnLASDTALWGAPKLGA-YVASKG 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVP 198
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 15-204 1.16e-31

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 115.84  E-value: 1.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKV---HTCARDETQlqERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVvvnYASSKAAAE--EVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  92 YqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKasGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:cd05362  79 F-GGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR--DGGRIINISSSLTAAYTPNYGAYAGSK 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05362 156 AAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 13-197 1.83e-31

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: 115.27  E-value: 1.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:cd08942   2 FSVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  93 QgKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS----GSIVLISSAAGVVHVNVGSI-Y 167
Cdd:cd08942  81 D-RLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGLENYsY 159

                       170       180       190
                ....*....|....*....|....*....|
gi 42570969 168 GATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:cd08942 160 GASKAAVHQLTRKLAKELAGEHITVNAIAP 189
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 20-204 3.46e-31

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: 114.32  E-value: 3.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDE-----TQLQERLREWQAKGFQvttsvCDVSSRDQRVKLMETVSSLYqG 94
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAILDRNEnpgaaAELQAINPKVKATFVQ-----CDVTSWEQLAAAFKKAIEKF-G 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  95 KLNILVNNVGtsIFKPTTEYTAEDFSF----VMATNLESAFHLSQLAHPLLKAS---GSGSIVLISSAAGVVHVNVGSIY 167
Cdd:cd05323  77 RVDILINNAG--ILDEKSYLFAGKLPPpwekTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLYPAPQFPVY 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42570969 168 GATKGAMNQLARNLACEWASD-NIRTNSVCPWYITTPL 204
Cdd:cd05323 155 SASKHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL 192
PRK06172 PRK06172
SDR family oxidoreductase;
15-202 3.54e-31

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 114.85  E-value: 3.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSsRDQRVK-LMETVSSLYq 93
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVT-RDAEVKaLVEQTIAAY- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPT-TEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK06172  83 GRLDYAFNNAGIEIEQGRlAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKH 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK06172 163 AVIGLTKSAAIEYAKKGIRVNAVCPAVIDT 192
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 14-208 3.72e-31

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: 114.49  E-value: 3.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAkgfqVTTSVCDVSSRDQRVKLMETVsslyq 93
Cdd:cd05351   4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG----IEPVCVDLSDWDATEEALGSV----- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASG-SGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:cd05351  75 GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTKA 154

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42570969 173 AMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:cd05351 155 ALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDN 190
PRK07814 PRK07814
SDR family oxidoreductase;
12-202 3.87e-31

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 114.88  E-value: 3.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   12 RWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:PRK07814   5 RFRLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPL-LKASGSGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:PRK07814  85 F-GRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLmLEHSGGGSVINISSTMGRLAGRGFAAYGTA 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  171 KGAMNQLARNLACEWASdNIRTNSVCPWYITT 202
Cdd:PRK07814 164 KAALAHYTRLAALDLCP-RIRVNAIAPGSILT 194
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 15-205 4.03e-31

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 114.50  E-value: 4.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTC-ARDETQLQErLREwqaKGfqVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLyNSAENEAKE-LRE---KG--VFTIKCDVGNRDQVKKSKEVVEKEF- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVG-SIYGATKG 172
Cdd:PRK06463  78 GRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGtTFYAITKA 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK06463 158 GIIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 19-206 4.84e-31

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: 113.49  E-value: 4.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGA-KVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLN 97
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKY-GGLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSI--FKPTTEyTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVhvnvGSIYGATKGAMN 175
Cdd:cd05324  81 ILVNNAGIAFkgFDDSTP-TREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSL----TSAYGVSKAALN 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 42570969 176 QLARNLACEWASDNIRTNSVCPWYITTPLSN 206
Cdd:cd05324 156 ALTRILAKELKETGIKVNACCPGWVKTDMGG 186
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 13-204 6.40e-31

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: 114.02  E-value: 6.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTsvcDVSSRDQRVKLMETVSSLY 92
Cdd:cd05345   1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQA---DVTKRADVEAMVEAALSKF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  93 qGKLNILVNNVG-TSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVvHVNVGSI-YGAT 170
Cdd:cd05345  78 -GRLDILVNNAGiTHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGL-RPRPGLTwYNAS 155

                       170       180       190
                ....*....|....*....|....*....|....
gi 42570969 171 KGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05345 156 KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL 189
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 15-209 7.93e-31

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: 113.63  E-value: 7.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCAR-DETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEF- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLA-HPLLKASGSGSIVLISSAAGVV----HVNvgsiYG 168
Cdd:cd05358  80 GTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAiKRFRKSKIKGKIINMSSVHEKIpwpgHVN----YA 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42570969 169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:cd05358 156 ASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAW 196
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 19-220 7.98e-31

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: 113.49  E-value: 7.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSlYQGKLNI 98
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKK-EVGDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:cd05339  80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42570969 179 RNLACEWAS---DNIRTNSVCPWYITTPLSNDVRPKFIFLLRTMK 220
Cdd:cd05339 160 ESLRLELKAygkPGIKTTLVCPYFINTGMFQGVKTPRPLLAPILE 204
PRK06484 PRK06484
short chain dehydrogenase; Validated
 17-203 9.58e-31

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 118.03  E-value: 9.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLqERLRE--------WQAkgfqvttsvcDVSSRDQRVKLMETV 88
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGA-KKLAEalgdehlsVQA----------DITDEAAVESAFAQI 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   89 SSLYqGKLNILVNNVGTS-IFKPTTEYTAEDFSFVMATNLESAFHLSQLAhpLLKASGSGSIVLISSAAGVVHVNVGSIY 167
Cdd:PRK06484 338 QARW-GRLDVLVNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAA--ARLMSQGGVIVNLGSIASLLALPPRNAY 414

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK06484 415 CASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETP 450
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
11-207 9.78e-31

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 113.68  E-value: 9.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   11 SRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKV----HTCARDETQlqerlREWQAKGFQVTTSVCDVSSRDQRVKLME 86
Cdd:PRK06935   9 DFFSLDGKVAIVTGGNTGLGQGYAVALAKAGADIiittHGTNWDETR-----RLIEKEGRKVTFVQVDLTKPESAEKVVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   87 TVSSLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSA---AGVVHVnv 163
Cdd:PRK06935  84 EALEEF-GKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMlsfQGGKFV-- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 42570969  164 gSIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITT----PLSND 207
Cdd:PRK06935 161 -PAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTantaPIRAD 207
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 14-208 1.07e-30

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 113.25  E-value: 1.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNEL- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK07666  83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFG 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK07666 163 VLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDL 197
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
15-204 1.32e-30

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 113.36  E-value: 1.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETqLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKE-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSI-YGATKGA 173
Cdd:PRK08226  82 RIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVADPGETaYALTKAA 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK08226 162 IVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 15-206 1.71e-30

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


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 113.06  E-value: 1.71e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQE---RLRE-WQAKGFQVTTsvcDVSSRDQRVKLMETVSS 90
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEvksECLElGAPSPHVVPL---DMSDLEDAEQVVEEALK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  91 LYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:cd05332  78 LF-GGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAAS 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42570969 171 KGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSN 206
Cdd:cd05332 157 KHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAM 192
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 19-209 2.16e-30

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 113.02  E-value: 2.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:cd08945   5 VALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARY-GPIDV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ--LAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:cd08945  84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKevLKAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 177 LARNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:cd08945 164 FTKALGLELARTGITVNAVCPGFVETPMAASVR 196
PRK07856 PRK07856
SDR family oxidoreductase;
14-205 3.26e-30

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 112.33  E-value: 3.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQlqerlrewQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK07856   3 DLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPE--------TVDGRPAEFHAADVRDPDQVAALVDAIVERH- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKA-SGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK07856  74 GRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSGRRPSPGTAAYGAAKA 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  173 AMNQLARNLACEWASDnIRTNSVCPWYITTPLS 205
Cdd:PRK07856 154 GLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQS 185
PRK06484 PRK06484
short chain dehydrogenase; Validated
 20-204 3.91e-30

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 116.49  E-value: 3.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLrewQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNIL 99
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERA---DSLGPDHHALAMDVSDEAQIREGFEQLHREF-GRIDVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  100 VNNVGTS--IFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSG-SIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:PRK06484  84 VNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGaAIVNVASGAGLVALPKRTAYSASKAAVIS 163

                        170       180
                 ....*....|....*....|....*...
gi 42570969  177 LARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06484 164 LTRSLACEWAAKGIRVNAVLPGYVRTQM 191
PRK06181 PRK06181
SDR family oxidoreductase;
17-202 6.02e-30

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 111.61  E-value: 6.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARF-GGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTA-EDFSFVMATNLESAFHLSQLAHPLLKASgSGSIVLISSAAGVVHVNVGSIYGATKGAMN 175
Cdd:PRK06181  80 DILVNNAGITMWSRFDELTDlSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHALH 158

                        170       180
                 ....*....|....*....|....*..
gi 42570969  176 QLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK06181 159 GFFDSLRIELADDGVAVTVVCPGFVAT 185
PRK07063 PRK07063
SDR family oxidoreductase;
15-207 9.11e-30

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 111.30  E-value: 9.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK--GFQVTTSVCDVSSRDQ-RVKLMETVSSL 91
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDvaGARVLAVPADVTDAASvAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 yqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSaagvVHVNvgSI----- 166
Cdd:PRK07063  85 --GPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIAS----THAF--KIipgcf 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42570969  167 -YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK07063 157 pYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTED 198
PRK06138 PRK06138
SDR family oxidoreductase;
15-204 1.51e-29

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 110.63  E-value: 1.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGG-RAFARQGDVGSAEAVEALVDFVAARW-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  175 NQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 14-204 1.60e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 110.52  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDET--QLQERLREWQAKGFqvttsVCDVSSRDQRVKLMETVSSL 91
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDvaEVAAQLLGGNAKGL-----VCDVSDSQSVEAAVAAVISA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:PRK06841  87 F-GRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASK 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06841 166 AGVVGMTKVLALEWGPYGITVNAISPTVVLTEL 198
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 15-211 3.23e-29

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: 109.40  E-value: 3.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQ------------LQERLREWQAKGFQVTTSVCDVSSRDQRV 82
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEgdngsakslpgtIEETAEEIEAAGGQALPIVVDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  83 KLMETVSSLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVN 162
Cdd:cd05338  81 ALVEATVDQF-GRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42570969 163 VGSIYGATKGAMNQLARNLACEWASDNIRTNSVCP-WYITTPLSNDVRPK 211
Cdd:cd05338 160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPsTAIETPAATELSGG 209
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 10-204 5.90e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 108.65  E-value: 5.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   10 NSRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSvCDVSSRDQRVKLmetvs 89
Cdd:PRK07060   2 NMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRLDVG-DDAAIRAALAAA----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   90 slyqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLISSAAGVVHVNVGSIYG 168
Cdd:PRK07060  76 ----GAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARhVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYC 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK07060 152 ASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 13-197 5.96e-29

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 109.33  E-value: 5.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 W-SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQ-ERLREWQakgfqvttsvCDVSSRDQRVKLMETVSS 90
Cdd:PRK06171   4 WlNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQhENYQFVP----------TDVSSAEEVNHTVAEIIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 LYqGKLNILVNNVGTSIFK---------PTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHV 161
Cdd:PRK06171  74 KF-GRIDGLVNNAGINIPRllvdekdpaGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGS 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  162 NVGSIYGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK06171 153 EGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAP 188
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 17-197 6.25e-29

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: 108.63  E-value: 6.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTsVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALGV-QCDVTSEAQVQSAFEQAVLEF-GGL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSI-YGATKGAMN 175
Cdd:cd08943  79 DIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAaYSAAKAAEA 158

                       170       180
                ....*....|....*....|..
gi 42570969 176 QLARNLACEWASDNIRTNSVCP 197
Cdd:cd08943 159 HLARCLALEGGEDGIRVNTVNP 180
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 15-204 7.82e-29

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: 108.35  E-value: 7.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVcdvsSRDQRVKLMETVSSLYQG 94
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDV----TDEQQVAALFERAVEEFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  95 KLNILVNNVG-TSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:cd08944  77 GLDLLVNNAGaMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 42570969 174 MNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd08944 157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPL 187
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 15-204 2.50e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 108.20  E-value: 2.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQ-LQERLREWQAKGFQVTTSVCDVSSRDQ-RVKLMETVSSLy 92
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLIPGDVSDEAFcKDAVEETVREL- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEY-TAEDFSFVMATNLESAFHLSQLAHPLLKaSGSgSIVlissaagvvhvNVGSI----- 166
Cdd:PRK06701 123 -GRLDILVNNAAFQYPQQSLEDiTAEQLDKTFKTNIYSYFHMTKAALPHLK-QGS-AII-----------NTGSItgyeg 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42570969  167 ------YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06701 189 netlidYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL 232
PRK06500 PRK06500
SDR family oxidoreductase;
15-204 3.44e-28

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 106.96  E-value: 3.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWqakGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAEL---GESALVIRADAGDVAAQKALAQALAEAF-G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLkASGSgSIVLISSaagvVHVNVG----SIYGAT 170
Cdd:PRK06500  80 RLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL-ANPA-SIVLNGS----INAHIGmpnsSVYAAS 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  171 KGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06500 154 KAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPL 187
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
19-210 3.67e-28

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 106.77  E-value: 3.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKV-------HTCARDeTQLQERLREWQAKGFQVttSVCDVSSRDQRVKLMETvssl 91
Cdd:PRK12824   4 IALVTGAKRGIGSAIARELLNDGYRViatyfsgNDCAKD-WFEEYGFTEDQVRLKEL--DVTDTEECAEALAEIEE---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YQGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:PRK12824  77 EEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAK 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK12824 157 AGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGP 195
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 19-205 3.67e-28

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: 105.91  E-value: 3.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDetqlQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRN----PEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRF-GRIDV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:cd08932  77 LVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALA 156

                       170       180
                ....*....|....*....|....*..
gi 42570969 179 RNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:cd08932 157 HALRQEGWDHGVRVSAVCPGFVDTPMA 183
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 17-204 6.86e-28

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 106.38  E-value: 6.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKV-----HTCARDETQLQERLREWqakGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIvlngfGDAAEIEAVRAGLAAKH---GVKVLYHGADLSKPAAIEDMVAYAQRQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  92 YqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:cd08940  79 F-GGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAK 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd08940 158 HGVVGLTKVVALETAGTGVTCNAICPGWVLTPL 190
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 15-202 7.22e-28

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 106.08  E-value: 7.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKL-G 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTtEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGV-VHVNVGSiYGATKGA 173
Cdd:PRK06113  88 KVDILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAEnKNINMTS-YASSKAA 165

                        170       180
                 ....*....|....*....|....*....
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK06113 166 ASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 17-214 8.14e-28

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: 106.15  E-value: 8.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQlQERLREW---QAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEK-GEEAAAEikkETGNAKVEVIQLDLSSLASVRQFAEEFLARF- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGtsIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVV---------HVNVG 164
Cdd:cd05327  79 PRLDILINNAG--IMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAgpidfndldLENNK 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42570969 165 S-----IYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKFIF 214
Cdd:cd05327 157 EyspykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLL 211
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 15-209 9.04e-28

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: 105.62  E-value: 9.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWqakGFQVTTSV-CDVSSRDQRVKLMETVSSLYq 93
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAEL---GDPDISFVhCDVTVEADVRAAVDTAVARF- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTT--EYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:cd05326  78 GRLDIMFNNAGVLGAPCYSilETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASK 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42570969 172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:cd05326 158 HAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGF 195
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 15-197 2.05e-27

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 104.59  E-value: 2.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSV-CDVSSRDQrvkLMETVSSLYQ 93
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIqCDVRDPEA---VEAAVDETLK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 --GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHP-LLKASGSGSIVLISS------AAGVVHVnvg 164
Cdd:cd05369  78 efGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKrLIEAKHGGSILNISAtyaytgSPFQVHS--- 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 165 siyGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:cd05369 155 ---AAAKAGVDALTRSLAVEWGPYGIRVNAIAP 184
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 18-209 2.21e-27

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: 104.67  E-value: 2.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  18 MTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKgFQVTTSVC--DVSSRDQRVKLMETVSSLYQgK 95
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAK-FPVKVLPLqlDVSDRESIEAALENLPEEFR-D 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  96 LNILVNNVGTSI-FKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:cd05346  79 IDILVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 42570969 175 NQLARNLACEWASDNIRTNSVCPWYITTPLSNdVR 209
Cdd:cd05346 159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEFSL-VR 192
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 14-204 2.52e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 104.98  E-value: 2.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERF- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHP-LLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK13394  83 GSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKhMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKH 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK13394 163 GLLGLARVLAKEGAKHNVRSHVVCPGFVRTPL 194
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 14-220 2.65e-27

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: 103.93  E-value: 2.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDEtqlqERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYQ 93
Cdd:cd05370   2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRRE----ERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 gKLNILVNNVGT----SIFKPTTeyTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGA 169
Cdd:cd05370  78 -NLDILINNAGIqrpiDLRDPAS--DLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCA 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42570969 170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKFIFLLRTMK 220
Cdd:cd05370 155 TKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKMP 205
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 13-204 4.44e-27

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 104.08  E-value: 4.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK07523   6 FDLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK07523  86 -GPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKG 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK07523 165 AVGNLTKGMATDWAKHGLQCNAIAPGYFDTPL 196
PRK06949 PRK06949
SDR family oxidoreductase;
15-207 5.05e-27

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 104.07  E-value: 5.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKG---FQVTTSVCDVSSRDQRVKLMETVSsl 91
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGgaaHVVSLDVTDYQSIKAAVAHAETEA-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 yqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLL-KASGSGS------IVLISSAAGVVHVNV 163
Cdd:PRK06949  85 --GTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQeVAKRMIaRAKGAGNtkpggrIINIASVAGLRVLPQ 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42570969  164 GSIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK06949 163 IGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHH 206
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 19-212 5.19e-27

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: 103.70  E-value: 5.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCA-RDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLN 97
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDlPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDF-GRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSIFKPTT--EYTAEDFSFVMATNLESAFHLSQ------LAHPLLKASGSGSIVLISS-AAGVVHVNVGSiYG 168
Cdd:cd05337  82 CLVNNAGIAVRPRGDllDLTEDSFDRLIAINLRGPFFLTQavarrmVEQPDRFDGPHRSIIFVTSiNAYLVSPNRGE-YC 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42570969 169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd05337 161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKY 204
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 14-203 6.89e-27

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 103.34  E-value: 6.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTsvCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGG--IDLVDPQAARRAVDEVNRQF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK12828  81 GRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAG 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK12828 161 VARLTEALAAELLDRGITVNAVLPSIIDTP 190
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 20-204 1.39e-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: 102.55  E-value: 1.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVcdvSSRDQRVKLMETVsslyqGKLNIL 99
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRLTPLDVADAA---AVREVCSRLLAEH-----GPIDAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS-AAGVVHVNVGSiYGATKGAMNQLA 178
Cdd:cd05331  73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASnAAHVPRISMAA-YGASKAALASLS 151

                       170       180
                ....*....|....*....|....*.
gi 42570969 179 RNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05331 152 KCLGLELAPYGVRCNVVSPGSTDTAM 177
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 17-203 1.61e-26

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: 102.16  E-value: 1.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQErlrewQAKGFQVTTSVCDVSSRDQRVKLMETVsslyqGKL 96
Cdd:cd05368   2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKE-----LERGPGITTRVLDVTDKEQVAALAKEE-----GRI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGS-IYGATKGAMN 175
Cdd:cd05368  72 DVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRfVYSTTKAAVI 151

                       170       180
                ....*....|....*....|....*...
gi 42570969 176 QLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:cd05368 152 GLTKSVAADFAQQGIRCNAICPGTVDTP 179
PRK06398 PRK06398
aldose dehydrogenase; Validated
 15-204 1.99e-26

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 102.60  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETqlqerlREWQAKGFQvttsvCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEP------SYNDVDYFK-----VDVSNKEQVIKGIDYVISKY-G 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:PRK06398  72 RIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  175 NQLARNLACEWASdNIRTNSVCPWYITTPL 204
Cdd:PRK06398 152 LGLTRSIAVDYAP-TIRCVAVCPGSIRTPL 180
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 20-215 3.78e-26

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: 101.25  E-value: 3.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQrVKLMETVSSLYQGKLNIL 99
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEER-NQLVIAELEAELGGLDLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLAR 179
Cdd:cd05350  80 IINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAE 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42570969 180 NLACEWASDNIRTNSVCPWYITTPLSNDVRPKFIFL 215
Cdd:cd05350 160 SLRYDVKKRGIRVTVINPGFIDTPLTANMFTMPFLM 195
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 20-212 3.88e-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: 101.14  E-value: 3.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK-GFQVTTSVCDVSSRDQRVK-LMETVSSLYQGkln 97
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKyGVETKTIAADFSAGDDIYErIEKELEGLDIG--- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSIFKPT--TEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMN 175
Cdd:cd05356  81 ILVNNVGISHSIPEyfLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42570969 176 QLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd05356 161 FFSRALYEEYKSQGIDVQSLLPYLVATKMSKIRKSSL 197
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 16-204 4.51e-26

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: 101.46  E-value: 4.51e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  16 GGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSV-CDVSSR-DQRVKLMETVSSLyq 93
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVpCDVTKEeDIKTLISVTVERF-- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASgSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:cd08933  86 GRIDCLVNNAGWhPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS-QGNIINLSSLVGSIGQKQAAPYVATKG 164

                       170       180       190
                ....*....|....*....|....*....|..
gi 42570969 173 AMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd08933 165 AITAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 14-213 5.19e-26

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 101.23  E-value: 5.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERL-REWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLvNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS----AAGVVHVNvgsiYG 168
Cdd:PRK12935  83 -GKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSiigqAGGFGQTN----YS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL----SNDVRPKFI 213
Cdd:PRK12935 158 AAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMvaevPEEVRQKIV 206
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 17-203 1.11e-25

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: 100.29  E-value: 1.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETqLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:cd08937   4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSEL-VHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERF-GRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVGTSIF-KPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAA--GVVHVNvgsiYGATKGA 173
Cdd:cd08937  82 DVLINNVGGTIWaKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIYRIP----YSAAKGG 157

                       170       180       190
                ....*....|....*....|....*....|
gi 42570969 174 MNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:cd08937 158 VNALTASLAFEHARDGIRVNAVAPGGTEAP 187
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 22-212 1.16e-25

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: 99.76  E-value: 1.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  22 VTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNILVN 101
Cdd:cd05360   5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERF-GRIDTWVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 102 NVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLARNL 181
Cdd:cd05360  84 NAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESL 163

                       170       180       190
                ....*....|....*....|....*....|...
gi 42570969 182 ACEWASD--NIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd05360 164 RAELAHDgaPISVTLVQPTAMNTPFFGHARSYM 196
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 14-207 1.51e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 100.00  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGvvhVNVG----SIYG 168
Cdd:PRK07478  82 GGLDIAFNNAGTlGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVG---HTAGfpgmAAYA 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK07478 159 ASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRA 197
PRK05867 PRK05867
SDR family oxidoreductase;
13-204 1.75e-25

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 99.72  E-value: 1.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK05867   5 FDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLISSAAGVVhVNVG---SIYG 168
Cdd:PRK05867  85 -GGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQaAAKAMVKQGQGGVIINTASMSGHI-INVPqqvSHYC 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK05867 163 ASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 14-204 3.10e-25

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 99.42  E-value: 3.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCAR-DETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLA-HPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:PRK08936  84 -GTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAiKYFVEHDIKGNIINMSSVHEQIPWPLFVHYAASK 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK08936 163 GGVKLMTETLAMEYAPKGIRVNNIGPGAINTPI 195
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 13-197 4.43e-25

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 98.80  E-value: 4.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERlrewQAKGFQVttSVCDVSSRDQRVKLMETVSsly 92
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDY----PFATFVL--DVSDAAAVAQVCQRLLAET--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS-AAGVVHVNVGSiYGATK 171
Cdd:PRK08220  75 -GPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSnAAHVPRIGMAA-YGASK 152

                        170       180
                 ....*....|....*....|....*.
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK08220 153 AALTSLAKCVGLELAPYGVRCNVVSP 178
PRK07774 PRK07774
SDR family oxidoreductase;
15-211 4.66e-25

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 98.66  E-value: 4.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAF-G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNvgTSIF---KPTTEYTA--EDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHvnvGSIYGA 169
Cdd:PRK07774  83 GIDYLVNN--AAIYggmKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLY---SNFYGL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:PRK07774 158 AKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPK 199
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 20-205 1.05e-24

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: 97.37  E-value: 1.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLG-AKVHTCARDETQLQErLREWQAKGFQVTTSVCDVSSRDQrvKLMETVSSLYQ-GKLN 97
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATE-LAALGASHSRLHILELDVTDEIA--ESAEAVAERLGdAGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAagvvhvnVGSI---------- 166
Cdd:cd05325  78 VLINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSR-------VGSIgdntsggwys 150

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42570969 167 YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:cd05325 151 YRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMG 189
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 8-205 1.08e-24

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: 97.61  E-value: 1.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   8 GENSRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMET 87
Cdd:cd08936   1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  88 VSSLYqGKLNILVNNVGTSIFKPTT-EYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSI 166
Cdd:cd08936  81 AVNLH-GGVDILVSNAAVNPFFGNIlDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGP 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42570969 167 YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:cd08936 160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFS 198
PRK07035 PRK07035
SDR family oxidoreductase;
14-197 1.35e-24

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 97.39  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERH- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTS-IFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK07035  84 GRLDILVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKA 163

                        170       180
                 ....*....|....*....|....*
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK07035 164 AVISMTKAFAKECAPFGIRVNALLP 188
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 19-204 1.43e-24

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: 97.45  E-value: 1.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARD-ETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLN 97
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNlEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKF-GSFD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAH-PLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:cd05366  83 VMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAArQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVRG 162

                       170       180
                ....*....|....*....|....*...
gi 42570969 177 LARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05366 163 LTQTAAQELAPKGITVNAYAPGIVKTEM 190
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 15-204 1.52e-24

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 97.33  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWqakGFQVTTSVCDVSSR-DQRVKLMETVSSLyq 93
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF---GDHVLVVEGDVTSYaDNQRAVDQTVDAF-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVG-----TSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYG 168
Cdd:PRK06200  79 GKLDCFVGNAGiwdynTSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGGGGPLYT 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  169 ATKGAMNQLARNLACEWASDnIRTNSVCPWYITTPL 204
Cdd:PRK06200 158 ASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDL 192
PRK06114 PRK06114
SDR family oxidoreductase;
13-217 1.80e-24

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 97.16  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVhTC--ARDETQLQERLREWQAKGFQVTTSVCDVSSR-DQRVKLMETVS 89
Cdd:PRK06114   4 FDLDGQVAFVTGAGSGIGQRIAIGLAQAGADV-ALfdLRTDDGLAETAEHIEAAGRRAIQIAADVTSKaDLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   90 SLyqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVhVNVG---SI 166
Cdd:PRK06114  83 EL--GALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGII-VNRGllqAH 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42570969  167 YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNdvRPKFIFLLR 217
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNT--RPEMVHQTK 208
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 14-198 4.68e-24

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 96.23  E-value: 4.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDE---TQLQERLrewqakGFQVTTSVCDVSSRDQRVKLMETVSS 90
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDAdngAAVAASL------GERARFIATDITDDAAIERAVATVVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 LYqGKLNILVNNVGTSIfKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:PRK08265  77 RF-GRVDILVNLACTYL-DDGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGG-GAIVNFTSISAKFAQTGRWLYPAS 153

                        170       180
                 ....*....|....*....|....*....
gi 42570969  171 KGAMNQLARNLACEWASDNIRTNSVCP-W 198
Cdd:PRK08265 154 KAAIRQLTRSMAMDLAPDGIRVNSVSPgW 182
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 15-204 4.71e-24

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: 96.36  E-value: 4.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDET-QLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYQ 93
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNV-------GTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHV-NVGs 165
Cdd:cd09763  81 GRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLfNVA- 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42570969 166 iYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd09763 160 -YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTEL 197
PRK07069 PRK07069
short chain dehydrogenase; Validated
 20-204 5.71e-24

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 95.55  E-value: 5.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAK-GFQVTTS-VCDVSSRDQRVKLMETVSSLYQGkL 96
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFlTDINDAAGLDAFAAEINAAhGEGVAFAaVQDVTDEAQWQALLAQAADAMGG-L 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:PRK07069  81 SVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVAS 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  177 LARNLA--CEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK07069 161 LTKSIAldCARRGLDVRCNSIHPTFIRTGI 190
PRK08628 PRK08628
SDR family oxidoreductase;
21-204 7.81e-24

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 95.41  E-value: 7.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDE--TQLQERLREWQAKGFQVTTsvcDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK08628  11 IVTGGASGIGAAISLRLAEEGAIPVIFGRSApdDEFAEELRALQPRAEFVQV---DLTDDAQCRDAVEQTVAKF-GRIDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIfKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK08628  87 LVNNAGVND-GVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTSGYAAAKGAQLALT 164

                        170       180
                 ....*....|....*....|....*.
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK08628 165 REWAVALAKDGVRVNAVIPAEVMTPL 190
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
20-208 8.33e-24

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 95.56  E-value: 8.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNIL 99
Cdd:PRK08643   5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTF-GDLNVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASG-SGSIVLISSAAGVVHvNVG-SIYGATKGAMNQL 177
Cdd:PRK08643  84 VNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINATSQAGVVG-NPElAVYSSTKFAVRGL 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 42570969  178 ARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK08643 163 TQTAARDLASEGITVNAYAPGIVKTPMMFDI 193
PRK08589 PRK08589
SDR family oxidoreductase;
19-208 9.04e-24

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 95.62  E-value: 9.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVhTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK08589   8 VAVITGASTGIGQASAIALAQEGAYV-LAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQF-GRVDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYGATKGAMNQL 177
Cdd:PRK08589  86 LFNNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAADLYRSGYNAAKGAVINF 164

                        170       180       190
                 ....*....|....*....|....*....|.
gi 42570969  178 ARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK08589 165 TKSIAIEYGRDGIRANAIAPGTIETPLVDKL 195
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 17-174 1.15e-23

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: 94.84  E-value: 1.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDetqlQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:COG3967   5 GNTILITGGTSGIGLALAKRLHARGNTVIITGRR----EEKLEEAAAANPGLHTIVLDVADPASIAALAEQVTAEF-PDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVGtsIFKP----TTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:COG3967  80 NVLINNAG--IMRAedllDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKA 157


                ..
gi 42570969 173 AM 174
Cdd:COG3967 158 AL 159
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 15-204 2.07e-23

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: 94.67  E-value: 2.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREW-QAKGFQVTTSVCDVSSRD--QRVkLMETVSS 90
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAiNYLPEEEDDAEETKKLiEEEGRKCLLIPGDLGDESfcRDL-VKEVVKE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  91 LyqGKLNILVNNVGTSIFKPTTEY-TAEDFSFVMATNLESAFHLSQLAHPLLKaSGSgSIVLISSaagvVHVNVGSI--- 166
Cdd:cd05355 103 F--GKLDILVNNAAYQHPQESIEDiTTEQLEKTFRTNIFSMFYLTKAALPHLK-KGS-SIINTTS----VTAYKGSPhll 174

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42570969 167 -YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05355 175 dYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPL 213
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 14-208 2.64e-23

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: 94.45  E-value: 2.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQF- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVGTSIFKPTT--------------EYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGsGSIVLISSAAGV 158
Cdd:cd08935  81 GTVDILINGAGGNHPDATTdpehyepeteqnffDLDEEGWEFVFDLNLNGSFLPSQvFGKDMLEQKG-GSIINISSMNAF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42570969 159 VHVNVGSIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:cd08935 160 SPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKL 209
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 17-197 3.04e-23

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 93.86  E-value: 3.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDEtQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSE-LVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAF-GRI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSI-FKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAA--GVVHVNvgsiYGATKGA 173
Cdd:PRK12823  86 DVLINNVGGTIwAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIAtrGINRVP----YSAAKGG 161

                        170       180
                 ....*....|....*....|....
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK12823 162 VNALTASLAFEYAEHGIRVNAVAP 185
PRK07201 PRK07201
SDR family oxidoreductase;
12-190 3.87e-23

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 96.94  E-value: 3.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   12 RWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:PRK07201 366 RGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAE 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGTSIFKPTTEYT--AEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGA 169
Cdd:PRK07201 446 H-GHVDYLVNNAGRSIRRSVENSTdrFHDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYVA 524

                        170       180
                 ....*....|....*....|.
gi 42570969  170 TKGAMNQLARNLACEWASDNI 190
Cdd:PRK07201 525 SKAALDAFSDVAASETLSDGI 545
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 14-209 4.20e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 94.99  E-value: 4.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEEL- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK07109  84 GPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHA 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 42570969  174 MNQLARNLACEWASD--NIRTNSVCPWYITTPLSNDVR 209
Cdd:PRK07109 164 IRGFTDSLRCELLHDgsPVSVTMVQPPAVNTPQFDWAR 201
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-206 1.95e-22

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 91.71  E-value: 1.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCA-RDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAkKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSgsIVLISSAAGVVHVNVGSIYGATK 171
Cdd:PRK06077  82 Y-GVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGGA--IVNIASVAGIRPAYGLSIYGAMK 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  172 GAMNQLARNLACEWASdNIRTNSVCPWYITTPLSN 206
Cdd:PRK06077 159 AAVINLTKYLALELAP-KIRVNAIAPGFVKTKLGE 192
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 10-202 2.09e-22

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 91.42  E-value: 2.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  10 NSRWSlgGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSV-CDVSSRDQRVKLMETV 88
Cdd:cd05343   1 MERWR--GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYqCDLSNEEQILSMFSAI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  89 SSLYQGkLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASG--SGSIVLISSAAG--VVHVNVG 164
Cdd:cd05343  79 RTQHQG-VDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGhrVPPVSVF 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42570969 165 SIYGATKGAMNQLARNLACE--WASDNIRTNSVCPWYITT 202
Cdd:cd05343 158 HFYAATKHAVTALTEGLRQElrEAKTHIRATSISPGLVET 197
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 17-197 3.30e-22

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: 90.86  E-value: 3.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGF-QVTTSVCDVSSRDQRVKLMETVSSLYqGK 95
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESYLEKF-GR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  96 LNILVNNVGTSIF---KPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVV----------HVN 162
Cdd:cd08930  81 IDILINNAYPSPKvwgSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIapdfriyentQMY 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 42570969 163 VGSIYGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:cd08930 161 SPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISP 195
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 19-209 7.35e-22

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 90.04  E-value: 7.35e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLG--AKVHTCARDETQLQERLREWQAkGFQVTTSVCDVSSRDQRVKLMETVSSLyQGKL 96
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIRKL-DGER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS-GSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:cd05367  79 DLLINNAGSlGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 42570969 175 NQLARNLACEwaSDNIRTNSVCPWYITTPLSNDVR 209
Cdd:cd05367 159 DMFFRVLAAE--EPDVRVLSYAPGVVDTDMQREIR 191
PRK12743 PRK12743
SDR family oxidoreductase;
19-212 1.44e-21

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 89.32  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMET-VSSLyqGKL 96
Cdd:PRK12743   4 VAIVTASDSGIGKACALLLAQQGFDIGiTWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKlIQRL--GRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLA-HPLLKASGSGSIVLISSaagvVHVN---VGSI-YGATK 171
Cdd:PRK12743  82 DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAaRHMVKQGQGGRIINITS----VHEHtplPGASaYTAAK 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPLSN----DVRPKF 212
Cdd:PRK12743 158 HALGGLTKAMALELVEHGILVNAVAPGAIATPMNGmddsDVKPDS 202
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 17-209 1.49e-21

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 90.02  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLL-GHV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHP-LLKASGSGSIVLISSAAGVVHvNVG-SIYGATKGAM 174
Cdd:PRK05876  85 DVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrLLEQGTGGHVVFTASFAGLVP-NAGlGAYGVAKYGV 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  175 NQLARNLACEWASDNIRTNSVCPWYITTPL-SNDVR 209
Cdd:PRK05876 164 VGLAETLAREVTADGIGVSVLCPMVVETNLvANSER 199
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 20-207 1.53e-21

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 89.03  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK12937   8 AIVTGASRGIGAAIARRLAADGFAVAvNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF-GRIDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKAsgSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK12937  87 LVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQ--GGRIINLSTSVIALPLPGYGPYAASKAAVEGLV 164

                        170       180
                 ....*....|....*....|....*....
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK12937 165 HVLANELRGRGITVNAVAPGPVATELFFN 193
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 18-212 2.55e-21

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 88.87  E-value: 2.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAiNDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAW-GRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFK--PTTEYTAEDFSFVMATNLESAFHLSQ------LAHPLLKASGSGSIVLISSA-AGVVHVNVGSiY 167
Cdd:PRK12745  82 DCLVNNAGVGVKVrgDLLDLTPESFDRVLAINLRGPFFLTQavakrmLAQPEPEELPHRSIVFVSSVnAIMVSPNRGE-Y 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:PRK12745 161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKY 205
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 19-211 3.37e-21

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: 87.85  E-value: 3.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGA-KVHTCARDETQLQERLREWQAKgfqVTTSVCDVSsrDQrvklmETVSSLYQG--K 95
Cdd:cd05354   5 TVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDK---VVPLRLDVT--DP-----ESIKAAAAQakD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  96 LNILVNNVGtsIFKPTTEYTAEDFS---FVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:cd05354  75 VDVVINNAG--VLKPATLLEEGALEalkQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKS 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42570969 173 AMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV-RPK 211
Cdd:cd05354 153 AAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAgGPK 192
PRK07062 PRK07062
SDR family oxidoreductase;
15-195 4.12e-21

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 88.56  E-value: 4.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQL---QERLReWQAKGFQVTTSVCDVSSRDQRVKLMETVSSL 91
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLasaEARLR-EKFPGARLLAARCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGV---VHVNVGSiyg 168
Cdd:PRK07062  85 F-GGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALqpePHMVATS--- 160

                        170       180
                 ....*....|....*....|....*..
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSV 195
Cdd:PRK07062 161 AARAGLLNLVKSLATELAPKGVRVNSI 187
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
20-195 6.35e-21

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 87.47  E-value: 6.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAK-VHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK08063   7 ALVTGSSRGIGKAIALRLAEEGYDiAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEF-GRLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS-AAGVVHVNVGSIyGATKGAMNQL 177
Cdd:PRK08063  86 FVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSlGSIRYLENYTTV-GVSKAALEAL 164

                        170
                 ....*....|....*...
gi 42570969  178 ARNLACEWASDNIRTNSV 195
Cdd:PRK08063 165 TRYLAVELAPKGIAVNAV 182
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 15-200 7.84e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 87.32  E-value: 7.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERF-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAgVVHVNVG-SIYGATKG 172
Cdd:PRK07890  82 RVDALVNNAFRvPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMV-LRHSQPKyGAYKMAKG 159

                        170       180
                 ....*....|....*....|....*...
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYI 200
Cdd:PRK07890 160 ALLAASQSLATELGPQGIRVNSVAPGYI 187
PRK08267 PRK08267
SDR family oxidoreductase;
21-211 7.88e-21

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 87.69  E-value: 7.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKgfQVTTSVCDVSSRDQRVKLMETVSSLYQGKLNILV 100
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAG--NAWTGALDVTDRAAWDAALADFAAATGGRLDVLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  101 NNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLARN 180
Cdd:PRK08267  83 NNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEA 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  181 LACEWASDNIRTNSVCPWYITTPL----SNDVRPK 211
Cdd:PRK08267 163 LDLEWRRHGIRVADVMPLFVDTAMldgtSNEVDAG 197
PRK09072 PRK09072
SDR family oxidoreductase;
15-207 8.98e-21

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 87.30  E-value: 8.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQRVKLMEtVSSLYQG 94
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPG-RHRWVVADLTSEAGREAVLA-RAREMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 kLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIvlissaagvvhVNVGSIYG------ 168
Cdd:PRK09072  81 -INVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMV-----------VNVGSTFGsigypg 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42570969  169 -----ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK09072 149 yasycASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNSE 192
PRK07074 PRK07074
SDR family oxidoreductase;
19-203 1.14e-20

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 87.13  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFqvTTSVCDVSSrDQRVKLMETVSSLYQGKLNI 98
Cdd:PRK07074   4 TALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARF--VPVACDLTD-AASLAAALANAAAERGPVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVvHVNVGSIYGATKGAMNQLA 178
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGM-AALGHPAYSAAKAGLIHYT 159

                        170       180
                 ....*....|....*....|....*
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK07074 160 KLLAVEYGRFGIRANAVAPGTVKTQ 184
PRK05866 PRK05866
SDR family oxidoreductase;
15-204 1.76e-20

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 87.10  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRI-G 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTA--EDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS---AAGVvhVNVGSIYGA 169
Cdd:PRK05866 117 GVDILINNAGRSIRRPLAESLDrwHDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwgvLSEA--SPLFSVYNA 194

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK05866 195 SKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK05650 PRK05650
SDR family oxidoreductase;
21-209 1.95e-20

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 86.63  E-value: 1.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   21 LVTGGSKGIGEAVVEELAMLGAKVhtCARD--ETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYQGkLNI 98
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRL--ALADvnEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGG-IDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK05650  81 IVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALS 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:PRK05650 161 ETLLVELADDEIGVHVVCPSFFQTNLLDSFR 191
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 17-205 2.36e-20

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: 86.19  E-value: 2.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTC-ARDETQLQERLREWQAKGFQvttsvCDVSSRDQRVKLMETVSSLYqGK 95
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVILdLPNSPGETVAKLGDNCRFVP-----VDVTSEKDVKAALALAKAKF-GR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  96 LNILVNNVGTSI------FKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKA----SGS--GSIVLISSAAGVvhvnV 163
Cdd:cd05371  76 LDIVVNCAGIAVaaktynKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKnepdQGGerGVIINTASVAAF----E 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42570969 164 GSI----YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:cd05371 152 GQIgqaaYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLL 197
PRK08264 PRK08264
SDR family oxidoreductase;
14-208 3.65e-20

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 85.33  E-value: 3.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGA-KVHTCARDetqlqerLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLy 92
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAaKVYAAARD-------PESVTDLGPRVVPLQLDVTDPASVAAAAEAASDV- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qgklNILVNNVGtsIFKPTT---EYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGA 169
Cdd:PRK08264  75 ----TILVNNAG--IFRTGSlllEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSA 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK08264 149 SKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGL 187
PRK12746 PRK12746
SDR family oxidoreductase;
14-205 1.16e-19

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 84.32  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHT-CARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 Q-----GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKAsgSGSIVLISSAAGVVHVNVGSIY 167
Cdd:PRK12746  83 QirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRA--EGRVINISSAEVRLGFTGSIAY 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDIN 198
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 15-203 1.28e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 84.19  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDET-QLQERLREWQAkgfqvttsvcDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK06523   7 LAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRPdDLPEGVEFVAA----------DLTTAEGCAAVARAVLERL- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIfKPTTEYTA---EDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSI-YGA 169
Cdd:PRK06523  76 GGVDILVHVLGGSS-APAGGFAAltdEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPESTTaYAA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK06523 155 AKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 15-212 1.29e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 84.29  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAK-VHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAF- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS-GSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK06198  83 GRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:PRK06198 163 ALATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIQREF 202
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 10-205 1.63e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 84.04  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   10 NSRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVS 89
Cdd:PRK08085   2 NDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   90 SlYQGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGA 169
Cdd:PRK08085  82 K-DIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK08085 161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
PRK07832 PRK07832
SDR family oxidoreductase;
18-209 2.00e-19

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 83.94  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVC-DVSSRDQRVKLMETVSSLYqGKL 96
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAH-GSM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMN 175
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIEtFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLR 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  176 QLARNLACEWASDNIRTNSVCPWYITTPLSNDVR 209
Cdd:PRK07832 160 GLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVE 193
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 21-204 2.17e-19

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 83.72  E-value: 2.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQ--AKGFQVTTSVCDVSSRDQ-RVKLMETVSSLyqGKLN 97
Cdd:cd05330   7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLeiAPDAEVLLIKADVSDEAQvEAYVDATVEQF--GRID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSIFK-PTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:cd05330  85 GFFNNAGIEGKQnLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVG 164

                       170       180
                ....*....|....*....|....*...
gi 42570969 177 LARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd05330 165 LTRNSAVEYGQYGIRINAIAPGAILTPM 192
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 15-197 2.24e-19

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 83.85  E-value: 2.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEF-G 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:PRK07576  86 PIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISAPQAFVPMPMQAHVCAAKAGV 164

                        170       180
                 ....*....|....*....|...
gi 42570969  175 NQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK07576 165 DMLTRTLALEWGPEGIRVNSIVP 187
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 15-205 3.84e-19

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: 82.78  E-value: 3.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQErLRewQAKGFQVTTSVCDVSS-RDQRVKLMETVSSLyq 93
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAE-LR--ADFGDAVVGVEGDVRSlADNERAVARCVERF-- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVG-----TSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYG 168
Cdd:cd05348  77 GKLDCFIGNAGiwdysTSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGGGPLYT 155

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42570969 169 ATKGAMNQLARNLACEWASdNIRTNSVCPWYITTPLS 205
Cdd:cd05348 156 ASKHAVVGLVKQLAYELAP-HIRVNGVAPGGMVTDLR 191
PRK08219 PRK08219
SDR family oxidoreductase;
18-209 4.33e-19

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 82.29  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELAMlGAKVHTCARDetqlQERLREWQAKGFQVTTSVCDVSSRDqrvKLMETVSSLyqGKLN 97
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP-THTLLLGGRP----AERLDELAAELPGATPFPVDLTDPE---AIAAAVEQL--GRLD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   98 ILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGvVHVNVG-SIYGATKGAMNQ 176
Cdd:PRK08219  74 VLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAG-LRANPGwGSYAASKFALRA 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  177 LARNLACEWAsDNIRTNSVCPWYITTPLSNDVR 209
Cdd:PRK08219 152 LADALREEEP-GNVRVTSVHPGRTDTDMQRGLV 183
PRK05855 PRK05855
SDR family oxidoreductase;
11-202 4.51e-19

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 85.03  E-value: 4.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   11 SRWSLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSS 90
Cdd:PRK05855 309 PRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRA 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 LYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS-GSIVLISSAAGVVHVNVGSIYGA 169
Cdd:PRK05855 389 EH-GVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRSLPAYAT 467

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK05855 468 SKAAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK09730 PRK09730
SDR family oxidoreductase;
19-207 5.46e-19

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 82.21  E-value: 5.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSlYQGKLN 97
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAvNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQ-HDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   98 ILVNNVGTSIFKPTTE-YTAEDFSFVMATNLESAF-----HLSQLAHpllKASGSG-SIVLISSAAGVV-----HVNvgs 165
Cdd:PRK09730  82 ALVNNAGILFTQCTVEnLTAERINRVLSTNVTGYFlccreAVKRMAL---KHGGSGgAIVNVSSAASRLgapgeYVD--- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42570969  166 iYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK09730 156 -YAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHAS 196
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 15-204 5.85e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 82.47  E-value: 5.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREwqAKGFQVTTsvcDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADE--VGGLFVPT---DVTDEDAVNALFDTAAETY-G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSifkPTTEYTAEDFSF-----VMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSI-YG 168
Cdd:PRK06057  79 SVDIAFNNAGIS---PPEDDSILNTGLdawqrVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIsYT 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06057 156 ASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPL 191
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 15-197 1.75e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 81.24  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQ---ERLREwqAKGFQVTTSVCDVSSRDQRVKLMETVssl 91
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEalaADLRA--AHGVDVAVHALDLSSPEAREQLAAEA--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 yqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGvVHVNVGSIYGAT- 170
Cdd:PRK06125  80 --GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAG-ENPDADYICGSAg 156

                        170       180
                 ....*....|....*....|....*..
gi 42570969  171 KGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK06125 157 NAALMAFTRALGGKSLDDGVRVVGVNP 183
PRK07454 PRK07454
SDR family oxidoreductase;
19-204 2.12e-18

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 80.77  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK07454   8 RALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQF-GCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS-AAGVVHVNVGSiYGATKGAMNQL 177
Cdd:PRK07454  87 LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSiAARNAFPQWGA-YCVSKAALAAF 165

                        170       180
                 ....*....|....*....|....*..
gi 42570969  178 ARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK07454 166 TKCLAEEERSHGIRVCTITLGAVNTPL 192
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
15-212 3.59e-18

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 80.46  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKlmETVSSLyqG 94
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVA--AAVERF--G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK07067  80 GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQaVARHMVEQGRGGKIINMASQAGRRGEALVSHYCATKAA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:PRK07067 160 VISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVDALF 198
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 21-204 5.06e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 80.08  E-value: 5.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDetqlQERLREWQAK-GFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNIL 99
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARD----TATLADLAEKyGDRLLPLALDVTDRAAVFAAVETAVEHF-GRLDIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLAR 179
Cdd:PRK08263  82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSE 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  180 NLACEWASDNIRTNSVCP------WY-----ITTPL 204
Cdd:PRK08263 162 ALAQEVAEFGIKVTLVEPggystdWAgtsakRATPL 197
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 22-206 5.11e-18

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: 79.42  E-value: 5.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  22 VTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKgfQVTTSVCDVSSRDQRVKLMETVSSLYQGKLNILVN 101
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAE--NVVAGALDVTDRAAWAAALADFAAATGGRLDALFN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 102 NVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLARNL 181
Cdd:cd08931  83 NAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEAL 162

                       170       180
                ....*....|....*....|....*
gi 42570969 182 ACEWASDNIRTNSVCPWYITTPLSN 206
Cdd:cd08931 163 DVEWARHGIRVADVWPWFVDTPILT 187
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 19-197 5.26e-18

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 80.08  E-value: 5.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKV-------HTCARDETQLQERLREWQAKGFQvttsvCDVSSRDQRVKLMETVSSL 91
Cdd:PRK12384   4 VAVVIGGGQTLGAFLCHGLAEEGYRVavadinsEKAANVAQEINAEYGEGMAYGFG-----ADATSEQSVLALSRGVDEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAF----HLSQLahpLLKASGSGSIVLISSAAGVVHVNVGSIY 167
Cdd:PRK12384  79 F-GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFlcarEFSRL---MIRDGIQGRIIQINSKSGKVGSKHNSGY 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK12384 155 SAAKFGGVGLTQSLALDLAEYGITVHSLML 184
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 19-214 5.93e-18

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: 79.42  E-value: 5.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERL-REWQAKGFQVTTsvcDVSSRDQRVKLMETVsSLYQGKLN 97
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVaAEAGERAIAIQA---DVRDRDQVQAMIEEA-KNHFGPVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNN-VGTSIFKPTTEYTA-----EDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS---AAGVVHVNVgsiYG 168
Cdd:cd05349  78 TIVNNaLIDFPFDPDQRKTFdtidwEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTnlfQNPVVPYHD---YT 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42570969 169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKFIF 214
Cdd:cd05349 155 TAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPKEVF 200
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 14-197 6.68e-18

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 79.94  E-value: 6.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK08277   7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDF- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEY---------------TAEDFSFVMATNLESAFHLSQL-AHPLLKASGsGSIVLISSAAG 157
Cdd:PRK08277  86 GPCDILINGAGGNHPKATTDNefhelieptktffdlDEEGFEFVFDLNLLGTLLPTQVfAKDMVGRKG-GNIINISSMNA 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 42570969  158 VVHVNVGSIYGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK08277 165 FTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAP 204
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 15-210 1.26e-17

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 78.85  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDF-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGtsIF-----------KPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS-GSIVLISSAAgvVHVN 162
Cdd:PRK08217  82 QLNGLINNAG--ILrdgllvkakdgKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSkGVIINISSIA--RAGN 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 42570969  163 VG-SIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK08217 158 MGqTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKP 206
PRK09135 PRK09135
pteridine reductase; Provisional
 20-197 1.31e-17

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 78.82  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKV----HTCARDETQLQERLRewQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGK 95
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVaihyHRSAAEADALAAELN--ALRPGSAAALQADLLDPDALPELVAACVAAF-GR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   96 LNILVNNvgTSIFKPT--TEYTAEDFSFVMATNLESAFHLSQLAHPLLKASgSGSIVLISSaagvVHVNVG----SIYGA 169
Cdd:PRK09135  86 LDALVNN--ASSFYPTplGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVNITD----IHAERPlkgyPVYCA 158

                        170       180
                 ....*....|....*....|....*...
gi 42570969  170 TKGAMNQLARNLACEWASDnIRTNSVCP 197
Cdd:PRK09135 159 AKAALEMLTRSLALELAPE-VRVNAVAP 185
PRK06182 PRK06182
short chain dehydrogenase; Validated
 19-174 1.44e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 78.85  E-value: 1.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDetqlQERLREWQAKGfqVTTSVCDVSSRDQRVKLMETVSSlYQGKLNI 98
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQGYTVYGAARR----VDKMEDLASLG--VHPLSLDVTDEASIKAAVDTIIA-EEGRIDV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:PRK06182  78 LVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFAL 153
PRK12742 PRK12742
SDR family oxidoreductase;
17-210 1.94e-17

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 77.88  E-value: 1.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKV-HTCARDETQLQERLREWQAKGFQVttsvcDVSSRDQrvkLMETVSSlyQGK 95
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVrFTYAGSKDAAERLAQETGATAVQT-----DSADRDA---VIDVVRK--SGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   96 LNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAhpLLKASGSGSIVLISSAAG-VVHVNVGSIYGATKGAM 174
Cdd:PRK12742  76 LDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEA--ARQMPEGGRIIIIGSVNGdRMPVAGMAAYAASKSAL 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  175 NQLARNLACEWASDNIRTNSVCPwyitTPLSNDVRP 210
Cdd:PRK12742 154 QGMARGLARDFGPRGITINVVQP----GPIDTDANP 185
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 15-211 2.27e-17

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 78.03  E-value: 2.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVhtcARDETQLqERLREWQAK-GFQVTTSVCDVSSRDQRVKLMETVSSLYQ 93
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIV---GLHGTRV-EKLEALAAElGERVKIFPANLSDRDEVKALGQKAEADLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GkLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLS-QLAHPLLKASgSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK12936  80 G-VDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTrELTHPMMRRR-YGRIINITSVVGVTGNPGQANYCASKA 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPK 211
Cdd:PRK12936 158 GMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDK 196
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 19-210 3.04e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 78.02  E-value: 3.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLrewqakgfQVTTSVCDVSSRDQRVKLMETVSSLyQGKLNI 98
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIP--------GVELLELDVTDDASVQAAVDEVIAR-AGRIDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK06179  77 LVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGYS 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTPL-SNDVRP 210
Cdd:PRK06179 157 ESLDHEVRQFGIRVSLVEPAYTKTNFdANAPEP 189
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 14-197 4.23e-17

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 77.36  E-value: 4.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKV---------HTCARDETQLQERLREWQAKGFQvttSVCDVSSRDQRVKL 84
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVvvndlggdrKGSGKSSSAADKVVDEIKAAGGK---AVANYDSVEDGEKI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  85 METVSSLYqGKLNILVNNVGT---SIFKPTTEytaEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGvVHV 161
Cdd:cd05353  79 VKTAIDAF-GRVDILVNNAGIlrdRSFAKMSE---EDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAG-LYG 153

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42570969 162 NVG-SIYGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:cd05353 154 NFGqANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP 190
PLN02253 PLN02253
xanthoxin dehydrogenase
 15-205 5.40e-17

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 77.56  E-value: 5.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVhtCARD-ETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKV--CIVDlQDDLGQNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKF- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSiFKPTTE---YTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVvhvnVGSI---- 166
Cdd:PLN02253  93 GTLDIMVNNAGLT-GPPCPDirnVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASA----IGGLgpha 167

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  167 YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PLN02253 168 YTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA 206
PRK06128 PRK06128
SDR family oxidoreductase;
8-204 8.76e-17

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 77.21  E-value: 8.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    8 GENSRWSLG---GMTALVTGGSKGIGEAVVEELAMLGAKV--HTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRV 82
Cdd:PRK06128  43 GEQSYKGFGrlqGRKALITGADSGIGRATAIAFAREGADIalNYLPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCR 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   83 KLME-TVSSLyqGKLNILVNNVGTSIF-KPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS----GSIVLISSAA 156
Cdd:PRK06128 123 QLVErAVKEL--GGLDILVNIAGKQTAvKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGASiintGSIQSYQPSP 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 42570969  157 GVVHvnvgsiYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06128 201 TLLD------YASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 17-197 1.18e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 76.26  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLM-ETVSSLyqGK 95
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVeQIDEKF--GR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   96 LNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLI------SSAAGVVHVnvgsiyG 168
Cdd:PRK07677  79 IDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQaVGKYWIEKGIKGNIINMvatyawDAGPGVIHS------A 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  169 ATKGAMNQLARNLACEWASD-NIRTNSVCP 197
Cdd:PRK07677 153 AAKAGVLAMTRTLAVEWGRKyGIRVNAIAP 182
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
20-210 1.20e-16

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 76.20  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKVHT-CARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK12938   6 AYVTGGMGGIGTSICQRLHKDGFKVVAgCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEV-GEIDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTS---IFKpttEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMN 175
Cdd:PRK12938  85 LVNNAGITrdvVFR---KMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIH 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  176 QLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK12938 162 GFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRP 196
PRK07577 PRK07577
SDR family oxidoreductase;
19-210 1.83e-16

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 75.15  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQlqerlrewqakGFQVTTSVCDVSSRDQRVKLMETVSSlyQGKLNI 98
Cdd:PRK07577   5 TVLVTGATKGIGLALSLRLANLGHQVIGIARSAID-----------DFPGELFACDLADIEQTAATLAQINE--IHPVDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAgVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK07577  72 IVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSALVGCT 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK07577 151 RTWALELAEYGITVNAVAPGPIETELFRQTRP 182
PRK06194 PRK06194
hypothetical protein; Provisional
 17-210 1.99e-16

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 76.21  E-value: 1.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:PRK06194   6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERF-GAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASG------SGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:PRK06194  85 HLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAekdpayEGHIVNTASMAGLLAPPAMGIYNVS 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42570969  171 KGAMNQLARNL--ACEWASDNIRTNSVCPWYITTPL--SNDVRP 210
Cdd:PRK06194 165 KHAVVSLTETLyqDLSLVTDQVGASVLCPYFVPTGIwqSERNRP 208
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 19-204 2.55e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 75.00  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDE-TQLQERLREWQAkgfqvttsvcDVSsrDQRVKLMETVsslyqGKLN 97
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQGAQVYGVDKQDkPDLSGNFHFLQL----------DLS--DDLEPLFDWV-----PSVD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   98 ILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:PRK06550  70 ILCNTAGIlDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAG 149

                        170       180
                 ....*....|....*....|....*...
gi 42570969  177 LARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK06550 150 FTKQLALDYAKDGIQVFGIAPGAVKTPM 177
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 14-197 4.21e-16

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 75.20  E-value: 4.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKV----HTCARDEtqlQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVS 89
Cdd:PRK07792   9 DLSGKVAVVTGAAAGLGRAEALGLARLGATVvvndVASALDA---SDVLDEIRAAGAKAVAVAGDISQRATADELVATAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   90 SLyqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLL----KASGS---GSIVLISSAAGVvhvn 162
Cdd:PRK07792  86 GL--GGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWrakaKAAGGpvyGRIVNTSSEAGL---- 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  163 VGSI----YGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK07792 160 VGPVgqanYGAAKAGITALTLSAARALGRYGVRANAICP 198
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 19-197 9.51e-16

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: 73.47  E-value: 9.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKV--HtCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAAEGYRVvvH-YNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAF-GRC 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVgtSIFKPTT--EYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSaAGVVHVNVGSI-YGATKGA 173
Cdd:cd05357  80 DVLVNNA--SAFYPTPlgQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIID-AMTDRPLTGYFaYCMSKAA 156

                       170       180
                ....*....|....*....|....
gi 42570969 174 MNQLARNLACEWASdNIRTNSVCP 197
Cdd:cd05357 157 LEGLTRSAALELAP-NIRVNGIAP 179
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 15-210 9.57e-16

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: 73.38  E-value: 9.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKG-----------FQVTTSVCDvssrdqrvK 83
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGgrqpqwfildlLTCTSENCQ--------Q 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  84 LMETVSSLYqGKLNILVNNVG-TSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVV-HV 161
Cdd:cd05340  74 LAQRIAVNY-PRLDGVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQgRA 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42570969 162 NVGSiYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRP 210
Cdd:cd05340 153 NWGA-YAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFP 200
PRK06139 PRK06139
SDR family oxidoreductase;
22-203 1.61e-15

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 73.99  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   22 VTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQrVKLMETVSSLYQGKLNILVN 101
Cdd:PRK06139  12 ITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQ-VKALATQAASFGGRIDVWVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  102 NVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLARNL 181
Cdd:PRK06139  91 NVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGFSEAL 170

                        170       180
                 ....*....|....*....|...
gi 42570969  182 ACEWASD-NIRTNSVCPWYITTP 203
Cdd:PRK06139 171 RGELADHpDIHVCDVYPAFMDTP 193
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 14-214 2.45e-15

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 72.41  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSK--GIGEAVVEELAMLGAKV---HTCARDETQ-----------LQErlrEWQAKGFQVTTSVCDVSS 77
Cdd:PRK12748   2 PLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIfftYWSPYDKTMpwgmhdkepvlLKE---EIESYGVRCEHMEIDLSQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   78 RDQRVKLMETVSSLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQL--AHPLLKASGSgsIVLISSA 155
Cdd:PRK12748  79 PYAPNRVFYAVSERL-GDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAfaKQYDGKAGGR--IINLTSG 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42570969  156 AgvvhvNVGSI-----YGATKGAMNQLARNLACEWASDNIRTNSVCP-----WYITTPLSNDVRPKFIF 214
Cdd:PRK12748 156 Q-----SLGPMpdelaYAATKGAIEAFTKSLAPELAEKGITVNAVNPgptdtGWITEELKHHLVPKFPQ 219
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 14-204 2.58e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 72.91  E-value: 2.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQ---ERLREWQAKGfQVTTSVCDVSSRDQRVKLMETVSS 90
Cdd:PRK05875   4 SFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAaaaEEIEALKGAG-AVRYEPADVTDEDQVARAVDAATA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 lYQGKLNILVNNVGTS-IFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS-AAGVVHVNVGSiYG 168
Cdd:PRK05875  83 -WHGRLHGVVHCAGGSeTIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSiAASNTHRWFGA-YG 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK05875 161 VTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 15-204 2.72e-15

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 73.72  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVhTCArDETQLQERLREwQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHV-VCL-DVPAAGEALAA-VANRVGGTALALDITAPDAPARIAEHLAERH-G 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ--LAHPLLKAsgSGSIVLISSAAGVVHvNVG-SIYGATK 171
Cdd:PRK08261 284 GLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEalLAAGALGD--GGRIVGVSSISGIAG-NRGqTNYAASK 360

                        170       180       190
                 ....*....|....*....|....*....|...
gi 42570969  172 GAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:PRK08261 361 AGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
PRK07041 PRK07041
SDR family oxidoreductase;
21-210 2.75e-15

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 71.99  E-value: 2.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQRVKLMETVsslyqGKLNILV 100
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGA-PVRTAALDITDEAAVDAFFAEA-----GPFDHVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  101 NNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHpllKASGsGSIVLISSAAGVVHVNVGSIYGATKGAMNQLARN 180
Cdd:PRK07041  75 ITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAAR---IAPG-GSLTFVSGFAAVRPSASGVLQGAINAALEALARG 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  181 LACEWASdnIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK07041 151 LALELAP--VRVNTVSPGLVDTPLWSKLAG 178
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 15-212 4.63e-15

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: 71.88  E-value: 4.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKlmETVSSLyqG 94
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVA--ALVDRW--G 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASG-SGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:cd05363  77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGrGGKIINMASQAGRRGEALVGVYCATKAA 156

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42570969 174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd05363 157 VISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKF 195
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 19-203 4.82e-15

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: 71.45  E-value: 4.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHtcARDETQLQERLREwqakGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:cd05361   3 IALVTHARHFAGPASAEALTEDGYTVV--CHDASFADAAERQ----AFESENPGTKALSEQKPEELVDAVLQAG-GAIDV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNN-VGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQL 177
Cdd:cd05361  76 LVSNdYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVAL 155

                       170       180
                ....*....|....*....|....*.
gi 42570969 178 ARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:cd05361 156 AESLAKELSRDNILVYAIGPNFFNSP 181
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 15-208 7.98e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 71.26  E-value: 7.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGA--KVHTCARDEtQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGAlvAIHYGNRKE-EAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 QG-----KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKasGSGSIVLISSAAGVVHVNVGSIY 167
Cdd:PRK12747  81 QNrtgstKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLR--DNSRIINISSAATRISLPDFIAY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK12747 159 SMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAEL 199
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 19-179 1.41e-14

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 69.05  E-value: 1.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969     19 TALVTGGSKGIGEAVVEELAMLGA-KVHTCAR---DETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE-G 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969     95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPL-LKAsgsgsIVLISSAAGVvhvnVGSI----YGA 169
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLpLDF-----FVLFSSIAGV----LGSPgqanYAA 151

                          170
                   ....*....|
gi 42570969    170 TKGAMNQLAR 179
Cdd:smart00822 152 ANAFLDALAE 161
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 14-207 1.46e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 70.77  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLqERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAEL-AALAAELGGDDRVLTVVADVTDLAAMQAAAEEAVERF- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK05872  84 GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYCASKAG 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK05872 163 VEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRD 196
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
13-202 1.61e-14

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 70.29  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAKVhtCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK08993   6 FSLEGKVAVVTGCDTGLGQGMALGLAEAGCDI--VGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSG----SIVLISSAAGVVHVnvgSIYG 168
Cdd:PRK08993  84 -GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGgkiiNIASMLSFQGGIRV---PSYT 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK08993 160 ASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
13-202 1.62e-14

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 70.32  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   13 WSLGGMTALVTGGSKGIGEAVVEELAMLGAK-VHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVssl 91
Cdd:PRK12481   4 FDLNGKVAIITGCNTGLGQGMAIGLAKAGADiVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEV--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 yQGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQ-LAHPLLKASGSGSIVLISSA---AGVVHVnvgSIY 167
Cdd:PRK12481  81 -MGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQaVAKQFVKQGNGGKIINIASMlsfQGGIRV---PSY 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK12481 157 TASKSAVMGLTRALATELSQYNINVNAIAPGYMAT 191
PRK06947 PRK06947
SDR family oxidoreductase;
19-202 2.38e-14

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 69.83  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLN 97
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARGWSVGiNYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAF-GRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   98 ILVNNVG-TSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKAS---GSGSIVLISSAA---GVVHVNVGsiYGAT 170
Cdd:PRK06947  83 ALVNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggRGGAIVNVSSIAsrlGSPNEYVD--YAGS 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  171 KGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK06947 161 KGAVDTLTLGLAKELGPHGVRVNAVRPGLIET 192
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 14-214 2.63e-14

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 69.81  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGS--KGIGEAVVEELAMLGAKV---HTCARDET-----------QLQERLRewqAKGFQVTTSVCDVSS 77
Cdd:PRK12859   3 QLKNKVAVVTGVSrlDGIGAAICKELAEAGADIfftYWTAYDKEmpwgvdqdeqiQLQEELL---KNGVKVSSMELDLTQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   78 RDQRVKLMETVSSLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLS-QLAHPLLKASGsGSIVLISSAA 156
Cdd:PRK12859  80 NDAPKELLNKVTEQL-GYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSsQFARGFDKKSG-GRIINMTSGQ 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42570969  157 GVVHVNVGSIYGATKGAMNQLARNLACEWASDNIRTNSVCP------WyITTPLSNDVRPKFIF 214
Cdd:PRK12859 158 FQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPgptdtgW-MTEEIKQGLLPMFPF 220
PRK05693 PRK05693
SDR family oxidoreductase;
19-202 6.11e-14

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 69.05  E-value: 6.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDEtqlqERLREWQAKGFqvTTSVCDVSSRDQRVKLMETVSSLYQGkLNI 98
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKA----EDVEALAAAGF--TAVQLDVNDGAALARLAEELEAEHGG-LDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKaSGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK05693  76 LINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLR-RSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALS 154

                        170       180
                 ....*....|....*....|....
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK05693 155 DALRLELAPFGVQVMEVQPGAIAS 178
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 14-205 8.17e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 68.43  E-value: 8.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDEtqlqERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDE----ALAKETAAELGLVVGGPLDVTDPASFAAFLDAVEADL- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK07825  77 GPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK07825 157 VVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
PRK07831 PRK07831
SDR family oxidoreductase;
15-197 1.43e-13

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 67.75  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGS-KGIGEAVVEELAMLGAKVHTCARDETQLQE---RLREWQAKGfQVTTSVCDVSSRDQRVKLMETVSS 90
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGEtadELAAELGLG-RVEAVVCDVTSEAQVDALIDAAVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 LYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGsivlissaaGVVhVNVGSI---- 166
Cdd:PRK07831  94 RL-GRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHG---------GVI-VNNASVlgwr 162

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 42570969  167 -------YGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK07831 163 aqhgqahYAAAKAGVMALTRCSALEAAEYGVRINAVAP 200
PRK08703 PRK08703
SDR family oxidoreductase;
14-210 1.86e-13

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 67.26  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKG----FQVTTSVCDvSSRDQRVKLMETVS 89
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGhpepFAIRFDLMS-AEEKEFEQFAATIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   90 SLYQGKLNILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYG 168
Cdd:PRK08703  82 EATQGKLDGIVHCAGYfYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 42570969  169 ATKGAMNQLARNLACEWAS-DNIRTNSVCPWYITTPLSNDVRP 210
Cdd:PRK08703 162 ASKAALNYLCKVAADEWERfGNLRANVLVPGPINSPQRIKSHP 204
PRK09186 PRK09186
flagellin modification protein A; Provisional
 14-197 2.31e-13

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 66.94  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQaKGFQV---TTSVCDVSSRDQRVKLMETVSS 90
Cdd:PRK09186   1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLG-KEFKSkklSLVELDITDQESLEEFLSKSAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 LYqGKLNILVNNV-------GTSIFkpttEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVV---- 159
Cdd:PRK09186  80 KY-GKIDGAVNCAyprnkdyGKKFF----DVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVapkf 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42570969  160 -HVNVGSI-----YGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK09186 155 eIYEGTSMtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
PRK07775 PRK07775
SDR family oxidoreductase;
19-197 2.46e-13

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 67.09  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSrDQRVK--LMETVSSLyqGKL 96
Cdd:PRK07775  12 PALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTD-PDSVKsfVAQAEEAL--GEI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:PRK07775  89 EVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEA 168

                        170       180
                 ....*....|....*....|.
gi 42570969  177 LARNLACEWASDNIRTNSVCP 197
Cdd:PRK07775 169 MVTNLQMELEGTGVRASIVHP 189
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 15-197 4.03e-13

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 66.43  E-value: 4.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGF-QVTTSVCDVS--SRDQRVKLMETVSSL 91
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGpQPAIIPLDLLtaTPQNYQQLADTIEEQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   92 YqGKLNILVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSaagvvhvNVGSI---- 166
Cdd:PRK08945  90 F-GRLDGVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSS-------SVGRQgran 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  167 ---YGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK08945 162 wgaYAVSKFATEGMMQVLADEYQGTNLRVNCINP 195
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 20-204 4.92e-13

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: 65.30  E-value: 4.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQerlrewqakgfqvttsvCDVSSRDQRVKLMETVsslyqGKLNIL 99
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQ-----------------VDITDEASIKALFEKV-----GHFDAI 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLkaSGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLAR 179
Cdd:cd11731  59 VSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVR 136

                       170       180
                ....*....|....*....|....*
gi 42570969 180 NLACEwASDNIRTNSVCPWYITTPL 204
Cdd:cd11731 137 AAAIE-LPRGIRINAVSPGVVEESL 160
PRK07024 PRK07024
SDR family oxidoreductase;
18-216 5.08e-13

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 66.11  E-value: 5.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALV--TGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQrvklMETVSSLY--- 92
Cdd:PRK07024   1 MPLKVfiTGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAA-RVSVYAADVRDADA----LAAAAADFiaa 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 QGKLNILVNNVGTSIFKPTTEytAED---FSFVMATNLesaFHLSQLAHPLL---KASGSGSIVLISSAAGVVHVNVGSI 166
Cdd:PRK07024  76 HGLPDVVIANAGISVGTLTEE--REDlavFREVMDTNY---FGMVATFQPFIapmRAARRGTLVGIASVAGVRGLPGAGA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 42570969  167 YGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKFIFLL 216
Cdd:PRK07024 151 YSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTAHNPYPMPFLM 200
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 17-202 5.24e-13

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: 66.06  E-value: 5.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSrdqrVKLMETVSSLYQGKL 96
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETL----VKFVVYAMLEKLGRI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKAsGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:cd09761  77 DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIK-NKGRIINIASTRAFQSEPDSEAYAASKGGLVA 155

                       170       180
                ....*....|....*....|....*.
gi 42570969 177 LARNLACEWASDnIRTNSVCPWYITT 202
Cdd:cd09761 156 LTHALAMSLGPD-IRVNCISPGWINT 180
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 15-201 9.81e-13

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 65.17  E-value: 9.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLqERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYQG 94
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKL-KRMKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 kLNILVNNVGTsifkpTTEYTAEDFSFV---MATNLESAFHLSQLAHPLLKaSGSgSIVLISSAAGV-----VHVNvgsi 166
Cdd:PRK05786  82 -IDGLVVTVGG-----YVEDTVEEFSGLeemLTNHIKIPLYAVNASLRFLK-EGS-SIVLVSSMSGIykaspDQLS---- 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  167 YGATKGAMNQLARNLACEWASDNIRTNSVCPWYIT 201
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPTTIS 184
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 19-190 1.22e-12

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: 64.71  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQE-RLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLN 97
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAlLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEI-GPLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQL 177
Cdd:cd05373  80 VLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRAL 159

                       170
                ....*....|...
gi 42570969 178 ARNLACEWASDNI 190
Cdd:cd05373 160 AQSMARELGPKGI 172
PRK06123 PRK06123
SDR family oxidoreductase;
20-202 1.70e-12

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 64.41  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREW-QAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAiRRQGGEALAVAADVADEADVLRLFEAVDREL-GRLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGtsIFKPTT---EYTAEDFSFVMATNLESAFHLSQLAHPLLK---ASGSGSIVLISSAAGvvhvNVGSI-----Y 167
Cdd:PRK06123  84 LVNNAG--ILEAQMrleQMDAARLTRIFATNVVGSFLCAREAVKRMStrhGGRGGAIVNVSSMAA----RLGSPgeyidY 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK06123 158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYT 192
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 19-214 1.80e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 64.73  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKV----HTCARDETQLQERLREwQAKGFQVttsvcDVSSRDQRVKLMETVSSLYQG 94
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVvvnyHQSEDAAEALADELGD-RAIALQA-----DVTDREQVQAMFATATEHFGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNN--VGTSiFKPTT-----EYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS---AAGVV--HVn 162
Cdd:PRK08642  81 PITTVVNNalADFS-FDGDArkkadDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTnlfQNPVVpyHD- 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 42570969  163 vgsiYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKFIF 214
Cdd:PRK08642 159 ----YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEVF 206
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 20-198 2.11e-12

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 65.71  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLRE--WQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLN 97
Cdd:COG3347 428 ALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAElgGGYGADAVDATDVDVTAEAAVAAAFGFAGLDI-GGSD 506

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASG-SGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:COG3347 507 IGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGlGGSSVFAVSKNAAAAAYGAAAAATAKAAAQH 586

                       170       180
                ....*....|....*....|..
gi 42570969 177 LARNLACEWASDNIRTNSVCPW 198
Cdd:COG3347 587 LLRALAAEGGANGINANRVNPD 608
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 17-212 2.31e-12

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 64.89  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK--GFQVTTSVCDVSSR-DQRV-KLMETVSSLY 92
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKysKTQIKTVVVDFSGDiDEGVkRIKETIEGLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 QGklnILVNNVGTS--IFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVN--VGSIYG 168
Cdd:PLN02780 133 VG---VLINNVGVSypYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSdpLYAVYA 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 42570969  169 ATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:PLN02780 210 ATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSF 253
PRK06914 PRK06914
SDR family oxidoreductase;
19-174 2.75e-12

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 64.27  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDEtQLQERLREwQAKGFQVTTSVcDVSSRD----QRVKLMETVSSLYqG 94
Cdd:PRK06914   5 IAIVTGASSGFGLLTTLELAKKGYLVIATMRNP-EKQENLLS-QATQLNLQQNI-KVQQLDvtdqNSIHNFQLVLKEI-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 19-182 1.26e-11

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: 62.09  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGA---KVHTCARD---ETQLQERLREwqAKGFQVTTSVCDVSSRDQrvkLMETVSSLY 92
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASDPSkrfKVYATMRDlkkKGRLWEAAGA--LAGGTLETLQLDVCDSKS---VAAAVERVT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  93 QGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:cd09806  77 ERHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKF 156

                       170
                ....*....|
gi 42570969 173 AMNQLARNLA 182
Cdd:cd09806 157 ALEGLCESLA 166
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 18-197 1.46e-11

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 62.08  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELAMLGAKVHTCARDetqlQERLREWQAK-GFQVTTSVCDVSSRDQRVKLMETVSSLYQgKL 96
Cdd:PRK10538   1 MIVLVTGATAGFGECITRRFIQQGHKVIATGRR----QERLQELKDElGDNLYIAQLDVRNRAAIEEMLASLPAEWR-NI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSI-FKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMN 175
Cdd:PRK10538  76 DVLVNNAGLALgLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVR 155

                        170       180
                 ....*....|....*....|..
gi 42570969  176 QLARNLACEWASDNIRTNSVCP 197
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEP 177
PRK12744 PRK12744
SDR family oxidoreductase;
14-203 1.69e-11

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 62.06  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAK---VH-TCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVS 89
Cdd:PRK12744   5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKavaIHyNSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   90 SLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLkaSGSGSIVLISSAAGVVHVNVGSIYGA 169
Cdd:PRK12744  85 AAF-GRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTLVTSLLGAFTPFYSAYAG 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 42570969  170 TKGAMNQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK12744 162 SKAPVEHFTRAASKEFGARGISVTAVGPGPMDTP 195
PRK06196 PRK06196
oxidoreductase; Provisional
 15-205 1.95e-11

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 62.39  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQakgfQVTTSVCDVSSRDQRVKLMETVSSLYQg 94
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGID----GVEVVMLDLADLESVRAFAERFLDSGR- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGTsIFKPTTeYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSA----AGV----VHVNVG-- 164
Cdd:PRK06196  99 RIDILINNAGV-MACPET-RVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAghrrSPIrwddPHFTRGyd 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 42570969  165 --SIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLS 205
Cdd:PRK06196 177 kwLAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQ 219
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 20-197 1.97e-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: 61.71  E-value: 1.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK-GFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:cd05322   5 AVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIF-KRVDL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGS-GSIVLISSAAGVVHVNVGSIYGATKGAMNQL 177
Cdd:cd05322  84 LVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFGGVGL 163

                       170       180
                ....*....|....*....|
gi 42570969 178 ARNLACEWASDNIRTNSVCP 197
Cdd:cd05322 164 TQSLALDLAEHGITVNSLML 183
PRK07985 PRK07985
SDR family oxidoreductase;
15-212 2.42e-11

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 61.93  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTC-----ARDETQLQERLREWQAKGFQVTTSVCDVS-SRDQRVKLMETV 88
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDEKfARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   89 sslyqGKLNILVNNVGTSIFKPT-TEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSgsIVLISSAAGVVHVNVGSIY 167
Cdd:PRK07985 127 -----GGLDIMALVAGKQVAIPDiADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGAS--IITTSSIQAYQPSPHLLDY 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 42570969  168 GATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL------SNDVRPKF 212
Cdd:PRK07985 200 AATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALqisggqTQDKIPQF 250
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 20-204 3.82e-11

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 60.23  E-value: 3.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKgfqvttsvcdvsSRDQRVKLMETVSSLYQ--GKLN 97
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGAL------------ARPADVAAELEVWALAQelGPLD 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  98 ILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLsqLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQL 177
Cdd:cd11730  69 LLVYAAGAILGKPLARTKPAAWRRILDANLTGAALV--LKHALALLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAY 146

                       170       180
                ....*....|....*....|....*..
gi 42570969 178 ARNLACEWasDNIRTNSVCPWYITTPL 204
Cdd:cd11730 147 VEVARKEV--RGLRLTLVRPPAVDTGL 171
PRK08017 PRK08017
SDR family oxidoreductase;
19-208 5.80e-11

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 60.48  E-value: 5.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLqERLREWQAKGFQVttsvcDVSSRDQRVKLMETVSSLYQGKLNI 98
Cdd:PRK08017   4 SVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV-ARMNSLGFTGILL-----DLDDPESVERAADEVIALTDNRLYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK08017  78 LFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWS 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRTRFTDNV 187
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 21-158 2.34e-10

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: 59.32  E-value: 2.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  21 LVTGGSKGIGEAVVEELAMLGAK--VHTCARDETQL-QERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLyqGKLN 97
Cdd:cd05274 154 LITGGLGGLGLLVARWLAARGARhlVLLSRRGPAPRaAARAALLRAGGARVSVVRCDVTDPAALAALLAELAAG--GPLA 231

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42570969  98 ILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLsqlaHPLLKASGSGSIVLISSAAGV 158
Cdd:cd05274 232 GVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNL----HELTPDLPLDFFVLFSSVAAL 288
PRK06482 PRK06482
SDR family oxidoreductase;
19-171 2.86e-10

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 58.59  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWqakGFQVTTSVCDVSSRDQRVKLMETVSSLYqGKLNI 98
Cdd:PRK06482   4 TWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARY---GDRLWVLQLDVTDSAAVRAVVDRAFAAL-GRIDV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:PRK06482  80 VVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATK 152
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 21-206 3.30e-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: 58.44  E-value: 3.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  21 LVTGGSKGIGEAVVEELAMLGAKVH-TCARDETQLQERLREwqAKGFQVTTSVCDVSSRDQRVKLMETVSSLYQGK-LNI 98
Cdd:cd09805   4 LITGCDSGFGNLLAKKLDSLGFTVLaGCLTKNGPGAKELRR--VCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKgLWG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSIFKPTTEYTA-EDFSFVMATNLESAFHLSQLAHPLLKASgSGSIVLISSAAGVVHVNVGSIYGATKGAMNQL 177
Cdd:cd09805  82 LVNNAGILGFGGDEELLPmDDYRKCMEVNLFGTVEVTKAFLPLLRRA-KGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                       170       180
                ....*....|....*....|....*....
gi 42570969 178 ARNLACEWASDNIRTNSVCPWYITTPLSN 206
Cdd:cd09805 161 SDSLRRELQPWGVKVSIIEPGNFKTGITG 189
PRK09134 PRK09134
SDR family oxidoreductase;
18-150 5.13e-10

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 57.63  E-value: 5.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELAMLG--AKVHtCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSlYQGK 95
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGfdVAVH-YNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASA-ALGP 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42570969   96 LNILVNNvgTSIFkpttEY-TAEDFSFV-----MATNLESAFHLSQLAHPLLKASGSGSIV 150
Cdd:PRK09134  88 ITLLVNN--ASLF----EYdSAASFTRAswdrhMATNLRAPFVLAQAFARALPADARGLVV 142
PRK08251 PRK08251
SDR family oxidoreductase;
21-202 7.49e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 57.25  E-value: 7.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK--GFQVTTSVCDVSSRDQRVKLMETVSSLYQGKLNI 98
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELGGLDRV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVN-------NVGTSIFKPTTEyTAEdfsfvmaTNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHV-NVGSIYGAT 170
Cdd:PRK08251  86 IVNagigkgaRLGTGKFWANKA-TAE-------TNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLpGVKAAYAAS 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  171 KGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK08251 158 KAGVASLGEGLRAELAKTPIKVSTIEPGYIRS 189
PRK08278 PRK08278
SDR family oxidoreductase;
14-197 8.35e-10

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 57.22  E-value: 8.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARdETQLQERL--------REWQAKGFQVTTSVCDVSSRDQ-RVKL 84
Cdd:PRK08278   3 SLSGKTLFITGASRGIGLAIALRAARDGANIVIAAK-TAEPHPKLpgtihtaaEEIEAAGGQALPLVGDVRDEDQvAAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   85 METVSSLyqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLIS------SAAGV 158
Cdd:PRK08278  82 AKAVERF--GGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSpplnldPKWFA 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  159 VHVNvgsiYGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK08278 160 PHTA----YTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 19-198 8.84e-10

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: 56.03  E-value: 8.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    19 TALVTGGSKGIGEAVVEELAMLGAK----VHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqG 94
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARhlvlLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEG-P 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    95 KLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLsqlaHPLLKASGSGSIVLISSAAGVvhvnVGSI----YGAT 170
Cdd:pfam08659  81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNL----HEATPDEPLDFFVLFSSIAGL----LGSPgqanYAAA 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 42570969   171 KGAMNQLARnlacEWASDNIRTNSV--CPW 198
Cdd:pfam08659 153 NAFLDALAE----YRRSQGLPATSInwGPW 178
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 17-212 9.23e-10

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 56.83  E-value: 9.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAK-GFQ-VTTSVCDVSSRDQRVKLMETVSSLYQg 94
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETEsGNQnIFLHIVDMSDPKQVWEFVEEFKEEGK- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  95 KLNILVNNVGTSIFKptTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHV----NVGSIYGAT 170
Cdd:cd09808  80 KLHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLVQKlntnNLQSERTAF 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42570969 171 KGAMnQLARN------LACEWASDN--IRTNSVCPWYITTPLSNDVRPKF 212
Cdd:cd09808 158 DGTM-VYAQNkrqqviMTEQWAKKHpeIHFSVMHPGWADTPAVRNSMPDF 206
PRK05854 PRK05854
SDR family oxidoreductase;
15-156 1.45e-09

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 56.61  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDET---QLQERLREwQAKGFQVTTSVCDVSSRDQRVKLMETVSSl 91
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAkgeAAVAAIRT-AVPDAKLSLRALDLSSLASVAALGEQLRA- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42570969   92 yQGK-LNILVNNVGTsIFKPTTEYTAEDFSFVMATNlesafHLSQLA---H--PLLKASGSGSIVLISSAA 156
Cdd:PRK05854  90 -EGRpIHLLINNAGV-MTPPERQTTADGFELQFGTN-----HLGHFAltaHllPLLRAGRARVTSQSSIAA 153
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 21-203 1.69e-09

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 55.79  E-value: 1.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  21 LVTGGSKGIGEAVVEELAMLGAKVhtCARDETQLQErlrewQAKGFQVTTSVCDVSSRDQRVKLMETVSslyqGKLNILV 100
Cdd:cd05334   5 LVYGGRGALGSAVVQAFKSRGWWV--ASIDLAENEE-----ADASIIVLDSDSFTEQAKQVVASVARLS----GKVDALI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 101 NNVGTSIFKPTTEYT-AEDFSFVMATNLESAFHLSQLAHPLLKasGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLAR 179
Cdd:cd05334  74 CVAGGWAGGSAKSKSfVKNWDLMWKQNLWTSFIASHLATKHLL--SGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQ 151

                       170       180
                ....*....|....*....|....*.
gi 42570969 180 NLACEW--ASDNIRTNSVCPWYITTP 203
Cdd:cd05334 152 SLAAENsgLPAGSTANAILPVTLDTP 177
PRK06101 PRK06101
SDR family oxidoreductase;
19-206 1.71e-09

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 56.03  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQErLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLYqgklni 98
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDE-LHTQSANIFTLAFDVTDHPGTKAALSQLPFIPELW------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 lVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLkaSGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK06101  76 -IFNAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHL--SCGHRVVIVGSIASELALPRAEAYGASKAAVAYFA 152

                        170       180
                 ....*....|....*....|....*...
gi 42570969  179 RNLACEWASDNIRTNSVCPWYITTPLSN 206
Cdd:PRK06101 153 RTLQLDLRPKGIEVVTVFPGFVATPLTD 180
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 18-197 2.46e-09

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 55.32  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTA--LVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQvttsvCDVSSRDQRVKLMETVSSLYQGk 95
Cdd:PRK06483   1 MPApiLITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAGAQCIQ-----ADFSTNAGIMAFIDELKQHTDG- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   96 LNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGsivlissAAGVVH-----VNVGS----I 166
Cdd:PRK06483  75 LRAIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHA-------ASDIIHitdyvVEKGSdkhiA 147

                        170       180       190
                 ....*....|....*....|....*....|.
gi 42570969  167 YGATKGAMNQLARNLACEWASdNIRTNSVCP 197
Cdd:PRK06483 148 YAASKAALDNMTLSFAAKLAP-EVKVNSIAP 177
PRK06953 PRK06953
SDR family oxidoreductase;
19-185 4.40e-09

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 54.69  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQeRLREWQAKGFQVttsvcDVSSRDQrvklmetVSSL---YQG- 94
Cdd:PRK06953   3 TVLIVGASRGIGREFVRQYRADGWRVIATARDAAALA-ALQALGAEALAL-----DVADPAS-------VAGLawkLDGe 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNVGtsIFKPTTE----YTAEDFSFVMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGV---VHVNVGSIY 167
Cdd:PRK06953  70 ALDAAVYVAG--VYGPRTEgvepITREDFDAVMHTNVLGPMQLLPILLPLVEAAG-GVLAVLSSRMGSigdATGTTGWLY 146

                        170
                 ....*....|....*...
gi 42570969  168 GATKGAMNQLARNLACEW 185
Cdd:PRK06953 147 RASKAALNDALRAASLQA 164
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 15-197 5.46e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 55.06  E-value: 5.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKV---------HTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLM 85
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVvvndigvglDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   86 ETVSSLYqGKLNILVNNVGT---SIFKPTTEytaEDFSFVMATNLESAFHLSQLAHPLLKA-SGSG-----SIVLISSAA 156
Cdd:PRK07791  84 DAAVETF-GGLDVLVNNAGIlrdRMIANMSE---EEWDAVIAVHLKGHFATLRHAAAYWRAeSKAGravdaRIINTSSGA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 42570969  157 GVVHvNVG-SIYGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:PRK07791 160 GLQG-SVGqGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 17-204 6.68e-09

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 54.78  E-value: 6.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREW--QAKGFQVTTSVCDVSSRDQRVKLMETVSSlYQG 94
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIrrDTLNHEVIVRHLDLASLKSIRAFAAEFLA-EED 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  95 KLNILVNNVGtsIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAA---GVVHV---------N 162
Cdd:cd09807  80 RLDVLINNAG--VMRCPYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAhkaGKINFddlnseksyN 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42570969 163 VGSIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPL 204
Cdd:cd09807 158 TGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK08416 PRK08416
enoyl-ACP reductase;
17-202 7.46e-09

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 54.39  E-value: 7.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKV-HTCARDETQLQERLREWQAK-GFQVTTSVCDVSSRDQRVKLMETVSSLYQg 94
Cdd:PRK08416   8 GKTLVISGGTRGIGKAIVYEFAQSGVNIaFTYNSNVEEANKIAEDLEQKyGIKAKAYPLNILEPETYKELFKKIDEDFD- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 KLNILVNNV---GTSI---------FKP---TTEYTAEDFSFVMAtnlesafhlSQLAHPLLKASGSGSIVLISSAAGVV 159
Cdd:PRK08416  87 RVDFFISNAiisGRAVvggytkfmrLKPkglNNIYTATVNAFVVG---------AQEAAKRMEKVGGGSIISLSSTGNLV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 42570969  160 HVNVGSIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK08416 158 YIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDT 200
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 19-209 9.65e-09

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: 54.04  E-value: 9.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVhtcardetqLQERLREWQAKgfqvttsvCDVSSRDQRVKLMETVSSLYQGKLNI 98
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHTV---------IGIDLREADVI--------ADLSTPEGRAAAIADVLARCSGVLDG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTSifkPTTeyTAEDfsfVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGV-------------------- 158
Cdd:cd05328  64 LVNCAGVG---GTT--VAGL---VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalaagtear 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42570969 159 -----------VHVNvgsiYGATKGAMNQLARNLACEWASD-NIRTNSVCPWYITTPLSNDVR 209
Cdd:cd05328 136 avalaehagqpGYLA----YAGSKEALTVWTRRRAATWLYGaGVRVNTVAPGPVETPILQAFL 194
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
20-209 1.03e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 53.92  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQ-LQERLREWQAKGFQVTTSVCDVSSRDQRVK------LMETVSSLY 92
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTENKeLTKLAEQYNSNLTFHSLDLQDVHELETNFNeilssiQEDNVSSIH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qgklniLVNNVGT-SIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKA-SGSGSIVLISSAAGVVHVNVGSIYGAT 170
Cdd:PRK06924  84 ------LINNAGMvAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDwKVDKRVINISSGAAKNPYFGWSAYCSS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 42570969  171 KGAMNQLARNLACEWA--SDNIRTNSVCPWYITTPLSNDVR 209
Cdd:PRK06924 158 KAGLDMFTQTVATEQEeeEYPVKIVAFSPGVMDTNMQAQIR 198
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 12-159 6.11e-08

ketoreductase (KR), subgroup 1, 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 KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif 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: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 52.17  E-value: 6.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  12 RWSLGGmTALVTGGSKGIGEAVVEELAMLGAK--VHTCAR--DETQLQERLREWQAKGFQVTTSVCDVSSRDQrvkLMET 87
Cdd:cd08952 226 PWRPRG-TVLVTGGTGALGAHVARWLARRGAEhlVLTSRRgpDAPGAAELVAELTALGARVTVAACDVADRDA---LAAL 301

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42570969  88 VSSLYQGK-LNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLsqlaHPLLKASGSGSIVLISSAAGVV 159
Cdd:cd08952 302 LAALPAGHpLTAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHL----DELTRDRDLDAFVLFSSIAGVW 370
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 15-197 6.46e-08

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: 51.68  E-value: 6.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARdETQLQERL--------REWQAKGFQVTTSVCDVSSRDQ-RVKLM 85
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAK-TAEPHPKLpgtiytaaEEIEAAGGKALPCIVDIRDEDQvRAAVE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  86 ETVSSLyqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGV------V 159
Cdd:cd09762  80 KAVEKF--GGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLnpkwfkN 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42570969 160 HVNvgsiYGATKGAMNQLARNLACEWASDNIRTNSVCP 197
Cdd:cd09762 158 HTA----YTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 20-223 7.89e-08

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: 51.45  E-value: 7.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    20 ALVTGGSKGIGEAVVEELAML----GAKVHTCARDETQLQERLREWQAK--GFQVTTSVCDVSSR---DQRVKLMETVSS 90
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEaglEQLLKALRELPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    91 LYQGKLNILVNNVGTSIFKPTTEYTAEDFSFVM---ATNLESAFHLSQLAHPLLKASGSG--SIVLISSAAGVVHVNVGS 165
Cdd:TIGR01500  83 PKGLQRLLLINNAGTLGDVSKGFVDLSDSTQVQnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNISSLCAIQPFKGWA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42570969   166 IYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVR-----PKFIFLLRTMKNKK 223
Cdd:TIGR01500 163 LYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVReesvdPDMRKGLQELKAKG 225
PRK09291 PRK09291
SDR family oxidoreductase;
19-197 8.88e-08

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 51.15  E-value: 8.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETvsslyqgKLNI 98
Cdd:PRK09291   4 TILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQAAEW-------DVDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLA 178
Cdd:PRK09291  77 LLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAIA 156

                        170
                 ....*....|....*....
gi 42570969  179 RNLACEWASDNIRTNSVCP 197
Cdd:PRK09291 157 EAMHAELKPFGIQVATVNP 175
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 20-203 1.18e-07

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 50.21  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  20 ALVTGGSKGIGEAVVEELAMLGAkvhtcardetqlqerlrewqakgfqvtTSVCDVSSRDqrvklmetvsslyqgklnIL 99
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGS---------------------------PKVLVVSRRD------------------VV 35

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 100 VNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQLAR 179
Cdd:cd02266  36 VHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQ 115

                       170       180
                ....*....|....*....|....
gi 42570969 180 NLACEWASDNIRTNSVCPWYITTP 203
Cdd:cd02266 116 QWASEGWGNGLPATAVACGTWAGS 139
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 19-197 1.27e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 50.68  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQ--ERLREWQAKGFqvttsVCDVSSRDQRVKLMETVSSLYqGKL 96
Cdd:PRK06180   6 TWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARAdfEALHPDRALAR-----LLDVTDFDAIDAVVADAEATF-GPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   97 NILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAMNQ 176
Cdd:PRK06180  80 DVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEG 159

                        170       180
                 ....*....|....*....|.
gi 42570969  177 LARNLACEWASDNIRTNSVCP 197
Cdd:PRK06180 160 ISESLAKEVAPFGIHVTAVEP 180
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
19-217 1.28e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 51.13  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQlQERLREWQakgfQVTTSVCDVSSRDQRVKLMETVSSLYqgklnI 98
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPG-AANLAALP----GVEFVRGDLRDPEALAAALAGVDAVV-----H 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  99 LVNNVGTsifkptteyTAEDFSFVMATNLESAFHLSQLAhpllKASGSGSIVLISSAA------GVV----HVNVGSIYG 168
Cdd:COG0451  71 LAAPAGV---------GEEDPDETLEVNVEGTLNLLEAA----RAAGVKRFVYASSSSvygdgeGPIdedtPLRPVSPYG 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42570969 169 ATKGAMNQLARNLAcewASDNIRTNSVCPWYITTPLSNDVRPKFIFLLR 217
Cdd:COG0451 138 ASKLAAELLARAYA---RRYGLPVTILRPGNVYGPGDRGVLPRLIRRAL 183
PRK09009 PRK09009
SDR family oxidoreductase;
18-185 1.71e-07

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 50.06  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELA--MLGAKVH-TCARDETQLQERLREWQAkgfqvttsvCDVSSRDQRVKLMETVSSlyqg 94
Cdd:PRK09009   1 MNILIVGGSGGIGKAMVKQLLerYPDATVHaTYRHHKPDFQHDNVQWHA---------LDVTDEAEIKQLSEQFTQ---- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   95 kLNILVNNVG---TSIFKPTTEYTAEDFSFV---MATNLESAFHLSQLAHPLLKASGSGSIVLISSaagvvhvNVGSI-- 166
Cdd:PRK09009  68 -LDWLINCVGmlhTQDKGPEKSLQALDADFFlqnITLNTLPSLLLAKHFTPKLKQSESAKFAVISA-------KVGSIsd 139

                        170       180
                 ....*....|....*....|....*..
gi 42570969  167 --------YGATKGAMNQLARNLACEW 185
Cdd:PRK09009 140 nrlggwysYRASKAALNMFLKTLSIEW 166
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 18-197 2.91e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 49.04  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELAmlgakvhtcARDEtqlqerlrewqakgfqvttsVCDV--SSRDQRVKLM--ETVSSLYQ 93
Cdd:PRK07578   1 MKILVIGASGTIGRAVVAELS---------KRHE--------------------VITAgrSSGDVQVDITdpASIRALFE 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   94 --GKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKAsgSGSIVLISSAAGVVHVNVGSIYGATK 171
Cdd:PRK07578  52 kvGKVDAVVSAAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYLND--GGSFTLTSGILSDEPIPGGASAATVN 129

                        170       180
                 ....*....|....*....|....*.
gi 42570969  172 GAMNQLARNLACEwASDNIRTNSVCP 197
Cdd:PRK07578 130 GALEGFVKAAALE-LPRGIRINVVSP 154
PRK08340 PRK08340
SDR family oxidoreductase;
18-203 3.93e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 49.42  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   18 MTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGfQVTTSVCDVSSRDQRVKLMETVSSLYqGKLN 97
Cdd:PRK08340   1 MNVLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELL-GGID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   98 ILVNNVGTSIFKPTTEYTAEDFSFVMATNLES---AFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGAM 174
Cdd:PRK08340  79 ALVWNAGNVRCEPCMLHEAGYSDWLEAALLHLvapGYLTTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGL 158

                        170       180
                 ....*....|....*....|....*....
gi 42570969  175 NQLARNLACEWASDNIRTNSVCPWYITTP 203
Cdd:PRK08340 159 VQLAKGVSRTYGGKGIRAYTVLLGSFDTP 187
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 15-202 4.81e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 49.08  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLqERLRE--WQAKGFQVTTSVCDVSSRDQRVKLMETVSSLy 92
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENL-KKAREkiKSESNVDVSYIVADLTKREDLERTVKELKNI- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   93 qGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKG 172
Cdd:PRK08339  84 -GEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRI 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 42570969  173 AMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK08339 163 SMAGLVRTLAKELGPKGITVNGIMPGIIRT 192
PRK08177 PRK08177
SDR family oxidoreductase;
19-184 9.05e-07

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 48.10  E-value: 9.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQlQERLREW-QAKGFQVTTsvcdvssrDQRVKLMETVSSLYQGKLN 97
Cdd:PRK08177   3 TALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQ-DTALQALpGVHIEKLDM--------NDPASLDQLLQRLQGQRFD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   98 ILVNNVGTS--IFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKAsGSGSIVLISSAAGVVHVNVGS---IYGATKG 172
Cdd:PRK08177  74 LLFVNAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRP-GQGVLAFMSSQLGSVELPDGGempLYKASKA 152

                        170
                 ....*....|..
gi 42570969  173 AMNQLARNLACE 184
Cdd:PRK08177 153 ALNSMTRSFVAE 164
PRK07102 PRK07102
SDR family oxidoreductase;
17-173 2.16e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 47.23  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQ-VTTSVCDVSSRDQRVKLMETVSslyqGK 95
Cdd:PRK07102   1 MKKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVaVSTHELDILDTASHAAFLDSLP----AL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   96 LNILVNNVGTSifkPTTEYTAEDFSF---VMATNLESAFHLSQLAHPLLKASGSGSIVLISSAAGvvhvNVGS----IYG 168
Cdd:PRK07102  77 PDIVLIAVGTL---GDQAACEADPALalrEFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAG----DRGRasnyVYG 149


                 ....*
gi 42570969  169 ATKGA 173
Cdd:PRK07102 150 SAKAA 154
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 4-159 5.25e-06

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 46.59  E-value: 5.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   4 EGGLGENSRWSLGGmTALVTGGSKGIGEAVVEELA-MLGAKVHTCAR-----DETQLQERLREWQAKGFQVTTSVCDVSS 77
Cdd:cd08953 193 PAGAAASAPLKPGG-VYLVTGGAGGIGRALARALArRYGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTD 271

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  78 RDQRVKLMETVSSLYqGKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQlahpLLKASGSGSIVLISSAAG 157
Cdd:cd08953 272 AAAVRRLLEKVRERY-GAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQ----ALADEPLDFFVLFSSVSA 346


                ..
gi 42570969 158 VV 159
Cdd:cd08953 347 FF 348
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 21-207 7.36e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 45.78  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   21 LVTGGSKGIGEAVVEELAMlGAKVHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLyqGKLNILV 100
Cdd:PRK06940   5 VVVIGAGGIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQTL--GPVTGLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  101 NNVGTS--------IFKPTTEYTA---EDFSFVMAtnlesafhlsqlahpllkASGSGsiVLISSAAGvvH--------- 160
Cdd:PRK06940  82 HTAGVSpsqaspeaILKVDLYGTAlvlEEFGKVIA------------------PGGAG--VVIASQSG--Hrlpaltaeq 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42570969  161 -----------------VNVGSI------YGATKGAmNQL-ARNLACEWASDNIRTNSVCPWYITTPLSND 207
Cdd:PRK06940 140 eralattpteellslpfLQPDAIedslhaYQIAKRA-NALrVMAEAVKWGERGARINSISPGIISTPLAQD 209
PRK07806 PRK07806
SDR family oxidoreductase;
14-154 8.71e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 45.48  E-value: 8.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERL-REWQAKGFQVTTSVCDVSSRDQRVKLMETVSSLY 92
Cdd:PRK07806   3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVvAEIEAAGGRASAVGADLTDEESVAALMDTAREEF 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42570969   93 qGKLNILVNNVGTSIfkptTEYTAEDFSfvMATNLESAFHLSQLAHPLLKAsgSGSIVLISS 154
Cdd:PRK07806  83 -GGLDALVLNASGGM----ESGMDEDYA--MRLNRDAQRNLARAALPLMPA--GSRVVFVTS 135
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
15-208 9.06e-06

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 45.48  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   15 LGGMTALVTG--GSKGIGEAVVEELAMLGAK--VHTCARDETQLQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETVSS 90
Cdd:PRK07370   4 LTGKKALVTGiaNNRSIAWGIAQQLHAAGAElgITYLPDEKGRFEKKVRELTEPLNPSLFLPCDVQDDAQIEETFETIKQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   91 LYqGKLNILVNNVGtsiFKPTTEYTAeDFSFV----MATNLE-SAFHLSQLAH---PLLkaSGSGSIVLISSAAGVVHVN 162
Cdd:PRK07370  84 KW-GKLDILVHCLA---FAGKEELIG-DFSATsregFARALEiSAYSLAPLCKaakPLM--SEGGSIVTLTYLGGVRAIP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 42570969  163 VGSIYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITTPLSNDV 208
Cdd:PRK07370 157 NYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAV 202
PRK05993 PRK05993
SDR family oxidoreductase;
19-212 2.40e-05

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 44.25  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQeRLrewQAKGfqVTTSVCDVSSRDQRVKLMETVSSLYQGKLNI 98
Cdd:PRK05993   6 SILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVA-AL---EAEG--LEAFQLDYAEPESIAALVAQVLELSGGRLDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   99 LVNNvGT-----SIFKPTTEYTAEDFSfvmaTNLESAFHLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGSIYGATKGA 173
Cdd:PRK05993  80 LFNN-GAygqpgAVEDLPTEALRAQFE----ANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 42570969  174 MNQLARNLACEWASDNIRTNSVCPWYITTPLSNDVRPKF 212
Cdd:PRK05993 155 IEGLSLTLRMELQGSGIHVSLIEPGPIETRFRANALAAF 193
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 17-195 5.14e-05

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: 42.95  E-value: 5.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTG--GSKGIGEAVVEELAMLGAKVHTCARDETqLQERLREWQAKGFQVT-TSVCDVSSRDQRVKLMETVSSLYq 93
Cdd:cd05372   1 GKRILITGiaNDRSIAWGIAKALHEAGAELAFTYQPEA-LRKRVEKLAERLGESAlVLPCDVSNDEEIKELFAEVKKDW- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 GKLNILVNNVG----TSIFKPTTEYTAEDFSFVMATnleSAFHLSQLAHPLLKASGSG-SIVLISSAAG---VVHVNVGS 165
Cdd:cd05372  79 GKLDGLVHSIAfapkVQLKGPFLDTSRKGFLKALDI---SAYSLVSLAKAALPIMNPGgSIVTLSYLGServVPGYNVMG 155

                       170       180       190
                ....*....|....*....|....*....|
gi 42570969 166 IygaTKGAMNQLARNLACEWASDNIRTNSV 195
Cdd:cd05372 156 V---AKAALESSVRYLAYELGRKGIRVNAI 182
PRK05717 PRK05717
SDR family oxidoreductase;
17-200 2.23e-04

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 41.03  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDetqlqerlrewQAKGFQVTTSV--------CDVSSRDQRVKLMETV 88
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLD-----------RERGSKVAKALgenawfiaMDVADEAQVAAGVAEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   89 SSLYqGKLNILVNNVGtsIFKPTTEyTAEDFSF-----VMATNLESAFHLSQLAHPLLKASGsGSIVLISSAAGVVHVNV 163
Cdd:PRK05717  79 LGQF-GRLDALVCNAA--IADPHNT-TLESLSLahwnrVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPD 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 42570969  164 GSIYGATKGAMNQLARNLACEWASDnIRTNSVCPWYI 200
Cdd:PRK05717 154 TEAYAASKGGLLALTHALAISLGPE-IRVNAVSPGWI 189
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 14-186 2.61e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 41.14  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   14 SLGGMTALVTGGSKGIGEAVVEELAMLGAKVH-----------TCARDET--QLQERLREWQAKGFQVTTSVCDVssrDQ 80
Cdd:PRK08303   5 PLRGKVALVAGATRGAGRGIAVELGAAGATVYvtgrstrarrsEYDRPETieETAELVTAAGGRGIAVQVDHLVP---EQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   81 RVKLMETVSSlYQGKLNILVNNV--GTSIF---KPTTEYTAEDFSFVMATNLESafHL--SQLAHPLLKASGSGSIVLIS 153
Cdd:PRK08303  82 VRALVERIDR-EQGRLDILVNDIwgGEKLFewgKPVWEHSLDKGLRMLRLAIDT--HLitSHFALPLLIRRPGGLVVEIT 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 42570969  154 SAAGVV---HVNVGSIYGATKGAMNQLARNLACEWA 186
Cdd:PRK08303 159 DGTAEYnatHYRLSVFYDLAKTSVNRLAFSLAHELA 194
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 10-156 2.74e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 41.16  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   10 NSRWSLG------GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDE---TQLQERLREwQAKGFQVTTSVCDVSSRDQ 80
Cdd:PRK06197   3 MTKWTAAdipdqsGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLdkgKAAAARITA-ATPGADVTLQELDLTSLAS 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42570969   81 RVKLMETVSSLYQgKLNILVNNVGTSIfkPTTEYTAEDFSFVMATNLESAFHLS-QLAHPLLKASGSgSIVLISSAA 156
Cdd:PRK06197  82 VRAAADALRAAYP-RIDLLINNAGVMY--TPKQTTADGFELQFGTNHLGHFALTgLLLDRLLPVPGS-RVVTVSSGG 154
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
73-195 5.08e-04

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 40.11  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   73 CDVSSRDQRVKLMETVSSLYqGKLNILVNNVGtsiFKPT-------TEYTAEDFSFVMATNLESAFHLSQLAHPLLkaSG 145
Cdd:PRK08415  62 LDVSKPEHFKSLAESLKKDL-GKIDFIVHSVA---FAPKealegsfLETSKEAFNIAMEISVYSLIELTRALLPLL--ND 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 42570969  146 SGSIVLISSAAGVVHVNVGSIYGATKGAMNQLARNLACEWASDNIRTNSV 195
Cdd:PRK08415 136 GASVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAI 185
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 19-179 1.94e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (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 oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase 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 consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses 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-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses 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 the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif 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: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 38.42  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  19 TALVTGGSKGIGEAVVEELAMLGAK--VHTCAR--DETQlQERLREWQAKGFQVTTSVCDVSSRDQRVKLMETV-SSLYq 93
Cdd:cd08955 151 TYLITGGLGGLGLLVAEWLVERGARhlVLTGRRapSAAA-RQAIAALEEAGAEVVVLAADVSDRDALAAALAQIrASLP- 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  94 gKLNILVNNVGTSIFKPTTEYTAEDFSFVMATNLESAFHLSQLAH--PLlkasgsGSIVLISSAAGVvhvnVGSI----Y 167
Cdd:cd08955 229 -PLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQdlPL------DFFVLFSSVASL----LGSPgqanY 297

                       170
                ....*....|..
gi 42570969 168 GATKGAMNQLAR 179
Cdd:cd08955 298 AAANAFLDALAH 309
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 17-154 2.32e-03

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: 38.35  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKV----HTCARDETQLQERLREWQAKGFQVTTsvCDVSSRDQRVKLMETVSSlY 92
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVilacRNMSRASAAVSRILEEWHKARVEAMT--LDLASLRSVQRFAEAFKA-K 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42570969  93 QGKLNILVNNVGtsIFKPTTEYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGSIVLISS 154
Cdd:cd09809  78 NSPLHVLVCNAA--VFALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSS 137
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 17-60 2.83e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 37.82  E-value: 2.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 42570969  17 GMTALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLqERLRE 60
Cdd:COG0604 140 GETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKA-ELLRA 182
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 20-182 3.37e-03

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 37.66  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969    20 ALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQErlrewqAKGFQVTTSVCDVSSRDQRVKLMETVsslyqgKLNIL 99
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNT------ARLADLRFVEGDLTDRDALEKLLADV------RPDAV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   100 VNNVGTSiFKPTTEYTAEDFsfvMATNLESAFHLSQLAH-----PLLKAS-----GSGSIVLISSAAGVVHVNVGSIYGA 169
Cdd:pfam01370  69 IHLAAVG-GVGASIEDPEDF---IEANVLGTLNLLEAARkagvkRFLFASssevyGDGAEIPQEETTLTGPLAPNSPYAA 144

                         170
                  ....*....|...
gi 42570969   170 TKGAMNQLARNLA 182
Cdd:pfam01370 145 AKLAGEWLVLAYA 157
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 21-185 4.72e-03

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 37.13  E-value: 4.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDEtqlqERLREWQAKGFQVTtsVCDVSSRDQRVKLMETVSSLYqgklnilv 100
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARGHPVRALVRDP----EKAAALAAAGVEVV--QGDLDDPESLAAALAGVDAVF-------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 101 nNVGTSIFKPTTEYTAEdfsfvMATNLESAfhlsqlahplLKASGSGSIVLISSAAgvVHVNVGSIYGATKGAMNQLARN 180
Cdd:COG0702  69 -LLVPSGPGGDFAVDVE-----GARNLADA----------AKAAGVKRIVYLSALG--ADRDSPSPYLRAKAAVEEALRA 130


                ....*
gi 42570969 181 LACEW 185
Cdd:COG0702 131 SGLPY 135
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 21-156 5.41e-03

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 36.96  E-value: 5.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969  21 LVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTTSVCdvsSRDqrvkLMETVSSLYQGKLNILV 100
Cdd:cd05263   2 FVTGGTGFLGRHLVKRLLENGFKVLVLVRSESLGEAHERIEEAGLEADRVRVL---EGD----LTQPNLGLSAAASRELA 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969 101 NNVgTSIF----KPTTEYTAEDfsfVMATNLESAFHLSQLAHpllkASGSGSIVLISSAA 156
Cdd:cd05263  75 GKV-DHVIhcaaSYDFQAPNED---AWRTNIDGTEHVLELAA----RLDIQRFHYVSTAY 126
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
73-202 5.67e-03

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 37.04  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   73 CDVSSRDQRVKLMETVSSLYqGKLNILVNNVGTSIFKPTT----EYTAEDFSFVMATNLESAFHLSQLAHPLLKASGSGS 148
Cdd:PRK08159  67 CDVTDEASIDAVFETLEKKW-GKLDFVVHAIGFSDKDELTgryvDTSRDNFTMTMDISVYSFTAVAQRAEKLMTDGGSIL 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42570969  149 IVLISSAAGVV-HVNVgsiYGATKGAMNQLARNLACEWASDNIRTNSVCPWYITT 202
Cdd:PRK08159 146 TLTYYGAEKVMpHYNV---MGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKT 197
PRK08862 PRK08862
SDR family oxidoreductase;
19-197 7.01e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 36.63  E-value: 7.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   19 TALVTGGSKGIGEAVVEELAMLGAKVHTCARDETQLQERLREWQAKGFQVTT-SVCDVSSRDQRvKLMETVSSLYQGKLN 97
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSfQLKDFSQESIR-HLFDAIEQQFNRAPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570969   98 ILVNNvgtsifkptteYTAEDFSFVMATNLESAF--HLSQLAHPLLKASGSGSIVLISSAAGVVHVNVGS------IYGA 169
Cdd:PRK08862  86 VLVNN-----------WTSSPLPSLFDEQPSESFiqQLSSLASTLFTYGQVAAERMRKRNKKGVIVNVIShddhqdLTGV 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42570969  170 TkgAMNQLARNLACEWASD----NIRTNSVCP 197
Cdd:PRK08862 155 E--SSNALVSGFTHSWAKEltpfNIRVGGVVP 184
 
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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