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Conserved domains on  [gi|372626419|ref|NP_001243235|]
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15-hydroxyprostaglandin dehydrogenase [NAD(+)] isoform 5 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 6-186 1.18e-56

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


The actual alignment was detected with superfamily member cd05323:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 244  Bit Score: 179.03  E-value: 1.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqCKAALDEQFEPQKTLFIQCDVADQQQLR------------- 72
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAaafkkaiekfgrv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------------GLMPVAQQPVYCASK 87
Cdd:cd05323   79 dilinnagildeksylfagklpppwektidvnltgvinttylalhymdknkggkggvivnigsvaGLYPAPQFPVYSASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  88 HGIVGFTRSAALAANlMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieykdhiKDMIKYYGILDPPLIANGLITLIED 167
Cdd:cd05323  159 HGVVGFTRSLADLLE-YKTGVRVNAICPGFTNTPLLPDLVAKE------------AEMLPSAPTQSPEVVAKAIVYLIED 225

                        250
                 ....*....|....*....
gi 372626419 168 DALNGAIMKITTSKGIHFQ 186
Cdd:cd05323  226 DEKNGAIWIVDGGKLIEIE 244
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-186 1.18e-56

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: 179.03  E-value: 1.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqCKAALDEQFEPQKTLFIQCDVADQQQLR------------- 72
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAaafkkaiekfgrv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------------GLMPVAQQPVYCASK 87
Cdd:cd05323   79 dilinnagildeksylfagklpppwektidvnltgvinttylalhymdknkggkggvivnigsvaGLYPAPQFPVYSASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  88 HGIVGFTRSAALAANlMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieykdhiKDMIKYYGILDPPLIANGLITLIED 167
Cdd:cd05323  159 HGVVGFTRSLADLLE-YKTGVRVNAICPGFTNTPLLPDLVAKE------------AEMLPSAPTQSPEVVAKAIVYLIED 225

                        250
                 ....*....|....*....
gi 372626419 168 DALNGAIMKITTSKGIHFQ 186
Cdd:cd05323  226 DEKNGAIWIVDGGKLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-131 4.70e-30

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 109.24  E-value: 4.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQLR------------- 72
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA--LGGKALFIQGDVTDRAQVKalveqaverlgrl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   73 ------------------------------------------------------------GLMPVAQQPVYCASKHGIVG 92
Cdd:pfam00106  79 dilvnnagitglgpfselsdedwervidvnltgvfnltravlpamikgsggrivnissvaGLVPYPGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 372626419   93 FTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEN 131
Cdd:pfam00106 159 FTRS--LALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-136 1.34e-26

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: 101.79  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQLR------------ 72
Cdd:COG1028    6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA--AGGRALAVAADVTDEAAVEalvaaavaafgr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -------------------------------------------------------------GLMPVAQQPVYCASKHGIV 91
Cdd:COG1028   84 ldilvnnagitppgpleelteedwdrvldvnlkgpflltraalphmrergggrivnissiaGLRGSPGQAAYAASKAAVV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 372626419  92 GFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 136
Cdd:COG1028  164 GLTRS--LALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREAL 206
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-146 7.59e-24

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 94.46  E-value: 7.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpqKTLFIQCDVADQQQLR-------- 72
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG--EARVLVFDVSDEAAVRalieaave 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------------GLMPVAQQPVYCASK 87
Cdd:PRK05653  79 afgaldilvnnagitrdallprmseedwdrvidvnltgtfnvvraalppmikarygrivnissvsGVTGNPGQTNYSAAK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 372626419  88 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMI 146
Cdd:PRK05653 159 AGVIGFTK--ALALELASRGITVNAVAPGFIDTDMTEGLPE--------EVKAEILKEI 207
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-124 3.77e-12

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: 63.11  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNL-EAGVQCKAALDEQFE------PQKTLFIQCDVADQQQLRGLMPV 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLCAdDPAVGYPLATRAELDavaaacPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   78 A------------------------QQPV--------------------------------------------------- 82
Cdd:TIGR04504  81 AverwgrldaavaaagviaggrplwETTDaeldllldvnlrgvwnlaraavpamlarpdprggrfvavasaaatrglphl 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 372626419   83 --YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:TIGR04504 161 aaYCAAKHAVVGLVRG--LAADLGGTGVTANAVSPGSTRTAMLA 202
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 6-124 1.02e-07

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: 50.44  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQ----CKAALDEQFE--PQKTLFIQCDVADQQQLRGLMPVAQ 79
Cdd:NF040491   1 RVALVTGAARGIGAATVRRLAARGYAVVAVDACAGDPAPyplgTEADLDALVAssPGRVETVVADVRDRAALAAAVALAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  80 Q------------------------------------------------PV----------------------------- 82
Cdd:NF040491  81 DrwgrldaavaaaaviaggrplwetppeeldalwdvdvrgvwnlaaaavPAllagpdprgcrfvavasaaghrglfhlaa 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 372626419  83 YCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:NF040491 161 YCAAKHAVVGLVR--GLAADLAGTGVTACAVSPGSTDTPMLA 200
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-75 4.73e-03

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: 36.31  E-value: 4.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372626419     6 KVALVTGAAQGIGRAFAEALLLKGA-KVALV------DWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQLRGLM 75
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLsrsgpdAPGAAALLAELEAAGAR-----VTVVACDVADRDALAAVL 72
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-186 1.18e-56

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: 179.03  E-value: 1.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqCKAALDEQFEPQKTLFIQCDVADQQQLR------------- 72
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAaafkkaiekfgrv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------------GLMPVAQQPVYCASK 87
Cdd:cd05323   79 dilinnagildeksylfagklpppwektidvnltgvinttylalhymdknkggkggvivnigsvaGLYPAPQFPVYSASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  88 HGIVGFTRSAALAANlMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieykdhiKDMIKYYGILDPPLIANGLITLIED 167
Cdd:cd05323  159 HGVVGFTRSLADLLE-YKTGVRVNAICPGFTNTPLLPDLVAKE------------AEMLPSAPTQSPEVVAKAIVYLIED 225

                        250
                 ....*....|....*....
gi 372626419 168 DALNGAIMKITTSKGIHFQ 186
Cdd:cd05323  226 DEKNGAIWIVDGGKLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-131 4.70e-30

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 109.24  E-value: 4.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQLR------------- 72
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA--LGGKALFIQGDVTDRAQVKalveqaverlgrl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   73 ------------------------------------------------------------GLMPVAQQPVYCASKHGIVG 92
Cdd:pfam00106  79 dilvnnagitglgpfselsdedwervidvnltgvfnltravlpamikgsggrivnissvaGLVPYPGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 372626419   93 FTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEN 131
Cdd:pfam00106 159 FTRS--LALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-178 8.06e-27

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: 101.98  E-value: 8.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   8 ALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqcKAALDEQFEPQKTLFIQCDVADQQQLR--------------- 72
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAL---AELAAIEALGGNAVAVQADVSDEEDVEalveealeefgrldi 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ----------------------------------------------------------GLMPVAQQPVYCASKHGIVGFT 94
Cdd:cd05233   78 lvnnagiarpgpleeltdedwdrvldvnltgvflltraalphmkkqgggrivnissvaGLRPLPGQAAYAASKAALEGLT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  95 RSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKdmikyygILDPPLIANGLITLIEDDA--LNG 172
Cdd:cd05233  158 RS--LALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGR-------LGTPEEVAEAVVFLASDEAsyITG 228


                 ....*.
gi 372626419 173 AIMKIT 178
Cdd:cd05233  229 QVIPVD 234
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-136 1.34e-26

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: 101.79  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQLR------------ 72
Cdd:COG1028    6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA--AGGRALAVAADVTDEAAVEalvaaavaafgr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -------------------------------------------------------------GLMPVAQQPVYCASKHGIV 91
Cdd:COG1028   84 ldilvnnagitppgpleelteedwdrvldvnlkgpflltraalphmrergggrivnissiaGLRGSPGQAAYAASKAAVV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 372626419  92 GFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 136
Cdd:COG1028  164 GLTRS--LALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREAL 206
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-146 7.59e-24

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 94.46  E-value: 7.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpqKTLFIQCDVADQQQLR-------- 72
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG--EARVLVFDVSDEAAVRalieaave 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------------GLMPVAQQPVYCASK 87
Cdd:PRK05653  79 afgaldilvnnagitrdallprmseedwdrvidvnltgtfnvvraalppmikarygrivnissvsGVTGNPGQTNYSAAK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 372626419  88 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMI 146
Cdd:PRK05653 159 AGVIGFTK--ALALELASRGITVNAVAPGFIDTDMTEGLPE--------EVKAEILKEI 207
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-124 2.96e-23

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 93.01  E-value: 2.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQLR-------- 72
Cdd:COG0300    1 MSLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRA--AGARVEVVALDVTDPDAVAalaeavla 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------------GLMPVAQQPVYCASK 87
Cdd:COG0300   79 rfgpidvlvnnagvggggpfeeldledlrrvfevnvfgpvrltrallplmrargrgrivnvssvaGLRGLPGMAAYAASK 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 372626419  88 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:COG0300  159 AALEGFSES--LRAELAPTGVRVTAVCPGPVDTPFTA 193
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-140 4.95e-23

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: 92.17  E-value: 4.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFepqktLFIQCDVADQQQLR-------- 72
Cdd:COG4221    1 MSDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRA-----LAVPLDVTDEAAVEaavaaava 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------------GLMPVAQQPVYCASK 87
Cdd:COG4221   76 efgrldvlvnnagvallgpleeldpedwdrmidvnvkgvlyvtraalpamrargsghivnissiaGLRPYPGGAVYAATK 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 372626419  88 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKD 140
Cdd:COG4221  156 AAVRGLSES--LRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEG 206
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-177 1.91e-19

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 82.58  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVAL-VDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQ---QQL----- 71
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKE--EGGDAIAVKADVSSEedvENLveqiv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 -----------------------------------------------------------------RGLMPVAQQPVYCAS 86
Cdd:PRK05565  79 ekfgkidilvnnagisnfglvtdmtdeewdrvidvnltgvmlltryalpymikrksgvivnissiWGLIGASCEVLYSAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  87 KHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieyKDHIKDMIKYYGILDPPLIANGLITLIE 166
Cdd:PRK05565 159 KGAVNAFTK--ALAKELAPSGIRVNAVAPGAIDTEMWSSFSEED--------KEGLAEEIPLGRLGKPEEIAKVVLFLAS 228

                        250
                 ....*....|...
gi 372626419 167 DDA--LNGAIMKI 177
Cdd:PRK05565 229 DDAsyITGQIITV 241
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-120 3.59e-18

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 79.55  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVqcKAALDEQFEPQKTLFIQCDVADQQQLRGLM------- 75
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAA--AAAEALQKAGGKAIGVAMDVTDEEAINAGIdyavetf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 ----------------PVAQQPV--------------------------------------------------YCASKHG 89
Cdd:PRK12429  80 ggvdilvnnagiqhvaPIEDFPTekwkkmiaimldgaflttkaalpimkaqgggriinmasvhglvgsagkaaYVSAKHG 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 372626419  90 IVGFTRSAALAAnlMNSGVRLNAICPGFVNT 120
Cdd:PRK12429 160 LIGLTKVVALEG--ATHGVTVNAICPGYVDT 188
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 6-169 1.23e-17

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: 77.97  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALDEQFE-PQKTLFIQCDVADQQQLRGLMPVAQ----- 79
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEA---AAETVEEIKAlGGNAAALEADVSDREAVEALVEKVEaefgp 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  80 ---------------------------------------QPV-----------------------------YCASKHGIV 91
Cdd:cd05333   78 vdilvnnagitrdnllmrmseedwdavinvnltgvfnvtQAViramikrrsgriinissvvglignpgqanYAASKAGVI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  92 GFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMI--KYYGilDPPLIANGLITLIEDDA 169
Cdd:cd05333  158 GFTKS--LAKELASRGITVNAVAPGFIDTDMTDALPE--------KVKEKILKQIplGRLG--TPEEVANAVAFLASDDA 225
PRK12826 PRK12826
SDR family oxidoreductase;
5-120 2.70e-17

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 77.26  E-value: 2.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqckAALDEQFEPQ--KTLFIQCDVADQQQLR---------- 72
Cdd:PRK12826   6 GRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDA----AATAELVEAAggKARARQVDVRDRAALKaavaagvedf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -------------GLMPVAQ---------------------QPV------------------------------YCASKH 88
Cdd:PRK12826  82 grldilvanagifPLTPFAEmddeqwervidvnltgtflltQAAlpaliragggrivltssvagprvgypglahYAASKA 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 372626419  89 GIVGFTRSAALaaNLMNSGVRLNAICPGFVNT 120
Cdd:PRK12826 162 GLVGFTRALAL--ELAARNITVNSVHPGGVDT 191
FabG-like PRK07231
SDR family oxidoreductase;
1-125 3.66e-17

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 76.79  E-value: 3.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqcKAALDEQFEPQKTLFIQCDVADQQQLR-------- 72
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAA---ERVAAEILAGGRAIAVAADVSDEADVEaavaaale 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ------------------------------------------------------------------GLMPVAQQPVYCAS 86
Cdd:PRK07231  78 rfgsvdilvnnagtthrngplldvdeaefdrifavnvkspylwtqaavpamrgegggaivnvastaGLRPRPGLGWYNAS 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 372626419  87 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILES 125
Cdd:PRK07231 158 KGAVITLTKA--LAAELGPDKIRVNAVAPVVVETGLLEA 194
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-130 3.80e-17

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 76.45  E-value: 3.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpQKTLFIQCDVADQQQLRGLmpVAQ- 79
Cdd:PRK12825   2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALG-RRAQAVQADVTDKAALEAA--VAAa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  80 ---------------------------------------------QPV-----------------------------YCA 85
Cdd:PRK12825  79 verfgridilvnnagifedkpladmsddewdevidvnlsgvfhllRAVvppmrkqrggrivnissvaglpgwpgrsnYAA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 372626419  86 SKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEE 130
Cdd:PRK12825 159 AKAGLVGLTKALAR--ELAEYGITVNMVAPGDIDTDMKEATIEEA 201
PRK07063 PRK07063
SDR family oxidoreductase;
5-125 1.06e-16

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 75.47  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQL------------- 71
Cdd:PRK07063   7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVaaavaaaeeafgp 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 ---------------------------------------RGLMP--VAQQ--------------------PvYCASKHGI 90
Cdd:PRK07063  87 ldvlvnnaginvfadplamtdedwrrcfavdldgawngcRAVLPgmVERGrgsivniasthafkiipgcfP-YPVAKHGL 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 372626419  91 VGFTRsaALAANLMNSGVRLNAICPGFVNTAILES 125
Cdd:PRK07063 166 LGLTR--ALGIEYAARNVRVNAIAPGYIETQLTED 198
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-120 1.44e-16

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 75.06  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQL--------- 71
Cdd:PRK07067   2 MRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPA-----AIAVSLDVTRQDSIdrivaaave 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 --------------------------------------------------------------------RGLMPVAqqpVY 83
Cdd:PRK07067  77 rfggidilfnnaalfdmapildisrdsydrlfavnvkglfflmqavarhmveqgrggkiinmasqagrRGEALVS---HY 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 372626419  84 CASKHGIVGFTRSAALAanLMNSGVRLNAICPGFVNT 120
Cdd:PRK07067 154 CATKAAVISYTQSAALA--LIRHGINVNAIAPGVVDT 188
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-120 1.85e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 74.98  E-value: 1.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALD------------EQF----------------- 53
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGlvvggpldvtdpASFaafldaveadlgpidvl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  54 --------------EPQKTLFIQCDV-----------ADQQ-------------QLRGLMPVAQQPVYCASKHGIVGFTr 95
Cdd:PRK07825  83 vnnagvmpvgpfldEPDAVTRRILDVnvygvilgsklAAPRmvprgrghvvnvaSLAGKIPVPGMATYCASKHAVVGFT- 161

                        170       180
                 ....*....|....*....|....*
gi 372626419  96 sAALAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK07825 162 -DAARLELRGTGVHVSVVLPSFVNT 185
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-126 2.19e-16

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 74.46  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQckAALDEQFE-PQKTLFIQCDVADQQQLR------- 72
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAE--ALVAEIGAlGGKALAVQGDVSDAESVEravdeak 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ------------------------------------------------------------------GLMPVAQQPVYCAS 86
Cdd:PRK05557  79 aefggvdilvnnagitrdnllmrmkeedwdrvidtnltgvfnltkavarpmmkqrsgriinissvvGLMGNPGQANYAAS 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 372626419  87 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESI 126
Cdd:PRK05557 159 KAGVIGFTKS--LARELASRGITVNAVAPGFIETDMTDAL 196
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-173 4.51e-16

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: 73.57  E-value: 4.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQ------------ 70
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDA-----ARFFHLDVTDEDGwtavvdtareaf 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 -------------------------------------------------------------LRGLMPVAQQPVYCASKHG 89
Cdd:cd05341   78 grldvlvnnagiltggtvetttleewrrlldinltgvflgtravippmkeagggsiinmssIEGLVGDPALAAYNASKGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  90 IVGFTRSAALAANLMNSGVRLNAICPGFVNTAIL-ESIEKEENMGQYIEYKDHikdmikyyGILDPPLIANGLITLIEDD 168
Cdd:cd05341  158 VRGLTKSAALECATQGYGIRVNSVHPGYIYTPMTdELLIAQGEMGNYPNTPMG--------RAGEPDEIAYAVVYLASDE 229


                 ....*..
gi 372626419 169 A--LNGA 173
Cdd:cd05341  230 SsfVTGS 236
PRK06172 PRK06172
SDR family oxidoreductase;
1-124 5.93e-16

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 73.63  E-value: 5.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQLRGLM----- 75
Cdd:PRK06172   3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREA--GGEALFVACDVTRDAEVKALVeqtia 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 -------------------PVAQQ--------------------------------------------------PVYCAS 86
Cdd:PRK06172  81 aygrldyafnnagieieqgRLAEGseaefdaimgvnvkgvwlcmkyqiplmlaqgggaivntasvaglgaapkmSIYAAS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 372626419  87 KHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILE 124
Cdd:PRK06172 161 KHAVIGLTKSAAI--EYAKKGIRVNAVCPAVIDTDMFR 196
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-142 1.84e-15

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: 72.01  E-value: 1.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQ-------------- 70
Cdd:cd05347    5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEK--EGVEATAFTCDVSDEEAikaaveaieedfgk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 -------------------------------LRGLMPVAQQ----------------------------PVYCASKHGIV 91
Cdd:cd05347   83 idilvnnagiirrhpaeefpeaewrdvidvnLNGVFFVSQAvarhmikqghgkiinicsllselggppvPAYAASKGGVA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 372626419  92 GFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEykDHI 142
Cdd:cd05347  163 GLTK--ALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDIL--KRI 209
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 6-177 7.90e-15

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 70.63  E-value: 7.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQ--------------- 70
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQveayvdatveqfgri 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 --------------------------------------LRGLMPVAQ---------------------QPVYCASKHGIV 91
Cdd:cd05330   84 dgffnnagiegkqnltedfgadefdkvvsinlrgvfygLEKVLKVMReqgsgmivntasvggirgvgnQSGYAAAKHGVV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  92 GFTRSAALAANlmNSGVRLNAICPGFVNTAILESIEK-------EENMGQYIEYkdhikDMIKYYGilDPPLIANGLITL 164
Cdd:cd05330  164 GLTRNSAVEYG--QYGIRINAIAPGAILTPMVEGSLKqlgpenpEEAGEEFVSV-----NPMKRFG--EPEEVAAVVAFL 234

                        250
                 ....*....|....*
gi 372626419 165 IEDDA--LNGAIMKI 177
Cdd:cd05330  235 LSDDAgyVNAAVVPI 249
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-122 1.27e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 70.07  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALDeqfePQKTLFIQCDVADQQQ------------- 70
Cdd:PRK06841  14 SGKVAVVTGGASGIGHAIAELFAAKGARVALLDRS-EDVAEVAAQLL----GGNAKGLVCDVSDSQSveaavaavisafg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 --------------------------------LRGLMPVAQQ----------------------------PVYCASKHGI 90
Cdd:PRK06841  89 ridilvnsagvallapaedvseedwdktidinLKGSFLMAQAvgrhmiaagggkivnlasqagvvalerhVAYCASKAGV 168

                        170       180       190
                 ....*....|....*....|....*....|..
gi 372626419  91 VGFTRsaALAANLMNSGVRLNAICPGFVNTAI 122
Cdd:PRK06841 169 VGMTK--VLALEWGPYGITVNAISPTVVLTEL 198
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-137 3.21e-14

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: 68.61  E-value: 3.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   12 GAA--QGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPqktlFIQCDVADQQQLR----------------- 72
Cdd:pfam13561   1 GAAneSGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAA----VLPCDVTDEEQVEalvaaavekfgrldilv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   73 --------------------------------------------------------GLMPVAQQPVYCASKHGIVGFTRS 96
Cdd:pfam13561  77 nnagfapklkgpfldtsredfdraldvnlyslfllakaalplmkeggsivnlssigAERVVPNYNAYGAAKAALEALTRY 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 372626419   97 aaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIE 137
Cdd:pfam13561 157 --LAVELGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAE 195
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-127 4.53e-14

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 68.41  E-value: 4.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGV------------------------QCKAALDEQF----- 53
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARataaeigpaacaisldvtdqasidRCVAALVDRWgsidi 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  54 ---------------------------EPQKTLFIQCDVADQQQLRG----LMPVAQQP---------VYCASKHGIVGF 93
Cdd:cd05363   81 lvnnaalfdlapivditresydrlfaiNVSGTLFMMQAVARAMIAQGrggkIINMASQAgrrgealvgVYCATKAAVISL 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 372626419  94 TRSAALaaNLMNSGVRLNAICPGFVNTAILESIE 127
Cdd:cd05363  161 TQSAGL--NLIRHGINVNAIAPGVVDGEHWDGVD 192
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
4-138 6.57e-14

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 67.83  E-value: 6.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQL------------ 71
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSK--DGGKAIAVKADVSDRDQVfaavrqvvdtfg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 --------RGLMP---------------------------------------------------VAQQP---VYCASKHG 89
Cdd:PRK08643  79 dlnvvvnnAGVAPttpietiteeqfdkvyninvggviwgiqaaqeafkklghggkiinatsqagVVGNPelaVYSSTKFA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 372626419  90 IVGFTRSAalAANLMNSGVRLNAICPGFVNTAILESIEKE--ENMGQYIEY 138
Cdd:PRK08643 159 VRGLTQTA--ARDLASEGITVNAYAPGIVKTPMMFDIAHQvgENAGKPDEW 207
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 4-72 7.53e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 67.73  E-value: 7.53e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQLR 72
Cdd:PRK08265   5 AGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGER-----ARFIATDITDDAAIE 68
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-147 1.92e-13

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: 66.34  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN------LEAGVQCKA------------ALDEQFEPQKTLF------ 60
Cdd:cd05368    2 GKVALITAAAQGIGRAIALAFAREGANVIATDINeeklkeLERGPGITTrvldvtdkeqvaALAKEEGRIDVLFncagfv 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  61 -----IQCDVADQQ------------QLRGLMP----------------------VAQQPVYCASKHGIVGFTRSaaLAA 101
Cdd:cd05368   82 hhgsiLDCEDDDWDfamnlnvrsmylMIKAVLPkmlarkdgsiinmssvassikgVPNRFVYSTTKAAVIGLTKS--VAA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 372626419 102 NLMNSGVRLNAICPGFVNTAILESIekeenMGQYIEYKDHIKDMIK 147
Cdd:cd05368  160 DFAQQGIRCNAICPGTVDTPSLEER-----IQAQPDPEEALKAFAA 200
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 4-130 1.95e-13

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: 66.63  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpQKTLFIQCDVADQQQLR----------- 72
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAG-YNAVAVGADVTDKDDVEalidqavekfg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ---------GLMPVA------------------------------------------------------QQPVYCASKHG 89
Cdd:cd05366   80 sfdvmvnnaGIAPITplltiteedlkkvyavnvfgvlfgiqaaarqfkklghggkiinassiagvqgfpNLGAYSASKFA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 372626419  90 IVGFTRSAalAANLMNSGVRLNAICPGFVNTAILESIEKEE 130
Cdd:cd05366  160 VRGLTQTA--AQELAPKGITVNAYAPGIVKTEMWDYIDEEV 198
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 5-142 2.91e-13

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 66.23  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfepQKTLFIQCDVADQQQ-------------- 70
Cdd:PRK12829  11 GLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPG----AKVTATVADVADPAQvervfdtaverfgg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 --------------------------------LRGLMPVAQQPV-----------------------------YCASKHG 89
Cdd:PRK12829  87 ldvlvnnagiagptggideitpeqweqtlavnLNGQFYFARAAVpllkasghggviialssvagrlgypgrtpYAASKWA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372626419  90 IVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESI---------EKEENMGQyiEYKDHI 142
Cdd:PRK12829 167 VVGLVKS--LAIELGPLGIRVNAILPGIVRGPRMRRViearaqqlgIGLDEMEQ--EYLEKI 224
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 6-140 3.13e-13

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: 65.46  E-value: 3.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAAlDEQFEPqktlfIQCDVADQQQLRGLM---------- 75
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEA-----VPYDARDPEDARALVdalrdrfgri 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 ---------------------------------------------------------------PVAQQPVYCASKHGIVG 92
Cdd:cd08932   75 dvlvhnagigrpttlregsdaeleahfsinviapaeltrallpalreagsgrvvflnslsgkrVLAGNAGYSASKFALRA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 372626419  93 FTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENM--GQYIEYKD 140
Cdd:cd08932  155 LAH--ALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFppEEMIQPKD 202
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-72 3.64e-13

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 67.18  E-value: 3.64e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepQKTLFIQCDVADQQQLR 72
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP---DRALGVACDVTDEAAVQ 486
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-170 7.23e-13

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: 65.05  E-value: 7.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFePQKTLFIQCDVADQQQ-------------- 70
Cdd:cd05352    8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKY-GVKTKAYKCDVSSQESvektfkqiqkdfgk 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 -------------------------------LRGLMPVAQ------------------------------QPVYCASKHG 89
Cdd:cd05352   87 idilianagitvhkpaldytyeqwnkvidvnLNGVFNCAQaaakifkkqgkgsliitasmsgtivnrpqpQAAYNASKAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  90 IVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMIKYYGILDPPLIANGLITLIEDDA 169
Cdd:cd05352  167 VIHLAKS--LAVEWAKYFIRVNSISPGYIDTDLTDFVDK--------ELRKKWESYIPLKRIALPEELVGAYLYLASDAS 236


                 .
gi 372626419 170 L 170
Cdd:cd05352  237 S 237
PRK07326 PRK07326
SDR family oxidoreductase;
1-120 9.79e-13

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 64.65  E-value: 9.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALDEQFEPQKTLFIQCDV---ADQQQL------ 71
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKE---LEEAAAELNNKGNVLGLAADVrdeADVQRAvdaiva 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 -------------RGLM-PVAQQPV-------------------------------------------------YCASKH 88
Cdd:PRK07326  79 afggldvlianagVGHFaPVEELTPeewrlvidtnltgafytikaavpalkrgggyiinisslagtnffaggaaYNASKF 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 372626419  89 GIVGFTRSAALaaNLMNSGVRLNAICPGFVNT 120
Cdd:PRK07326 159 GLVGFSEAAML--DLRQYGIKVSTIMPGSVAT 188
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-137 1.11e-12

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 64.61  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVAD---------------- 67
Cdd:PRK12939   6 AGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA--GGRAHAIAADLADpasvqrffdaaaaalg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  68 -----------------------------------------------QQQLRG----------LMPVAQQPVYCASKHGI 90
Cdd:PRK12939  84 gldglvnnagitnsksateldidtwdavmnvnvrgtflmlraalphlRDSGRGrivnlasdtaLWGAPKLGAYVASKGAV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 372626419  91 VGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIE 137
Cdd:PRK12939 164 IGMTRS--LARELGGRGITVNAIAPGLTATEATAYVPADERHAYYLK 208
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-124 2.42e-12

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: 63.62  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRGLMPVAQQ--- 80
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRqfg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  81 --------------------PV--------------------------------------------------YCASKHGI 90
Cdd:cd08940   81 gvdilvnnagiqhvapiedfPTekwdaiialnlsavfhttrlalphmkkqgwgriiniasvhglvasanksaYVAAKHGV 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 372626419  91 VGFTRSAALAAnlMNSGVRLNAICPGFVNTAILE 124
Cdd:cd08940  161 VGLTKVVALET--AGTGVTCNAICPGWVLTPLVE 192
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-135 3.07e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 63.51  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfEPQKTLFIQCDVADQQ--------------Q 70
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEK-EGVKCLLIPGDVSDEAfckdaveetvrelgR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 LRGLMPVA--QQPV--------------------------------------------------------YCASKHGIVG 92
Cdd:PRK06701 125 LDILVNNAafQYPQqsleditaeqldktfktniysyfhmtkaalphlkqgsaiintgsitgyegnetlidYSATKGAIHA 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 372626419  93 FTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQY 135
Cdd:PRK06701 205 FTRS--LAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEKVSQF 245
PRK07774 PRK07774
SDR family oxidoreductase;
1-75 3.33e-12

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 63.23  E-value: 3.33e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQLRGLM 75
Cdd:PRK07774   2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVA--DGGTAIAVQVDVSDPDSAKAMA 74
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-124 3.77e-12

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: 63.11  E-value: 3.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNL-EAGVQCKAALDEQFE------PQKTLFIQCDVADQQQLRGLMPV 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLCAdDPAVGYPLATRAELDavaaacPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   78 A------------------------QQPV--------------------------------------------------- 82
Cdd:TIGR04504  81 AverwgrldaavaaagviaggrplwETTDaeldllldvnlrgvwnlaraavpamlarpdprggrfvavasaaatrglphl 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 372626419   83 --YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:TIGR04504 161 aaYCAAKHAVVGLVRG--LAADLGGTGVTANAVSPGSTRTAMLA 202
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-177 4.20e-12

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 62.86  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKV---------ALVDWNLEAGVQ----------------CKAALDEQFEPQKTL- 59
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRViatyfsgndCAKDWFEEYGFTedqvrlkeldvtdteeCAEALAEIEEEEGPVd 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  60 -------------FIQCDVADQQQ-----LRGLMPVAQ----------------------------QPVYCASKHGIVGF 93
Cdd:PRK12824  83 ilvnnagitrdsvFKRMSHQEWNDvintnLNSVFNVTQplfaamceqgygriinissvnglkgqfgQTNYSAAKAGMIGF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  94 TRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENmgqyieykDHIKDMIKYYGILDPPLIANGLITLIEDDA--LN 171
Cdd:PRK12824 163 TK--ALASEGARYGITVNCIAPGYIATPMVEQMGPEVL--------QSIVNQIPMKRLGTPEEIAAAVAFLVSEAAgfIT 232


                 ....*.
gi 372626419 172 GAIMKI 177
Cdd:PRK12824 233 GETISI 238
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-124 9.93e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 62.05  E-value: 9.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqcKAALDEqfepQKTLFIQCDVADQQQLRGLMPVA------ 78
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAG---KAAADE----VGGLFVPTDVTDEDAVNALFDTAaetygs 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  79 ----------------------------------------------------------------------QQPVYCASKH 88
Cdd:PRK06057  80 vdiafnnagisppeddsilntgldawqrvqdvnltsvylcckaalphmvrqgkgsiintasfvavmgsatSQISYTASKG 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 372626419  89 GIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:PRK06057 160 GVLAMSRE--LGVQFARQGIRVNALCPGPVNTPLLQ 193
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 4-79 1.33e-11

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: 61.54  E-value: 1.33e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDeqfepqKTLFIQCDVADQQQLRGLMPVAQ 79
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGD------NCRFVPVDVTSEKDVKAALALAK 70
PRK06138 PRK06138
SDR family oxidoreductase;
1-126 1.85e-11

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 61.32  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepQKTLFIQCDVADQQQLRGL------ 74
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAG---GRAFARQGDVGSAEAVEALvdfvaa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 ----------------------------------------------MPVAQQ---------------------PVYCASK 87
Cdd:PRK06138  78 rwgrldvlvnnagfgcggtvvttdeadwdavmrvnvggvflwakyaIPIMQRqgggsivntasqlalaggrgrAAYVASK 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 372626419  88 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI 126
Cdd:PRK06138 158 GAIASLTR--AMALDHATDGIRVNAVAPGTIDTPYFRRI 194
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 5-72 2.53e-11

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 60.87  E-value: 2.53e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCkaALDEQFEPqKTLFIQCDVADQQQLR 72
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKV--AEAAQGGP-RALGVQCDVTSEAQVQ 65
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 5-123 3.83e-11

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: 60.16  E-value: 3.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqckAALDEQFEPQKTLFIQCDVADQQQLRGLMPVA------ 78
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAG----QAVAAELGDPDISFVHCDVTVEADVRAAVDTAvarfgr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  79 ------------QQP---------------------------------------------------------VYCASKHG 89
Cdd:cd05326   80 ldimfnnagvlgAPCysiletsleefervldvnvygaflgtkhaarvmipakkgsivsvasvagvvgglgphAYTASKHA 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 372626419  90 IVGFTRSAalAANLMNSGVRLNAICPGFVNTAIL 123
Cdd:cd05326  160 VLGLTRSA--ATELGEHGIRVNCVSPYGVATPLL 191
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-70 5.68e-11

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 59.59  E-value: 5.68e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN----LEAGVQCKAAldeqfePQKTLFIQCDVADQQQ 70
Cdd:PRK08217   1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNqeklEEAVAECGAL------GTEVRGYAANVTDEED 68
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-131 5.93e-11

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 59.81  E-value: 5.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEA----------GVQC-------------KAALDEQFEPQKTLFI 61
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDISPEIekladelcgrGHRCtavvadvrdpasvAAAIKRAKEKEGRIDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  62 QC------------DVADQQQ-------LRGLMPVAQ-----------------------------QPVYCASKHGIVGF 93
Cdd:PRK08226  86 LVnnagvcrlgsflDMSDEDRdfhidinIKGVWNVTKavlpemiarkdgrivmmssvtgdmvadpgETAYALTKAAIVGL 165

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 372626419  94 TRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEEN 131
Cdd:PRK08226 166 TK--SLAVEYAQSGIRVNAICPGYVRTPMAESIARQSN 201
PRK06181 PRK06181
SDR family oxidoreductase;
5-122 1.18e-10

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 58.84  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQ-------------- 70
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADH--GGEALVVPTDVSDAEAcerlieaavarfgg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 -----------------------------------------------------------LRGLMPVAQQPVYCASKHGIV 91
Cdd:PRK06181  79 idilvnnagitmwsrfdeltdlsvfervmrvnylgavycthaalphlkasrgqivvvssLAGLTGVPTRSGYAASKHALH 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 372626419  92 GFTRSaaLAANLMNSGVRLNAICPGFVNTAI 122
Cdd:PRK06181 159 GFFDS--LRIELADDGVAVTVVCPGFVATDI 187
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 3-72 1.21e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 59.21  E-value: 1.21e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALDEQFEPQKTLFIQCDVADQQQLR 72
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAE---LAALAAELGGDDRVLTVVADVTDLAAMQ 73
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-177 1.43e-10

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 58.64  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALvdwnLEAGVQCKAaldEQFEPQKTLFIQCDVADQQQLRG------- 73
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAV----LYNSAENEA---KELREKGVFTIKCDVGNRDQVKKskevvek 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  74 ----------------LMPVAQ---------------QPVYC---------ASKHGIV-------------------GFT 94
Cdd:PRK06463  76 efgrvdvlvnnagimyLMPFEEfdeekynkmikinlnGAIYTtyeflpllkLSKNGAIvniasnagigtaaegttfyAIT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  95 RSAA------LAANLMNSGVRLNAICPGFVNTAIL------ESIEKEENMgqyieYKDhiKDMIKYYGIldPPLIANGLI 162
Cdd:PRK06463 156 KAGIiiltrrLAFELGKYGIRVNAVAPGWVETDMTlsgksqEEAEKLREL-----FRN--KTVLKTTGK--PEDIANIVL 226

                        250
                 ....*....|....*..
gi 372626419 163 TLIEDDA--LNGAIMKI 177
Cdd:PRK06463 227 FLASDDAryITGQVIVA 243
PRK05855 PRK05855
SDR family oxidoreductase;
5-125 1.91e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 59.22  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALDEQFEPQKTLFiQCDVADQQQL------------- 71
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDID-EAAAERTAELIRAAGAVAHAY-RVDVSDADAMeafaewvraehgv 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 ------------------------------------------------RGL-------------MPVAQQPVYCASKHGI 90
Cdd:PRK05855 393 pdivvnnagigmaggfldtsaedwdrvldvnlwgvihgcrlfgrqmveRGTgghivnvasaaayAPSRSLPAYATSKAAV 472

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 372626419  91 VGFtrSAALAANLMNSGVRLNAICPGFVNTAILES 125
Cdd:PRK05855 473 LML--SECLRAELAAAGIGVTAICPGFVDTNIVAT 505
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-129 2.52e-10

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 58.71  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFepqktLFIQCDVADQQQLR------------ 72
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDH-----HALAMDVSDEAQIRegfeqlhrefgr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ----------------------------------------------------------------GLMPVAQQPVYCASKH 88
Cdd:PRK06484  80 idvlvnnagvtdptmtatldttleefarlqainltgaylvarealrlmieqghgaaivnvasgaGLVALPKRTAYSASKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 372626419  89 GIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKE 129
Cdd:PRK06484 160 AVISLTRS--LACEWAAKGIRVNAVLPGYVRTQMVAELERA 198
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 6-120 2.98e-10

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: 57.52  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQckAALDEQFEpqKTLFIQCDVADQQQLR------------- 72
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARD-EARLA--AAAAQELE--GVLGLAGDVRDEADVRravdameeafggl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ---------GLM-PVAQQPV--------------------------------------------------YCASKHGIVG 92
Cdd:cd08929   76 dalvnnagvGVMkPVEELTPeewrlvldtnltgafycihkaapallrrgggtivnvgslagknafkggaaYNASKFGLLG 155

                        170       180
                 ....*....|....*....|....*...
gi 372626419  93 FTRSAALaaNLMNSGVRLNAICPGFVNT 120
Cdd:cd08929  156 LSEAAML--DLREANIRVVNVMPGSVDT 181
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-72 3.10e-10

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 57.69  E-value: 3.10e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLR 72
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLVELDITDQESLE 71
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 5-75 4.59e-10

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: 56.88  E-value: 4.59e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAAL--DEQFEPQKTLFIQCDVADQQQLRGLM 75
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIeaEANASGQKVSYISADLSDYEEVEQAF 73
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-98 4.95e-10

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: 56.96  E-value: 4.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQkTLFIQCDVADQQQLRGLMpvaqqpVY 83
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNR-VIALELDITSKESIKELI------ES 73

                         90
                 ....*....|....*.
gi 372626419  84 CASKHGIV-GFTRSAA 98
Cdd:cd08930   74 YLEKFGRIdILINNAY 89
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-177 6.99e-10

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 57.55  E-value: 6.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfepqKTLFIQCDVADQQQLRGLM--------- 75
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGD-----EHLSVQADITDEAAVESAFaqiqarwgr 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 ---------------PVAQQPV------------------------------------------------YCASKHGIVG 92
Cdd:PRK06484 344 ldvlvnnagiaevfkPSLEQSAedftrvydvnlsgafacaraaarlmsqggvivnlgsiasllalpprnaYCASKAAVTM 423

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  93 FTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQyieykDHIKDMIKYYGILDPPLIANGLITLIEDDA--L 170
Cdd:PRK06484 424 LSRS--LACEWAPAGIRVNTVAPGYIETPAVLALKASGRADF-----DSIRRRIPLGRLGDPEEVAEAIAFLASPAAsyV 496


                 ....*..
gi 372626419 171 NGAIMKI 177
Cdd:PRK06484 497 NGATLTV 503
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-79 9.05e-10

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: 56.51  E-value: 9.05e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEaGVQcKAALDEQFEPQKTLFIQCDVADQQQLRGLMPVAQ 79
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRE-NLE-RAASELRAGGAGVLAVVADLTDPEDIDRLVEKAG 73
PRK07062 PRK07062
SDR family oxidoreductase;
3-72 1.09e-09

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 56.20  E-value: 1.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLR 72
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEADVA 75
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 5-72 1.09e-09

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: 56.08  E-value: 1.09e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLR 72
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVR 68
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-169 1.23e-09

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: 55.85  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVA------------LVDWNLEAGVQCKA----------------ALDEQFEP- 55
Cdd:cd05358    3 GKVALVTGASSGIGKAIAIRLATAGANVVvnyrskedaaeeVVEEIKAVGGKAIAvqadvskeedvvalfqSAIKEFGTl 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  56 ----------QKTLFIQCDVADQQQ-----LRGLMPVAQQPV-----------------------------YCASKHGIV 91
Cdd:cd05358   83 dilvnnaglqGDASSHEMTLEDWNKvidvnLTGQFLCAREAIkrfrkskikgkiinmssvhekipwpghvnYAASKGGVK 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419  92 GFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEnmgqyiEYKDHIKDMIKYYGILDPPLIANGLITLIEDDA 169
Cdd:cd05358  163 MMTKT--LAQEYAPKGIRVNAIAPGAINTPINAEAWDDP------EQRADLLSLIPMGRIGEPEEIAAAAAWLASDEA 232
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 3-72 1.27e-09

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 56.06  E-value: 1.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQLR 72
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAA--GGEALAVKADVLDKESLE 75
PRK07074 PRK07074
SDR family oxidoreductase;
6-120 1.51e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 55.93  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAAL-DEQFEPqktlfIQCDVADQQQLRGL---------- 74
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALgDARFVP-----VACDLTDAASLAAAlanaaaergp 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 --------------------------------------------------------------MPVAQQPVYCASKHGIVG 92
Cdd:PRK07074  78 vdvlvanagaaraaslhdttpaswradnalnleaaylcveavlegmlkrsrgavvnigsvngMAALGHPAYSAAKAGLIH 157

                        170       180
                 ....*....|....*....|....*...
gi 372626419  93 FTRSaaLAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK07074 158 YTKL--LAVEYGRFGIRANAVAPGTVKT 183
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-129 1.54e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 55.72  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALdeQFEPQKTLFIQCDVADQQQLRGLM--------- 75
Cdd:PRK08213  12 GKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHL--EALGIDALWIAADVADEADIERLAeetlerfgh 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 --------------PVAQQPV-------------------------------------------------------YCAS 86
Cdd:PRK08213  90 vdilvnnagatwgaPAEDHPVeawdkvmnlnvrglfllsqavakrsmiprgygriinvasvaglggnppevmdtiaYNTS 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 372626419  87 KHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT----AILESIEKE 129
Cdd:PRK08213 170 KGAVINFTR--ALAAEWGPHGIRVNAIAPGFFPTkmtrGTLERLGED 214
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 4-146 1.71e-09

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: 55.49  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLE----AGVQCKAALDEQFEP-----------------QKTL--F 60
Cdd:cd05364    2 SGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAErleeTRQSCLQAGVSEKKIllvvadlteeegqdriiSTTLakF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  61 IQCDV-------------ADQQ----------QLRGLMPVAQQ---------------------------PVYCASKHGI 90
Cdd:cd05364   82 GRLDIlvnnagilakgggEDQDieeydkvmnlNLRAVIYLTKLavphliktkgeivnvssvaggrsfpgvLYYCISKAAL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419  91 VGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEENmgQYIEYKDHIKDMI 146
Cdd:cd05364  162 DQFTRCTAL--ELAPKGVRVNSVSPGVIVTGFHRRMGMPEE--QYIKFLSRAKETH 213
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 1-78 1.93e-09

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 55.62  E-value: 1.93e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQLRGLMPVA 78
Cdd:PRK06113   7 LRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQL--GGQAFACRCDITSEQELSALADFA 82
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 83-126 1.95e-09

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: 55.62  E-value: 1.95e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 372626419  83 YCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI 126
Cdd:cd08945  154 YSASKHGVVGFTK--ALGLELARTGITVNAVCPGFVETPMAASV 195
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-121 2.48e-09

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 54.97  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQ-----CKAALDEQFEPQKTLFIQCDV-------------- 65
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLSgnfhfLQLDLSDDLEPLFDWVPSVDIlcntagilddykpl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  66 -----ADQQQL------------RGLMP--VAQQP-------------------VYCASKHGIVGFTRSaaLAANLMNSG 107
Cdd:PRK06550  85 ldtslEEWQHIfdtnltstflltRAYLPqmLERKSgiiinmcsiasfvaggggaAYTASKHALAGFTKQ--LALDYAKDG 162

                        170
                 ....*....|....
gi 372626419 108 VRLNAICPGFVNTA 121
Cdd:PRK06550 163 IQVFGIAPGAVKTP 176
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-131 2.73e-09

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 54.89  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKValvdwnleagvqckAALDEQFEPQKTL---FIQCDVAD--------QQ 69
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKV--------------IGFDQAFLTQEDYpfaTFVLDVSDaaavaqvcQR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  70 QL--------------------------------------------RGLMPVAQQ----------------P-----VYC 84
Cdd:PRK08220  70 LLaetgpldvlvnaagilrmgatdslsdedwqqtfavnaggafnlfRAVMPQFRRqrsgaivtvgsnaahvPrigmaAYG 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 372626419  85 ASKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEEN 131
Cdd:PRK08220 150 ASKAALTSLAKCVGL--ELAPYGVRCNVVSPGSTDTDMQRTLWVDED 194
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-125 2.88e-09

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: 54.80  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALdeqfePQKTLFIQCDVADQQQLRGLM------- 75
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI-----AGGALALRVDVTDEQQVAALFeraveef 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 -----------------PVAQQPV--------------------------------------------------YCASKH 88
Cdd:cd08944   76 ggldllvnnagamhltpAIIDTDLavwdqtmainlrgtflccrhaaprmiargggsivnlssiagqsgdpgygaYGASKA 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 372626419  89 GIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILES 125
Cdd:cd08944  156 AIRNLTRT--LAAELRHAGIRCNALAPGLIDTPLLLA 190
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-135 3.57e-09

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: 54.99  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALV-------------DWNLEAGVQ-------------CKAALDEQFEPQKT 58
Cdd:cd05355   26 GKKALITGGDSGIGRAVAIAFAREGADVAINylpeeeddaeetkKLIEEEGRKcllipgdlgdesfCRDLVKEVVKEFGK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  59 LFIQCDVADQQQ---------------------------LRGLMP--------------VAQQPV-----YCASKHGIVG 92
Cdd:cd05355  106 LDILVNNAAYQHpqesieditteqlektfrtnifsmfylTKAALPhlkkgssiinttsvTAYKGSphlldYAATKGAIVA 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 372626419  93 FTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQY 135
Cdd:cd05355  186 FTRG--LSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSEF 226
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-124 3.67e-09

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 54.90  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLE------------------------------------------ 40
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDganavadeinkaggkaigvamdvtnedavnagidkvaerfgs 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  41 -------AGVQCKAALdEQFEPQ---KTLFIQCD---------------------VADQQQLRGLMPVAQQPVYCASKHG 89
Cdd:PRK13394  85 vdilvsnAGIQIVNPI-ENYSFAdwkKMQAIHVDgaflttkaalkhmykddrggvVIYMGSVHSHEASPLKSAYVTAKHG 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 372626419  90 IVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:PRK13394 164 LLGLAR--VLAKEGAKHNVRSHVVCPGFVRTPLVD 196
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 6-177 3.87e-09

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: 54.21  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfEPQKTLFIQCDVADQQQLRGLMPVAQQ----- 80
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNA-LRNSAVLVQADLSDFAACADLVAAAFRafgrc 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  81 --------------------------------------------------------------------PVYCASKHGIVG 92
Cdd:cd05357   80 dvlvnnasafyptplgqgsedawaelfginlkapylliqafarrlagsrngsiiniidamtdrpltgyFAYCMSKAALEG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  93 FTRSAA--LAANlmnsgVRLNAICPGFVNtailesiekeENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDAL 170
Cdd:cd05357  160 LTRSAAleLAPN-----IRVNGIAPGLIL----------LPEDMDAEYRENALRKVPLKRRPSAEEIADAVIFLLDSNYI 224


                 ....*..
gi 372626419 171 NGAIMKI 177
Cdd:cd05357  225 TGQIIKV 231
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-120 4.14e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 54.63  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   2 HVNGKVALVTGAAQGIGRAFAEALLLKGAK-VALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQ---------- 70
Cdd:PRK06198   3 RLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEAL--GAKAVFVQADLSDVEDcrrvvaaade 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 -----------------------------------LRG---LMPVA-----------------------QQP---VYCAS 86
Cdd:PRK06198  81 afgrldalvnaagltdrgtildtspelfdrhfavnVRApffLMQEAiklmrrrkaegtivnigsmsahgGQPflaAYCAS 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 372626419  87 KHGIVGFTRSAALAanLMNSGVRLNAICPGFVNT 120
Cdd:PRK06198 161 KGALATLTRNAAYA--LLRNRIRVNGLNIGWMAT 192
PRK05717 PRK05717
SDR family oxidoreductase;
4-71 5.20e-09

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 54.12  E-value: 5.20e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQL 71
Cdd:PRK05717   9 NGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGEN-----AWFIAMDVADEAQV 71
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-136 5.73e-09

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 53.97  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGA-----------------------KVALVDWNLEAGVQCKAALDEQFEPQKTLF 60
Cdd:PRK06935  14 DGKVAIVTGGNTGLGQGYAVALAKAGAdiiitthgtnwdetrrliekegrKVTFVQVDLTKPESAEKVVKEALEEFGKID 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  61 IQCDVA--------------DQQQLRGL---------MPVAQQ------------------------PVYCASKHGIVGF 93
Cdd:PRK06935  94 ILVNNAgtirraplleykdeDWNAVMDInlnsvyhlsQAVAKVmakqgsgkiiniasmlsfqggkfvPAYTASKHGVAGL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 372626419  94 TRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 136
Cdd:PRK06935 174 TK--AFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRNDEI 214
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 5-75 6.24e-09

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 53.89  E-value: 6.24e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRGLM 75
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQSVLALS 72
PRK07831 PRK07831
SDR family oxidoreductase;
5-130 6.36e-09

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 53.88  E-value: 6.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAA-QGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRGLM-------- 75
Cdd:PRK07831  17 GKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGRVEAVVCDVTSEAQVDALIdaaverlg 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 ---------------PV-------------------------------------------------AQ--QPVYCASKHG 89
Cdd:PRK07831  97 rldvlvnnaglggqtPVvdmtddewsrvldvtltgtfratraalrymrarghggvivnnasvlgwrAQhgQAHYAAAKAG 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 372626419  90 IVGFTRSAALAAnlMNSGVRLNAICPGFVNTAILESIEKEE 130
Cdd:PRK07831 177 VMALTRCSALEA--AEYGVRINAVAPSIAMHPFLAKVTSAE 215
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-127 6.43e-09

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: 53.79  E-value: 6.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALDEQFEPQKTLFIqCDVADQQQLR-------------- 72
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDIN-EKGAEETANNVRKAGGKVHYYK-CDVSKREEVYeaakkikkevgdvt 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------------------------GLMPVAQQPVYCASKHGIVGF 93
Cdd:cd05339   79 ilinnagvvsgkkllelpdeeiektfevntlahfwttkaflpdmlernhghivtiasvaGLISPAGLADYCASKAAAVGF 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 372626419  94 TRSAALAANLMN-SGVRLNAICPGFVNTAILESIE 127
Cdd:cd05339  159 HESLRLELKAYGkPGIKTTLVCPYFINTGMFQGVK 193
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 5-36 7.65e-09

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 53.80  E-value: 7.65e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVD 36
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVD 39
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-72 8.04e-09

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: 53.70  E-value: 8.04e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALdeQFEPQKTLFIQCDVADQQQLR 72
Cdd:cd08934    3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEL--EAEGGKALVLELDVTDEQQVD 68
PRK07069 PRK07069
short chain dehydrogenase; Validated
 8-126 8.22e-09

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 53.56  E-value: 8.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   8 ALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAA-LDEQFEPQKTLFIQCDVADQQQ-----------LRGL- 74
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAeINAAHGEGVAFAAVQDVTDEAQwqallaqaadaMGGLs 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 -------------------------MPV-----------------AQQP-------------------VYCASKHGIVGF 93
Cdd:PRK07069  82 vlvnnagvgsfgaieqieldewrrvMAInvesiflgckhalpylrASQPasivnissvaafkaepdytAYNASKAAVASL 161

                        170       180       190
                 ....*....|....*....|....*....|...
gi 372626419  94 TRSAALAANLMNSGVRLNAICPGFVNTAILESI 126
Cdd:PRK07069 162 TKSIALDCARRGLDVRCNSIHPTFIRTGIVDPI 194
PLN02253 PLN02253
xanthoxin dehydrogenase
 5-65 9.27e-09

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 53.67  E-value: 9.27e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepQKTLFIQCDV 65
Cdd:PLN02253  18 GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGE---PNVCFFHCDV 75
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-72 1.25e-08

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: 52.97  E-value: 1.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALdEQFEPQKTLFIQCDVADQQQLR 72
Cdd:cd05369    3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEI-SSATGGRAHPIQCDVRDPEAVE 69
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 4-135 1.28e-08

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: 53.05  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVA------------LVDWNLEAGVQ---CKAALDEQ------FEPQKTLFIQ 62
Cdd:cd05362    2 AGKVALVTGASRGIGRAIAKRLARDGASVVvnyasskaaaeeVVAEIEAAGGKaiaVQADVSDPsqvarlFDAAEKAFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  63 CDVA--------------------DQQ---QLRGLMPVAQQP--------------------------VYCASKHGIVGF 93
Cdd:cd05362   82 VDILvnnagvmlkkpiaetseeefDRMftvNTKGAFFVLQEAakrlrdggriinisssltaaytpnygAYAGSKAAVEAF 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 372626419  94 TRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQY 135
Cdd:cd05362  162 TR--VLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGY 201
PRK07454 PRK07454
SDR family oxidoreductase;
6-125 1.57e-08

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 52.65  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRA----FAEA--------------------LLLKGAKVAL--VDW-NLEAGVQCKAALDEQFEPQKT 58
Cdd:PRK07454   7 PRALITGASSGIGKAtalaFAKAgwdlalvarsqdalealaaeLRSTGVKAAAysIDLsNPEAIAPGIAELLEQFGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  59 L-----------FIQCDVADQQQL------------RGLMP----------------VAQQP-----VYCASKHGIVGFT 94
Cdd:PRK07454  87 LinnagmaytgpLLEMPLSDWQWViqlnltsvfqccSAVLPgmrargggliinvssiAARNAfpqwgAYCVSKAALAAFT 166

                        170       180       190
                 ....*....|....*....|....*....|.
gi 372626419  95 RsaALAANLMNSGVRLNAICPGFVNTAILES 125
Cdd:PRK07454 167 K--CLAEEERSHGIRVCTITLGAVNTPLWDT 195
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 5-41 2.09e-08

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 53.00  E-value: 2.09e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEA 41
Cdd:COG3347  425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEA 461
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-169 2.51e-08

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 52.31  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALvdwNLEAGVQCKAALDEQF--EPQKTLFIQCDVADQQQLRGLMPVAQ- 79
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLVNELgkEGHDVYAVQADVSKVEDANRLVEEAVn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  80 ------------------------------------------------------------------------QPVYCASK 87
Cdd:PRK12935  81 hfgkvdilvnnagitrdrtfkklnredwervidvnlssvfnttsavlpyiteaeegriisissiigqaggfgQTNYSAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  88 HGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEenmgqyIEYKDHIKDMIKYYGILDPplIANGLITLIED 167
Cdd:PRK12935 161 AGMLGFTKSLAL--ELAKTNVTVNAICPGFIDTEMVAEVPEE------VRQKIVAKIPKKRFGQADE--IAKGVVYLCRD 230


                 ..
gi 372626419 168 DA 169
Cdd:PRK12935 231 GA 232
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-70 2.91e-08

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 52.32  E-value: 2.91e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNleagvqckaalDEQFEPQKTLFIQCDVADQQQ 70
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-----------GGDGQHENYQFVPTDVSSAEE 63
PRK07856 PRK07856
SDR family oxidoreductase;
4-75 3.23e-08

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 51.86  E-value: 3.23e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKValvdwnleagVQCKAALDEQFEPQKTLFIQCDVADQQQLRGLM 75
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATV----------VVCGRRAPETVDGRPAEFHAADVRDPDQVAALV 66
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-115 3.23e-08

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 52.09  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnLEAGVQCKAALDE-QFEPQKTLFIQCDVADQQQLRGLMPVAQ-- 79
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVND--VASALDASDVLDEiRAAGAKAVAVAGDISQRATADELVATAVgl 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  80 -----------------------------------------------------------------------------QPV 82
Cdd:PRK07792  88 ggldivvnnagitrdrmlfnmsdeewdaviavhlrghflltrnaaaywrakakaaggpvygrivntsseaglvgpvgQAN 167

                        170       180       190
                 ....*....|....*....|....*....|...
gi 372626419  83 YCASKHGIVGFTRSAALAanLMNSGVRLNAICP 115
Cdd:PRK07792 168 YGAAKAGITALTLSAARA--LGRYGVRANAICP 198
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-120 3.44e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 51.64  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKV--------ALVDWNLEAG-------VQCKAALDEQFEPQKTL--FIQC 63
Cdd:PRK07060   5 FDFSGKSVLVTGASSGIGRACAVALAQRGARVvaaarnaaALDRLAGETGceplrldVGDDAAIRAALAAAGAFdgLVNC 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  64 ----------DVADQQ-------QLRGLMPVAQQPV-----------------------------YCASKHGIVGFTRSa 97
Cdd:PRK07060  85 agiaslesalDMTAEGfdrvmavNARGAALVARHVAramiaagrggsivnvssqaalvglpdhlaYCASKAALDAITRV- 163

                        170       180
                 ....*....|....*....|...
gi 372626419  98 aLAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK07060 164 -LCVELGPHGIRVNSVNPTVTLT 185
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-75 3.89e-08

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: 51.54  E-value: 3.89e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfepqkTLFIQCDVADQQQLRGLM 75
Cdd:cd05370    1 MKLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN------IHTIVLDVGDAESVEALA 69
PRK08264 PRK08264
SDR family oxidoreductase;
1-31 3.99e-08

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 51.43  E-value: 3.99e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAK 31
Cdd:PRK08264   2 MDIKGKVVLVTGANRGIGRAFVEQLLARGAA 32
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-169 4.46e-08

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: 51.32  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   8 ALVTGAAQGIGRAFAEALLLKGAKVALVD--WNLEAG-----------VQCKAALDEQ----FEPQKTLFIQCDVA---- 66
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDlpFVLLLEygdplrltpldVADAAAVREVcsrlLAEHGPIDALVNCAgvlr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  67 ----------DQQQ------------LRGLMPV----------------AQQP-----VYCASKHGIVGFTRSAALaaNL 103
Cdd:cd05331   81 pgatdplsteDWEQtfavnvtgvfnlLQAVAPHmkdrrtgaivtvasnaAHVPrismaAYGASKAALASLSKCLGL--EL 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419 104 MNSGVRLNAICPGFVNTAILESIEKEEN-MGQYIEYK-DHIKDMIKYYGILDPPLIANGLITLIEDDA 169
Cdd:cd05331  159 APYGVRCNVVSPGSTDTAMQRTLWHDEDgAAQVIAGVpEQFRLGIPLGKIAQPADIANAVLFLASDQA 226
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-67 4.54e-08

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 51.50  E-value: 4.54e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQckAALDE-QFEPQKTLFIQCDVAD 67
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELA--ATQQElRALGVEVIFFPADVAD 63
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 3-120 4.95e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 51.85  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVqckAALDEQFEPQ--KTLFIQCDVADQQQLR-------- 72
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARG-EEGL---EALAAEIRAAggEALAVVADVADAEAVQaaadraee 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------------------------------------GLM------------------------PVAQQPVYCASK 87
Cdd:PRK07109  82 elgpidtwvnnamvtvfgpfedvtpeefrrvtevtylgvvhGTLaalrhmrprdrgaiiqvgsalayrSIPLQSAYCAAK 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 372626419  88 HGIVGFTRSaaLAANLM--NSGVRLNAICPGFVNT 120
Cdd:PRK07109 162 HAIRGFTDS--LRCELLhdGSPVSVTMVQPPAVNT 194
PRK09242 PRK09242
SDR family oxidoreductase;
4-67 5.90e-08

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 51.29  E-value: 5.90e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVAD 67
Cdd:PRK09242   8 DGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSD 71
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-137 6.88e-08

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: 50.91  E-value: 6.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVA---DQQQL---------- 71
Cdd:cd05329    6 GKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREK--GFKVEGSVCDVSsrsERQELmdtvashfgg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 -------------------------------------------------------------RGLMPVAQQPVYCASKHGI 90
Cdd:cd05329   84 klnilvnnagtnirkeakdyteedyslimstnfeaayhlsrlahpllkasgngnivfissvAGVIAVPSGAPYGATKGAL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 372626419  91 VGFTRSaaLAANLMNSGVRLNAICPGFVNTAILES-IEKEENMGQYIE 137
Cdd:cd05329  164 NQLTRS--LACEWAKDNIRVNAVAPWVIATPLVEPvIQQKENLDKVIE 209
PRK05867 PRK05867
SDR family oxidoreductase;
3-126 7.23e-08

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 50.80  E-value: 7.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgVQCKAalDE-QFEPQKTLFIQCDVADQQQLRGL------- 74
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDA-LEKLA--DEiGTSGGKVVPVCCDVSQHQQVTSMldqvtae 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 ---------------------MPVAQ----------------------------------------------QPV--YCA 85
Cdd:PRK05867  84 lggidiavcnagiitvtpmldMPLEEfqrlqntnvtgvfltaqaaakamvkqgqggviintasmsghiinvpQQVshYCA 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 372626419  86 SKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI 126
Cdd:PRK05867 164 SKAAVIHLTK--AMAVELAPHKIRVNSVSPGYILTELVEPY 202
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 5-77 7.67e-08

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: 51.00  E-value: 7.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQkTLFIQCDVADQQQLRGLMPV 77
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGS-CKFVPCDVTKEEDIKTLISV 80
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-120 7.87e-08

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 51.38  E-value: 7.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDW-----NL-------------------EAGVQCKAALDEQFEP----- 55
Cdd:PRK08261 210 GKVALVTGAARGIGAAIAEVLARDGAHVVCLDVpaageALaavanrvggtalalditapDAPARIAEHLAERHGGldivv 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  56 -------QKTL----------FIQCDVADQQQL------RGLMP-------VAQ---------QPVYCASKHGIVGFTRs 96
Cdd:PRK08261 290 hnagitrDKTLanmdearwdsVLAVNLLAPLRIteallaAGALGdggrivgVSSisgiagnrgQTNYAASKAGVIGLVQ- 368

                        170       180
                 ....*....|....*....|....
gi 372626419  97 aALAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK08261 369 -ALAPLLAERGITINAVAPGFIET 391
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 5-124 8.06e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 50.87  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQ--KTLFIQCDVADQQQLRGL-------- 74
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAAggKALGLAFDVRDFAATRAAldagveef 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 ---------------MPVAQ---------------------QPV------------------------------YCASKH 88
Cdd:PRK12827  86 grldilvnnagiatdAAFAElsieewddvidvnldgffnvtQAAlppmirarrggrivniasvagvrgnrgqvnYAASKA 165

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 372626419  89 GIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:PRK12827 166 GLIGLTK--TLANELAPRGITVNAVAPGAINTPMAD 199
PRK07832 PRK07832
SDR family oxidoreductase;
6-127 8.66e-08

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 50.81  E-value: 8.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWN---LEAGVQCKAALDEQFEPQKTLfiqcDVADQQQLRG--------- 73
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDadgLAQTVADARALGGTVPEHRAL----DISDYDAVAAfaadihaah 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  74 -----LMPVA-------------QQ-----------PV------------------------------------YCASKH 88
Cdd:PRK07832  77 gsmdvVMNIAgisawgtvdrlthEQwrrmvdvnlmgPIhvietfvppmvaagrgghlvnvssaaglvalpwhaaYSASKF 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 372626419  89 GIVGFtrSAALAANLMNSGVRLNAICPGFVNTAILESIE 127
Cdd:PRK07832 157 GLRGL--SEVLRFDLARHGIGVSVVVPGAVKTPLVNTVE 193
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 6-124 1.02e-07

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: 50.44  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQ----CKAALDEQFE--PQKTLFIQCDVADQQQLRGLMPVAQ 79
Cdd:NF040491   1 RVALVTGAARGIGAATVRRLAARGYAVVAVDACAGDPAPyplgTEADLDALVAssPGRVETVVADVRDRAALAAAVALAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  80 Q------------------------------------------------PV----------------------------- 82
Cdd:NF040491  81 DrwgrldaavaaaaviaggrplwetppeeldalwdvdvrgvwnlaaaavPAllagpdprgcrfvavasaaghrglfhlaa 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 372626419  83 YCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 124
Cdd:NF040491 161 YCAAKHAVVGLVR--GLAADLAGTGVTACAVSPGSTDTPMLA 200
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 6-147 1.16e-07

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: 50.31  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleAGVQCKAAL-DEQFEPQKTLF-IQCDVADQQ-------------- 69
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVI-------ATARNPDKLeSLGELLNDNLEvLELDVTDEEsikaavkevierfg 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  70 ---------------------------------------------QLR--------------GLMPVAQQPVYCASKHGI 90
Cdd:cd05374   74 ridvlvnnagyglfgpleetsieevrelfevnvfgplrvtraflpLMRkqgsgrivnvssvaGLVPTPFLGPYCASKAAL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 372626419  91 VGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIK 147
Cdd:cd05374  154 EALSES--LRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEISPYAPERKEIK 208
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 4-75 1.17e-07

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: 50.47  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALV-----------DWNLEAGVQCKAALDEQfEPQKTLFIQCDVADQQQLR 72
Cdd:cd05338    2 SGKVAFVTGASRGIGRAIALRLAKAGATVVVAaktasegdngsAKSLPGTIEETAEEIEA-AGGQALPIVVDVRDEDQVR 80


                 ...
gi 372626419  73 GLM 75
Cdd:cd05338   81 ALV 83
PRK07201 PRK07201
SDR family oxidoreductase;
3-75 1.57e-07

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 50.72  E-value: 1.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALDEQFEPQKTLFI-QCDVADQQQLRGLM 75
Cdd:PRK07201 369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEA---LDELVAEIRAKGGTAHAyTCDLTDSAAVDHTV 439
PRK06194 PRK06194
hypothetical protein; Provisional
 5-80 1.61e-07

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 50.01  E-value: 1.61e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPqkTLFIQCDVADQQQLRGLMPVAQQ 80
Cdd:PRK06194   6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAE--VLGVRTDVSDAAQVEALADAALE 79
PRK06114 PRK06114
SDR family oxidoreductase;
3-72 2.15e-07

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 49.78  E-value: 2.15e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfEPQKTLFIQCDVADQQQLR 72
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEA-AGRRAIQIAADVTSKADLR 74
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 4-120 2.43e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 49.52  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKV------------------------------ALVDWNLE-----------AG 42
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVfgtsrnparaapipgvelleldvtddasvqAAVDEVIAragridvlvnnAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  43 VQCKAALDEQFEPQ-KTLFiqcDV----------------ADQQQLR--------GLMPVAQQPVYCASKHGIVGFTRSa 97
Cdd:PRK06179  83 VGLAGAAEESSIAQaQALF---DTnvfgilrmtravlphmRAQGSGRiinissvlGFLPAPYMALYAASKHAVEGYSES- 158

                        170       180
                 ....*....|....*....|...
gi 372626419  98 aLAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK06179 159 -LDHEVRQFGIRVSLVEPAYTKT 180
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-74 2.67e-07

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: 49.10  E-value: 2.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALdeQFEPQKTLFIQCDVADQQQLRGL 74
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAI--QQAGGQAIGLECNVTSEQDLEAV 66
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-74 3.28e-07

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: 49.00  E-value: 3.28e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNleagvqcKAALDE---QFEPQKTlfIQCDVADQQQLRGL 74
Cdd:COG3967    1 MKLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRR-------EEKLEEaaaANPGLHT--IVLDVADPASIAAL 68
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-120 3.53e-07

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 49.02  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN-------------------------LEAGVQCKAALDEQFE- 54
Cdd:PRK12828   3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGaaplsqtlpgvpadalriggidlvdPQAARRAVDEVNRQFGr 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  55 -----------PQKTL---------------FIQCDVADQQQLRGLMPVAQQPV-----------------YCASKHGIV 91
Cdd:PRK12828  83 ldalvniagafVWGTIadgdadtwdrmygvnVKTTLNASKAALPALTASGGGRIvnigagaalkagpgmgaYAAAKAGVA 162

                        170       180
                 ....*....|....*....|....*....
gi 372626419  92 GFTRsaALAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK12828 163 RLTE--ALAAELLDRGITVNAVLPSIIDT 189
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 4-121 3.54e-07

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: 48.99  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQLR----------- 72
Cdd:cd08935    4 KNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITAL--GGRAIALAADVLDRASLErareeivaqfg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ----------GLMPVA--------------------------------------QQ------------------------ 80
Cdd:cd08935   82 tvdilingagGNHPDAttdpehyepeteqnffdldeegwefvfdlnlngsflpsQVfgkdmleqkggsiinissmnafsp 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 372626419  81 ----PVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA 121
Cdd:cd08935  162 ltkvPAYSAAKAAVSNFTQW--LAVEFATTGVRVNAIAPGFFVTP 204
PRK08267 PRK08267
SDR family oxidoreductase;
9-125 3.84e-07

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 48.78  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   9 LVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGV-----------------------QCKAALDE-------------- 51
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDIN-EAGLaalaaelgagnawtgaldvtdraAWDAALADfaaatggrldvlfn 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  52 --------QFE--PQKTLFIQCDV----------ADQQQLR--------------GLMPVAQQPVYCASKHGIVGFTRsa 97
Cdd:PRK08267  84 nagilrggPFEdiPLEAHDRVIDInvkgvlngahAALPYLKatpgarvintssasAIYGQPGLAVYSATKFAVRGLTE-- 161

                        170       180
                 ....*....|....*....|....*...
gi 372626419  98 ALAANLMNSGVRLNAICPGFVNTAILES 125
Cdd:PRK08267 162 ALDLEWRRHGIRVADVMPLFVDTAMLDG 189
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-71 4.00e-07

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 48.80  E-value: 4.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEagvQCkAALDEQFePQKTLFIQCDV---ADQQQL 71
Cdd:PRK06200   2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAE---KL-ASLRQRF-GDHVLVVEGDVtsyADNQRA 70
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 5-36 4.38e-07

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: 48.68  E-value: 4.38e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVD 36
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVD 35
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-93 4.50e-07

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 48.55  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVaLVDWN--LEAGVQCKAALDEQfepqkTLFIQCDVADQQQLRGLMPVA 78
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARV-VVNYHqsEDAAEALADELGDR-----AIALQADVTDREQVQAMFATA 74

                         90
                 ....*....|....*....
gi 372626419  79 Q----QPVYCASKHGIVGF 93
Cdd:PRK08642  75 TehfgKPITTVVNNALADF 93
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-70 4.83e-07

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 48.53  E-value: 4.83e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALDEQFEpQKTLFIQCDVADQQQ 70
Cdd:PRK07666   3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLART-EENLKAVAEEVEAYG-VKVVIATADVSDYEE 70
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-177 5.45e-07

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: 48.54  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQLRGLMPVA-- 78
Cdd:cd05345    1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEA-----AIAIQADVTKRADVEAMVEAAls 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  79 -----------------QQPV-------------------------------------------------------YCAS 86
Cdd:cd05345   76 kfgrldilvnnagithrNKPMlevdeeefdrvfavnvksiylsaqalvphmeeqgggviiniastaglrprpgltwYNAS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  87 KHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI---EKEENMGQYieykdhiKDMIKYYGILDPPLIANGLIT 163
Cdd:cd05345  156 KGWVVTATK--AMAVELAPRNIRVNCLCPVAGETPLLSMFmgeDTPENRAKF-------RATIPLGRLSTPDDIANAALY 226

                        250
                 ....*....|....*.
gi 372626419 164 LIEDDA--LNGAIMKI 177
Cdd:cd05345  227 LASDEAsfITGVALEV 242
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-53 5.67e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 48.50  E-value: 5.67e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQF 53
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAH 55
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-104 8.28e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.05  E-value: 8.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   9 LVTGAAQGIGRAFAEALLLKGAKVALVDwNLEAGVQCKAALDeQFEpqktlFIQCDVADQQQLRGLMpvaQQP---VYCA 85
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLD-RSPPGAANLAALP-GVE-----FVRGDLRDPEALAAAL---AGVdavVHLA 72

                         90
                 ....*....|....*....
gi 372626419  86 SKHGIVGFTRSAALAANLM 104
Cdd:COG0451   73 APAGVGEEDPDETLEVNVE 91
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-122 1.04e-06

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: 47.58  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALV--DWN-LEAGV----------------------QCKAALDEQFEP-- 55
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSarREErLEEVKseclelgapsphvvpldmsdleDAEQVVEEALKLfg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  56 ------------QKTLFIQCDVADQQQL---------------------------------RGLMPVAQQPVYCASKHGI 90
Cdd:cd05332   81 gldilinnagisMRSLFHDTSIDVDRKImevnyfgpvaltkaalphliersqgsivvvssiAGKIGVPFRTAYAASKHAL 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 372626419  91 VGFTRSaaLAANLMNSGVRLNAICPGFVNTAI 122
Cdd:cd05332  161 QGFFDS--LRAELSEPNISVTVVCPGLIDTNI 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 6-80 1.70e-06

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: 47.07  E-value: 1.70e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfepQKTLFIQCDVADQQQLRGLMPVAQQ 80
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAG----ERAIAIQADVRDRDQVQAMIEEAKN 71
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-74 1.74e-06

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 47.02  E-value: 1.74e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpQKTLFIQCDVADQQQLRGL 74
Cdd:PRK08063   4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALG-RKALAVKANVGDVEKIKEM 72
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-70 1.78e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 46.98  E-value: 1.78e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQ 70
Cdd:PRK07097  10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRE--LGIEAHGYVCDVTDEDG 73
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-72 1.82e-06

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: 46.80  E-value: 1.82e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQLR 72
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPN-----LFFVHGDVADETLVK 63
PRK06949 PRK06949
SDR family oxidoreductase;
5-122 1.88e-06

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 47.06  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfEPQKTLFIQCDVADQQQLR------------ 72
Cdd:PRK06949   9 GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEA--EGGAAHVVSLDVTDYQSIKaavahaeteagt 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ---------------------------------------------------------------------GLMPVAQQPVY 83
Cdd:PRK06949  87 idilvnnsgvsttqklvdvtpadfdfvfdtntrgaffvaqevakrmiarakgagntkpggriiniasvaGLRVLPQIGLY 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 372626419  84 CASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAI 122
Cdd:PRK06949 167 CMSKAAVVHMTR--AMALEWGRHGINVNAICPGYIDTEI 203
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-67 1.97e-06

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: 46.83  E-value: 1.97e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFePQKTLFIQCDVAD 67
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKY-GVETKTIAADFSA 62
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-140 2.13e-06

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: 46.46  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGA-KVALVDWNLEAGVQCKAALDEQFepQKTLFIQCDVADQQQLRGL---------- 74
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEG--LSVRFHQLDVTDDASIEAAadfveekygg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 ------------------MPVAQQ------------------------------------------PVYCASKHGIVGFT 94
Cdd:cd05324   79 ldilvnnagiafkgfddsTPTREQaretmktnffgtvdvtqallpllkkspagrivnvssglgsltSAYGVSKAALNALT 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 372626419  95 RsaALAANLMNSGVRLNAICPGFVNTAilesiekeenMGQYIEYKD 140
Cdd:cd05324  159 R--ILAKELKETGIKVNACCPGWVKTD----------MGGGKAPKT 192
PRK06500 PRK06500
SDR family oxidoreductase;
5-120 2.23e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 46.49  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEqfepqKTLFIQCD---VADQQQL---------- 71
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGE-----SALVIRADagdVAAQKALaqalaeafgr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  72 ---------------------------------------RGLMPVAQQP-------------------VYCASKHGIVGF 93
Cdd:PRK06500  81 ldavfinagvakfapledwdeamfdrsfntnvkgpyfliQALLPLLANPasivlngsinahigmpnssVYAASKAALLSL 160

                        170       180
                 ....*....|....*....|....*..
gi 372626419  94 TRSaaLAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK06500 161 AKT--LSGELLPRGIRVNAVSPGPVQT 185
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-67 2.32e-06

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: 46.69  E-value: 2.32e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372626419   7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpQKTLFIQCDVAD 67
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAG-RRAIYFQADIGE 62
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-154 3.68e-06

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 45.98  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnleagvqckaaLDEQfEPQKTLFIQCDVADQQQLR------------ 72
Cdd:PRK06398   6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFD------------IKEP-SYNDVDYFKVDVSNKEQVIkgidyviskygr 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 ----------------GLMP-------------------------------------------VAQQPV--YCASKHGIV 91
Cdd:PRK06398  73 idilvnnagiesygaiHAVEedewdriinvnvngiflmskytipymlkqdkgviiniasvqsfAVTRNAaaYVTSKHAVL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419  92 GFTRSAALA-ANLmnsgVRLNAICPGFVNTAILESIEKEEnMGqyiEYKDHIKDMIKYYGILDP 154
Cdd:PRK06398 153 GLTRSIAVDyAPT----IRCVAVCPGSIRTPLLEWAAELE-VG---KDPEHVERKIREWGEMHP 208
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-72 4.15e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 46.17  E-value: 4.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLR 72
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVR 83
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 4-67 4.77e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 45.80  E-value: 4.77e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqcKAALDEQFePQKTLFIQCDVAD 67
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTAT----LADLAEKY-GDRLLPLALDVTD 60
PRK05650 PRK05650
SDR family oxidoreductase;
9-74 5.01e-06

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 45.80  E-value: 5.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419   9 LVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQLRGL 74
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREA--GGDGFYQRCDVRDYSQLTAL 67
PRK08589 PRK08589
SDR family oxidoreductase;
3-134 5.43e-06

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 45.54  E-value: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLE----------AGVQCKA----------------ALDEQFEPQ 56
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAvsetvdkiksNGGKAKAyhvdisdeqqvkdfasEIKEQFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  57 KTLFIQCDVaDQQ------------------QLRG--LMPVAQQPV-------------------------YCASKHGIV 91
Cdd:PRK08589  84 DVLFNNAGV-DNAagriheypvdvfdkimavDMRGtfLMTKMLLPLmmeqggsiintssfsgqaadlyrsgYNAAKGAVI 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 372626419  92 GFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIE--KEENMGQ 134
Cdd:PRK08589 163 NFTKSIAI--EYGRDGIRANAIAPGTIETPLVDKLTgtSEDEAGK 205
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-71 6.85e-06

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: 45.20  E-value: 6.85e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPqkTLF-IQCDVADQQQL 71
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYP--TLFpYQCDLSNEEQI 71
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 5-77 7.55e-06

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: 45.15  E-value: 7.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALDEQFEPqktlfIQCDVAD-QQQLRGLMPV 77
Cdd:cd05351    7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRT-QADLDSLVRECPGIEP-----VCVDLSDwDATEEALGSV 74
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 80-133 8.11e-06

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 44.91  E-value: 8.11e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 372626419  80 QPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAI---LESIEKEENMG 133
Cdd:PRK12936 149 QANYCASKAGMIGFSKS--LAQEIATRNVTVNCVAPGFIESAMtgkLNDKQKEAIMG 203
PRK07035 PRK07035
SDR family oxidoreductase;
5-51 9.07e-06

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 45.01  E-value: 9.07e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALDE 51
Cdd:PRK07035   8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDG---CQAVADA 51
PRK09134 PRK09134
SDR family oxidoreductase;
6-78 1.08e-05

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 44.53  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleagVQCKAALDEQFE--------PQKTLFIQCDVADQQQLRGLMPV 77
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVA---------VHYNRSRDEAEAlaaeiralGRRAVALQADLADEAEVRALVAR 80


                 .
gi 372626419  78 A 78
Cdd:PRK09134  81 A 81
PRK09072 PRK09072
SDR family oxidoreductase;
1-122 1.10e-05

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 44.55  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLE---------------------------------------- 40
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEklealaarlpypgrhrwvvadltseagreavlararemgg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  41 -------AGVQCKAALDEQFEPQKTLFIQCDVADQQQL-RGLMPVAQQP---------------------VYCASKHGIV 91
Cdd:PRK09072  81 invlinnAGVNHFALLEDQDPEAIERLLALNLTAPMQLtRALLPLLRAQpsamvvnvgstfgsigypgyaSYCASKFALR 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 372626419  92 GFtrSAALAANLMNSGVRLNAICPGFVNTAI 122
Cdd:PRK09072 161 GF--SEALRRELADTGVRVLYLAPRATRTAM 189
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 19-177 1.29e-05

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: 44.41  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  19 RAFAEAL---LLKGAKVALVDWNLEAGVQCKAALDEqfepqktLFIQCDVADQQQLRGLMPVAQQPVYCA---SKHGIVG 92
Cdd:cd05328   88 RALMEALlprLRKGHGPAAVVVSSIAGAGWAQDKLE-------LAKALAAGTEARAVALAEHAGQPGYLAyagSKEALTV 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  93 FTRSAALAAnLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEykdhiKDMIKYYGILDPPLIANGLITLIEDDA--L 170
Cdd:cd05328  161 WTRRRAATW-LYGAGVRVNTVAPGPVETPILQAFLQDPRGGESVD-----AFVTPMGRRAEPDEIAPVIAFLASDAAswI 234


                 ....*..
gi 372626419 171 NGAIMKI 177
Cdd:cd05328  235 NGANLFV 241
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 6-132 1.60e-05

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: 43.98  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVqckAALDEQFEPQKTLFIQCDVADQQQLRGLM---------- 75
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDID-EDGL---AALAAELGAENVVAGALDVTDRAAWAAALadfaaatggr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 --------------PVAQQP--------------------------------------------------VYCASKHGIV 91
Cdd:cd08931   77 ldalfnnagvgrggPFEDVPlaahdrmvdinvkgvlngayaalpylkatpgarvintasssaiygqpdlaVYSATKFAVR 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 372626419  92 GFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENM 132
Cdd:cd08931  157 GLTE--ALDVEWARHGIRVADVWPWFVDTPILTKGETGAAP 195
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 7-72 1.61e-05

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: 44.20  E-value: 1.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   7 VALVTGAAQGIGRAFAEALLLKG--AKVALVDWNLEAGVQCKAALdeqFEPQKTLFIQCDVADQQQLR 72
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEEL---RPGLRVTTVKADLSDAAGVE 65
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-80 2.10e-05

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 43.58  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVdwnlEAGVQCKA-ALDEQFEPQ--KTLFIQCDVADQQQLRGLMPV 77
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVN----YAGSAAAAdELVAEIEAAggRAIAVQADVADAAAVTRLFDA 76


                 ...
gi 372626419  78 AQQ 80
Cdd:PRK12937  77 AET 79
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
83-177 2.20e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 43.52  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  83 YCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNT---AILESIEKE--ENMGQYIEYKDHIKdmikyygILDPPLI 157
Cdd:PRK06924 154 YCSSKAGLDMFTQTVATEQEEEEYPVKIVAFSPGVMDTnmqAQIRSSSKEdfTNLDRFITLKEEGK-------LLSPEYV 226

                         90       100
                 ....*....|....*....|.
gi 372626419 158 ANGLITLIEDDAL-NGAIMKI 177
Cdd:PRK06924 227 AKALRNLLETEDFpNGEVIDI 247
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-40 2.33e-05

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: 43.49  E-value: 2.33e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLE 40
Cdd:cd05348    3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAE 39
PRK09135 PRK09135
pteridine reductase; Provisional
 1-116 2.43e-05

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 43.38  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRGLM----- 75
Cdd:PRK09135   2 MTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAELNALRPGSAAALQADLLDPDALPELVaacva 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  76 -------------------------------------------------------------------PVAQQPVYCASKH 88
Cdd:PRK09135  82 afgrldalvnnassfyptplgsiteaqwddlfasnlkapfflsqaaapqlrkqrgaivnitdihaerPLKGYPVYCAAKA 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 372626419  89 GIVGFTRSAA--LAANlmnsgVRLNAICPG 116
Cdd:PRK09135 162 ALEMLTRSLAleLAPE-----VRVNAVAPG 186
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 6-120 2.56e-05

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: 43.42  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFePQKTLFIQCDVADQQQLR------------- 72
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKF-PVKVLPLQLDVSDRESIEaalenlpeefrdi 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  73 -----------GLMPVAQQP--------------------------------------------------VYCASKHGIV 91
Cdd:cd05346   80 dilvnnaglalGLDPAQEADledwetmidtnvkgllnvtrlilpimiarnqghiinlgsiagrypyaggnVYCATKAAVR 159

                        170       180
                 ....*....|....*....|....*....
gi 372626419  92 GFtrSAALAANLMNSGVRLNAICPGFVNT 120
Cdd:cd05346  160 QF--SLNLRKDLIGTGIRVTNIEPGLVET 186
PRK06128 PRK06128
SDR family oxidoreductase;
5-139 4.71e-05

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 42.92  E-value: 4.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVAL-------------VDWNLEAGVQ-------------CKAALDEQFEPQKT 58
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIALnylpeeeqdaaevVQLIQAEGRKavalpgdlkdeafCRQLVERAVKELGG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  59 LFIQCDVADQQQLRG------------------------------LMPV-----------AQQPV-----YCASKHGIVG 92
Cdd:PRK06128 135 LDILVNIAGKQTAVKdiaditteqfdatfktnvyamfwlckaaipHLPPgasiintgsiqSYQPSptlldYASTKAAIVA 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 372626419  93 FTRsaALAANLMNSGVRLNAICPGFVNTAILES----IEKEENMGQYIEYK 139
Cdd:PRK06128 215 FTK--ALAKQVAEKGIRVNAVAPGPVWTPLQPSggqpPEKIPDFGSETPMK 263
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 5-72 4.95e-05

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: 43.12  E-value: 4.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALL-LKGAKVALV---------DWNLEAGVQCKAALDEqfepqkTLFIQCDVADQQQLR 72
Cdd:cd08953  205 GGVYLVTGGAGGIGRALARALArRYGARLVLLgrsplppeeEWKAQTLAALEALGAR------VLYISADVTDAAAVR 276
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-68 5.23e-05

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: 42.39  E-value: 5.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKvalvdwNLEAGVQCKAALDEQFE--PQKTLFIQCDVADQ 68
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAK------KVYAAVRDPGSAAHLVAkyGDKVVPLRLDVTDP 62
PRK06139 PRK06139
SDR family oxidoreductase;
1-79 5.51e-05

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 42.79  E-value: 5.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEA----GVQCKAALDEqfepqkTLFIQCDVADQQQLRGLMP 76
Cdd:PRK06139   3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEAlqavAEECRALGAE------VLVVPTDVTDADQVKALAT 76


                 ...
gi 372626419  77 VAQ 79
Cdd:PRK06139  77 QAA 79
PRK06196 PRK06196
oxidoreductase; Provisional
 5-51 5.68e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 42.75  E-value: 5.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDE 51
Cdd:PRK06196  26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDG 72
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-74 6.12e-05

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: 42.47  E-value: 6.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALDEQFEPQKTLFIQCDVADQQQLRGL 74
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEA---CADAAEELSAYGECIAIPADLSSEEGIEAL 72
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-177 6.59e-05

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 42.40  E-value: 6.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVA---------------------------LVDWNLEAGVQ--CKAALDE 51
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnakkraeemnetlkmvkenggegigvLADVSTREGCEtlAKATIDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  52 -----------------------------QFEPQKTLFIQCDVADQQQLR------------GLMPVAQQPVYCASKHGI 90
Cdd:PRK06077  82 ygvadilvnnaglglfspflnvddklidkHISTDFKSVIYCSQELAKEMReggaivniasvaGIRPAYGLSIYGAMKAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  91 VGFTRSAALAanlMNSGVRLNAICPGFVNTAILESIEKEENMGQYiEYKDHIKDMIKyygILDPPLIANGLITLIEDDAL 170
Cdd:PRK06077 162 INLTKYLALE---LAPKIRVNAIAPGFVKTKLGESLFKVLGMSEK-EFAEKFTLMGK---ILDPEEVAEFVAAILKIESI 234


                 ....*..
gi 372626419 171 NGAIMKI 177
Cdd:PRK06077 235 TGQVFVL 241
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-34 1.05e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 41.84  E-value: 1.05e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVAL 34
Cdd:PRK07478   2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVV 35
PRK06720 PRK06720
hypothetical protein; Provisional
 1-42 1.05e-04

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 41.11  E-value: 1.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAG 42
Cdd:PRK06720  12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESG 53
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 8-125 1.22e-04

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: 41.57  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   8 ALVTGAAQGIGRAFAEALLLKGAKVALVDW-NLEAGVQCKAALDEQfePQKTLFIQCDVADQQ----------------- 69
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEEL--GGKAVVVRADVSQPQdveemfaavkerfgrld 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  70 ----------------------------QLRGLMPVAQQ-------------------------PVYCA---SKHGIVGF 93
Cdd:cd05359   79 vlvsnaaagafrplseltpahwdakmntNLKALVHCAQQaaklmrergggrivaisslgsiralPNYLAvgtAKAALEAL 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 372626419  94 TRSaaLAANLMNSGVRLNAICPGFVNTAILES 125
Cdd:cd05359  159 VRY--LAVELGPRGIRVNAVSPGVIDTDALAH 188
PRK08703 PRK08703
SDR family oxidoreductase;
5-35 1.44e-04

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 41.46  E-value: 1.44e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALV 35
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVILV 36
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 3-71 1.53e-04

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 41.02  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFI----QCDVADQQQL 71
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFIldllTCTSENCQQL 74
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-36 1.81e-04

(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: 41.15  E-value: 1.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVD 36
Cdd:cd05353    3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVND 36
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-36 1.96e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 41.20  E-value: 1.96e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVD 36
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVND 37
PRK06124 PRK06124
SDR family oxidoreductase;
5-75 2.01e-04

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 40.85  E-value: 2.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN---LEAGVQCKAALDEQFEPqktlfIQCDVADQQQLRGLM 75
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNaatLEAAVAALRAAGGAAEA-----LAFDIADEEAVAAAF 79
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 73-144 3.16e-04

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: 40.14  E-value: 3.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419  73 GLMPVAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA----ILESIEKEENMGQYIEYKDHIKD 144
Cdd:cd09806  141 GLQGLPFNDVYCASKFALEGLCES--LAVQLLPFNVHLSLIECGPVHTAfmekVLGSPEEVLDRTADDITTFHFFY 214
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 4-74 3.22e-04

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: 40.51  E-value: 3.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEagVQCKAALDE-QFEPQKTLFIQCDVADQQQLRGL 74
Cdd:cd09763    2 SGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIL--PQLPGTAEEiEARGGKCIPVRCDHSDDDEVEAL 71
PRK07814 PRK07814
SDR family oxidoreductase;
3-78 3.27e-04

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 40.15  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALvdwnleaGVQCKAALDEQFEP-----QKTLFIQCDVADQQQLRGLMPV 77
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLI-------AARTESQLDEVAEQiraagRRAHVVAADLAHPEATAGLAGQ 80


                 .
gi 372626419  78 A 78
Cdd:PRK07814  81 A 81
PRK09730 PRK09730
SDR family oxidoreductase;
6-71 3.32e-04

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 40.22  E-value: 3.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVAlVDW--NLEAGVQCKAALDEQfePQKTLFIQCDVADQQQL 71
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVA-VNYqqNLHAAQEVVNLITQA--GGKAFVLQADISDENQV 66
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 8-126 3.78e-04

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: 40.01  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   8 ALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfEPQKTLFIqCDVADQQQ----------------- 70
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNP-NPSVEVEI-LDVTDEERnqlviaeleaelggldl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  71 --------------------------------LRGLMPVAQQ------------------------PVYCASKHGIVGFT 94
Cdd:cd05350   79 viinagvgkgtslgdlsfkafretidtnllgaAAILEAALPQfrakgrghlvlissvaalrglpgaAAYSASKAALSSLA 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 372626419  95 RSaaLAANLMNSGVRLNAICPGFVNTAILESI 126
Cdd:cd05350  159 ES--LRYDVKKRGIRVTVINPGFIDTPLTANM 188
PRK08628 PRK08628
SDR family oxidoreductase;
1-135 4.92e-04

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 39.56  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALdEQFEPQkTLFIQCDVADQQQLRGLmpVAQq 80
Cdd:PRK08628   3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRS-APDDEFAEEL-RALQPR-AEFVQVDLTDDAQCRDA--VEQ- 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419  81 pvyCASKHGivgftRSAALAANL-MNSGVRLNAICPGFVntailESIEKeeNMGQY 135
Cdd:PRK08628  77 ---TVAKFG-----RIDGLVNNAgVNDGVGLEAGREAFV-----ASLER--NLIHY 117
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 7-120 5.18e-04

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: 39.67  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfePQKTLFIQCDVADQQQLRGL------------ 74
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVREL--GGEAIAVVADVADAAQVERAadtaverfgrid 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 ----------------MPVAQ---------------------------------------------QPVYCASKHGIVGF 93
Cdd:cd05360   80 twvnnagvavfgrfedVTPEEfrrvfdvnylghvygtlaalphlrrrgggalinvgsllgyrsaplQAAYSASKHAVRGF 159

                        170       180
                 ....*....|....*....|....*..
gi 372626419  94 TRSAALAANLMNSGVRLNAICPGFVNT 120
Cdd:cd05360  160 TESLRAELAHDGAPISVTLVQPTAMNT 186
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 4-32 6.86e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 39.12  E-value: 6.86e-04
                         10        20
                 ....*....|....*....|....*....
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKV 32
Cdd:PRK06523   8 AGKRALVTGGTKGIGAATVARLLEAGARV 36
PRK12746 PRK12746
SDR family oxidoreductase;
2-34 6.98e-04

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 39.25  E-value: 6.98e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 372626419   2 HVNGKVALVTGAAQGIGRAFAEALLLKGAKVAL 34
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAI 35
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 4-67 7.43e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 39.13  E-value: 7.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqcKAALDEQFePQKTLFIQCDVAD 67
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAA----RADFEALH-PDRALARLLDVTD 61
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-34 8.74e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 38.98  E-value: 8.74e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVAL 34
Cdd:PRK07523  10 GRRALVTGSSQGIGYALAEGLAQAGAEVIL 39
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-34 1.16e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 38.52  E-value: 1.16e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVAL 34
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAI 33
PRK08340 PRK08340
SDR family oxidoreductase;
9-75 1.20e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 38.63  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372626419   9 LVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALDEQFEPQKTLFIQCDVADQQQLRGLM 75
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEEN---LEKALKELKEYGEVYAVKADLSDKDDLKNLV 67
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
81-136 1.29e-03

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 38.35  E-value: 1.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419  81 PVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 136
Cdd:PRK12481 154 PSYTASKSAVMGLTR--ALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAI 207
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 5-67 1.48e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 38.12  E-value: 1.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALdEQFEPQkTLFIQCDVAD 67
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI-EQFPGQ-VLTVQMDVRN 61
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 63-116 1.53e-03

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: 38.37  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 372626419   63 CDVADQQQLRGLMpvaqqpVYCASKHGIVGFTRSAALaaNLMNSGVRLNAICPG 116
Cdd:TIGR02685 159 CDAMTDQPLLGFT------MYTMAKHALEGLTRSAAL--ELAPLQIRVNGVAPG 204
PRK06914 PRK06914
SDR family oxidoreductase;
4-71 1.66e-03

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 38.08  E-value: 1.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQL 71
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSI 69
PRK05866 PRK05866
SDR family oxidoreductase;
3-35 1.72e-03

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 38.18  E-value: 1.72e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 372626419   3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALV 35
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAV 70
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 9-72 1.97e-03

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: 37.90  E-value: 1.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372626419   9 LVTGAAQGIGRAFAEALLLKGAKVALVDwNLEAGvqCKAALDEQfEPQKTLFIQCDVADQQQLR 72
Cdd:cd05247    3 LVTGGAGYIGSHTVVELLEAGYDVVVLD-NLSNG--HREALPRI-EKIRIEFYEGDIRDRAALD 62
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
80-129 2.06e-03

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 38.07  E-value: 2.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 372626419  80 QPVYCASKHGIVGFTrsAALAANLMNSGVRLNAICPGFVNTAILESIEKE 129
Cdd:PRK12938 150 QTNYSTAKAGIHGFT--MSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPD 197
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-75 2.33e-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: 38.13  E-value: 2.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372626419   9 LVTGAAQGIGRAFAEALLLKGAK-VALVDWN-LEAGVQCKAALDEQFEPQKTLfIQCDVADQQQLRGLM 75
Cdd:cd05274  154 LITGGLGGLGLLVARWLAARGARhLVLLSRRgPAPRAAARAALLRAGGARVSV-VRCDVTDPAALAALL 221
PRK06947 PRK06947
SDR family oxidoreductase;
6-80 2.46e-03

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 37.48  E-value: 2.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQfEPQKTLFIQCDVADQQQLRGLMPVAQQ 80
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRA-AGGRACVVAGDVANEADVIAMFDAVQS 76
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
 5-32 2.83e-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: 37.55  E-value: 2.83e-03
                         10        20
                 ....*....|....*....|....*....
gi 372626419   5 GKVALVTGAAQG-IGRAFAEALLLKGAKV 32
Cdd:cd08950    7 GKVALVTGAGPGsIGAEVVAGLLAGGATV 35
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 5-88 2.84e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. 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: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 37.60  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAK-VALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRGLMPvAQQPVY 83
Cdd:cd05237    2 GKTILVTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSRFPHDKLRFIIGDVRDKERLRRAFK-ERGPDI 80


                 ....*....
gi 372626419  84 C----ASKH 88
Cdd:cd05237   81 VfhaaALKH 89
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 73-115 3.14e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 37.35  E-value: 3.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 372626419  73 GLMPVAQQPVYCASKHGIVGFTRSAAlaANLMNSGVRLNAICP 115
Cdd:PRK07791 160 GLQGSVGQGNYSAAKAGIAALTLVAA--AELGRYGVTVNAIAP 200
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 70-120 3.50e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 37.36  E-value: 3.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 372626419  70 QLRGLMP--VAqqpvYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 120
Cdd:PRK12748 156 QSLGPMPdeLA----YAATKGAIEAFTKS--LAPELAEKGITVNAVNPGPTDT 202
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 4-169 3.65e-03

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 37.01  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQcKAALDEQFEPQKTLFIQCDVADQQQLRGL--------- 74
Cdd:PRK08936   6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEAN-DVAEEIKKAGGEAIAVKGDVTVESDVVNLiqtavkefg 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  75 ------------MPVAQQPV-----------------------------------------------------YCASKHG 89
Cdd:PRK08936  85 tldvminnagieNAVPSHEMsledwnkvintnltgaflgsreaikyfvehdikgniinmssvheqipwplfvhYAASKGG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419  90 IVGFTRSaaLAANLMNSGVRLNAICPGFVNTAIleSIEKEENMGQYieykDHIKDMIKYYGILDPPLIANGLITLIEDDA 169
Cdd:PRK08936 165 VKLMTET--LAMEYAPKGIRVNNIGPGAINTPI--NAEKFADPKQR----ADVESMIPMGYIGKPEEIAAVAAWLASSEA 236
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 8-75 4.40e-03

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 36.89  E-value: 4.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372626419    8 ALVTGAAQGIGRAFAEALLLKGAKVALVDwNLEAGVQCKAALDEQfepqktlFIQCDVADQQQLRGLM 75
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLD-RLTSASNTARLADLR-------FVEGDLTDRDALEKLL 60
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
81-136 4.51e-03

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 36.78  E-value: 4.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 372626419  81 PVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 136
Cdd:PRK08993 156 PSYTASKSGVMGVTR--LMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEI 209
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 5-71 4.57e-03

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: 36.80  E-value: 4.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQL 71
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQV 67
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-75 4.73e-03

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: 36.31  E-value: 4.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372626419     6 KVALVTGAAQGIGRAFAEALLLKGA-KVALV------DWNLEAGVQCKAALDEQfepqkTLFIQCDVADQQQLRGLM 75
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLsrsgpdAPGAAALLAELEAAGAR-----VTVVACDVADRDALAAVL 72
PRK12743 PRK12743
SDR family oxidoreductase;
83-120 5.07e-03

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 36.55  E-value: 5.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 372626419  83 YCASKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNT 120
Cdd:PRK12743 153 YTAAKHALGGLTKAMAL--ELVEHGILVNAVAPGAIAT 188
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 5-74 5.07e-03

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: 36.79  E-value: 5.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372626419   5 GKVALVTGAA--QGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpqKTLFIQCDVADQQQLRGL 74
Cdd:cd05372    1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGE--SALVLPCDVSNDEEIKEL 70
PRK06182 PRK06182
short chain dehydrogenase; Validated
 6-32 5.65e-03

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 36.48  E-value: 5.65e-03
                         10        20
                 ....*....|....*....|....*..
gi 372626419   6 KVALVTGAAQGIGRAFAEALLLKGAKV 32
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTV 30
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 5-74 5.93e-03

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: 36.67  E-value: 5.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEpQKTLFIQCDVADQQQLRGL 74
Cdd:cd05322    2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYG-EKAYGFGADATNEQSVIAL 70
PRK07023 PRK07023
SDR family oxidoreductase;
76-126 7.47e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 36.14  E-value: 7.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 372626419  76 PVAQQPVYCASKHGIVGFTRSAALAAnlmNSGVRLNAICPGFVNTAILESI 126
Cdd:PRK07023 143 AYAGWSVYCATKAALDHHARAVALDA---NRALRIVSLAPGVVDTGMQATI 190
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 5-32 8.65e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 36.13  E-value: 8.65e-03
                         10        20
                 ....*....|....*....|....*...
gi 372626419   5 GKVALVTGAAQGIGRAFAEALLLKGAKV 32
Cdd:PRK08303   8 GKVALVAGATRGAGRGIAVELGAAGATV 35
PRK08278 PRK08278
SDR family oxidoreductase;
1-72 9.15e-03

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 36.03  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372626419   1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALV------DWNLEAGVQCKAaldEQFEPQ--KTLFIQCDVADQQQLR 72
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAaktaepHPKLPGTIHTAA---EEIEAAggQALPLVGDVRDEDQVA 78
 
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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