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Conserved domains on  [gi|1191833562|ref|XP_020927637|]
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15-hydroxyprostaglandin dehydrogenase [NAD(+)] isoform X3 [Sus scrofa]

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 ...
 6-141 5.26e-60

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 cd05323:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 244  Bit Score: 185.20  E-value: 5.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  86 DILVNNAGVNNEK----------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAG 141
Cdd:cd05323    79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAG 144
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-141 5.26e-60

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: 185.20  E-value: 5.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  86 DILVNNAGVNNEK----------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAG 141
Cdd:cd05323    79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAG 144
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-142 4.70e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 150.84  E-value: 4.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA--LGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGK 142
Cdd:pfam00106  79 DILVNNAGITglgpfselSDEDWERVIDVNLTGVFNLTRAVLPAMIKG---SGGRIVNISSVAGL 140
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-142 2.09e-40

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: 135.30  E-value: 2.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:COG1028     6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA--AGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGK 142
Cdd:COG1028    84 LDILVNNAGITPpgpleeltEEDWDRVLDVNLKGPFLLTRAALPHMRER---GGGRIVNISSIAGL 146
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-142 1.35e-35

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 122.96  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpqKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK05653    1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG--EARVLVFDVSDEAAVRALIEAAVE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  81 HFGRLDILVNNAGVNN--------EKNWEKTLQINLvsviSGTYLG----LDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK05653   79 AFGALDILVNNAGITRdallprmsEEDWDRVIDVNL----TGTFNVvraaLPPMIKARYGR---IVNISSVSGV 145
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-111 3.05e-13

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 64.65  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDW-NFEAGVKCKAALDEQFE------PQKTLFIQCDVADQAQLRDTFRK 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLcADDPAVGYPLATRAELDavaaacPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1191833562  78 VVDHFGRLDILVNNAGV---------NNEKNWEKTLQINLVSV 111
Cdd:TIGR04504  81 AVERWGRLDAAVAAAGViaggrplweTTDAELDLLLDVNLRGV 123
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 6-111 2.50e-10

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 56.61  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVK----CKAALDEQFE--PQKTLFIQCDVADQAQLRDTFRKVV 79
Cdd:NF040491    1 RVALVTGAARGIGAATVRRLAARGYAVVAVDACAGDPAPyplgTEADLDALVAssPGRVETVVADVRDRAALAAAVALAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1191833562  80 DHFGRLDILVNNAGV---------NNEKNWEKTLQINLVSV 111
Cdd:NF040491   81 DRWGRLDAAVAAAAViaggrplweTPPEELDALWDVDVRGV 121
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-94 2.35e-05

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: 42.08  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562    6 KVALVTGAAQGIGRASAEALLLKGA-KVALV------DWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKV 78
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLsrsgpdAPGAAALLAELEAAGAR-----VTVVACDVADRDALAAVLAAI 75

                           90
                   ....*....|....*.
gi 1191833562   79 VDHFGRLDILVNNAGV 94
Cdd:smart00822  76 PAVEGPLTGVIHAAGV 91
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-141 5.26e-60

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: 185.20  E-value: 5.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  86 DILVNNAGVNNEK----------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAG 141
Cdd:cd05323    79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAG 144
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-142 4.70e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 150.84  E-value: 4.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA--LGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGK 142
Cdd:pfam00106  79 DILVNNAGITglgpfselSDEDWERVIDVNLTGVFNLTRAVLPAMIKG---SGGRIVNISSVAGL 140
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-142 2.09e-40

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: 135.30  E-value: 2.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:COG1028     6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA--AGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGK 142
Cdd:COG1028    84 LDILVNNAGITPpgpleeltEEDWDRVLDVNLKGPFLLTRAALPHMRER---GGGRIVNISSIAGL 146
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-142 7.94e-40

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: 133.56  E-value: 7.94e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkcKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRLDI 87
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAL---AELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  88 LVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGK 142
Cdd:cd05233    78 LVNNAGIArpgpleelTDEDWDRVLDVNLTGVFLLTRAALPHMKKQG---GGRIVNISSVAGL 137
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-142 2.36e-37

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: 127.22  E-value: 2.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFepqktLFIQCDVADQAQLRDTFRKVVD 80
Cdd:COG4221     1 MSDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRA-----LAVPLDVTDEAAVEAAVAAAVA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGK 142
Cdd:COG4221    76 EFGRLDVLVNNAGVAllgpleelDPEDWDRMIDVNVKGVLYVTRAALPAMRARG---SGHIVNISSIAGL 142
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-142 1.35e-35

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 122.96  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpqKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK05653    1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG--EARVLVFDVSDEAAVRALIEAAVE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  81 HFGRLDILVNNAGVNN--------EKNWEKTLQINLvsviSGTYLG----LDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK05653   79 AFGALDILVNNAGITRdallprmsEEDWDRVIDVNL----TGTFNVvraaLPPMIKARYGR---IVNISSVSGV 145
FabG-like PRK07231
SDR family oxidoreductase;
1-141 2.57e-34

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 119.93  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkcKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK07231    1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAA---ERVAAEILAGGRAIAVAADVSDEADVEAAVAAALE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:PRK07231   78 RFGSVDILVNNAGTThrngplldvDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG---GGAIVNVASTAG 144
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-141 2.76e-34

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 119.59  E-value: 2.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:COG0300     1 MSLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRA--AGARVEVVALDVTDPDAVAALAEAVLA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:COG0300    79 RFGPIDVLVNNAGVGgggpfeelDLEDLRRVFEVNVFGPVRLTRALLPLMRARG---RGRIVNVSSVAG 144
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-142 1.44e-33

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 118.06  E-value: 1.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVkcKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK12429    2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAA--AAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  83 GRLDILVNNAG---VNNEKN-----WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK12429   80 GGVDILVNNAGiqhVAPIEDfptekWKKMIAIMLDGAFLTTKAALPIMKAQGGGR---IINMASVHGL 144
PRK07063 PRK07063
SDR family oxidoreductase;
5-138 3.32e-32

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 114.76  E-value: 3.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK07063    7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFGP 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSS 138
Cdd:PRK07063   87 LDVLVNNAGINvfadplamTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGS---IVNIAS 145
PRK12826 PRK12826
SDR family oxidoreductase;
5-141 3.42e-32

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 114.24  E-value: 3.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkckAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK12826    6 GRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDA----AATAELVEAAggKARARQVDVRDRAALKAAVAAGVEDF 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK12826   82 GRLDILVANAGIFPltpfaemdDEQWERVIDVNLTGTFLLTQAALPALIRAGGGR---IVLTSSVAG 145
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-141 3.84e-31

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 111.44  E-value: 3.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkcKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKV 78
Cdd:PRK05557    1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAG---AEALVAEIGALggKALAVQGDVSDAESVERAVDEA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  79 VDHFGRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK05557   78 KAEFGGVDILVNNAGITRDNLlmrmkeedWDRVIDTNLTGVFNLTKAVARPMMKQRSGR---IINISSVVG 145
PRK07326 PRK07326
SDR family oxidoreductase;
1-142 1.18e-30

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 110.10  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK07326    2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKE---LEEAAAELNNKGNVLGLAADVRDEADVQRAVDAIVA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQnggeGGIIINMSSLAGK 142
Cdd:PRK07326   79 AFGGLDVLIANAGVGHFAPveeltpeeWRLVIDTNLTGAFYTIKAAVPALKRG----GGYIINISSLAGT 144
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-141 2.52e-30

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: 109.39  E-value: 2.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05341     3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDA-----ARFFHLDVTDEDGWTAVVDTAREAF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd05341    78 GRLDVLVNNAGILTGGTvetttleeWRRLLDINLTGVFLGTRAVIPPMKEAGGGS---IINMSSIEG 141
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-141 3.73e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 109.36  E-value: 3.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVKCKAALDeqfePQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK06841   14 SGKVAVVTGGASGIGHAIAELFAAKGARVALLDRS-EDVAEVAAQLL----GGNAKGLVCDVSDSQSVEAAVAAVISAFG 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLgldyMSKQNGGE-----GGIIINMSSLAG 141
Cdd:PRK06841   89 RIDILVNSAGVAllapaedvSEEDWDKTIDINL----KGSFL----MAQAVGRHmiaagGGKIVNLASQAG 151
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-141 5.27e-30

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: 108.29  E-value: 5.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  12 GAA--QGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPqktlFIQCDVADQAQLRDTFRKVVDHFGRLDILV 89
Cdd:pfam13561   1 GAAneSGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAA----VLPCDVTDEEQVEALVAAAVEKFGRLDILV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  90 NNAGVNN----------EKNWEKTLQINLVSVISGTYLGLDYMskqngGEGGIIINMSSLAG 141
Cdd:pfam13561  77 NNAGFAPklkgpfldtsREDFDRALDVNLYSLFLLAKAALPLM-----KEGGSIVNLSSIGA 133
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-141 2.44e-29

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 106.85  E-value: 2.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVAL-VDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVV 79
Cdd:PRK05565    1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKE--EGGDAIAVKADVSSEEDVENLVEQIV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  80 DHFGRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:PRK05565   79 EKFGKIDILVNNAGISNfglvtdmtDEEWDRVIDVNLTGVMLLTRYALPYMIKRK---SGVIVNISSIWG 145
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 4-143 3.45e-29

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 106.60  E-value: 3.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDeqfepqKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGD------NCRFVPVDVTSEKDVKAALALAKAKFG 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  84 RLDILVNNAGV-------NNEKN-------WEKTLQINLVSVISGTYLGLDYMSKQ---NGGEGGIIINMSSLAGKD 143
Cdd:cd05371    75 RLDIVVNCAGIavaaktyNKKGQqphslelFQRVINVNLIGTFNVIRLAAGAMGKNepdQGGERGVIINTASVAAFE 151
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 4-142 7.76e-29

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 105.86  E-value: 7.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK08265    5 AGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGER-----ARFIATDITDDAAIERAVATVVARFG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNA------GVNNEKN-WEKTLQINLVSVISGTYLGLDYMSKQnggeGGIIINMSSLAGK 142
Cdd:PRK08265   80 RVDILVNLActylddGLASSRAdWLAALDVNLVSAAMLAQAAHPHLARG----GGAIVNFTSISAK 141
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-142 9.91e-29

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 105.49  E-value: 9.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK07067    2 MRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPA-----AIAVSLDVTRQDSIDRIVAAAVE 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  81 HFGRLDILVNNAGV--------NNEKNWEKTLQINlvsvISGTYLGLDYMSKQ--NGGEGGIIINMSSLAGK 142
Cdd:PRK07067   77 RFGGIDILFNNAALfdmapildISRDSYDRLFAVN----VKGLFFLMQAVARHmvEQGRGGKIINMASQAGR 144
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
4-141 2.20e-28

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 104.81  E-value: 2.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK08643    1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSK--DGGKAIAVKADVSDRDQVFAAVRQVVDTFG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAG 141
Cdd:PRK08643   79 DLNVVVNNAGVApttpietiTEEQFDKVYNINVGGVIWGIQAAQEAFKKL--GHGGKIINATSQAG 142
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 5-142 4.02e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 103.98  E-value: 4.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepqKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK12829   11 GLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGA----KVTATVADVADPAQVERVFDTAVERFGG 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  85 LDILVNNAGVNN---------EKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGK 142
Cdd:PRK12829   87 LDVLVNNAGIAGptggideitPEQWEQTLAVNLNGQFYFARAAVPLLKAS--GHGGVIIALSSVAGR 151
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-142 5.58e-28

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: 103.39  E-value: 5.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE-QFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd08934     3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVD---RLEALADElEAEGGKALVLELDVTDEQQVDAAVERTVEALG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:cd08934    80 RLDILVNNAGImllgpvedADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGT---IVNISSVAGR 143
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 4-141 5.59e-28

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: 103.61  E-value: 5.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd05366     1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAG-YNAVAVGADVTDKDDVEALIDQAVEKFG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAG 141
Cdd:cd05366    80 SFDVMVNNAGIApitplltiTEEDLKKVYAVNVFGVLFGIQAAARQFKKLGH--GGKIINASSIAG 143
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-142 6.08e-28

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: 103.51  E-value: 6.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVKcKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARN-RENLE-RAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  85 LDILVNNAG---------VNNEKnWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGK 142
Cdd:cd05344    79 VDILVNNAGgpppgpfaeLTDED-WLEAFDLKLLSVIRIVRAVLPGMKER---GWGRIVNISSLTVK 141
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 6-142 1.01e-27

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: 102.63  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDEQFE-PQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEE---AAAETVEEIKAlGGNAAALEADVSDREAVEALVEKVEAEFGP 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:cd05333    78 VDILVNNAGITrdnllmrmSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGR---IINISSVVGL 140
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-141 9.17e-27

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 100.33  E-value: 9.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK12825    2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALG-RRAQAVQADVTDKAALEAAVAAAVE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK12825   81 RFGRIDILVNNAGIFedkpladmSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGR---IVNISSVAG 146
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-141 9.83e-27

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 100.47  E-value: 9.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfeagvkckaalDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK06171    7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-----------GGDGQHENYQFVPTDVSSAEEVNHTVAEIIEKF 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  83 GRLDILVNNAGVN-----------------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:PRK06171   76 GRIDGLVNNAGINiprllvdekdpagkyelNEAAFDKMFNINQKGVFLMSQAVARQMVKQH---DGVIVNMSSEAG 148
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 4-144 1.32e-26

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: 99.79  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEP-QKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05364     2 SGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSeKKILLVVADLTEEEGQDRIISTTLAKF 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggiIINMSSLAGKDS 144
Cdd:cd05364    82 GRLDILVNNAGILakgggedqDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGE----IVNVSSVAGGRS 147
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-108 2.42e-26

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 103.00  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK08324  422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP---DRALGVACDVTDEAAVQAAFEEAALAFGG 498

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1191833562  85 LDILVNNAGV--------NNEKNWEKTLQINL 108
Cdd:PRK08324  499 VDIVVSNAGIaisgpieeTSDEDWRRSFDVNA 530
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-142 2.64e-26

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: 99.44  E-value: 2.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd08940     1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  84 RLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:cd08940    81 GVDILVNNAGIQHvapiedfpTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGR---IINIASVHGL 144
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-141 6.68e-26

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 98.32  E-value: 6.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKckaaldeQFEPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK06463    3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAK-------ELREKGVFTIKCDVGNRDQVKKSKEVVEK 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  81 HFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:PRK06463   76 EFGRVDVLVNNAGImylmpfeeFDEEKYNKMIKINLNGAIYTTYEFLPLLKLS---KNGAIVNIASNAG 141
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-138 1.03e-25

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: 97.40  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05352     8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKY-GVKTKAYKCDVSSQESVEKTFKQIQKDFGK 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLGLDYMSKQ--NGGEGGIII--NMSS 138
Cdd:cd05352    87 IDILIANAGITvhkpaldyTYEQWNKVIDVNL----NGVFNCAQAAAKIfkKQGKGSLIItaSMSG 148
PRK07831 PRK07831
SDR family oxidoreductase;
5-141 1.13e-25

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 97.80  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAA-QGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK07831   17 GKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGRVEAVVCDVTSEAQVDALIDAAVERLG 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAG 141
Cdd:PRK07831   97 RLDVLVNNAGLGGQTPvvdmtddeWSRVLDVTLTGTFRATRAALRYMRAR--GHGGVIVNNASVLG 160
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-138 1.15e-25

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: 97.45  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05358     3 GKVALVTGASSGIGKAIAIRLATAGANVVV---NYRSKEDAAEEVVEEIKAVggKAIAVQADVSKEEDVVALFQSAIKEF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  83 GRLDILVNNAGVNNE--------KNWEKTLQINLvsviSGTYLG----LDYMSKQNggEGGIIINMSS 138
Cdd:cd05358    80 GTLDILVNNAGLQGDasshemtlEDWNKVIDVNL----TGQFLCareaIKRFRKSK--IKGKIINMSS 141
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-139 1.43e-25

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: 97.04  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05347     5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKA-EEAQQLIEK-EGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSL 139
Cdd:cd05347    83 IDILVNNAGIIrrhpaeefPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGK---IINICSL 142
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-138 4.69e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 95.95  E-value: 4.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkcKAALDEQfepqKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06057    7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAG---KAAADEV----GGLFVPTDVTDEDAVNALFDTAAETYGS 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  85 LDILVNNAGVNNEKN----------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSS 138
Cdd:PRK06057   80 VDIAFNNAGISPPEDdsilntgldaWQRVQDVNLTSVYLCCKAALPHMVRQGKGS---IINTAS 140
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-141 5.52e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 96.26  E-value: 5.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06701   46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEK-EGVKCLLIPGDVSDEAFCKDAVEETVRELGR 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAG 141
Cdd:PRK06701  125 LDILVNNAAFQypqqslediTAEQLDKTFKTNIYSYFHMTKAALPHLKQ-----GSAIINTGSITG 185
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 5-140 6.21e-25

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: 95.75  E-value: 6.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  85 LDILVNNAGVNN------EKNWEKTLQINlvsvisgtYLG--------LDYMSKQNGGEggiIINMSSLA 140
Cdd:cd05327    81 LDILINNAGIMApprrltKDGFELQFAVN--------YLGhflltnllLPVLKASAPSR---IVNVSSIA 139
PRK05855 PRK05855
SDR family oxidoreductase;
5-140 1.18e-24

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 98.13  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVKCKAALDEQFEPQKTLFiQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK05855  315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDID-EAAAERTAELIRAAGAVAHAY-RVDVSDADAMEAFAEWVRAEHGV 392

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLA 140
Cdd:PRK05855  393 PDIVVNNAGIgmaggfldTSAEDWDRVLDVNLWGVIHGCRLFGRQMVER--GTGGHIVNVASAA 454
PRK06172 PRK06172
SDR family oxidoreductase;
1-141 1.80e-24

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 94.43  E-value: 1.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK06172    3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREA--GGEALFVACDVTRDAEVKALVEQTIA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  81 HFGRLDILVNNAGV---------NNEKNWEKTLQINLvsviSGTYLGLDY----MSKQNGGEggiIINMSSLAG 141
Cdd:PRK06172   81 AYGRLDYAFNNAGIeieqgrlaeGSEAEFDAIMGVNV----KGVWLCMKYqiplMLAQGGGA---IVNTASVAG 147
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-142 1.88e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 94.62  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDeqfepqKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK07825    3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG------LVVGGPLDVTDPASFAAFLDAVEADL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  83 GRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK07825   77 GPIDVLVNNAGVmpvgpfldEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGH---VVNVASLAGK 141
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-140 2.89e-24

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 93.87  E-value: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWN----FEAGVKCKAAldeqfePQKTLFIQCDVADQAQLRDTFR 76
Cdd:PRK08217    1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNqeklEEAVAECGAL------GTEVRGYAANVTDEEDVEATFA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  77 KVVDHFGRLDILVNNAGVNNE-----------------KNWEKTLQINLvsviSGTYL-GLDYMSKQ-NGGEGGIIINMS 137
Cdd:PRK08217   75 QIAEDFGQLNGLINNAGILRDgllvkakdgkvtskmslEQFQSVIDVNL----TGVFLcGREAAAKMiESGSKGVIINIS 150


                  ...
gi 1191833562 138 SLA 140
Cdd:PRK08217  151 SIA 153
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 6-143 3.85e-24

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: 92.96  E-value: 3.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVkcKAALDEQFEpqKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRVGICARD-EARL--AAAAAQELE--GVLGLAGDVRDEADVRRAVDAMEEAFGGL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  86 DILVNNAGVNNEKN--------WEKTLQINLvsvISGTYLGLDYMSKQNGGEGGIIINMSSLAGKD 143
Cdd:cd08929    76 DALVNNAGVGVMKPveeltpeeWRLVLDTNL---TGAFYCIHKAAPALLRRGGGTIVNVGSLAGKN 138
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-138 5.23e-24

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: 93.04  E-value: 5.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE--QFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05369     3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPE---VLEAAAEEisSATGGRAHPIQCDVRDPEAVEAAVDETLKEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  83 GRLDILVNNAGVN--------NEKNWEKTLQINLVsvisGTYlgldYMSKQNG------GEGGIIINMSS 138
Cdd:cd05369    80 GKIDILINNAAGNflapaeslSPNGFKTVIDIDLN----GTF----NTTKAVGkrlieaKHGGSILNISA 141
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 5-141 7.35e-24

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: 92.98  E-value: 7.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQkTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd08933     9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGS-CKFVPCDVTKEEDIKTLISVTVERFGR 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVNNEKNW-EKT--------LQINLVSVISGTYLGLDYMSKQNGGeggiIINMSSLAG 141
Cdd:cd08933    88 IDCLVNNAGWHPPHQTtDETsaqefrdlLNLNLISYFLASKYALPHLRKSQGN----IINLSSLVG 149
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-142 1.83e-23

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 91.29  E-value: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVKCKAALDEQFEpQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK07666    3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLART-EENLKAVAEEVEAYG-VKVVIATADVSDYEEVTAAIEQLKN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK07666   81 ELGSIDILINNAGISKFGKfleldpaeWEKIIQVNLMGVYYATRAVLPSMIERQSGD---IINISSTAGQ 147
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 5-141 2.04e-23

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: 91.36  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDeqfePQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05326     4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELG----DPDISFVHCDVTVEADVRAAVDTAVARFGR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  85 LDILVNNAGV----------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd05326    80 LDIMFNNAGVlgapcysileTSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGS---IVSVASVAG 143
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 5-110 2.29e-23

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: 91.30  E-value: 2.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCkaALDEQFEPqKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKV--AEAAQGGP-RALGVQCDVTSEAQVQSAFEQAVLEFGG 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1191833562  85 LDILVNNAGV--------NNEKNWEKTLQINLVS 110
Cdd:cd08943    78 LDIVVSNAGIatsspiaeTSLEDWNRSMDINLTG 111
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-142 3.53e-23

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: 91.14  E-value: 3.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkckAALDEQFEPQkTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAA----RATAAEIGPA-ACAISLDVTDQASIDRCVAALVDRW 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVNN-----EKNWEKTLQINLVSViSGTYLGLDYMSKQ--NGGEGGIIINMSSLAGK 142
Cdd:cd05363    76 GSIDILVNNAALFDlapivDITRESYDRLFAINV-SGTLFMMQAVARAmiAQGRGGKIINMASQAGR 141
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-144 4.54e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 90.60  E-value: 4.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDE--QFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIA---TYFSGNDCAKDWFEeyGFTEDQVRLKELDVTDTEECAEALAEIEEEEG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  84 RLDILVNNAGVNNEK--------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGKDS 144
Cdd:PRK12824   80 PVDILVNNAGITRDSvfkrmshqEWNDVINTNLNSVFNVTQPLFAAMCEQGYGR---IINISSVNGLKG 145
PRK06138 PRK06138
SDR family oxidoreductase;
1-138 5.11e-23

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 90.60  E-value: 5.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK06138    1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAG---GRAFARQGDVGSAEAVEALVDFVAA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLGLDY----MSKQNGGEggiIINMSS 138
Cdd:PRK06138   78 RWGRLDVLVNNAGFGcggtvvttDEADWDAVMRVNV----GGVFLWAKYaipiMQRQGGGS---IVNTAS 140
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-139 5.78e-23

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 90.16  E-value: 5.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfeagvKCKAALDEQFEPQ----KTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK08063    4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNYAR-----SRKAAEETAEEIEalgrKALAVKANVGDVEKIKEMFAQIDE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  81 HFGRLDILVNNA--GVN------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSL 139
Cdd:PRK08063   79 EFGRLDVFVNNAasGVLrpamelEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGK---IISLSSL 142
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 6-141 7.43e-23

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: 90.27  E-value: 7.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd05330     4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  86 DILVNNAGVNNEKN---------WEKTLQINLvsviSGTYLGLDYMSKQNGGEG-GIIINMSSLAG 141
Cdd:cd05330    84 DGFFNNAGIEGKQNltedfgadeFDKVVSINL----RGVFYGLEKVLKVMREQGsGMIVNTASVGG 145
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 6-141 9.05e-23

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: 89.60  E-value: 9.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVAlvdwnfeAGVKCKAAL-DEQFEPQKTLF-IQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVI-------ATARNPDKLeSLGELLNDNLEvLELDVTDEESIKAAVKEVIERFG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:cd05374    74 RIDVLVNNAGYGlfgpleetSIEEVRELFEVNVFGPLRVTRAFLPLMRKQ---GSGRIVNVSSVAG 136
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-141 9.40e-23

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: 89.76  E-value: 9.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:cd05345     1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEA-----AIAIQADVTKRADVEAMVEAALS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:cd05345    76 KFGRLDILVNNAGIThrnkpmlevDEEEFDRVFAVNVKSIYLSAQALVPHMEEQG---GGVIINIASTAG 142
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-142 1.27e-22

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 89.29  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQF--EPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK12935    4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLVNELgkEGHDVYAVQADVSKVEDANRLVEEAVN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSLAGK 142
Cdd:PRK12935   81 HFGKVDILVNNAGITrdrtfkklNREDWERVIDVNLSSVFNTTSAVLPYITE---AEEGRIISISSIIGQ 147
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 5-141 3.01e-22

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 88.62  E-value: 3.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK12827    6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAAggKALGLAFDVRDFAATRAALDAGVEEF 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVNNEK--------NWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAG 141
Cdd:PRK12827   86 GRLDILVNNAGIATDAafaelsieEWDDVIDVNLDGFFNVTQAALPPMIRARR--GGRIVNIASVAG 150
PRK07069 PRK07069
short chain dehydrogenase; Validated
 8-141 4.84e-22

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 87.84  E-value: 4.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAA-LDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRLD 86
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAeINAAHGEGVAFAAVQDVTDEAQWQALLAQAADAMGGLS 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  87 ILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSLAG 141
Cdd:PRK07069   82 VLVNNAGVGSFGAieqieldeWRRVMAINVESIFLGCKHALPYLRA---SQPASIVNISSVAA 141
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-138 6.13e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 87.72  E-value: 6.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK12939    6 AGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA--GGRAHAIAADLADPASVQRFFDAAAAALG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  84 RLDILVNNAGVNNEK--------NWEKTLQINLvsviSGTYLgldyMSKQNG-----GEGGIIINMSS 138
Cdd:PRK12939   84 GLDGLVNNAGITNSKsateldidTWDAVMNVNV----RGTFL----MLRAALphlrdSGRGRIVNLAS 143
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 3-111 6.64e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 88.49  E-value: 6.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK05872    7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAE---LAALAAELGGDDRVLTVVADVTDLAAMQAAAEEAVERF 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVNN--------EKNWEKTLQINLVSV 111
Cdd:PRK05872   84 GGIDVVVANAGIASggsvaqvdPDAFRRVIDVNLLGV 120
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 4-138 6.87e-22

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 87.86  E-value: 6.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKcKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK08936    6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEAN-DVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  84 RLDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNggEGGIIINMSS 138
Cdd:PRK08936   85 TLDVMINNAGIENAvpshemslEDWNKVINTNLTGAFLGSREAIKYFVEHD--IKGNIINMSS 145
PRK07774 PRK07774
SDR family oxidoreductase;
1-140 1.15e-21

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 87.11  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK07774    2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVA--DGGTAIAVQVDVSDPDSAKAMADATVS 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  81 HFGRLDILVNNAGVNNE-----------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLA 140
Cdd:PRK07774   80 AFGGIDYLVNNAAIYGGmkldllitvpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGA---IVNQSSTA 147
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 5-142 1.36e-21

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 87.01  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK12384    2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGR 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLVsvisGTYLGLDYMSKQ--NGGEGGIIINMSSLAGK 142
Cdd:PRK12384   82 VDLLVYNAGIAkaafitdfQLGDFDRSLQVNLV----GYFLCAREFSRLmiRDGIQGRIIQINSKSGK 145
PRK09242 PRK09242
SDR family oxidoreductase;
4-141 1.70e-21

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 86.72  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK09242    8 DGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHWD 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:PRK09242   88 GLHILVNNAGGNirkaaidyTEDEWRGIFETNLFSAFELSRYAHPLLKQH---ASSAIVNIGSVSG 150
PRK07856 PRK07856
SDR family oxidoreductase;
4-141 2.59e-21

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 86.14  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKValvdwnfeagVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK07856    5 TGRVVLVTGGTRGIGAGIARAFLAAGATV----------VVCGRRAPETVDGRPAEFHAADVRDPDQVAALVDAIVERHG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAG 141
Cdd:PRK07856   75 RLDVLVNNAGgspyalaaEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPG--GGSIVNIGSVSG 138
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 4-138 2.79e-21

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: 85.91  E-value: 2.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVAL------VDWNFEA----GVKCKAALDEQFEPQKTLFIQCDVADQAQLRD 73
Cdd:cd05338     2 SGKVAFVTGASRGIGRAIALRLAKAGATVVVaaktasEGDNGSAkslpGTIEETAEEIEAAGGQALPIVVDVRDEDQVRA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  74 TFRKVVDHFGRLDILVNNAGV----NNE----KNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSS 138
Cdd:cd05338    82 LVEATVDQFGRLDILVNNAGAiwlsLVEdtpaKRFDLMQRVNLRGTYLLSQAALPHMVKA---GQGHILNISP 151
PRK06914 PRK06914
SDR family oxidoreductase;
4-142 3.02e-21

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 86.23  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRdTFRKVVDHFG 83
Cdd:PRK06914    2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIH-NFQLVLKEIG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  84 RLDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK06914   81 RIDLLVNNAGYANGgfveeipvEEYRKQFETNVFGAISVTQAVLPYMRKQKSGK---IINISSISGR 144
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 4-141 3.28e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 86.25  E-value: 3.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkcKAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK08263    2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTAT----LADLAEKY-GDRLLPLALDVTDRAAVFAAVETAVEHFG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK08263   77 RLDIVVNNAGYGlfgmieevTESEARAQIDTNFFGALWVTQAVLPYLREQRSGH---IIQISSIGG 139
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 4-141 3.47e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 86.11  E-value: 3.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKValvdwnFEAGVKC-KAALDEQFEpqktlFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK06179    3 NSKVALVTGASSGIGRATAEKLARAGYRV------FGTSRNPaRAAPIPGVE-----LLELDVTDDASVQAAVDEVIARA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVN-----NEKNWEKTLQI---NLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK06179   72 GRIDVLVNNAGVGlagaaEESSIAQAQALfdtNVFGILRMTRAVLPHMRAQGSGR---IINISSVLG 135
PRK06181 PRK06181
SDR family oxidoreductase;
5-142 4.00e-21

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 85.80  E-value: 4.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADH--GGEALVVPTDVSDAEACERLIEAAVARFGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  85 LDILVNNAGVNNEKNWEKT---------LQINLVSVISGTYLGLDYMsKQNGGEggiIINMSSLAGK 142
Cdd:PRK06181   79 IDILVNNAGITMWSRFDELtdlsvfervMRVNYLGAVYCTHAALPHL-KASRGQ---IVVVSSLAGL 141
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 1-143 4.03e-21

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 85.67  E-value: 4.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK06113    7 LRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQL--GGQAFACRCDITSEQELSALADFALS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 HFGRLDILVNNAGVNNEK-------NWEKTLQINLVSVISGTYLGLDYMSKqNGgeGGIIINMSSLAGKD 143
Cdd:PRK06113   85 KLGKVDILVNNAGGGGPKpfdmpmaDFRRAYELNVFSFFHLSQLVAPEMEK-NG--GGVILTITSMAAEN 151
PRK07062 PRK07062
SDR family oxidoreductase;
3-139 4.48e-21

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 85.48  E-value: 4.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK07062    6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARF 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  83 GRLDILVNNAG---VNNEKN-----WEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSL 139
Cdd:PRK07062   86 GGVDMLVNNAGqgrVSTFADttddaWRDELELKYFSVINPTRAFLPLLRAS---AAASIVCVNSL 147
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-140 4.95e-21

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 85.21  E-value: 4.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfeagvkcKAALDE---QFEPQKTlfIQCDVADQAQLRDTFRK 77
Cdd:COG3967     1 MKLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRR-------EEKLEEaaaANPGLHT--IVLDVADPASIAALAEQ 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  78 VVDHFGRLDILVNNAGV-------NNEKNWEK---TLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSS-LA 140
Cdd:COG3967    72 VTAEFPDLNVLINNAGImraedllDEAEDLADaerEITTNLLGPIRLTAAFLPHLKAQ---PEAAIVNVSSgLA 142
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-142 6.71e-21

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: 84.95  E-value: 6.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPqKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAP-SPHVVPLDMSDLEDAEQVVEEALKLF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  83 GRLDILVNNAGVNNEKNW--------EKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGK 142
Cdd:cd05332    80 GGLDILINNAGISMRSLFhdtsidvdRKIMEVNYFGPVALTKAALPHLIERS---QGSIVVVSSIAGK 144
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 7-141 6.76e-21

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: 84.74  E-value: 6.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFGRLD 86
Cdd:cd05360     2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVREL--GGEAIAVVADVADAAQVERAADTAVERFGRID 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  87 ILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:cd05360    80 TWVNNAGVAvfgrfedvTPEEFRRVFDVNYLGHVYGTLAALPHLRRRG---GGALINVGSLLG 139
PRK07454 PRK07454
SDR family oxidoreductase;
6-142 9.59e-21

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 84.24  E-value: 9.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:PRK07454    7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST--GVKAAAYSIDLSNPEAIAPGIAELLEQFGCP 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  86 DILVNNAGV--NNE------KNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGK 142
Cdd:PRK07454   85 DVLINNAGMayTGPllemplSDWQWVIQLNLTSVFQCCSAVLPGMRAR---GGGLIINVSSIAAR 146
PRK06114 PRK06114
SDR family oxidoreductase;
3-141 1.59e-20

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 84.06  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK06114    6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEA-AGRRAIQIAADVTSKADLRAAVARTEAEL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKqNGgeGGIIINMSSLAG 141
Cdd:PRK06114   85 GALTLAVNAAGIANanpaeemeEEQWQTVMDINLTGVFLSCQAEARAMLE-NG--GGSIVNIASMSG 148
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 3-141 1.76e-20

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 84.18  E-value: 1.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK08277    8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAA--GGEALAVKADVLDKESLEQARQQILEDF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  83 GRLDILVNNAGVNN-----------------------EKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSL 139
Cdd:PRK08277   86 GPCDILINGAGGNHpkattdnefhelieptktffdldEEGFEFVFDLNLLGTLLPTQVFAKDMVGR---KGGNIINISSM 162


                  ..
gi 1191833562 140 AG 141
Cdd:PRK08277  163 NA 164
PRK07035 PRK07035
SDR family oxidoreductase;
5-141 2.39e-20

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 83.53  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkCKAALDEQFEP-QKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK07035    8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDG---CQAVADAIVAAgGKAEALACHIGEMEQIDALFAHIRERHG 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  84 RLDILVNNAGVN---------NEKNWEKTLQINlvsvISGTYlgldYMSKQNG-----GEGGIIINMSSLAG 141
Cdd:PRK07035   85 RLDILVNNAAANpyfghildtDLGAFQKTVDVN----IRGYF----FMSVEAGklmkeQGGGSIVNVASVNG 148
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-138 3.69e-20

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: 83.01  E-value: 3.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd09761     1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPN-----LFFVHGDVADETLVKFVVYAMLEKLGR 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  85 LDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNggegGIIINMSS 138
Cdd:cd09761    76 IDVLVNNAARGSKGIlssllleeWDRILSVNLTGPYELSRYCRDELIKNK----GRIINIAS 133
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-141 4.37e-20

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: 82.95  E-value: 4.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE-QFEPQKTLF-IQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05343     6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVD---KIEALAAEcQSAGYPTLFpYQCDLSNEEQILSMFSAIRTQH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGiIINMSSLAG 141
Cdd:cd05343    83 QGVDVCINNAGLarpepllsGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGH-IININSMSG 148
PRK07201 PRK07201
SDR family oxidoreductase;
3-138 4.96e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 85.00  E-value: 4.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDEQFEPQKTLFI-QCDVADQAQLRDTFRKVVDH 81
Cdd:PRK07201  369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGE---ALDELVAEIRAKGGTAHAyTCDLTDSAAVDHTVKDILAE 445

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  82 FGRLDILVNNAG----------VNNEKNWEKTLQINL---VSVISGTylgLDYMSKQNGGEggiIINMSS 138
Cdd:PRK07201  446 HGHVDYLVNNAGrsirrsvensTDRFHDYERTMAVNYfgaVRLILGL---LPHMRERRFGH---VVNVSS 509
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-107 5.76e-20

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 82.62  E-value: 5.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFeagvkcKAALDEQFEPqktlfIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK08220    4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAF------LTQEDYPFAT-----FVLDVSDAAAVAQVCQRLLA 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1191833562  81 HFGRLDILVNNAGV--------NNEKNWEKTLQIN 107
Cdd:PRK08220   73 ETGPLDVLVNAAGIlrmgatdsLSDEDWQQTFAVN 107
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-141 7.48e-20

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: 82.15  E-value: 7.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALdeqfePQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI-----AGGALALRVDVTDEQQVAALFERAVEEF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  83 GRLDILVNNAGVNNE---------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd08944    76 GGLDLLVNNAGAMHLtpaiidtdlAVWDQTMAINLRGTFLCCRHAAPRMIARGGGS---IVNLSSIAG 140
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 6-142 7.84e-20

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: 81.64  E-value: 7.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAAlDEQFEPqktlfIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEA-----VPYDARDPEDARALVDALRDRFGRI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:cd08932    75 DVLVHNAGIGrpttlregSDAELEAHFSINVIAPAELTRALLPALREAGSGR---VVFLNSLSGK 136
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 4-138 8.26e-20

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: 81.94  E-value: 8.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:cd05362     2 AGKVALVTGASRGIGRAIAKRLARDGASVVV---NYASSKAAAEEVVAEIEAAggKAIAVQADVSDPSQVARLFDAAEKA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  82 FGRLDILVNNAGV--------NNEKNWEKTLQINlvsvISGTYLGLDYMSKqNGGEGGIIINMSS 138
Cdd:cd05362    79 FGGVDILVNNAGVmlkkpiaeTSEEEFDRMFTVN----TKGAFFVLQEAAK-RLRDGGRIINISS 138
PRK05717 PRK05717
SDR family oxidoreductase;
4-144 9.10e-20

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 81.86  E-value: 9.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK05717    9 NGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGEN-----AWFIAMDVADEAQVAAGVAEVLGQFG 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  84 RLDILVNNAGVNNEKN----------WEKTLQINLvsviSGTYLGLDYMSKQNGGEGGIIINMSSLAGKDS 144
Cdd:PRK05717   84 RLDALVCNAAIADPHNttleslslahWNRVLAVNL----TGPMLLAKHCAPYLRAHNGAIVNLASTRARQS 150
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 8-140 9.60e-20

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: 81.63  E-value: 9.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALvdwNF----EAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVI---NYrkskDAAAEVAAEIEEL--GGKAVVVRADVSQPQDVEEMFAAVKERFG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLA 140
Cdd:cd05359    76 RLDVLVSNAAAGafrplselTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGR---IVAISSLG 137
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-141 1.14e-19

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 81.87  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVkcKAALDEQFEP-QKTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLN-QDGA--NAVADEINKAgGKAIGVAMDVTNEDAVNAGIDKVAER 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  82 FGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggEGGIIINMSSLAG 141
Cdd:PRK13394   82 FGSVDILVSNAGIQivnpienySFADWKKMQAIHVDGAFLTTKAALKHMYKDD--RGGVVIYMGSVHS 147
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 6-144 1.44e-19

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: 81.17  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKF-PVKVLPLQLDVSDRESIEAALENLPEEFRDI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  86 DILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGKDS 144
Cdd:cd05346    80 DILVNNAGLalgldpaqeADLEDWETMIDTNVKGLLNVTRLILPIMIARN---QGHIINLGSIAGRYP 144
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-141 1.58e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 81.53  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALdeQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK08213   12 GKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHL--EALGIDALWIAADVADEADIERLAEETLERFGH 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  85 LDILVNNAGVN---------NEKnWEKTLQINlvsvISGTYL-----GLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK08213   90 VDILVNNAGATwgapaedhpVEA-WDKVMNLN----VRGLFLlsqavAKRSMIPRGYGR---IINVASVAG 152
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 5-141 2.04e-19

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: 80.76  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAAL--DEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIeaEANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVNNEKNWE--------KTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:cd08939    81 GPPDLVVNCAGISIPGLFEdltaeefeRGMDVNYFGSLNVAHAVLPLMKEQ---RPGHIVFVSSQAA 144
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-141 2.39e-19

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: 80.59  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvkcKAALDEQFEPQKTlfIQCDVADQAQLRDTFRKvvdhFGR 84
Cdd:cd05368     2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEE-----KLKELERGPGITT--RVLDVTDKEQVAALAKE----EGR 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd05368    71 IDVLFNCAGFvhhgsildCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS---IINMSSVAS 132
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-141 2.89e-19

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: 79.97  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGA-KVALVDWNFEAGVKCKAALDEQFepQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEG--LSVRFHQLDVTDDASIEAAADFVEEKYGG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd05324    79 LDILVNNAGIafkgfddstPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGR---IVNVSSGLG 141
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-141 3.13e-19

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: 80.31  E-value: 3.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALdeQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRLD 86
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAI--QQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGIT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  87 ILVNNAG---------VNNEKNWEKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAG 141
Cdd:cd05365    79 ILVNNAGgggpkpfdmPMTEEDFEWAFKLNLFSAFRLSQLCAPHM-QKAG--GGAILNISSMSS 139
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-116 3.70e-19

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 80.39  E-value: 3.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKckAALDE-QFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK12745    3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELA--ATQQElRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1191833562  85 LDILVNNAGVN----------NEKNWEKTLQINLvsviSGTY 116
Cdd:PRK12745   81 IDCLVNNAGVGvkvrgdlldlTPESFDRVLAINL----RGPF 118
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-139 4.16e-19

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 80.16  E-value: 4.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVdwNFEAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK06935   14 DGKVAIVTGGNTGLGQGYAVALAKAGADIIIT--THGTNWDETRRLIEK-EGRKVTFVQVDLTKPESAEKVVKEALEEFG 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSL 139
Cdd:PRK06935   91 KIDILVNNAGTirraplleYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGK---IINIASM 151
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-139 4.19e-19

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 80.26  E-value: 4.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVAlvdwNFEAGVKCKAALDeqfepqktlFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06398    6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVI----NFDIKEPSYNDVD---------YFKVDVSNKEQVIKGIDYVISKYGR 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSL 139
Cdd:PRK06398   73 IDILVNNAGIEsygaihavEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD---KGVIINIASV 132
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-141 4.62e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 82.20  E-value: 4.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfepqKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06484  269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGD-----EHLSVQADITDEAAVESAFAQIQARWGR 343

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVNNE---------KNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAG 141
Cdd:PRK06484  344 LDVLVNNAGIAEVfkpsleqsaEDFTRVYDVNLSGAFACARAAARLMSQ-----GGVIVNLGSIAS 404
PLN02253 PLN02253
xanthoxin dehydrogenase
 5-141 5.11e-19

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 80.64  E-value: 5.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfepQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PLN02253   18 GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGE---PNVCFFHCDVTVEDDVSRAVDFTVDKFGT 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  85 LDILVNNAGVNNEK----------NWEKTLQINLVsvisGTYLGLDY----MSKQNGGEggiIINMSSLAG 141
Cdd:PLN02253   95 LDIMVNNAGLTGPPcpdirnvelsEFEKVFDVNVK----GVFLGMKHaariMIPLKKGS---IVSLCSVAS 158
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 3-141 5.52e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 81.12  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVkckAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK07109    6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARG-EEGL---EALAAEIRAAggEALAVVADVADAEAVQAAADRAEE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:PRK07109   82 ELGPIDTWVNNAMVTvfgpfedvTPEEFRRVTEVTYLGVVHGTLAALRHMRPRD---RGAIIQVGSALA 147
PRK09730 PRK09730
SDR family oxidoreductase;
6-142 6.09e-19

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 79.89  E-value: 6.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAV---NYQQNLHAAQEVVNLITQAggKAFVLQADISDENQVVAMFTAIDQHDE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  84 RLDILVNNAGVNNEKNWEKTL---QIN--LVSVISGTYL----GLDYMSKQNGGEGGIIINMSSLAGK 142
Cdd:PRK09730   79 PLAALVNNAGILFTQCTVENLtaeRINrvLSTNVTGYFLccreAVKRMALKHGGSGGAIVNVSSAASR 146
PRK06194 PRK06194
hypothetical protein; Provisional
 5-141 6.12e-19

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 80.44  E-value: 6.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPqkTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06194    6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAE--VLGVRTDVSDAAQVEALADAALERFGA 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYM---SKQNGGEGGIIINMSSLAG 141
Cdd:PRK06194   84 VHLLFNNAGVgagglvweNSLADWEWVLGVNLWGVIHGVRAFTPLMlaaAEKDPAYEGHIVNTASMAG 151
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-141 7.96e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 81.43  E-value: 7.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFepqktLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06484    5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDH-----HALAMDVSDEAQIREGFEQLHREFGR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  85 LDILVNNAGVNNE----------KNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAG 141
Cdd:PRK06484   80 IDVLVNNAGVTDPtmtatldttlEEFARLQAINLTGAYLVAREALRLMIEQ--GHGAAIVNVASGAG 144
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-94 9.14e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 79.28  E-value: 9.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   2 HVNGKVALVTGAAQGIGRASAEALLLKGAK-VALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK06198    3 RLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEAL--GAKAVFVQADLSDVEDCRRVVAAADE 80

                          90
                  ....*....|....
gi 1191833562  81 HFGRLDILVNNAGV 94
Cdd:PRK06198   81 AFGRLDALVNAAGL 94
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-141 1.12e-18

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: 78.92  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQkTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNR-VIALELDITSKESIKELIESYLEKFG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  84 RLDILVNNAGVNN-----------EKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:cd08930    80 RIDILINNAYPSPkvwgsrfeefpYEQWNEVLNVNLGGAFLCSQAFIKLFKKQG---KGSIINIASIYG 145
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-141 1.28e-18

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 79.07  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDwnfeAGVKCKAALDEQFEP-QKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK08226    6 GKTALITGALQGIGEGIARVFARHGANLILLD----ISPEIEKLADELCGRgHRCTAVVADVRDPASVAAAIKRAKEKEG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK08226   82 RIDILVNNAGVcrlgsfldMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGR---IVMMSSVTG 144
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-138 1.91e-18

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: 78.87  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALV-------------DWNFEAGVKCkaaldeqfepqktLFIQCDVADQAQL 71
Cdd:cd05355    26 GKKALITGGDSGIGRAVAIAFAREGADVAINylpeeeddaeetkKLIEEEGRKC-------------LLIPGDLGDESFC 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  72 RDTFRKVVDHFGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSS 138
Cdd:cd05355    93 RDLVKEVVKEFGKLDILVNNAAYQhpqesiediTTEQLEKTFRTNIFSMFYLTKAALPHLKK-----GSSIINTTS 163
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-141 2.11e-18

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 78.08  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDwnfeagVKCKAALDEQFEpqktlFIQCDVADQAQlrdtfrKVVDHFGR 84
Cdd:PRK06550    5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVD------KQDKPDLSGNFH-----FLQLDLSDDLE------PLFDWVPS 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:PRK06550   68 VDILCNTAGIlddykplldTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER---KSGIIINMCSIAS 130
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-141 2.34e-18

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 78.22  E-value: 2.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVAlvdwnfeagVKCKAALDEQFEPQK--------TLFIQCDVADQAQLR 72
Cdd:PRK06077    2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVV---------VNAKKRAEEMNETLKmvkenggeGIGVLADVSTREGCE 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  73 DTFRKVVDHFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLAG 141
Cdd:PRK06077   73 TLAKATIDRYGVADILVNNAGLGlfspflnvDDKLIDKHISTDFKSVIYCSQELAKEMR-----EGGAIVNIASVAG 144
PRK06124 PRK06124
SDR family oxidoreductase;
5-141 3.17e-18

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 77.83  E-value: 3.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWN---FEAGVKCKAALDEQFEPqktlfIQCDVADQAQLRDTFRKVVDH 81
Cdd:PRK06124   11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNaatLEAAVAALRAAGGAAEA-----LAFDIADEEAVAAAFARIDAE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  82 FGRLDILVNNAGVNNEKNWEKT--------LQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK06124   86 HGRLDILVNNVGARDRRPLAELddaairalLETDLVAPILLSRLAAQRMKRQGYGR---IIAITSIAG 150
PRK05650 PRK05650
SDR family oxidoreductase;
9-141 3.79e-18

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 77.77  E-value: 3.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFGRLDIL 88
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREA--GGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  89 VNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK05650   82 VNNAGVASGgffeelslEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGR---IVNIASMAG 139
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-138 4.73e-18

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 77.47  E-value: 4.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKV 78
Cdd:PRK12937    1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAV---NYAGSAAAADELVAEIEAAggRAIAVQADVADAAAVTRLFDAA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  79 VDHFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMskqngGEGGIIINMSS 138
Cdd:PRK12937   78 ETAFGRIDVLVNNAGVmplgtiadFDLEDFDRTIATNLRGAFVVLREAARHL-----GQGGRIINLST 140
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 4-141 5.97e-18

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: 77.50  E-value: 5.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd08935     4 KNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITAL--GGRAIALAADVLDRASLERAREEIVAQFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  84 RLDILVNNAGVNN----------------------EKNWEKTLQINLVsvisGTYLGLDYMSKQ-NGGEGGIIINMSSLA 140
Cdd:cd08935    82 TVDILINGAGGNHpdattdpehyepeteqnffdldEEGWEFVFDLNLN----GSFLPSQVFGKDmLEQKGGSIINISSMN 157


                  .
gi 1191833562 141 G 141
Cdd:cd08935   158 A 158
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-141 6.57e-18

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: 77.10  E-value: 6.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHF-G 83
Cdd:cd05329     6 GKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREK--GFKVEGSVCDVSSRSERQELMDTVASHFgG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAG 141
Cdd:cd05329    84 KLNILVNNAGTNirkeakdyTEEDYSLIMSTNFEAAYHLSRLAHPLL-KASG--NGNIVFISSVAG 146
PRK08628 PRK08628
SDR family oxidoreductase;
1-138 1.20e-17

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 76.54  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDwNFEAGVKCKAALdEQFEPQkTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK08628    3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFG-RSAPDDEFAEEL-RALQPR-AEFVQVDLTDDAQCRDAVEQTVA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  81 HFGRLDILVNNAGVNNEKNWE-------KTLQINLVSVISGTYLGLDYMSKQNGGeggiIINMSS 138
Cdd:PRK08628   80 KFGRIDGLVNNAGVNDGVGLEagreafvASLERNLIHYYVMAHYCLPHLKASRGA----IVNISS 140
PRK08589 PRK08589
SDR family oxidoreductase;
3-142 1.29e-17

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 76.74  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKtlfIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK08589    4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIKSNGGKAKA---YHVDISDEQQVKDFASEIKEQF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  83 GRLDILVNNAGVNNEKN---------WEKTLQINLvsviSGTYLGLDYMSKQNGGEGGIIINMSSLAGK 142
Cdd:PRK08589   81 GRVDVLFNNAGVDNAAGriheypvdvFDKIMAVDM----RGTFLMTKMLLPLMMEQGGSIINTSSFSGQ 145
PRK08267 PRK08267
SDR family oxidoreductase;
9-141 1.37e-17

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 76.13  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVkckAALDEQFEPQKTLFIQCDVADqaqlRDTFRKVVDHF-----G 83
Cdd:PRK08267    5 FITGAASGIGRATALLFAAEGWRVGAYDIN-EAGL---AALAAELGAGNAWTGALDVTD----RAAWDAALADFaaatgG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:PRK08267   77 RLDVLFNNAGIlrggpfedIPLEAHDRVIDINVKGVLNGAHAALPYLKATP---GARVINTSSASA 139
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 5-140 2.54e-17

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 75.37  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWN---FEAGVKCKAALDEqfepqkTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:PRK12823    8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelvHEVAAELRAAGGE------ALALTADLETYAGAQAAMAAAVEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  82 FGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLA 140
Cdd:PRK12823   82 FGRIDVLINNVGGTiwakpfeeyEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQG---GGAIVNVSSIA 146
PRK06139 PRK06139
SDR family oxidoreductase;
1-141 7.26e-17

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 75.14  E-value: 7.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEA----GVKCKAALDEqfepqkTLFIQCDVADQAQLRDTFR 76
Cdd:PRK06139    3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEAlqavAEECRALGAE------VLVVPTDVTDADQVKALAT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  77 KVVDHFGRLDILVNNAGVNNEKNWEKT--------LQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAG 141
Cdd:PRK06139   77 QAASFGGRIDVWVNNVGVGAVGRFEETpieaheqvIQTNLIGYMRDAHAALPIFKKQG---HGIFINMISLGG 146
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-139 7.78e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 74.33  E-value: 7.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK07097   10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRE--LGIEAHGYVCDVTDEDGVQAMVSQIEKEVGV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  85 LDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSL 139
Cdd:PRK07097   88 IDILVNNAGIIKRipmlemsaEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGK---IINICSM 147
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 8-141 9.17e-17

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: 73.90  E-value: 9.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfEPQKTLFIqCDVADQAQLRDTFRKVVDHFGRLDI 87
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNP-NPSVEVEI-LDVTDEERNQLVIAELEAELGGLDL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  88 LVNNAGVNNEKNWE--------KTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd05350    79 VIINAGVGKGTSLGdlsfkafrETIDTNLLGAAAILEAALPQFRAKGRGH---LVLISSVAA 137
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 6-141 1.17e-16

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: 73.25  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVKckaALDEQFEPQKTLFIQCDVADqaqlRDTFRKVVDHF--- 82
Cdd:cd08931     1 KAIFITGAASGIGRETALLFARNGWFVGLYDID-EDGLA---ALAAELGAENVVAGALDVTD----RAAWAAALADFaaa 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  83 --GRLDILVNNAGVNNEKNWEK--------TLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:cd08931    73 tgGRLDALFNNAGVGRGGPFEDvplaahdrMVDINVKGVLNGAYAALPYLKAT---PGARVINTASSSA 138
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-141 1.21e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 73.60  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfeagvkcKAALDEQFEPQKTLFIQCDVADQAQLRDTFrkvvD 80
Cdd:PRK07060    5 FDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARN-------AAALDRLAGETGCEPLRLDVGDDAAIRAAL----A 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLGLDYMSKQ--NGGEGGIIINMSSLAG 141
Cdd:PRK07060   74 AAGAFDGLVNCAGIAslesaldmTAEGFDRVMAVNA----RGAALVARHVARAmiAAGRGGSIVNVSSQAA 140
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-141 1.35e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 73.43  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwnfeaGVKCKAALD---EQFEPQ--KTLFIQCDVADQAQLRDTF 75
Cdd:PRK07478    2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVV-------GARRQAELDqlvAEIRAEggEAVALAGDVRDEAYAKALV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  76 RKVVDHFGRLDILVNNAGVNNE---------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK07478   75 ALAVERFGGLDIAFNNAGTLGEmgpvaemslEGWRETLATNLTSAFLGAKHQIPAMLARGGGS---LIFTSTFVG 146
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-141 1.43e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 73.29  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALdeqfePQKTLFI-QCDVADQAQLRDTFRKVV 79
Cdd:PRK12828    3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGV-----PADALRIgGIDLVDPQAARRAVDEVN 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  80 DHFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK12828   78 RQFGRLDALVNIAGAfvwgtiadGDADTWDRMYGVNVKTTLNASKAALPALTASGGGR---IVNIGAGAA 144
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-138 1.94e-16

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: 72.72  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwnfeAGvKCKAALDEQfepQKTLF----IQCDVADQAQLRDTFR 76
Cdd:cd05370     1 MKLTGNTVLITGGTSGIGLALARKFLEAGNTVII------TG-RREERLAEA---KKELPnihtIVLDVGDAESVEALAE 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  77 KVVDHFGRLDILVNNAGVNNEKNWEK----------TLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSS 138
Cdd:cd05370    71 ALLSEYPNLDILINNAGIQRPIDLRDpasdldkadtEIDTNLIGPIRLIKAFLPHLKKQP---EATIVNVSS 139
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-141 2.47e-16

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: 72.66  E-value: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVKCKAALDEQFEPQKTLFIqCDVADQAQLRDTFRKVVDHFGRLD 86
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDIN-EKGAEETANNVRKAGGKVHYYK-CDVSKREEVYEAAKKIKKEVGDVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  87 ILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd05339    79 ILINNAGVvsgkklleLPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGH---IVTIASVAG 138
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-141 2.72e-16

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: 72.64  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVDHfgr 84
Cdd:cd05356     1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKY-GVETKTIAADFSAGDDIYERIEKELEG--- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  85 LDI--LVNNAGVN----------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:cd05356    77 LDIgiLVNNVGIShsipeyfletPEDELQDIINVNVMATLKMTRLILPGMVKR---KKGAIVNISSFAG 142
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 4-141 5.23e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 72.26  E-value: 5.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkcKAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK06180    3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAA----RADFEALH-PDRALARLLDVTDFDAIDAVVADAEATFG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGVNNEKNWEKT--------LQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK06180   78 PIDVLVNNAGYGHEGAIEESplaemrrqFEVNVFGAVAMTKAVLPGMRARRRGH---IVNITSMGG 140
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-141 6.19e-16

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 71.94  E-value: 6.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK09186    3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLVELDITDQESLEEFLSKSAEKYG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  84 RLDILVNNAGVNNeKNWEKT------------LQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:PRK09186   83 KIDGAVNCAYPRN-KDYGKKffdvslddfnenLSLHLGSSFLFSQQFAKYFKKQ---GGGNLVNISSIYG 148
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-141 8.21e-16

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: 71.36  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd08942     4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEA---CADAAEELSAYGECIAIPADLSSEEGIEALVARVAERS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSK-QNGGEGGIIINMSSLAG 141
Cdd:cd08942    81 DRLDVLVNNAGATwgapleafPESGWDKVMDINVKSVFFLTQALLPLLRAaATAENPARVINIGSIAG 148
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-141 8.53e-16

(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: 71.20  E-value: 8.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDW--NFEAGVKCKAALDEQFEPQKTLFIQC-----DVADQAQLRDTf 75
Cdd:cd05353     3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggDRKGSGKSSSAADKVVDEIKAAGGKAvanydSVEDGEKIVKT- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  76 rkVVDHFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:cd05353    82 --AIDAFGRVDILVNNAGIlrdrsfakMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGR---IINTSSAAG 150
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-140 1.34e-15

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: 70.95  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpQKTLFIQCDVADQAQLRDTFRKVVDHFGRLD 86
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAG-RRAIYFQADIGELSDHEALLDQAWEDFGRLD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  87 ILVNNAGVN----------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGI---IINMSSLA 140
Cdd:cd05337    82 CLVNNAGIAvrprgdlldlTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFDGPhrsIIFVTSIN 148
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-141 1.62e-15

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 71.79  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGvkckAALDEQFEPQKTLFIQCDV-ADQAQLRDTfRKVVDHFG 83
Cdd:PRK08261  210 GKVALVTGAARGIGAAIAEVLARDGAHVVCLDVP-AAG----EALAAVANRVGGTALALDItAPDAPARIA-EHLAERHG 283

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  84 RLDILVNNAGVN--------NEKNWEKTLQINLVS--VISGTYLGLDYMskqngGEGGIIINMSSLAG 141
Cdd:PRK08261  284 GLDIVVHNAGITrdktlanmDEARWDSVLAVNLLAplRITEALLAAGAL-----GDGGRIVGVSSISG 346
PRK12743 PRK12743
SDR family oxidoreductase;
6-138 2.62e-15

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 70.06  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRS-HGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  86 DILVNNAGVNNEK--------NWEKTLQINLvsviSGTYLGLDYMSKQ--NGGEGGIIINMSS 138
Cdd:PRK12743   82 DVLVNNAGAMTKApfldmdfdEWRKIFTVDV----DGAFLCSQIAARHmvKQGQGGRIINITS 140
PRK06123 PRK06123
SDR family oxidoreductase;
6-142 2.96e-15

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 69.81  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK06123    3 KVMIITGASRGIGAATALLAAERGYAVCL---NYLRNRDAAEAVVQAIRRQggEALAVAADVADEADVLRLFEAVDRELG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  84 RLDILVNNAGVNNEK---------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGK 142
Cdd:PRK06123   80 RLDALVNNAGILEAQmrleqmdaaRLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSMAAR 147
PRK06500 PRK06500
SDR family oxidoreductase;
5-108 3.03e-15

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 69.98  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfepqKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06500    6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGE-----SALVIRADAGDVAAQKALAQALAEAFGR 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINL 108
Cdd:PRK06500   81 LDAVFINAGVAkfapledwDEAMFDRSFNTNV 112
PRK06947 PRK06947
SDR family oxidoreductase;
6-142 3.50e-15

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 69.83  E-value: 3.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRA-AGGRACVVAGDVANEADVIAMFDAVQSAFGRL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  86 DILVNNAGVNNEK------NWEKTLQINLVSVIsGTYL----GLDYMSKQNGGEGGIIINMSSLAGK 142
Cdd:PRK06947   82 DALVNNAGIVAPSmpladmDAARLRRMFDTNVL-GAYLcareAARRLSTDRGGRGGAIVNVSSIASR 147
PRK07832 PRK07832
SDR family oxidoreductase;
6-141 3.93e-15

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 69.69  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWN---FEAGVKCKAALDEQFEPQKTLfiqcDVADQAQLRDTFRKVVDHF 82
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDadgLAQTVADARALGGTVPEHRAL----DISDYDAVAAFAADIHAAH 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKqnGGEGGIIINMSSLAG 141
Cdd:PRK07832   77 GSMDVVMNIAGISawgtvdrlTHEQWRRMVDVNLMGPIHVIETFVPPMVA--AGRGGHLVNVSSAAG 141
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-94 4.25e-15

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 69.60  E-value: 4.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCkAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK06200    2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAE---KL-ASLRQRF-GDHVLVVEGDVTSYADNQRAVDQTVD 76

                          90
                  ....*....|....
gi 1191833562  81 HFGRLDILVNNAGV 94
Cdd:PRK06200   77 AFGKLDCFVGNAGI 90
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-140 4.92e-15

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: 69.04  E-value: 4.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfepqktlfIQCDVADQAQLRDTFRKVVDHFGRLDI 87
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRL---------TPLDVADAAAVREVCSRLLAEHGPIDA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  88 LVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLA 140
Cdd:cd05331    72 LVNCAGVlrpgatdpLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGA---IVTVASNA 129
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 7-142 9.88e-15

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: 68.47  E-value: 9.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKG--AKVALVDWNFEAGVKCKAALdeqFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEEL---RPGLRVTTVKADLSDAAGVEQLLEAIRKLDGE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  85 LDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDymSKQNGGEGGIIINMSSLAGK 142
Cdd:cd05367    78 RDLLINNAGSlgpvskiefIDLDELQKYFDLNLTSPVCLTSTLLR--AFKKRGLKKTVVNVSSGAAV 142
PRK09135 PRK09135
pteridine reductase; Provisional
 1-108 1.21e-14

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 68.03  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK09135    2 MTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAELNALRPGSAAALQADLLDPDALPELVAACVA 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1191833562  81 HFGRLDILVNNA--------GVNNEKNWEKTLQINL 108
Cdd:PRK09135   82 AFGRLDALVNNAssfyptplGSITEAQWDDLFASNL 117
PRK07074 PRK07074
SDR family oxidoreductase;
6-141 2.08e-14

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 67.87  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAAL-DEQFEPqktlfIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK07074    3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALgDARFVP-----VACDLTDAASLAAALANAAAERGP 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  85 LDILVNNAGV--------NNEKNWEKTLQINLvsviSGTYLG----LDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK07074   78 VDVLVANAGAaraaslhdTTPASWRADNALNL----EAAYLCveavLEGMLKRSRGA---VVNIGSVNG 139
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 5-142 2.50e-14

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 68.79  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:COG3347   425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAFGFAGLDIGG 504

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  85 LDILVNNAG-VNNEKNWEKT--LQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGK 142
Cdd:COG3347   505 SDIGVANAGiASSSPEEETRlsFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSK 565
PRK06182 PRK06182
short chain dehydrogenase; Validated
 6-142 3.19e-14

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 67.29  E-value: 3.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKValvdwnFEAgvkckAALDEQFEPQKTLFIQC---DVADQAQLRDTFRKVVDHF 82
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTV------YGA-----ARRVDKMEDLASLGVHPlslDVTDEASIKAAVDTIIAEE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  83 GRLDILVNNAGVNNEKNWE--------KTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK06182   73 GRIDVLVNNAGYGSYGAIEdvpidearRQFEVNLFGAARLTQLVLPHMRAQRSGR---IINISSMGGK 137
PRK07814 PRK07814
SDR family oxidoreductase;
3-142 4.72e-14

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 66.73  E-value: 4.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwnfeaGVKCKAALDEQFEP-----QKTLFIQCDVADQAQLRDTFRK 77
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLI-------AARTESQLDEVAEQiraagRRAHVVAADLAHPEATAGLAGQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  78 VVDHFGRLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAGK 142
Cdd:PRK07814   81 AVEAFGRLDIVVNNVGgtmpnpllSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSG--GGSVINISSTMGR 151
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 5-138 7.44e-14

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: 66.33  E-value: 7.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05322     2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYG-EKAYGFGADATNEQSVIALSKGVDEIFKR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVNNE--------KNWEKTLQINLVsvisGTYLGLDYMSK---QNGGEGGII-INMSS 138
Cdd:cd05322    81 VDLLVYSAGIAKSakitdfelGDFDRSLQVNLV----GYFLCAREFSKlmiRDGIQGRIIqINSKS 142
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-141 8.40e-14

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 66.73  E-value: 8.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDwnFEAGVKCKAALDE-QFEPQKTLFIQCDVADQAQLRDTFRKVVDh 81
Cdd:PRK07792   10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVND--VASALDASDVLDEiRAAGAKAVAVAGDISQRATADELVATAVG- 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  82 FGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDY---MSKQNGGE-GGIIINMSSLAG 141
Cdd:PRK07792   87 LGGLDIVVNNAGITrdrmlfnmSDEEWDAVIAVHLRGHFLLTRNAAAYwraKAKAAGGPvYGRIVNTSSEAG 158
PRK08264 PRK08264
SDR family oxidoreductase;
1-141 1.13e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 65.30  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGA-KVAlvdwnfeAGVKCKAALDEQFEpqKTLFIQCDVADQAQLRDtfrkVV 79
Cdd:PRK08264    2 MDIKGKVVLVTGANRGIGRAFVEQLLARGAaKVY-------AAARDPESVTDLGP--RVVPLQLDVTDPASVAA----AA 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  80 DHFGRLDILVNNAGVN---------NEKNWEKTLQINlvsvisgtYLGLDYMS-------KQNGgeGGIIINMSSLAG 141
Cdd:PRK08264   69 EAASDVTILVNNAGIFrtgslllegDEDALRAEMETN--------YFGPLAMArafapvlAANG--GGAIVNVLSVLS 136
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 6-92 1.17e-13

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: 65.56  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfepQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAG----ERAIAIQADVRDRDQVQAMIEEAKNHFGPV 76


                  ....*..
gi 1191833562  86 DILVNNA 92
Cdd:cd05349    77 DTIVNNA 83
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 6-137 1.70e-13

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: 64.99  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNA-LRNSAVLVQADLSDFAACADLVAAAFRAFGRC 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  86 DILVNNAGV--------NNEKNWEKTLQINLvsvISGTYLGLDYMSKQNGGEGGIIINMS 137
Cdd:cd05357    80 DVLVNNASAfyptplgqGSEDAWAELFGINL---KAPYLLIQAFARRLAGSRNGSIINII 136
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 5-141 1.76e-13

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 65.04  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAA--QGIGRASAEALLLKGAKVALVDWNfEAGVKCKAALDEQFEPqkTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:COG0623     5 GKRGLITGVAndRSIAWGIAKALHEEGAELAFTYQG-EALKKRVEPLAEELGS--ALVLPCDVTDDEQIDALFDEIKEKW 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  83 GRLDILV-------NNAGVN-----NEKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLAG 141
Cdd:COG0623    82 GKLDFLVhsiafapKEELGGrfldtSREGFLLAMDISAYSLVALAKAAEPLMN-----EGGSIVTLTYLGA 147
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 6-142 1.82e-13

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: 65.25  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE-QFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd08945     4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEE---GLATTVKElREAGVEADGRTCDVRSVPEIEALVAAAVARYGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLdymskQNGGEG----GIIINMSSLAGK 142
Cdd:cd08945    81 IDVLVNNAGRSgggataelADELWLDVVETNLTGVFRVTKEVL-----KAGGMLergtGRIINIASTGGK 145
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 5-140 2.08e-13

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: 64.86  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWN---FEAGVKCKAALDEqfepqkTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:cd08937     4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSelvHEVLAEILAAGDA------AHVHTADLETYAGAQGVVRAAVER 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  82 FGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLA 140
Cdd:cd08937    78 FGRVDVLINNVGGTiwakpyehyEEEQIEAEIRRSLFPTLWCCRAVLPHMLER---QQGVIVNVSSIA 142
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-111 3.05e-13

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 64.65  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDW-NFEAGVKCKAALDEQFE------PQKTLFIQCDVADQAQLRDTFRK 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLcADDPAVGYPLATRAELDavaaacPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1191833562  78 VVDHFGRLDILVNNAGV---------NNEKNWEKTLQINLVSV 111
Cdd:TIGR04504  81 AVERWGRLDAAVAAAGViaggrplweTTDAELDLLLDVNLRGV 123
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-94 3.56e-13

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: 64.30  E-value: 3.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVkckAALDEQFEpQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:cd05348     3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRS-AEKV---AELRADFG-DAVVGVEGDVRSLADNERAVARCVERFG 77

                          90
                  ....*....|.
gi 1191833562  84 RLDILVNNAGV 94
Cdd:cd05348    78 KLDCFIGNAGI 88
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-94 3.98e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 64.66  E-value: 3.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLR---DTFRKvvdH 81
Cdd:PRK06197   16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRaaaDALRA---A 92

                          90
                  ....*....|...
gi 1191833562  82 FGRLDILVNNAGV 94
Cdd:PRK06197   93 YPRIDLLINNAGV 105
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 4-142 4.89e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 64.15  E-value: 4.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVAlvdwnfeagVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK06523    8 AGKRALVTGGTKGIGAATVARLLEAGARVV---------TTARSRPDDL--PEGVEFVAADLTTAEGCAAVARAVLERLG 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  84 RLDILVNNAG----------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGK 142
Cdd:PRK06523   77 GVDILVHVLGgssapaggfaALTDEEWQDELNLNLLAAVRLDRALLPGMIARG---SGVIIHVTSIQRR 142
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 5-140 5.80e-13

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: 63.64  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfEAGVKCKAALDEQFEPqktlfIQCDVADQaqlrDTFRKVVDHFGR 84
Cdd:cd05351     7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRT-QADLDSLVRECPGIEP-----VCVDLSDW----DATEEALGSVGP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLA 140
Cdd:cd05351    77 VDLLVNNAAVAilqpflevTKEAFDRSFDVNVRAVIHVSQIVARGMIAR--GVPGSIVNVSSQA 138
PRK08278 PRK08278
SDR family oxidoreductase;
1-117 7.87e-13

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 63.38  E-value: 7.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCK-----AAldEQFEPQ--KTLFIQCDVADQAQLRD 73
Cdd:PRK08278    2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKLPgtihtAA--EEIEAAggQALPLVGDVRDEDQVAA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  74 TFRKVVDHFGRLDILVNNAGVNNEKNWEKT--------LQINlvsvISGTYL 117
Cdd:PRK08278   80 AVAKAVERFGGIDICVNNASAINLTGTEDTpmkrfdlmQQIN----VRGTFL 127
PRK05867 PRK05867
SDR family oxidoreductase;
3-141 8.49e-13

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 63.52  E-value: 8.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkCKAALDE-QFEPQKTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDA---LEKLADEiGTSGGKVVPVCCDVSQHQQVTSMLDQVTAE 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562  82 FGRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAG 141
Cdd:PRK05867   84 LGGIDIAVCNAGIITvtpmldmpLEEFQRLQNTNVTGVFLTAQAAAKAMVKQ--GQGGVIINTASMSG 149
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-139 8.85e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 63.25  E-value: 8.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIqcDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK07523   10 GRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAF--DVTDHDAVRAAIDAFEAEIGP 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  85 LDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSL 139
Cdd:PRK07523   88 IDILVNNAGMQFrtpledfpADAFERLLRTNISSVFYVGQAVARHMIARGAGK---IINIASV 147
PRK06482 PRK06482
SDR family oxidoreductase;
4-142 8.86e-13

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 63.60  E-value: 8.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVAlvdwnfeAGVKCKAALDEQFE--PQKTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:PRK06482    1 MSKTWFITGASSGFGRGMTERLLARGDRVA-------ATVRRPDALDDLKAryGDRLWVLQLDVTDSAAVRAVVDRAFAA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  82 FGRLDILVNNAG---------VNNEKnWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK06482   74 LGRIDVVVSNAGyglfgaaeeLSDAQ-IRRQIDTNLIGSIQVIRAALPHLRRQGGGR---IVQVSSEGGQ 139
PRK09072 PRK09072
SDR family oxidoreductase;
1-141 1.23e-12

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 63.04  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDEQFEPQKTLFIQCDVADqAQLRDTFRKVVD 80
Cdd:PRK09072    1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAE---KLEALAARLPYPGRHRWVVADLTS-EAGREAVLARAR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAG 141
Cdd:PRK09072   77 EMGGINVLINNAGVNhfalledqDPEAIERLLALNLTAPMQLTRALLPLLRAQ---PSAMVVNVGSTFG 142
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 5-144 1.59e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 62.46  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAAL-DEQFEPQKTLFiqcDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK08085    9 GKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLrQEGIKAHAAPF---NVTHKQEVEAAIEHIEKDIG 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562  84 RLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIIN---MSSLAGKDS 144
Cdd:PRK08085   86 PIDVLINNAGIQRrhpftefpEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGK---IINicsMQSELGRDT 154
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-95 2.00e-12

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 62.41  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK08642    1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVV---NYHQSEDAAEALADEL-GDRAIALQADVTDREQVQAMFATATE 76

                          90
                  ....*....|....*.
gi 1191833562  81 HFGR-LDILVNNAGVN 95
Cdd:PRK08642   77 HFGKpITTVVNNALAD 92
PRK06196 PRK06196
oxidoreductase; Provisional
 5-94 3.41e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 62.01  E-value: 3.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfepqkTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06196   26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDG------VEVVMLDLADLESVRAFAERFLDSGRR 99

                          90
                  ....*....|
gi 1191833562  85 LDILVNNAGV 94
Cdd:PRK06196  100 IDILINNAGV 109
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 4-137 4.81e-12

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 60.92  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCK-----AALDEQFEPQKTLFIQCDVADQAQLRDTFRKV 78
Cdd:cd09762     2 AGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPgtiytAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  79 VDHFGRLDILVNNAGVNNEKNWEKT--------LQINLvsviSGTYLG----LDYMSKqngGEGGIIINMS 137
Cdd:cd09762    82 VEKFGGIDILVNNASAISLTGTLDTpmkrydlmMGVNT----RGTYLCskacLPYLKK---SKNPHILNLS 145
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 5-142 9.80e-12

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: 60.56  E-value: 9.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  85 LDILVNNAGV------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGK 142
Cdd:cd09807    81 LDVLINNAGVmrcpysKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKS---APSRIVNVSSLAHK 141
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 4-106 1.06e-11

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: 60.54  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAaldEQFEPQ--KTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:cd09763     2 SGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTA---EEIEARggKCIPVRCDHSDDDEVEALFERVARE 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1191833562  82 F-GRLDILVNNA--------GVNNEKNWEKTLQI 106
Cdd:cd09763    79 QqGRLDILVNNAyaavqlilVGVAKPFWEEPPTI 112
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-139 1.60e-11

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 59.92  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVdwnfeaGVKCKAALDEQFEP--QKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK12481    6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGV------GVAEAPETQAQVEAlgRKFHFITADLIQQKDIDSIVSQAVE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  81 HFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSL 139
Cdd:PRK12481   80 VMGHIDILINNAGIirrqdlleFGNKDWDDVININQKTVFFLSQAVAKQFVKQ--GNGGKIINIASM 144
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-141 1.74e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 59.67  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQktlfIQCDVADQAQLRDTfRKVVD 80
Cdd:PRK06125    3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVD----VAVHALDLSSPEAR-EQLAA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  81 HFGRLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAG 141
Cdd:PRK06125   78 EAGDIDILVNNAGaipgggldDVDDAAWRAGWELKVFGYIDLTRLAYPRM-KARG--SGVIVNVIGAAG 143
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 5-136 1.98e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 59.69  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALdEQFEPQkTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI-EQFPGQ-VLTVQMDVRNPEDVQKMVEQIDEKFGR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVN--------NEKNWEKTLQInlvsVISGTYlgldYMSKQNG------GEGGIIINM 136
Cdd:PRK07677   79 IDALINNAAGNficpaedlSVNGWNSVIDI----VLNGTF----YCSQAVGkywiekGIKGNIINM 136
PRK06128 PRK06128
SDR family oxidoreductase;
5-93 3.98e-11

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 59.10  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALvdwNF----EAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK06128   55 GRKALITGADSGIGRATAIAFAREGADIAL---NYlpeeEQDAAEVVQLIQA-EGRKAVALPGDLKDEAFCRQLVERAVK 130

                          90
                  ....*....|...
gi 1191833562  81 HFGRLDILVNNAG 93
Cdd:PRK06128  131 ELGGLDILVNIAG 143
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-108 4.46e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 58.92  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKV--------------------ALVDWNFEAGVKCKAALDeqfepqktlfiq 62
Cdd:PRK07791    4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVvvndigvgldgsasggsaaqAVVDEIVAAGGEAVANGD------------ 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  63 cDVADQAQLRDTFRKVVDHFGRLDILVNNAGV--------NNEKNWEKTLQINL 108
Cdd:PRK07791   72 -DIADWDGAANLVDAAVETFGGLDVLVNNAGIlrdrmianMSEEEWDAVIAVHL 124
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-139 4.88e-11

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 58.35  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAeaLLLKGAKVALVDWNFEAGVKCKAALdeQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK08993   10 GKVAVVTGCDTGLGQGMA--LGLAEAGCDIVGINIVEPTETIEQV--TALGRRFLSLTADLRKIDGIPALLERAVAEFGH 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSL 139
Cdd:PRK08993   86 IDILVNNAGLirredaieFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQ--GNGGKIINIASM 146
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 3-108 6.55e-11

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: 57.97  E-value: 6.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFI-QCDVADQAQLRDTFRKVVDH 81
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFIlDLLTCTSENCQQLAQRIAVN 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1191833562  82 FGRLDILVNNAGV---------NNEKNWEKTLQINL 108
Cdd:cd05340    82 YPRLDGVLHNAGLlgdvcplseQNPQVWQDV*QVNV 117
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-138 7.97e-11

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 57.78  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQ--GIGRASAEALLLKGAKVALVDWN-FEAGVKCKAALDEQFEPQKTLF---IQC-----DVADQA 69
Cdd:PRK12748    1 LPLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSpYDKTMPWGMHDKEPVLLKEEIEsygVRCehmeiDLSQPY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  70 QLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINL-----VSVISGTYLGLDYMSKQNGGEGGIIINMSS 138
Cdd:PRK12748   81 APNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLdkhyaVNVRATMLLSSAFAKQYDGKAGGRIINLTS 154
PRK08219 PRK08219
SDR family oxidoreductase;
6-111 8.92e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 57.25  E-value: 8.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALllkgakvaLVDWNFEAGVKCKAALDE---QFEPQKTLfiQCDVADQaqlrDTFRKVVDHF 82
Cdd:PRK08219    4 PTALITGASRGIGAAIAREL--------APTHTLLLGGRPAERLDElaaELPGATPF--PVDLTDP----EAIAAAVEQL 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGV--------NNEKNWEKTLQINLVSV 111
Cdd:PRK08219   70 GRLDVLVHNAGVadlgpvaeSTVDEWRATLEVNVVAP 106
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-141 9.30e-11

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: 57.42  E-value: 9.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKvalvdwNFEAGVKCKAALDEQFE--PQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:cd05354     1 IKDKTVLVTGANRGIGKAFVESLLAHGAK------KVYAAVRDPGSAAHLVAkyGDKVVPLRLDVTDPESIKAAAAQAKD 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  81 hfgrLDILVNNAGVNNEKNW---------EKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAG 141
Cdd:cd05354    75 ----VDVVINNAGVLKPATLleegalealKQEMDVNVFGLLRLAQAFAPVL-KANG--GGAIVNLNSVAS 137
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-141 1.02e-10

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: 57.55  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVaLVDWNFEAGVKcKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd08936    10 NKVALVTASTDGIGLAIARRLAQDGAHV-VVSSRKQQNVD-RAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGG 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  85 LDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIinmSSLAG 141
Cdd:cd08936    88 VDILVSNAAVNpffgnildsTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIV---SSVAA 150
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-141 1.03e-10

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: 57.50  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKValvdwnfeAGVKCKAAldeqfepqktlFIQCDVADQAQLRDTFRKVV-DHFGRLDI 87
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTV--------IGIDLREA-----------DVIADLSTPEGRAAAIADVLaRCSGVLDG 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  88 LVNNAGVNNEKNWEKTLQINlvsvisgtYLGLDYMSKQ-----NGGEGGIIINMSSLAG 141
Cdd:cd05328    64 LVNCAGVGGTTVAGLVLKVN--------YFGLRALMEAllprlRKGHGPAAVVVSSIAG 114
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 5-141 2.10e-10

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 56.82  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAA--QGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpqKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:cd05372     1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGE--SALVLPCDVSNDEEIKELFAEVKKDW 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  83 GRLDILV-------NNAGVN-----NEKNWEKTLQINLVSVISGTYLGLDYMskqngGEGGIIINMSSLAG 141
Cdd:cd05372    79 GKLDGLVhsiafapKVQLKGpfldtSRKGFLKALDISAYSLVSLAKAALPIM-----NPGGSIVTLSYLGS 144
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 6-111 2.50e-10

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 56.61  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVK----CKAALDEQFE--PQKTLFIQCDVADQAQLRDTFRKVV 79
Cdd:NF040491    1 RVALVTGAARGIGAATVRRLAARGYAVVAVDACAGDPAPyplgTEADLDALVAssPGRVETVVADVRDRAALAAAVALAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1191833562  80 DHFGRLDILVNNAGV---------NNEKNWEKTLQINLVSV 111
Cdd:NF040491   81 DRWGRLDAAVAAAAViaggrplweTPPEELDALWDVDVRGV 121
PRK09134 PRK09134
SDR family oxidoreductase;
6-108 2.72e-10

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 56.47  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVAlvdwnfeagVKCKAALDEQFE--------PQKTLFIQCDVADQAQLRDTFRK 77
Cdd:PRK09134   10 RAALVTGAARRIGRAIALDLAAHGFDVA---------VHYNRSRDEAEAlaaeiralGRRAVALQADLADEAEVRALVAR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1191833562  78 VVDHFGRLDILVNNAGVNNEKN--------WEKTLQINL 108
Cdd:PRK09134   81 ASAALGPITLLVNNASLFEYDSaasftrasWDRHMATNL 119
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 3-141 5.26e-10

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 55.69  E-value: 5.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEpqktlFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK12936    4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVK-----IFPANLSDRDEVKALGQKAEADL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK12936   79 EGVDILVNNAGITkdglfvrmSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGR---IINITSVVG 142
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
6-142 8.33e-10

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 55.02  E-value: 8.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVAlvdwnfeAGVKCKAALDEQF-EPQKTL---FI--QCDVADQAQLRDTFRKVV 79
Cdd:PRK12938    4 RIAYVTGGMGGIGTSICQRLHKDGFKVV-------AGCGPNSPRRVKWlEDQKALgfdFIasEGNVGDWDSTKAAFDKVK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  80 DHFGRLDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGK 142
Cdd:PRK12938   77 AEVGEIDVLVNNAGITRDvvfrkmtrEDWTAVIDTNLTSLFNVTKQVIDGMVERGWGR---IINISSVNGQ 144
PRK07806 PRK07806
SDR family oxidoreductase;
2-92 8.55e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 55.11  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   2 HVNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwNFEAGVKCKAALDEQFEPQ--KTLFIQCDVADQAQLRDTFRKVV 79
Cdd:PRK07806    3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVV---NYRQKAPRANKVVAEIEAAggRASAVGADLTDEESVAALMDTAR 79

                          90
                  ....*....|...
gi 1191833562  80 DHFGRLDILVNNA 92
Cdd:PRK07806   80 EEFGGLDALVLNA 92
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 7-92 1.15e-09

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 54.93  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVD----HF 82
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCQADLSNSATLFSRCEAIIDacfrAF 82

                          90
                  ....*....|
gi 1191833562  83 GRLDILVNNA 92
Cdd:TIGR02685  83 GRCDVLVNNA 92
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-109 1.71e-09

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 54.21  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDwNFEAGVKCKAALDeQFEpqktlFIQCDVADQAQLRDTFRKVvdhfgrlDIL 88
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLD-RSPPGAANLAALP-GVE-----FVRGDLRDPEALAAALAGV-------DAV 68

                          90       100
                  ....*....|....*....|...
gi 1191833562  89 VNNAGV--NNEKNWEKTLQINLV 109
Cdd:COG0451    69 VHLAAPagVGEEDPDETLEVNVE 91
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 5-98 1.75e-09

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: 54.68  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALL-LKGAKVALV---------DWNFEAGVKCKAALDEqfepqkTLFIQCDVADQAQLRDT 74
Cdd:cd08953   205 GGVYLVTGGAGGIGRALARALArRYGARLVLLgrsplppeeEWKAQTLAALEALGAR------VLYISADVTDAAAVRRL 278

                          90       100
                  ....*....|....*....|....
gi 1191833562  75 FRKVVDHFGRLDILVNNAGVNNEK 98
Cdd:cd08953   279 LEKVRERYGAIDGVIHAAGVLRDA 302
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 4-108 2.26e-09

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 53.72  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE--QFEPQKTLFIQCDV--ADQAQLRDTFRKVV 79
Cdd:PRK08945   11 KDRIILVTGAGDGIGREAALTYARHGATVILLGRTEE---KLEAVYDEieAAGGPQPAIIPLDLltATPQNYQQLADTIE 87

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1191833562  80 DHFGRLDILVNNAGV---------NNEKNWEKTLQINL 108
Cdd:PRK08945   88 EQFGRLDGVLHNAGLlgelgpmeqQDPEVWQDVMQVNV 125
PRK05866 PRK05866
SDR family oxidoreductase;
3-93 3.33e-09

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 53.59  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVdwnfeagVKCKAALDEQFEP-----QKTLFIQCDVADQAQLRDTFRK 77
Cdd:PRK05866   38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAV-------ARREDLLDAVADRitragGDAMAVPCDLSDLDAVDALVAD 110

                          90
                  ....*....|....*.
gi 1191833562  78 VVDHFGRLDILVNNAG 93
Cdd:PRK05866  111 VEKRIGGVDILINNAG 126
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 5-117 5.20e-09

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: 52.98  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd09808     1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKK 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1191833562  85 LDILVNNAG--VNNEKNWEKTLQINLVSVISGTYL 117
Cdd:cd09808    81 LHVLINNAGcmVNKRELTEDGLEKNFATNTLGTYI 115
PRK06720 PRK06720
hypothetical protein; Provisional
 1-94 1.39e-08

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 50.74  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGvkcKAALDEQFE-PQKTLFIQCDVADQAQLRDTFRKVV 79
Cdd:PRK06720   12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESG---QATVEEITNlGGEALFVSYDMEKQGDWQRVISITL 88

                          90
                  ....*....|....*
gi 1191833562  80 DHFGRLDILVNNAGV 94
Cdd:PRK06720   89 NAFSRIDMLFQNAGL 103
PRK07577 PRK07577
SDR family oxidoreductase;
6-140 2.12e-08

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 50.88  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKValvdwnfeAGVKCKAALDeqFEPQktlFIQCDVADQAQLRDTFRKVVDHFGrL 85
Cdd:PRK07577    4 RTVLVTGATKGIGLALSLRLANLGHQV--------IGIARSAIDD--FPGE---LFACDLADIEQTAATLAQINEIHP-V 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191833562  86 DILVNNAGVNNEKNWEK--------TLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLA 140
Cdd:PRK07577   70 DAIVNNVGIALPQPLGKidlaalqdVYDLNVRAAVQVTQAFLEGMKLR---EQGRIVNICSRA 129
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 7-141 2.12e-08

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 50.91  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFepqktLFIQCDVADQAQLRDTFRKVVDHFGRLD 86
Cdd:PRK10538    2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNL-----YIAQLDVRNRAAIEEMLASLPAEWRNID 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  87 ILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAG 141
Cdd:PRK10538   77 VLVNNAGLalglepahkASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGH---IINIGSTAG 137
PRK06949 PRK06949
SDR family oxidoreductase;
5-94 2.14e-08

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 51.30  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK06949    9 GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEA--EGGAAHVVSLDVTDYQSIKAAVAHAETEAGT 86

                          90
                  ....*....|
gi 1191833562  85 LDILVNNAGV 94
Cdd:PRK06949   87 IDILVNNSGV 96
PRK05693 PRK05693
SDR family oxidoreductase;
6-93 3.18e-08

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 50.56  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKValvdWnfeAGVKcKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:PRK05693    2 PVVLITGCSSGIGRALADAFKAAGYEV----W---ATAR-KAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGL 73


                  ....*...
gi 1191833562  86 DILVNNAG 93
Cdd:PRK05693   74 DVLINNAG 81
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 8-141 4.88e-08

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: 49.99  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAK--VALVdwNFEAGVKCKAALDEQFEpqKTLFIQCDVADQAQlrDTFRKVVDHFG-- 83
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNtvIATC--RDPSAATELAALGASHS--RLHILELDVTDEIA--ESAEAVAERLGda 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191833562  84 RLDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSLAG 141
Cdd:cd05325    75 GLDVLINNAGIlhsygpaseVDSEDLLEVFQVNVLGPLLLTQAFLPLLLK---GARAKIINISSRVG 138
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 5-95 7.96e-08

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 49.69  E-value: 7.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDEQFEPQKTLFIQcdVADQAQLRDTFRKVvdhfgr 84
Cdd:PRK07424  178 GKTVAVTGASGTLGQALLKELHQQGAKVVALTSNSD---KITLEINGEDLPVKTLHWQ--VGQEAALAELLEKV------ 246

                          90
                  ....*....|.
gi 1191833562  85 lDILVNNAGVN 95
Cdd:PRK07424  247 -DILIINHGIN 256
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
6-142 8.17e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 49.30  E-value: 8.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDwnfEAGVKCKAALDEQFEPQKTlFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVISIS---RTENKELTKLAEQYNSNLT-FHSLDLQDVHELETNFNEILSSIQED 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  86 DI----LVNNAGV----------NNEKnWEKTLQINLVS--VISGTYLgldymsKQNGGEGG--IIINMSSLAGK 142
Cdd:PRK06924   78 NVssihLINNAGMvapikpiekaESEE-LITNVHLNLLApmILTSTFM------KHTKDWKVdkRVINISSGAAK 145
PRK07985 PRK07985
SDR family oxidoreductase;
3-139 8.19e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 49.61  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwNF-----EAGVKCKAALDEQfePQKTLFIQCDVADQAQLRDTFRK 77
Cdd:PRK07985   47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAI---SYlpveeEDAQDVKKIIEEC--GRKAVLLPGDLSDEKFARSLVHE 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  78 VVDHFGRLDILVNNAG----VNNEKN-----WEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSL 139
Cdd:PRK07985  122 AHKALGGLDIMALVAGkqvaIPDIADltseqFQKTFAINVFALFWLTQEAIPLLPK-----GASIITTSSI 187
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 5-140 1.28e-07

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: 48.86  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDwnfeagvkckaaLDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05334     1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASID------------LAENEEADASIIVLDSDSFTEQAKQVVASVARLSGK 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  85 LDILVNNAG---------VNNEKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLA 140
Cdd:cd05334    69 VDALICVAGgwaggsaksKSFVKNWDLMWKQNLWTSFIASHLATKHLL-----SGGLLVLTGAKA 128
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 4-95 1.43e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 48.80  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE-QFEPQKTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK07576    8 AGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQE---KVDAAVAQlQQAGPEGLGVSADVRDYAAVEAAFAQIADEF 84

                          90
                  ....*....|...
gi 1191833562  83 GRLDILVNNAGVN 95
Cdd:PRK07576   85 GPIDVLVSGAAGN 97
PRK08340 PRK08340
SDR family oxidoreductase;
9-93 1.48e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 48.65  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDWNFEAgvkCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRLDIL 88
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKKGARVVISSRNEEN---LEKALKELKEYGEVYAVKADLSDKDDLKNLVKEAWELLGGIDAL 80


                  ....*
gi 1191833562  89 VNNAG 93
Cdd:PRK08340   81 VWNAG 85
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
5-89 1.62e-07

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 48.56  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAA--QGIGRASAEALLLKGAKVALVDWNFEAGvKCKAALDEQFEP-QKTLFIQCDVADQAQLRDTFRKVVDH 81
Cdd:PRK07370    6 GKKALVTGIAnnRSIAWGIAQQLHAAGAELGITYLPDEKG-RFEKKVRELTEPlNPSLFLPCDVQDDAQIEETFETIKQK 84


                  ....*...
gi 1191833562  82 FGRLDILV 89
Cdd:PRK07370   85 WGKLDILV 92
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
5-89 2.62e-07

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 48.01  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAA--QGIGRASAEALLLKGAKVALVDWNfEAGVKCKAALDEQFEPqkTLFIQCDVADQAQLRDTFRKVVDHF 82
Cdd:PRK07533   10 GKRGLVVGIAneQSIAWGCARAFRALGAELAVTYLN-DKARPYVEPLAEELDA--PIFLPLDVREPGQLEAVFARIAEEW 86


                  ....*..
gi 1191833562  83 GRLDILV 89
Cdd:PRK07533   87 GRLDFLL 93
PRK12744 PRK12744
SDR family oxidoreductase;
1-93 2.66e-07

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 48.20  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MH-VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGV----KCKAALDEQfePQKTLFIQCDVADQAQLRDTF 75
Cdd:PRK12744    3 DHsLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKadaeETVAAVKAA--GAKAVAFQADLTTAAAVEKLF 80

                          90
                  ....*....|....*...
gi 1191833562  76 RKVVDHFGRLDILVNNAG 93
Cdd:PRK12744   81 DDAKAAFGRPDIAINTVG 98
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-140 3.06e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 47.64  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALvdwnfeaGVKCKAALDE---QFEP--QKTLFIQCDVADQAQLRDTFRKVV 79
Cdd:PRK07890    5 GKVVVVSGVGPGLGRTLAVRAARAGADVVL-------AARTAERLDEvaaEIDDlgRRALAVPTDITDEDQCANLVALAL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  80 DHFGRLDILVNNA-------GVNNE--KNWEKTLQINLVSVISGTYLGLDYMSKQnggeGGIIINMSSLA 140
Cdd:PRK07890   78 ERFGRVDALVNNAfrvpsmkPLADAdfAHWRAVIELNVLGTLRLTQAFTPALAES----GGSIVMINSMV 143
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-138 4.14e-07

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 47.47  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGA--AQGIGRASAEALLLKGAKVALVDW-NFEAGVKCKAALDEQFEPQKTLF--------IQCDVADQAQLRD 73
Cdd:PRK12859    6 NKVAVVTGVsrLDGIGAAICKELAEAGADIFFTYWtAYDKEMPWGVDQDEQIQLQEELLkngvkvssMELDLTQNDAPKE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  74 TFRKVVDHFGRLDILVNNAGVNNEKNWEkTLQINL------VSVISGTYLGLDYMSKQNGGEGGIIINMSS 138
Cdd:PRK12859   86 LLNKVTEQLGYPHILVNNAAYSTNNDFS-NLTAEEldkhymVNVRATTLLSSQFARGFDKKSGGRIINMTS 155
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 6-94 5.46e-07

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 47.13  E-value: 5.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGA-KVALVDWNFEagvKCKAALDEQ-FEPQKTLFIQCDVADQaqlrDTFRKVVDHF- 82
Cdd:cd09810     2 GTVVITGASSGLGLAAAKALARRGEwHVVMACRDFL---KAEQAAQEVgMPKDSYSVLHCDLASL----DSVRQFVDNFr 74

                          90
                  ....*....|....*
gi 1191833562  83 ---GRLDILVNNAGV 94
Cdd:cd09810    75 rtgRPLDALVCNAAV 89
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 7-95 5.73e-07

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: 46.99  E-value: 5.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDEQFEPQKT--LFIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREA---KLEALLVDIIRDAGGsaKAVPTDARDEDEVIALFDLIEEEIGP 77

                          90
                  ....*....|.
gi 1191833562  85 LDILVNNAGVN 95
Cdd:cd05373    78 LEVLVYNAGAN 88
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 9-140 1.74e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 45.95  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE--QFEPQKTL-FIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:PRK05875   11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPD---KLAAAAEEieALKGAGAVrYEPADVTDEDQVARAVDAATAWHGRL 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  86 DILVNNAGVN---------NEKNWEKTLQINlvsvISGTYLGLDYMSKQ--NGGeGGIIINMSSLA 140
Cdd:PRK05875   88 HGVVHCAGGSetigpitqiDSDAWRRTVDLN----VNGTMYVLKHAARElvRGG-GGSFVGISSIA 148
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
54-141 1.76e-06

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 45.76  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  54 EPQKTL--FIQCDVADQAQLRDTFRKVVdhfGRLDILVNNAGVNNEKNWEKTLQINlvsvisgtYLGLDYMSKQ---NGG 128
Cdd:PRK12428   19 EPGMTLdgFIQADLGDPASIDAAVAALP---GRIDALFNIAGVPGTAPVELVARVN--------FLGLRHLTEAllpRMA 87

                          90
                  ....*....|...
gi 1191833562 129 EGGIIINMSSLAG 141
Cdd:PRK12428   88 PGGAIVNVASLAG 100
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 5-91 1.93e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 45.76  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKValvdwnFEAGVKCKAALDEQFEPQ--------------KTLFIQCDVADQAQ 70
Cdd:PRK08303    8 GKVALVAGATRGAGRGIAVELGAAGATV------YVTGRSTRARRSEYDRPEtieetaelvtaaggRGIAVQVDHLVPEQ 81

                          90       100
                  ....*....|....*....|.
gi 1191833562  71 LRDTFRKVVDHFGRLDILVNN 91
Cdd:PRK08303   82 VRALVERIDREQGRLDILVND 102
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 7-91 3.78e-06

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: 44.87  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvkcKAALDEQFEPQKTLFIQCDVADQAQLRDTfrkVVDHFGRLD 86
Cdd:cd05361     3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFA-----DAAERQAFESENPGTKALSEQKPEELVDA---VLQAGGAID 74


                  ....*
gi 1191833562  87 ILVNN 91
Cdd:cd05361    75 VLVSN 79
PRK12742 PRK12742
SDR family oxidoreductase;
5-94 4.59e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 44.36  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVdwnfEAGVKCKAaldEQFEPQK-TLFIQCDVADqaqlRDTFRKVVDHFG 83
Cdd:PRK12742    6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFT----YAGSKDAA---ERLAQETgATAVQTDSAD----RDAVIDVVRKSG 74

                          90
                  ....*....|.
gi 1191833562  84 RLDILVNNAGV 94
Cdd:PRK12742   75 ALDILVVNAGI 85
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 9-82 5.18e-06

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. 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: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 44.45  E-value: 5.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDwNFEAGvkCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRK----VVDHF 82
Cdd:cd05247     3 LVTGGAGYIGSHTVVELLEAGYDVVVLD-NLSNG--HREALPRI-EKIRIEFYEGDIRDRAALDKVFAEhkidAVIHF 76
PRK05854 PRK05854
SDR family oxidoreductase;
5-94 5.41e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 44.29  E-value: 5.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfeaGVKCKAALDE--QFEPQKTLFIQ----CDVADQAQLRDTFRKV 78
Cdd:PRK05854   14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRN---RAKGEAAVAAirTAVPDAKLSLRaldlSSLASVAALGEQLRAE 90

                          90
                  ....*....|....*..
gi 1191833562  79 vdhfGR-LDILVNNAGV 94
Cdd:PRK05854   91 ----GRpIHLLINNAGV 103
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 5-107 5.49e-06

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: 44.51  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLR---DTFRKVVDH 81
Cdd:cd09809     1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQrfaEAFKAKNSP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1191833562  82 fgrLDILVNNAGV------NNEKNWEKTLQIN 107
Cdd:cd09809    81 ---LHVLVCNAAVfalpwtLTEDGLETTFQVN 109
PRK08251 PRK08251
SDR family oxidoreductase;
6-141 7.02e-06

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 43.77  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:PRK08251    3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELGGL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  86 DILVNNAGVNN---------EKNwEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAG 141
Cdd:PRK08251   83 DRVIVNAGIGKgarlgtgkfWAN-KATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRG 146
PRK12746 PRK12746
SDR family oxidoreductase;
2-105 7.39e-06

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 43.87  E-value: 7.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   2 HVNGKVALVTGAAQGIGRASAEALLLKGAKVALvdwnfEAGvKCKAALDEQFEP-----QKTLFIQCDVADQaqlrDTFR 76
Cdd:PRK12746    3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAI-----HYG-RNKQAADETIREiesngGKAFLIEADLNSI----DGVK 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1191833562  77 KVVDHF----------GRLDILVNNAGVNNEKNWEKTLQ 105
Cdd:PRK12746   73 KLVEQLknelqirvgtSEIDILVNNAGIGTQGTIENTTE 111
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 6-141 1.16e-05

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 43.42  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALLLKGAKV-ALVDWNFEAGVKckaALDEQFEPQKTLfIQCDVADQAQLRDTFRKVVDHFGR 84
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVlAGCLTKNGPGAK---ELRRVCSDRLRT-LQLDVTKPEQIKRAAQWVKEHVGE 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  85 LDI--LVNNAGVN---------NEKNWEKTLQINLVSVISGT--YLGLDYMSKqnggegGIIINMSSLAG 141
Cdd:cd09805    77 KGLwgLVNNAGILgfggdeellPMDDYRKCMEVNLFGTVEVTkaFLPLLRRAK------GRVVNVSSMGG 140
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 8-126 1.28e-05

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: 43.05  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALVDwNFEAGVKCKAALDEQfepqktlFIQCDVADQAQLRDTFRKVvdhfgRLDI 87
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLD-RLTSASNTARLADLR-------FVEGDLTDRDALEKLLADV-----RPDA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1191833562  88 LVNNAGV----NNEKNWEKTLQINLVsvisGTYLGLDYMSKQN 126
Cdd:pfam01370  68 VIHLAAVggvgASIEDPEDFIEANVL----GTLNLLEAARKAG 106
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 8-124 1.34e-05

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: 42.95  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALVDwnfeagvkckaaldeqfepQKTLFIQCDVADQAQLRDTFRKVvdhfGRLDI 87
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVITAG-------------------RSSGDYQVDITDEASIKALFEKV----GHFDA 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1191833562  88 LVNNAGVNN--------EKNWEKTL------QINLVSVisgtylGLDYMSK 124
Cdd:cd11731    58 IVSTAGDAEfaplaeltDADFQRGLnskllgQINLVRH------GLPYLND 102
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-110 1.59e-05

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 42.86  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEqfepQKTLFIQcDVADQAQLRDTFRKvVDHFGRLDIL 88
Cdd:cd08951    11 FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPG----AAGVLIG-DLSSLAETRKLADQ-VNAIGRFDAV 84

                          90       100
                  ....*....|....*....|....*....
gi 1191833562  89 VNNAGVNNEKN-------WEKTLQINLVS 110
Cdd:cd08951    85 IHNAGILSGPNrktpdtgIPAMVAVNVLA 113
PRK07024 PRK07024
SDR family oxidoreductase;
10-94 2.14e-05

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 42.61  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562  10 VTGAAQGIGRASAEALLLKGAKVALvdwnfeagVKCKAALDEQFEPQKTLFIQC-----DVADQAQLRDTFRKVVDHFGR 84
Cdd:PRK07024    7 ITGASSGIGQALAREYARQGATLGL--------VARRTDALQAFAARLPKAARVsvyaaDVRDADALAAAAADFIAAHGL 78

                          90
                  ....*....|
gi 1191833562  85 LDILVNNAGV 94
Cdd:PRK07024   79 PDVVIANAGI 88
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 5-141 2.31e-05

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 42.64  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQ-FEPQKtlfIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK05876    6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEgFDVHG---VMCDVRHREEVTHLADEAFRLLG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191833562  84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAG 141
Cdd:PRK05876   83 HVDVVFSNAGIvvggpiveMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQ--GTGGHVVFTASFAG 146
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-94 2.35e-05

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: 42.08  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562    6 KVALVTGAAQGIGRASAEALLLKGA-KVALV------DWNFEAGVKCKAALDEQfepqkTLFIQCDVADQAQLRDTFRKV 78
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLsrsgpdAPGAAALLAELEAAGAR-----VTVVACDVADRDALAAVLAAI 75

                           90
                   ....*....|....*.
gi 1191833562   79 VDHFGRLDILVNNAGV 94
Cdd:smart00822  76 PAVEGPLTGVIHAAGV 91
PRK08703 PRK08703
SDR family oxidoreductase;
5-51 3.82e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 41.84  E-value: 3.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEagvKCKAALDE 51
Cdd:PRK08703    6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHQK---KLEKVYDA 49
PRK07023 PRK07023
SDR family oxidoreductase;
8-94 4.12e-05

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 41.54  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGakVALVDWNFEAGVKCKAALDEQFEpqktlFIQCDVADQAQL-----RDTFRKVVDHF 82
Cdd:PRK07023    4 AIVTGHSRGLGAALAEQLLQPG--IAVLGVARSRHPSLAAAAGERLA-----EVELDLSDAAAAaawlaGDLLAAFVDGA 76

                          90
                  ....*....|..
gi 1191833562  83 GRLdILVNNAGV 94
Cdd:PRK07023   77 SRV-LLINNAGT 87
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-89 6.34e-05

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 41.25  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAA--QGIGRASAEALLLKGAKVALVDWNfeagVKCKAALDeQFEPQKTLFIQCDVADQAQLRDTFRKV 78
Cdd:PRK06079    3 GILSGKKIVVMGVAnkRSIAWGCAQAIKDQGATVIYTYQN----DRMKKSLQ-KLVDEEDLLVECDVASDESIERAFATI 77

                          90
                  ....*....|.
gi 1191833562  79 VDHFGRLDILV 89
Cdd:PRK06079   78 KERVGKIDGIV 88
PRK08416 PRK08416
enoyl-ACP reductase;
2-92 8.41e-05

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 40.91  E-value: 8.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   2 HVNGKVALVTGAAQGIGRASAEALLLKGAKVALV-DWNFEAGVKCKAALDEQFEpQKTLFIQCDVADQAQLRDTFRKVVD 80
Cdd:PRK08416    5 EMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDLEQKYG-IKAKAYPLNILEPETYKELFKKIDE 83

                          90
                  ....*....|..
gi 1191833562  81 HFGRLDILVNNA 92
Cdd:PRK08416   84 DFDRVDFFISNA 95
PRK07775 PRK07775
SDR family oxidoreductase;
8-109 1.06e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 40.51  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVAL----VDWNFEAGVKCKAALDEQFEpqktlfIQCDVADQAQLRDTFRKVVDHFG 83
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPVALgarrVEKCEELVDKIRADGGEAVA------FPLDVTDPDSVKSFVAQAEEALG 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1191833562  84 RLDILVNNAG---------VNNEKnWEKTLQINLV 109
Cdd:PRK07775   87 EIEVLVSGAGdtyfgklheISTEQ-FESQVQIHLV 120
PRK12367 PRK12367
short chain dehydrogenase; Provisional
 4-110 1.08e-04

short chain dehydrogenase; Provisional


Pssm-ID: 237079  Cd Length: 245  Bit Score: 40.38  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   4 NGKVALVTGAAQGIGRASAEALLLKGAKValVDWNFEAGVKCKAALDeqfEPQKTlfIQCDVADQAQLRDTFRKvvdhfg 83
Cdd:PRK12367   13 QGKRIGITGASGALGKALTKAFRAKGAKV--IGLTHSKINNSESNDE---SPNEW--IKWECGKEESLDKQLAS------ 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1191833562  84 rLDILVNNAGVNN-----EKNWEKTLQINLVS 110
Cdd:PRK12367   80 -LDVLILNHGINPggrqdPENINKALEINALS 110
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 9-92 1.40e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 40.30  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVkckaaldEQFEPQKTLFIQCDVADQAQLRDTFRKVVDHFGRLDIL 88
Cdd:PRK06483    6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAI-------DGLRQAGAQCIQADFSTNAGIMAFIDELKQHTDGLRAI 78


                  ....
gi 1191833562  89 VNNA 92
Cdd:PRK06483   79 IHNA 82
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 8-98 3.66e-04

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs 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: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 38.54  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   8 ALVTGAAQGIGRASAEALLLKGAKVALVdwnfeagVKCKAALDEQFEPQKtLFIQCDVADQAQLRDTFRKVvdhfgrlDI 87
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHEVTLL-------VRNTKRLSKEDQEPV-AVVEGDLRDLDSLSDAVQGV-------DV 65

                          90
                  ....*....|.
gi 1191833562  88 LVNNAGVNNEK 98
Cdd:cd05226    66 VIHLAGAPRDT 76
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 7-140 4.01e-04

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 38.74  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   7 VALVTGAAQGIGRASAEALLL----KGAKVALVDWNFEAGVKCKAALDEQFEPQKTLFIQCDVADQAQLRDTFRKVV--- 79
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALRelp 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191833562  80 --DHFGRLdILVNNAG-----------VNNEKNWEKTLQINLVSVISGTYLGLDYMsKQNGGEGGIIINMSSLA 140
Cdd:TIGR01500  82 rpKGLQRL-LLINNAGtlgdvskgfvdLSDSTQVQNYWALNLTSMLCLTSSVLKAF-KDSPGLNRTVVNISSLC 153
PRK08862 PRK08862
SDR family oxidoreductase;
1-138 7.97e-04

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 37.78  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   1 MHVNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNfeagvkcKAALDEQFE-----PQKTLFIQCDVADQAQLRDTF 75
Cdd:PRK08862    1 MDIKSSIILITSAGSVLGRTISCHFARLGATLILCDQD-------QSALKDTYEqcsalTDNVYSFQLKDFSQESIRHLF 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191833562  76 RKVVDHFGR-LDILVNN------AGVNNEKNWEKTlqINLVSVISGTYLGL-----DYMSKQNggEGGIIINMSS 138
Cdd:PRK08862   74 DAIEQQFNRaPDVLVNNwtssplPSLFDEQPSESF--IQQLSSLASTLFTYgqvaaERMRKRN--KKGVIVNVIS 144
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
5-110 8.09e-04

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 38.19  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQ------GIGRASAEAlllkGAKVALVdWNFEAGVKCKAALDEQFEpqKTLFIQCDVADQAQLRDTFRKV 78
Cdd:PRK08159   10 GKRGLILGVANnrsiawGIAKACRAA----GAELAFT-YQGDALKKRVEPLAAELG--AFVAGHCDVTDEASIDAVFETL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1191833562  79 VDHFGRLDILVNNAGVNN------------EKNWEKTLQINLVS 110
Cdd:PRK08159   83 EKKWGKLDFVVHAIGFSDkdeltgryvdtsRDNFTMTMDISVYS 126
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-94 9.53e-04

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 37.54  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAK-VALVDWNFEAGVKCKAALDEqFEPQKT--LFIQCDVADQAQLRDTFRKVVDHFGRL 85
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQALIAE-LEARGVevVVVACDVSDPDAVAALLAEIKAEGPPI 82


                  ....*....
gi 1191833562  86 DILVNNAGV 94
Cdd:pfam08659  83 RGVIHAAGV 91
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-34 1.74e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 36.98  E-value: 1.74e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVAL 34
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAI 33
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 6-94 2.15e-03

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: 36.67  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALL---LKGAKVALVDWNFEAGVKCKAALDEQFePQKTLFIQCDVADQAQLRDTFRKVVDhf 82
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLAsdpSKRFKVYATMRDLKKKGRLWEAAGALA-GGTLETLQLDVCDSKSVAAAVERVTE-- 77

                          90
                  ....*....|..
gi 1191833562  83 GRLDILVNNAGV 94
Cdd:cd09806    78 RHVDVLVCNAGV 89
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 9-78 2.55e-03

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. 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: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 36.81  E-value: 2.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDwNFEAGVKckaaldEQFEP--QKTLFIQCDVADQAQLRDTFRKV 78
Cdd:cd05256     3 LVTGGAGFIGSHLVERLLERGHEVIVLD-NLSTGKK------ENLPEvkPNVKFIEGDIRDDELVEFAFEGV 67
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
 5-32 3.77e-03

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs; KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif 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: 187653 [Multi-domain]  Cd Length: 259  Bit Score: 36.01  E-value: 3.77e-03
                          10        20
                  ....*....|....*....|....*....
gi 1191833562   5 GKVALVTGAAQG-IGRASAEALLLKGAKV 32
Cdd:cd08950     7 GKVALVTGAGPGsIGAEVVAGLLAGGATV 35
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
 9-94 4.15e-03

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. 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: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 36.16  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAKVALVDwNFEA--GVKCKAALDEQF-EPQKTLFIQCDVADQAQLRDTFRKVvdHFGRL 85
Cdd:cd05253     4 LVTGAAGFIGFHVAKRLLERGDEVVGID-NLNDyyDVRLKEARLELLgKSGGFKFVKGDLEDREALRRLFKDH--EFDAV 80


                  ....*....
gi 1191833562  86 DILVNNAGV 94
Cdd:cd05253    81 IHLAAQAGV 89
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 6-102 4.31e-03

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 35.83  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   6 KVALVTGAAQGIGRASAEALL-----LKGAKVALVDWNFEAGVKCKAALDEQFEPQKTLF--IQCDVADQAQLRDTFRKV 78
Cdd:cd08941     2 KVVLVTGANSGLGLAICERLLaeddeNPELTLILACRNLQRAEAACRALLASHPDARVVFdyVLVDLSNMVSVFAAAKEL 81

                          90       100
                  ....*....|....*....|....*.
gi 1191833562  79 VDHFGRLDILVNNAG--VNNEKNWEK 102
Cdd:cd08941    82 KKRYPRLDYLYLNAGimPNPGIDWIG 107
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-94 5.89e-03

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 35.82  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   9 LVTGAAQGIGRASAEALLLKGAK-VALVDWN-FEAGVKCKAALDEQFEPQKTLfIQCDVADQAQLRDTFRKvVDHFGRLD 86
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGARhLVLLSRRgPAPRAAARAALLRAGGARVSV-VRCDVTDPAALAALLAE-LAAGGPLA 231


                  ....*...
gi 1191833562  87 ILVNNAGV 94
Cdd:cd05274   232 GVIHAAGV 239
PLN02240 PLN02240
UDP-glucose 4-epimerase
 5-85 5.98e-03

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 35.71  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   5 GKVALVTGAAQGIGRASAEALLLKGAKVALVDwNF----EAGVKCKAALDEQFEpQKTLFIQCDVADQAQLRDTFRK--- 77
Cdd:PLN02240    5 GRTILVTGGAGYIGSHTVLQLLLAGYKVVVID-NLdnssEEALRRVKELAGDLG-DNLVFHKVDLRDKEALEKVFAStrf 82


                  ....*....
gi 1191833562  78 -VVDHFGRL 85
Cdd:PLN02240   83 dAVIHFAGL 91
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 3-143 6.34e-03

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 35.60  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191833562   3 VNGKVALVTGAAQGIGRASAEALLLKGAKVALVDWNFEAGVKCKAALDEQfEPQKTLFIQCDVADQAQLRDTFRKVVDhF 82
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSE-SNVDVSYIVADLTKREDLERTVKELKN-I 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191833562  83 GRLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGKD 143
Cdd:PRK08339   84 GEPDIFFFSTGgpkpgyfmEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGR---IIYSTSVAIKE 149
 
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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