NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|41152209|ref|NP_958488|]
View 

retinol dehydrogenase 10-B [Danio rerio]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143197)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
38-302 6.86e-144

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: 405.86  E-value: 6.86e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQlkpstgssdrvqelpllqpkVYTYMCDVSKR 117
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGK--------------------VHYYKCDVSKR 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLF 197
Cdd:cd05339  61 EEVYEAAKKIKKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 198 TTAGVEDYCASKFGAIGFHESLSHELKAADKDGIKMTLVCPFLVDTGMFEGCKIRKEMapFFPPLKPEYCVKQAMRAILT 277
Cdd:cd05339 141 SPAGLADYCASKAAAVGFHESLRLELKAYGKPGIKTTLVCPYFINTGMFQGVKTPRPL--LAPILEPEYVAEKIVRAILT 218
                       250       260
                ....*....|....*....|....*
gi 41152209 278 DQPMICTPRVMYMVTFMKTVLPFDA 302
Cdd:cd05339 219 NQQMLYLPFYAYFLPILKRTLPTPV 243
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
38-302 6.86e-144

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: 405.86  E-value: 6.86e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQlkpstgssdrvqelpllqpkVYTYMCDVSKR 117
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGK--------------------VHYYKCDVSKR 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLF 197
Cdd:cd05339  61 EEVYEAAKKIKKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 198 TTAGVEDYCASKFGAIGFHESLSHELKAADKDGIKMTLVCPFLVDTGMFEGCKIRKEMapFFPPLKPEYCVKQAMRAILT 277
Cdd:cd05339 141 SPAGLADYCASKAAAVGFHESLRLELKAYGKPGIKTTLVCPYFINTGMFQGVKTPRPL--LAPILEPEYVAEKIVRAILT 218
                       250       260
                ....*....|....*....|....*
gi 41152209 278 DQPMICTPRVMYMVTFMKTVLPFDA 302
Cdd:cd05339 219 NQQMLYLPFYAYFLPILKRTLPTPV 243
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
33-304 2.26e-69

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 217.04  E-value: 2.26e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqELPLLQPKVYTYMC 112
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAA--------------------ELRAAGARVEVVAL 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:COG0300  62 DVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSS 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEgckiRKEMAPFFPPLKPEYCVKQAM 272
Cdd:COG0300 142 VAGLRGLPGMAAYAASKAALEGFSESLRAELA---PTGVRVTAVCPGPVDTPFTA----RAGAPAGRPLLSPEEVARAIL 214
                       250       260       270
                ....*....|....*....|....*....|....
gi 41152209 273 RAILTDQPMICTPRVMYMVTFMKTVLP--FDAIV 304
Cdd:COG0300 215 RALERGRAEVYVGWDARLLARLLRLLPrlFDRLL 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
37-247 4.14e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.38  E-value: 4.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209    37 QVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsNEETAEMAreiyrqlkpstgssdrvQELPLLQPKVYTYMCDVSK 116
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRS---EEKLEAVA-----------------KELGALGGKALFIQGDVTD 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:pfam00106  61 RAQVKALVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGL 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 41152209   197 FTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFE 247
Cdd:pfam00106 141 VPYPGGSAYSASKAAVIGFTRSLALELA---PHGIRVNAVAPGGVDTDMTK 188
PRK07825 PRK07825
short chain dehydrogenase; Provisional
33-313 4.35e-42

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 147.01  E-value: 4.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmarEIyrqlkpstgssDRVQELPLlqpkvytymc 112
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAA---EL-----------GLVVGGPL---------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK07825  58 DVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVAS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKirkeMAPFFPPLKPEYCVKQAM 272
Cdd:PRK07825 138 LAGKIPVPGMATYCASKHAVVGFTDAARLELRGT---GVHVSVVLPSFVNTELIAGTG----GAKGFKNVEPEDVAAAIV 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 41152209  273 RAILTDQPMICTPRVMYMVTFMKTVLPFDAIVCMYKFIGAD 313
Cdd:PRK07825 211 GTVAKPRPEVRVPRALGPLAQAQRLLPRRVREALNRLLGGD 251
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
38-161 1.77e-07

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: 50.56  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209     38 VCVITGAGSGLGRLFALEFARRRA-TLVLwdinrqsneetaemareIYRQLKPSTGSSDRVQELPLLQPKVYTYMCDVSK 116
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVL-----------------LSRSGPDAPGAAALLAELEAAGARVTVVACDVAD 64
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 41152209    117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTM 161
Cdd:smart00822  65 RDALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVL 109
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
38-302 6.86e-144

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: 405.86  E-value: 6.86e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQlkpstgssdrvqelpllqpkVYTYMCDVSKR 117
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGK--------------------VHYYKCDVSKR 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLF 197
Cdd:cd05339  61 EEVYEAAKKIKKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 198 TTAGVEDYCASKFGAIGFHESLSHELKAADKDGIKMTLVCPFLVDTGMFEGCKIRKEMapFFPPLKPEYCVKQAMRAILT 277
Cdd:cd05339 141 SPAGLADYCASKAAAVGFHESLRLELKAYGKPGIKTTLVCPYFINTGMFQGVKTPRPL--LAPILEPEYVAEKIVRAILT 218
                       250       260
                ....*....|....*....|....*
gi 41152209 278 DQPMICTPRVMYMVTFMKTVLPFDA 302
Cdd:cd05339 219 NQQMLYLPFYAYFLPILKRTLPTPV 243
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
33-304 2.26e-69

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 217.04  E-value: 2.26e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqELPLLQPKVYTYMC 112
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAA--------------------ELRAAGARVEVVAL 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:COG0300  62 DVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSS 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEgckiRKEMAPFFPPLKPEYCVKQAM 272
Cdd:COG0300 142 VAGLRGLPGMAAYAASKAALEGFSESLRAELA---PTGVRVTAVCPGPVDTPFTA----RAGAPAGRPLLSPEEVARAIL 214
                       250       260       270
                ....*....|....*....|....*....|....
gi 41152209 273 RAILTDQPMICTPRVMYMVTFMKTVLP--FDAIV 304
Cdd:COG0300 215 RALERGRAEVYVGWDARLLARLLRLLPrlFDRLL 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
33-292 3.30e-53

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 174.99  E-value: 3.30e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMareiyrqlkpstgssdrvqelplLQPKVYTYMC 112
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAE-----------------------LGGRALAVPL 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:COG4221  59 DVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISS 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCK---IRKEMAPF--FPPLKPEYc 267
Cdd:COG4221 139 IAGLRPYPGGAVYAATKAAVRGLSESLRAELR---PTGIRVTVIEPGAVDTEFLDSVFdgdAEAAAAVYegLEPLTPED- 214
                       250       260
                ....*....|....*....|....*
gi 41152209 268 VKQAMRAILTDQPMICTPRVMYMVT 292
Cdd:COG4221 215 VAEAVLFALTQPAHVNVNELVLRPT 239
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
39-265 5.64e-53

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: 174.39  E-value: 5.64e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  39 CVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpstgssdrvqelpllQPKVYTYMCDVSKRE 118
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEAL---------------------GGNAVAVQADVSDEE 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 119 SVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFT 198
Cdd:cd05233  60 DVEALVEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRP 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152209 199 TAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM------FEGCKIRKEMAPFFPPLKPE 265
Cdd:cd05233 140 LPGQAAYAASKAALEGLTRSLALELA---PYGIRVNAVAPGLVDTPMlaklgpEEAEKELAAAIPLGRLGTPE 209
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
35-248 1.51e-49

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: 165.73  E-value: 1.51e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqELPLLQPKVYTYMCDV 114
Cdd:COG1028   5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAA--------------------ELRAAGGRALAVAADV 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:COG1028  65 TDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIA 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41152209 195 GLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEG 248
Cdd:COG1028 145 GLRGSPGQAAYAASKAAVVGLTRSLALELA---PRGIRVNAVAPGPIDTPMTRA 195
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
37-247 4.14e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.38  E-value: 4.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209    37 QVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsNEETAEMAreiyrqlkpstgssdrvQELPLLQPKVYTYMCDVSK 116
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRS---EEKLEAVA-----------------KELGALGGKALFIQGDVTD 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:pfam00106  61 RAQVKALVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGL 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 41152209   197 FTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFE 247
Cdd:pfam00106 141 VPYPGGSAYSASKAAVIGFTRSLALELA---PHGIRVNAVAPGGVDTDMTK 188
PRK07825 PRK07825
short chain dehydrogenase; Provisional
33-313 4.35e-42

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 147.01  E-value: 4.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmarEIyrqlkpstgssDRVQELPLlqpkvytymc 112
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAA---EL-----------GLVVGGPL---------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK07825  58 DVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVAS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKirkeMAPFFPPLKPEYCVKQAM 272
Cdd:PRK07825 138 LAGKIPVPGMATYCASKHAVVGFTDAARLELRGT---GVHVSVVLPSFVNTELIAGTG----GAKGFKNVEPEDVAAAIV 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 41152209  273 RAILTDQPMICTPRVMYMVTFMKTVLPFDAIVCMYKFIGAD 313
Cdd:PRK07825 211 GTVAKPRPEVRVPRALGPLAQAQRLLPRRVREALNRLLGGD 251
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
34-303 1.98e-39

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: 139.64  E-value: 1.98e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsNEETAEmarEIYRQLKpstgssdrvqELPLLQPKVYTYmcD 113
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVL--SAR--REERLE---EVKSECL----------ELGAPSPHVVPL--D 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:cd05332  62 MSDLEDAEQVVEEALKLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCPFLVDTGMFE---GCKIRKEMAPFFPPLK---PEYC 267
Cdd:cd05332 142 AGKIGVPFRTAYAASKHALQGFFDSLRAEL---SEPNISVTVVCPGLIDTNIAMnalSGDGSMSAKMDDTTANgmsPEEC 218
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 41152209 268 VKQAMRAILTDQPMICTPRVMYMV-TFMKTVLP--FDAI 303
Cdd:cd05332 219 ALEILKAIALRKREVFYARQVPLLaVYLRQLFPglFDWL 257
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
36-275 1.08e-36

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 131.99  E-value: 1.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsNEETAEMAREIYRQLKPSTGSsdrvqelpllqpKVYTYMCDVS 115
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVII--VAR--SESKLEEAVEEIEAEANASGQ------------KVSYISADLS 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:cd08939  65 DYEEVEQAFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 196 LFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMFE--------GCKIRKEMApffPPLKPEYC 267
Cdd:cd08939 145 LVGIYGYSAYCPSKFALRGLAESLRQELKP---YNIRVSVVYPPDTDTPGFEeenktkpeETKAIEGSS---GPITPEEA 218

                ....*...
gi 41152209 268 VKQAMRAI 275
Cdd:cd08939 219 ARIIVKGL 226
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
37-276 8.89e-36

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: 129.43  E-value: 8.89e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  37 QVCVITGAGSGLGRLFALEFARRRATLVLwdINRqSNEETAEMAREIYRQlkpstGSsdrvqelpllqpKVYTYMCDVSK 116
Cdd:cd05360   1 QVVVITGASSGIGRATALAFAERGAKVVL--AAR-SAEALHELAREVREL-----GG------------EAIAVVADVAD 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:cd05360  61 AAQVERAADTAVERFGRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGY 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 197 FTTAGVEDYCASKFGAIGFHESLSHELkAADKDGIKMTLVCPFLVDTGMFEGCKIRKEMAPFFPPlkPEYCVKQAMRAIL 276
Cdd:cd05360 141 RSAPLQAAYSASKHAVRGFTESLRAEL-AHDGAPISVTLVQPTAMNTPFFGHARSYMGKKPKPPP--PIYQPERVAEAIV 217
PRK05855 PRK05855
SDR family oxidoreductase;
28-291 1.19e-35

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 135.88  E-value: 1.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   28 RPReKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpsTGssdrvqelpllqPKV 107
Cdd:PRK05855 308 RPR-GPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRA--------AG------------AVA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  108 YTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGV-VSGRhLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-G 185
Cdd:PRK05855 367 HAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGIgMAGG-FLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgG 445
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  186 HIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM-----FEGC------KIRKE 254
Cdd:PRK05855 446 HIVNVASAAAYAPSRSLPAYATSKAAVLMLSECLRAELAAA---GIGVTAICPGFVDTNIvattrFAGAdaedeaRRRGR 522
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 41152209  255 MAPFFP--PLKPEYCVKQAMRAILTDQPMI-CTP--RVMYMV 291
Cdd:PRK05855 523 ADKLYQrrGYGPEKVAKAIVDAVKRNKAVVpVTPeaHAGYGV 564
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
33-245 1.03e-34

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 126.73  E-value: 1.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqELPLLQPKVYTYMC 112
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAE--------------------EVEAYGVKVVIATA 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK07666  64 DVSDYEEVTAAIEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISS 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM 245
Cdd:PRK07666 144 TAGQKGAAVTSAYSASKFGVLGLTESLMQEVR---KHNIRVTALTPSTVATDM 193
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
37-260 1.32e-34

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: 126.51  E-value: 1.32e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  37 QVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpstgssdrvqelplLQPKVYTYMCDVSK 116
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKA--------------------LGGNAAALEADVSD 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:cd05333  61 REAVEALVEKVEAEFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGL 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209 197 FTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGC--KIRKEMAPFFP 260
Cdd:cd05333 141 IGNPGQANYAASKAGVIGFTKSLAKELA---SRGITVNAVAPGFIDTDMTDALpeKVKEKILKQIP 203
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
38-292 1.05e-32

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: 121.64  E-value: 1.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLWDINrqsnEETAEMAreiyrQLKPSTGSsdrvqelpllqPKVYTYMCDVSKR 117
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKGAKVAILDRN----ENPGAAA-----ELQAINPK-----------VKATFVQCDVTSW 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDC--PDELIERTMMVNCHAHFWTTKAFLPKMLELNHGH---IVTVAS 192
Cdd:cd05323  62 EQLAAAFKKAIEKFGRVDILINNAGILDEKSYLFAgkLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGS 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadKDGIKMTLVCPFLVDTGMFEGCKI-RKEMAPFFPPLKPEYCVKQA 271
Cdd:cd05323 142 VAGLYPAPQFPVYSASKHGVVGFTRSLADLLEY--KTGVRVNAICPGFTNTPLLPDLVAkEAEMLPSAPTQSPEVVAKAI 219
                       250       260
                ....*....|....*....|....*
gi 41152209 272 MRAILTD----QPMICTPRVMYMVT 292
Cdd:cd05323 220 VYLIEDDekngAIWIVDGGKLIEIE 244
PRK12826 PRK12826
SDR family oxidoreductase;
32-245 1.11e-32

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 121.95  E-value: 1.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYrqlkpstgssdrvqelpllqPKVYTYM 111
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAG--------------------GKARARQ 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:PRK12826  62 VDVRDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTS 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  192 SSLGLFT-TAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGM 245
Cdd:PRK12826 142 SVAGPRVgYPGLAHYAASKAGLVGFTRALALELAA---RNITVNSVHPGGVDTPM 193
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
32-247 3.69e-32

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 120.30  E-value: 3.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEmarEIYRQLKPSTGssdrvqelpllqpKVYTYM 111
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVV---INYASSEAGAE---ALVAEIGALGG-------------KALAVQ 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:PRK05557  62 GDVSDAESVERAVDEAKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINIS 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209  192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFE 247
Cdd:PRK05557 142 SVVGLMGNPGQANYAASKAGVIGFTKSLARELASR---GITVNAVAPGFIETDMTD 194
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
40-288 4.03e-32

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 120.41  E-value: 4.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  40 VITGAGSGLGRLFALEFARRR----ATlvlwdinrqsneetaemAReiyrqlkpstgSSDRVQELP-LLQPKVYTYMCDV 114
Cdd:cd05374   4 LITGCSSGIGLALALALAAQGyrviAT-----------------AR-----------NPDKLESLGeLLNDNLEVLELDV 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:cd05374  56 TDEESIKAAVKEVIERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVA 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 195 GLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKIRKEMAPFFPPLKPEycVKQAMRA 274
Cdd:cd05374 136 GLVPTPFLGPYCASKAALEALSESLRLELAPF---GIKVTIIEPGPVRTGFADNAAGSALEDPEISPYAPE--RKEIKEN 210
                       250
                ....*....|....
gi 41152209 275 ILTDQPMICTPRVM 288
Cdd:cd05374 211 AAGVGSNPGDPEKV 224
FabG-like PRK07231
SDR family oxidoreductase;
32-247 4.13e-31

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 117.62  E-value: 4.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmarEIyrqlkpstGSSDRVQELPllqpkvytym 111
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAA---EI--------LAGGRAIAVA---------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGVV-SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTV 190
Cdd:PRK07231  60 ADVSDEADVEAAVAAALERFGSVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNV 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMFE 247
Cdd:PRK07231 140 ASTAGLRPRPGLGWYNASKGAVITLTKALAAELGP---DKIRVNAVAPVVVETGLLE 193
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
32-248 4.37e-31

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 117.57  E-value: 4.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqELPLLQPKVYTYM 111
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAA--------------------ELRAAGGEARVLV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:PRK05653  61 FDVSDEAAVRALIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNIS 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209  192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEG 248
Cdd:PRK05653 141 SVSGVTGNPGQTNYSAAKAGVIGFTKALALELA---SRGITVNAVAPGFIDTDMTEG 194
PRK06181 PRK06181
SDR family oxidoreductase;
36-304 9.57e-31

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 117.00  E-value: 9.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyrqlkpstgssdrvQELPLLQPKVYTYMCDVS 115
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLA--------------------QELADHGGEALVVPTDVS 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPD-ELIERTMMVNCHAHFWTTKAFLPKmLELNHGHIVTVASSL 194
Cdd:PRK06181  61 DAEACERLIEAAVARFGGIDILVNNAGITMWSRFDELTDlSVFERVMRVNYLGAVYCTHAALPH-LKASRGQIVVVSSLA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTgmfegcKIRKEMAPF------FPPLK----- 263
Cdd:PRK06181 140 GLTGVPTRSGYAASKHALHGFFDSLRIELAD---DGVAVTVVCPGFVAT------DIRKRALDGdgkplgKSPMQeskim 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 41152209  264 -PEYCVKQAMRAILTDQPMICTPRVMYMVTFMKTVLP--FDAIV 304
Cdd:PRK06181 211 sAEECAEAILPAIARRKRLLVMSLRGRLGRWLKLIAPglVDKIA 254
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
33-265 1.25e-30

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 116.12  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREIYRQLKpstgssDRVQELpllqpkvytyMC 112
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVV---VHYRSDEEAAEELVEAVEALG------RRAQAV----------QA 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK12825  64 DVTDKAALEAAVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISS 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGC-----KIRKEMAPFFPPLKPE 265
Cdd:PRK12825 144 VAGLPGWPGRSNYAAAKAGLVGLTKALARELA---EYGITVNMVAPGDIDTDMKEATieearEAKDAETPLGRSGTPE 218
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
36-275 7.83e-30

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 113.85  E-value: 7.83e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqSNEETAEMAREIYRQLKPSTGssdrvqelpllqpkvyTYMCDVS 115
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVIL--ISR-TQEKLDAVAKEIEEKYGVETK----------------TIAADFS 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVgDIDLLINNAGVvsGRH----LLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:cd05356  62 AGDDIYERIEKELEGL-DIGILVNNVGI--SHSipeyFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNIS 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMfegCKIRKemAPFFPPlKPEYCVKQA 271
Cdd:cd05356 139 SFAGLIPTPLLATYSASKAFLDFFSRALYEEYK---SQGIDVQSLLPYLVATKM---SKIRK--SSLFVP-SPEQFVRSA 209

                ....
gi 41152209 272 MRAI 275
Cdd:cd05356 210 LNTL 213
PRK05650 PRK05650
SDR family oxidoreductase;
40-245 1.87e-29

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 113.60  E-value: 1.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   40 VITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpstgssdrvqelplLQPKVYTYMCDVSKRES 119
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLRE--------------------AGGDGFYQRCDVRDYSQ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  120 VYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTT 199
Cdd:PRK05650  64 LTALAQACEEKWGGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQG 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 41152209  200 AGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM 245
Cdd:PRK05650 144 PAMSSYNVAKAGVVALSETLLVELA---DDEIGVHVVCPSFFQTNL 186
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
35-285 1.91e-29

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 112.95  E-value: 1.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsneETAEMAREIYrqlkpstgssdrvqelpllqPKVYTYMCDV 114
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDIN-----EEKLKELERG--------------------PGITTRVLDV 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAekvrSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:cd05368  56 TDKEQVAALA----KEEGRIDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVA 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 195 GLF-TTAGVEDYCASKFGAIGFHESLshelkAAD--KDGIKMTLVCPFLVDTGMFEGcKIRKEMAPffpplkpeycvKQA 271
Cdd:cd05368 132 SSIkGVPNRFVYSTTKAAVIGLTKSV-----AADfaQQGIRCNAICPGTVDTPSLEE-RIQAQPDP-----------EEA 194
                       250
                ....*....|....*.
gi 41152209 272 MRAILTDQPM--ICTP 285
Cdd:cd05368 195 LKAFAARQPLgrLATP 210
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-245 2.71e-29

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 112.63  E-value: 2.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVL-WDINRQSNEETAEMAREiyrqlkpstgssdrvqelplLQPKVYTYMCD 113
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKE--------------------EGGDAIAVKAD 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:PRK05565  64 VSSEEDVENLVEQIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSI 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41152209  194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM 245
Cdd:PRK05565 144 WGLIGASCEVLYSASKGAVNAFTKALAKELA---PSGIRVNAVAPGAIDTEM 192
PRK07109 PRK07109
short chain dehydrogenase; Provisional
32-276 3.41e-29

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 114.63  E-value: 3.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsNEET-AEMAREIYRQlkpstGssdrVQELPLLqpkvyty 110
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFARRGAKVVL--LAR--GEEGlEALAAEIRAA-----G----GEALAVV------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  111 mCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTV 190
Cdd:PRK07109  64 -ADVADAEAVQAAADRAEEELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkAADKDGIKMTLVCPFLVDTGMFEGCKIR--KEMAPFFPPLKPEycv 268
Cdd:PRK07109 143 GSALAYRSIPLQSAYCAAKHAIRGFTDSLRCEL-LHDGSPVSVTMVQPPAVNTPQFDWARSRlpVEPQPVPPIYQPE--- 218

                 ....*...
gi 41152209  269 kQAMRAIL 276
Cdd:PRK07109 219 -VVADAIL 225
PRK06172 PRK06172
SDR family oxidoreductase;
32-247 1.64e-28

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 110.61  E-value: 1.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIyrqlkpsTGSSDRVQelpllqpkvytym 111
Cdd:PRK06172   3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREA-------GGEALFVA------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRH-LLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTV 190
Cdd:PRK06172  63 CDVTRDAEVKALVEQTIAAYGRLDYAFNNAGIEIEQGrLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNT 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFE 247
Cdd:PRK06172 143 ASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYA---KKGIRVNAVCPAVIDTDMFR 196
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
36-248 1.88e-28

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 110.54  E-value: 1.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsNEETAEMAreiyrqlkpstgssdrVQELPLLQPKVYTYMCDVS 115
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLN---LEEAAKST----------------IQEISEAGYNAVAVGADVT 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVASSL 194
Cdd:cd05366  63 DKDDVEALIDQAVEKFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHgGKIINASSIA 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41152209 195 GLFTTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCPFLVDTGMFEG 248
Cdd:cd05366 143 GVQGFPNLGAYSASKFAVRGLTQTAAQEL--APK-GITVNAYAPGIVKTEMWDY 193
PRK06138 PRK06138
SDR family oxidoreductase;
36-281 1.89e-28

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 110.63  E-value: 1.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpstGSSDRVqelpllqpkvytYMCDVS 115
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA---------GGRAFA------------RQGDVG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:PRK06138  64 SAEAVEALVDFVAARWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  196 LFTTAGVEDYCASKfGAIGfheSLSHELkAAD--KDGIKMTLVCPFLVDTGMFegckirkemAPFFPPLKPEYCVKQAMR 273
Cdd:PRK06138 144 LAGGRGRAAYVASK-GAIA---SLTRAM-ALDhaTDGIRVNAVAPGTIDTPYF---------RRIFARHADPEALREALR 209

                 ....*...
gi 41152209  274 AIltdQPM 281
Cdd:PRK06138 210 AR---HPM 214
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
41-300 2.43e-28

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: 110.11  E-value: 2.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  41 ITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAR--EIYRQLKpstgssdrvQELPLLQPKVYTYMCDVSKRE 118
Cdd:cd05350   3 ITGASSGIGRALAREFAKAGYNVAL-------------AARrtDRLDELK---------AELLNPNPSVEVEILDVTDEE 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 119 SVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFT 198
Cdd:cd05350  61 RNQLVIAELEAELGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRG 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 199 TAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEgckirkEMAPFFPPLKPEYCVKQAMRAILTD 278
Cdd:cd05350 141 LPGAAAYSASKAALSSLAESLRYDVK---KRGIRVTVINPGFIDTPLTA------NMFTMPFLMSVEQAAKRIYKAIKKG 211
                       250       260
                ....*....|....*....|...
gi 41152209 279 QPMICTP-RVMYMVTFMKtVLPF 300
Cdd:cd05350 212 AAEPTFPwRLAVPLRLLK-LLPE 233
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
38-248 6.15e-28

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 108.60  E-value: 6.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAREIyRQLKPSTGSSDRVQELPllqpkvytymCDVSKR 117
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSL-------------GLRNP-EDLAALSASGGDVEAVP----------YDARDP 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLF 197
Cdd:cd08932  58 EDARALVDALRDRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKR 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 41152209 198 TTAGVEDYCASKFGAIGFHESLSHELkaADkDGIKMTLVCPFLVDTGMFEG 248
Cdd:cd08932 138 VLAGNAGYSASKFALRALAHALRQEG--WD-HGVRVSAVCPGFVDTPMAQG 185
PRK06194 PRK06194
hypothetical protein; Provisional
35-303 1.05e-27

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 109.33  E-value: 1.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqELPLLQPKVYTYMCDV 114
Cdd:PRK06194   5 AGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVA--------------------ELRAQGAEVLGVRTDV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN------HGHIV 188
Cdd:PRK06194  65 SDAAQVEALADAALERFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAekdpayEGHIV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  189 TVASSLGLFT--TAGVedYCASKFGAIGFHESLSHELKAADkDGIKMTLVCPFLVDTGMFEGCKIR-KEMAPFFPPLKPE 265
Cdd:PRK06194 145 NTASMAGLLAppAMGI--YNVSKHAVVSLTETLYQDLSLVT-DQVGASVLCPYFVPTGIWQSERNRpADLANTAPPTRSQ 221
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 41152209  266 YcVKQAMRAILTDQPMICTPRVMYMVtfmktvlpFDAI 303
Cdd:PRK06194 222 L-IAQAMSQKAVGSGKVTAEEVAQLV--------FDAI 250
PRK12939 PRK12939
short chain dehydrogenase; Provisional
33-247 1.47e-27

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 108.14  E-value: 1.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsneetAEMAREIYRQLKPSTGssdrvqelpllqpKVYTYMC 112
Cdd:PRK12939   4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGL-------AAEARELAAALEAAGG-------------RAHAIAA 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK12939  64 DLADPASVQRFFDAAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLAS 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMFE 247
Cdd:PRK12939 144 DTALWGAPKLGAYVASKGAVIGMTRSLARELGG---RGITVNAIAPGLTATEATA 195
PRK05876 PRK05876
short chain dehydrogenase; Provisional
36-245 2.99e-27

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 108.12  E-value: 2.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAReiyrqlkpSTGSSdrvqelpllqpkVYTYMCDVS 115
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLR--------AEGFD------------VHGVMCDVR 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHG-HIVTVASSL 194
Cdd:PRK05876  66 HREEVTHLADEAFRLLGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGgHVVFTASFA 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGM 245
Cdd:PRK05876 146 GLVPNAGLGAYGVAKYGVVGLAETLAREVTA---DGIGVSVLCPMVVETNL 193
PRK06841 PRK06841
short chain dehydrogenase; Provisional
33-243 3.12e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 107.44  E-value: 3.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDInrqsNEETAEMAREIyrqlkpstGSSDRVqelpllqpkvyTYMC 112
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDR----SEDVAEVAAQL--------LGGNAK-----------GLVC 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK06841  69 DVSDSQSVEAAVAAVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLAS 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  193 SLGlftTAGVED---YCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDT 243
Cdd:PRK06841 149 QAG---VVALERhvaYCASKAGVVGMTKVLALEWG---PYGITVNAISPTVVLT 196
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
40-277 1.26e-26

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 105.07  E-value: 1.26e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  40 VITGAGSGLGRLFALEFARRRATLVlWDINRQsneetaemaREIYRQLKPSTGSSDRVQELPLlqpkvytymcDVSKRES 119
Cdd:cd05325   2 LITGASRGIGLELVRQLLARGNNTV-IATCRD---------PSAATELAALGASHSRLHILEL----------DVTDEIA 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 120 VylTAEKVRSEVGD--IDLLINNAGVV-SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS---S 193
Cdd:cd05325  62 E--SAEAVAERLGDagLDVLINNAGILhSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSrvgS 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMfegckiRKEMAPFFPPLKPEYCVKQaMR 273
Cdd:cd05325 140 IGDNTSGGWYSYRASKAALNMLTKSLAVELKR---DGITVVSLHPGWVRTDM------GGPFAKNKGPITPEESVAG-LL 209

                ....
gi 41152209 274 AILT 277
Cdd:cd05325 210 KVID 213
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
46-263 1.54e-26

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: 104.82  E-value: 1.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209    46 SGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIyrqlkpstgssdrvqelpllqpKVYTYMCDVSKRESVYLTAE 125
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEEL----------------------GAAVLPCDVTDEEQVEALVA 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   126 KVRSEVGDIDLLINNAGVV--SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnHGHIVTVASSLGLFTTAGVE 203
Cdd:pfam13561  64 AAVEKFGRLDILVNNAGFApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE--GGSIVNLSSIGAERVVPNYN 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152209   204 DYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCKIRKEMAPFF---PPLK 263
Cdd:pfam13561 142 AYGAAKAALEALTRYLAVELG---PRGIRVNAISPGPIKTLAASGIPGFDELLAAAearAPLG 201
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
33-245 1.99e-26

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 105.09  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEmarEIYRQLKPSTGssdrvqelpllqpKVYTYMC 112
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVV---INYNSSKEAAE---NLVNELGKEGH-------------DVYAVQA 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK12935  64 DVSKVEDANRLVEEAVNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISS 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM 245
Cdd:PRK12935 144 IIGQAGGFGQTNYSAAKAGMLGFTKSLALELA---KTNVTVNAICPGFIDTEM 193
PRK05872 PRK05872
short chain dehydrogenase; Provisional
28-225 3.20e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 105.44  E-value: 3.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   28 RPREKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRqsnEETAEMAREIyrqlkpstGSSDRVqelpllqpkv 107
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEE---AELAALAAEL--------GGDDRV---------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  108 YTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElNHGHI 187
Cdd:PRK05872  60 LTVVADVTDLAAMQAAAEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIE-RRGYV 138
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 41152209  188 VTVASSLGLFTTAGVEDYCASKFGAigfhESLSHELKA 225
Cdd:PRK05872 139 LQVSSLAAFAAAPGMAAYCASKAGV----EAFANALRL 172
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
35-258 3.47e-26

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: 104.28  E-value: 3.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAreiyrqlkpstgssdrVQELPLLQPKVYTYMCDV 114
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGASVV---VNYASSKAAAEEV----------------VAEIEAAGGKAIAVQADV 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLpKMLELNhGHIVTVASSL 194
Cdd:cd05362  63 SDPSQVARLFDAAEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAA-KRLRDG-GRIINISSSL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209 195 GLFTTAGVEDYCASKfGAI-GFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKIR------KEMAPF 258
Cdd:cd05362 141 TAAYTPNYGAYAGSK-AAVeAFTRVLAKELGGR---GITVNAVAPGPVDTDMFYAGKTEeavegyAKMSPL 207
PRK07832 PRK07832
SDR family oxidoreductase;
39-251 8.71e-26

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 103.97  E-value: 8.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   39 CVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAReiyrqlkpSTGSSdrVQELPLLqpkvytymcDVSKRE 118
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADAR--------ALGGT--VPEHRAL---------DISDYD 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  119 SVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVASSLGLF 197
Cdd:PRK07832  64 AVAAFAADIHAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRgGHLVNVSSAAGLV 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  198 TTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCKI 251
Cdd:PRK07832 144 ALPWHAAYSASKFGLRGLSEVLRFDLA---RHGIGVSVVVPGAVKTPLVNTVEI 194
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
34-281 1.76e-25

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 102.96  E-value: 1.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsnEETAEMAREIyrqlkpstGSSDRvqelpllqpKVYTYMCD 113
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDIS----PEIEKLADEL--------CGRGH---------RCTAVVAD 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:PRK08226  63 VRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  194 LG-LFTTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCPFLVDTGMFEGckirkeMAPFFPPLKPEycvkQAM 272
Cdd:PRK08226 143 TGdMVADPGETAYALTKAAIVGLTKSLAVEY--AQS-GIRVNAICPGYVRTPMAES------IARQSNPEDPE----SVL 209

                 ....*....
gi 41152209  273 RAILTDQPM 281
Cdd:PRK08226 210 TEMAKAIPL 218
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
34-243 1.96e-25

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 102.23  E-value: 1.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRQsneetAEMAREIYRQLKPSTGssdrvqelpllqpKVYTYMCD 113
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAI--AARR-----VDRLEALADELEAEGG-------------KALVLELD 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:cd08934  61 VTDEQQVDAAVERTVEALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSV 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDT 243
Cdd:cd08934 141 AGRVAVRNSAVYNATKFGVNAFSEGLRQEVT---ERGVRVVVIEPGTVDT 187
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
33-256 2.16e-25

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 102.44  E-value: 2.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrQSNEETAEMAREIYRQlkpstgssdrvqelpllqpKVYTYMC 112
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRN-EEKAEEAQQLIEKEGV-------------------EATAFTC 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd05347  62 DVSDEEAIKAAVEAIEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICS 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCKIRKEMA 256
Cdd:cd05347 142 LLSELGGPPVPAYAASKGGVAGLTKALATEWA---RHGIQVNAIAPGYFATEMTEAVVADPEFN 202
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
36-272 3.43e-25

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: 101.23  E-value: 3.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREIyrqlkpstgssdrvqelpllqPKVYTYMCDVS 115
Cdd:cd05370   5 GNTVLITGGTSGIGLALARKFLEAGNTVI---ITGRREERLAEAKKEL---------------------PNIHTIVLDVG 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDEL--IERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:cd05370  61 DAESVEALAEALLSEYPNLDILINNAGIQRPIDLRDPASDLdkADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSG 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKIRKEMAPFfpPLKPEYCVKQAM 272
Cdd:cd05370 141 LAFVPMAANPVYCATKAALHSYTLALRHQLKDT---GVEVVEIVPPAVDTELHEERRNPDGGTPR--KMPLDEFVDEVV 214
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
38-245 7.82e-25

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: 100.00  E-value: 7.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGrlfaLEFARRRATLVLWDI---NRqsNEETAEMAREiyrQLKpSTGSSDRVQELpllqpkvytymcDV 114
Cdd:cd05324   2 VALVTGANRGIG----FEIVRQLAKSGPGTViltAR--DVERGQAAVE---KLR-AEGLSVRFHQL------------DV 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPD-ELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:cd05324  60 TDDASIEAAADFVEEKYGGLDILVNNAGIAFKGFDDSTPTrEQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSG 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41152209 194 LGLFTTAgvedYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM 245
Cdd:cd05324 140 LGSLTSA----YGVSKAALNALTRILAKELK---ETGIKVNACCPGWVKTDM 184
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
33-247 2.41e-24

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: 99.39  E-value: 2.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEEtaeMAREIyrqlkPSTGSSDRVqelpllqpkvytymc 112
Cdd:cd05345   2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAER---VAADI-----GEAAIAIQA--------------- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVV-SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:cd05345  59 DVTKRADVEAMVEAALSKFGRLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIA 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209 192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFE 247
Cdd:cd05345 139 STAGLRPRPGLTWYNASKGWVVTATKAMAVELAPR---NIRVNCLCPVAGETPLLS 191
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
40-243 2.50e-24

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: 99.28  E-value: 2.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  40 VITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAREIyrqlkpstgssDRVQELPL-----LQPKVYTYMCDV 114
Cdd:cd05346   4 LITGASSGIGEATARRFAKAGAKLIL-------------TGRRA-----------ERLQELADelgakFPVKVLPLQLDV 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSG-RHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:cd05346  60 SDRESIEAALENLPEEFRDIDILVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSI 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDT 243
Cdd:cd05346 140 AGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGT---GIRVTNIEPGLVET 186
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
36-227 3.01e-24

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: 99.00  E-value: 3.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVL-------WDIN-----RQSNEETAEMAREIyrqlkpstgssdRVQELPLl 103
Cdd:cd05338   3 GKVAFVTGASRGIGRAIALRLAKAGATVVVaaktaseGDNGsakslPGTIEETAEEIEAA------------GGQALPI- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 104 qpkvytyMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN 183
Cdd:cd05338  70 -------VVDVRDEDQVRALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAG 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 41152209 184 HGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAD 227
Cdd:cd05338 143 QGHILNISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHG 186
PRK12829 PRK12829
short chain dehydrogenase; Provisional
27-277 3.12e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 99.36  E-value: 3.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   27 IRPREKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETaemareiyrqlkpstgssdrVQELPllQPK 106
Cdd:PRK12829   2 AIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAAT--------------------AARLP--GAK 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  107 VYTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGvVSGRH--LLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH 184
Cdd:PRK12829  60 VTATVADVADPAQVERVFDTAVERFGGLDVLVNNAG-IAGPTggIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGH 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  185 G-HIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGC--KIRKEMAPFFPP 261
Cdd:PRK12829 139 GgVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELG---PLGIRVNAILPGIVRGPRMRRVieARAQQLGIGLDE 215
                        250
                 ....*....|....*.
gi 41152209  262 LKPEYCVKQAMRAILT 277
Cdd:PRK12829 216 MEQEYLEKISLGRMVE 231
PRK12828 PRK12828
short chain dehydrogenase; Provisional
31-255 3.82e-24

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 98.72  E-value: 3.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   31 EKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsneetaemAREIYRQLKPSTGSSDRVQELpllqpkvyty 110
Cdd:PRK12828   2 EHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRG----------AAPLSQTLPGVPADALRIGGI---------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  111 mcDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTV 190
Cdd:PRK12828  62 --DLVDPQAARRAVDEVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNI 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaaDKdGIKMTLVCPFLVDTGMfegckIRKEM 255
Cdd:PRK12828 140 GAGAALKAGPGMGAYAAAKAGVARLTEALAAELL--DR-GITVNAVLPSIIDTPP-----NRADM 196
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
36-247 5.45e-24

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: 98.67  E-value: 5.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDInRQSNEETAEMAREIYRQlkpstgssdrvqelpllQPKVYTYMCDVS 115
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGF-GDAAEIEAVRAGLAAKH-----------------GVKVLYHGADLS 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:cd08940  64 KPAAIEDMVAYAQRQFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHG 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41152209 196 LFTTAGVEDYCASKFGAIGFHESLSheLKAADKdGIKMTLVCPFLVDTGMFE 247
Cdd:cd08940 144 LVASANKSAYVAAKHGVVGLTKVVA--LETAGT-GVTCNAICPGWVLTPLVE 192
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
33-266 6.73e-24

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 98.16  E-value: 6.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDInrqsneetaemAREIYRQLKPSTGSSDRVQELPLLQPKVYTYMC 112
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDL-----------GGDRKGSGKSSSAADKVVDEIKAAGGKAVANYD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKvrsEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd05353  71 SVEDGEKIVKTAID---AFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSS 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPfLVDTGMFEGCkirkeMAP-FFPPLKPEY 266
Cdd:cd05353 148 AAGLYGNFGQANYSAAKLGLLGLSNTLAIEGA---KYNITCNTIAP-AAGSRMTETV-----MPEdLFDALKPEY 213
PRK07201 PRK07201
SDR family oxidoreductase;
26-285 7.40e-24

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 102.34  E-value: 7.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   26 FIRPREK-SVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRQSnEETAEMAREIyrqlkPSTGSsdrvqelpllq 104
Cdd:PRK07201 360 ARRRDLRgPLVGKVVLITGASSGIGRATAIKVAEAGATVFL--VARNG-EALDELVAEI-----RAKGG----------- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  105 pKVYTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDEL--IERTMMVNCHAHFWTTKAFLPKMLEL 182
Cdd:PRK07201 421 -TAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVNNAGRSIRRSVENSTDRFhdYERTMAVNYFGAVRLILGLLPHMRER 499
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  183 NHGHIVTVaSSLGLFTTAG-VEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMFEGCKIRKEmapfFPP 261
Cdd:PRK07201 500 RFGHVVNV-SSIGVQTNAPrFSAYVASKAALDAFSDVAASETLS---DGITFTTIHMPLVRTPMIAPTKRYNN----VPT 571
                        250       260
                 ....*....|....*....|....
gi 41152209  262 LKPEYCVKQAMRAILTDQPMICTP 285
Cdd:PRK07201 572 ISPEEAADMVVRAIVEKPKRIDTP 595
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
34-243 1.11e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 97.65  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpsTGssdrvqelpllqPKVYTYMCD 113
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQK--------AG------------GKAIGVAMD 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:PRK12429  62 VTDEEAINAGIDYAVETFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASV 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 41152209  194 LGLFTTAGVEDYCASKFGAIGFHESLSHElkaADKDGIKMTLVCPFLVDT 243
Cdd:PRK12429 142 HGLVGSAGKAAYVSAKHGLIGLTKVVALE---GATHGVTVNAICPGYVDT 188
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
35-248 2.71e-23

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 96.63  E-value: 2.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqelpLLQPKVYTYMCDV 114
Cdd:PRK07067   5 QGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAAL-----------------------EIGPAAIAVSLDV 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHG-HIVTVASS 193
Cdd:PRK07067  62 TRQDSIDRIVAAAVERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQ 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEG 248
Cdd:PRK07067 142 AGRRGEALVSHYCATKAAVISYTQSAALALI---RHGINVNAIAPGVVDTPMWDQ 193
PRK08264 PRK08264
SDR family oxidoreductase;
33-282 3.32e-23

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 96.11  E-value: 3.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRAtlvlwdinrqsneetaemaREIY---RQLKPSTGSSDRVQELPLlqpkvyt 109
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGA-------------------AKVYaaaRDPESVTDLGPRVVPLQL------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  110 ymcDVSKRESVYLTAEKVrsevGDIDLLINNAGVVS-GRHLLDCPDELIERTMMVNCHAHFWTTKAFLPkMLELN-HGHI 187
Cdd:PRK08264  57 ---DVTDPASVAAAAEAA----SDVTILVNNAGIFRtGSLLLEGDEDALRAEMETNYFGPLAMARAFAP-VLAANgGGAI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  188 VTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTgmfegckirkEMAPFFPPLK--PE 265
Cdd:PRK08264 129 VNVLSVLSWVNFPNLGTYSASKAAAWSLTQALRAELAP---QGTRVLGVHPGPIDT----------DMAAGLDAPKasPA 195
                        250
                 ....*....|....*..
gi 41152209  266 YCVKQAMRAILTDQPMI 282
Cdd:PRK08264 196 DVARQILDALEAGDEEV 212
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-254 6.13e-23

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 95.62  E-value: 6.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREIyrqlkpstgssdrvqelpllqpKVYTYMCDV 114
Cdd:PRK06463   6 KGKVALITGGTRGIGRAIAEAFLREGAKVA---VLYNSAENEAKELREK----------------------GVFTIKCDV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:PRK06463  61 GNRDQVKKSKEVVEKEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNA 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209  195 GLFTTA-GVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCKIRKE 254
Cdd:PRK06463 141 GIGTAAeGTTFYAITKAGIIILTRRLAFELG---KYGIRVNAVAPGWVETDMTLSGKSQEE 198
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
34-264 1.15e-22

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: 94.86  E-value: 1.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEEtaeMAREIyrqlkPSTGSSDRVqelpllqpkvytymcD 113
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQA---VVAQI-----AGGALALRV---------------D 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRH-LLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd08944  58 VTDEQQVAALFERAVEEFGGLDLLVNNAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSS 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMfegckIRKEMAPFFPPLKP 264
Cdd:cd08944 138 IAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHA---GIRCNALAPGLIDTPL-----LLAKLAGFEGALGP 201
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
36-287 1.19e-22

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 94.84  E-value: 1.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEF----------ARRRATLvlwdinrqsneetAEMAREIyrqlkpstgssdrvqelpllqP 105
Cdd:COG3967   5 GNTILITGGTSGIGLALAKRLhargntviitGRREEKL-------------EEAAAAN---------------------P 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 106 KVYTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDEL--IERTMMVNCHAHFWTTKAFLPKMLELN 183
Cdd:COG3967  51 GLHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIMRAEDLLDEAEDLadAEREITTNLLGPIRLTAAFLPHLKAQP 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 184 HGHIVTVASSLGL--FTTAGVedYCASKfGAIGFH-ESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKIRKEMAPffp 260
Cdd:COG3967 131 EAAIVNVSSGLAFvpLAVTPT--YSATK-AALHSYtQSLRHQLKDT---SVKVIELAPPAVDTDLTGGQGGDPRAMP--- 201
                       250       260
                ....*....|....*....|....*..
gi 41152209 261 plkPEYCVKQAMRAILTDQPMICTPRV 287
Cdd:COG3967 202 ---LDEFADEVMAGLETGKYEILVGRV 225
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
36-244 1.42e-22

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: 94.65  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrQLKPSTGSSDRVQelpllqpkvytymCDVS 115
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAAS-------ELRAGGAGVLAVV-------------ADLT 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:cd05344  61 DPEDIDRLVEKAGDAFGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTV 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41152209 196 L-----FTTAGVedycaSKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTG 244
Cdd:cd05344 141 KepepnLVLSNV-----ARAGLIGLVKTLSRELA---PDGVTVNSVLPGYIDTE 186
PRK06180 PRK06180
short chain dehydrogenase; Provisional
35-238 1.66e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 94.98  E-value: 1.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLwdinrqsneeTA--EMAREIYRQLKPstgssDRVqeLPLLqpkvytymC 112
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVG----------TVrsEAARADFEALHP-----DRA--LARL--------L 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK06180  58 DVTDFDAIDAVVADAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITS 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCP 238
Cdd:PRK06180 138 MGGLITMPGIGYYCGSKFALEGISESLAKEVAPF---GIHVTAVEP 180
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
33-260 2.03e-22

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: 94.32  E-value: 2.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrQLKPSTGSsdrvqelpllqpKVYTYMC 112
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAE-------ELAKKYGV------------KTKAYKC 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd05352  66 DVSSQESVEKTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITAS 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209 193 SLGlfTTAGVED----YCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM--FEGCKIRKEMAPFFP 260
Cdd:cd05352 146 MSG--TIVNRPQpqaaYNASKAAVIHLAKSLAVEWA---KYFIRVNSISPGYIDTDLtdFVDKELRKKWESYIP 214
PRK06914 PRK06914
SDR family oxidoreductase;
35-238 2.19e-22

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 94.71  E-value: 2.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLvlwdINRQSNEETAEMAREIYRQLKPSTgsSDRVQELpllqpkvytymcDV 114
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLV----IATMRNPEKQENLLSQATQLNLQQ--NIKVQQL------------DV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYlTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:PRK06914  64 TDQNSIH-NFQLVLKEIGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSIS 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCP 238
Cdd:PRK06914 143 GRVGFPGLSPYVSSKYALEGFSESLRLELKPF---GIDVALIEP 183
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
32-294 3.80e-22

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: 93.22  E-value: 3.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsNEETAEMAREIyrqlkpstGSSDRVQELpllqpkvytym 111
Cdd:cd05341   1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDIL---DEEGQAAAAEL--------GDAARFFHL----------- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 112 cDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:cd05341  59 -DVTDEDGWTAVVDTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELkAADKDGIKMTLVCPFLVDTGMFEGCKIRKEmAPFFPPLKPeycvkqA 271
Cdd:cd05341 138 SIEGLVGDPALAAYNASKGAVRGLTKSAALEC-ATQGYGIRVNSVHPGYIYTPMTDELLIAQG-EMGNYPNTP------M 209
                       250       260
                ....*....|....*....|...
gi 41152209 272 MRAiltDQPMictpRVMYMVTFM 294
Cdd:cd05341 210 GRA---GEPD----EIAYAVVYL 225
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
33-211 4.81e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 93.59  E-value: 4.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsnEETAEMAREIYRQLKPstgssdrvqelpllqpKVYTYMC 112
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDIN----QELVDKGLAAYRELGI----------------EAHGYVC 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK07097  67 DVTDEDGVQAMVSQIEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICS 146
                        170
                 ....*....|....*....
gi 41152209  193 SLGLFTTAGVEDYCASKFG 211
Cdd:PRK07097 147 MMSELGRETVSAYAAAKGG 165
PRK09291 PRK09291
SDR family oxidoreductase;
41-247 8.90e-22

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 92.75  E-value: 8.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   41 ITGAGSGLGRLFALEFARRR----ATLVLWDinrQSNEETAEMAREiyrqlkpstGSSDRVQELPLLQPkvytymcdvsk 116
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGhnviAGVQIAP---QVTALRAEAARR---------GLALRVEKLDLTDA----------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  117 resvyltAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:PRK09291  64 -------IDRAQAAEWDVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGL 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  197 FTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTG----MFE 247
Cdd:PRK09291 137 ITGPFTGAYCASKHALEAIAEAMHAELKPF---GIQVATVNPGPYLTGfndtMAE 188
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
29-248 1.82e-21

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 95.30  E-value: 1.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   29 PREKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAreiyrqlkpstGSSDRVQELPllqpkvy 108
Cdd:PRK08324 415 PKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAEL-----------GGPDRALGVA------- 476
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  109 tymCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHI 187
Cdd:PRK08324 477 ---CDVTDEAAVQAAFEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSI 553
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  188 VTVASSLGLFTTAGVEDYCASKFGAIgfheSLSHELkAAD--KDGIKMTLVCPFLV--DTGMFEG 248
Cdd:PRK08324 554 VFIASKNAVNPGPNFGAYGAAKAAEL----HLVRQL-ALElgPDGIRVNGVNPDAVvrGSGIWTG 613
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
34-248 1.97e-21

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 91.53  E-value: 1.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqelpLLQPKVYTYMCD 113
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAA-----------------------EIGPAACAISLD 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVAS 192
Cdd:cd05363  58 VTDQASIDRCVAALVDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRgGKIINMAS 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEG 248
Cdd:cd05363 138 QAGRRGEALVGVYCATKAAVISLTQSAGLNLI---RHGINVNAIAPGVVDGEHWDG 190
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
36-279 2.01e-21

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: 91.90  E-value: 2.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsNEETAEMAR-EIYRQLKPStgssdrvqelpllqpKVYTYMCDV 114
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVII--ACR--NEEKGEEAAaEIKKETGNA---------------KVEVIQLDL 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDcpDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:cd05327  62 SSLASVRQFAEEFLARFPRLDILINNAGIMAPPRRLT--KDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIA 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 195 GLFTTAGVED--------------YCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCKIRKEMAPFFP 260
Cdd:cd05327 140 HRAGPIDFNDldlennkeyspykaYGQSKLANILFTRELARRLE---GTGVTVNALHPGVVRTELLRRNGSFFLLYKLLR 216
                       250       260
                ....*....|....*....|..
gi 41152209 261 PLK---PEYCVKQAMRAILTDQ 279
Cdd:cd05327 217 PFLkksPEQGAQTALYAATSPE 238
PRK07024 PRK07024
SDR family oxidoreductase;
40-275 3.60e-21

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 90.76  E-value: 3.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   40 VITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAR--EIYRQLkpstgssdrVQELPLLqPKVYTYMCDVSKR 117
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGL-------------VARrtDALQAF---------AARLPKA-ARVSVYAADVRDA 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRhLLDCPDEL--IERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:PRK07024  63 DALAAAAADFIAAHGLPDVVIANAGISVGT-LTEEREDLavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  196 LFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCKIRkeMaPFFppLKPEYCVKQAMRAI 275
Cdd:PRK07024 142 VRGLPGAGAYSASKAAAIKYLESLRVELR---PAGVRVVTIAPGYIRTPMTAHNPYP--M-PFL--MDADRFAARAARAI 213
PRK08267 PRK08267
SDR family oxidoreductase;
41-248 4.57e-21

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 90.77  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   41 ITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyrqlkpstgssdrvQELPllQPKVYTYMCDVSKRESV 120
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALA--------------------AELG--AGNAWTGALDVTDRAAW 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  121 -YLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTT 199
Cdd:PRK08267  64 dAALADFAAATGGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQ 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 41152209  200 AGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEG 248
Cdd:PRK08267 144 PGLAVYSATKFAVRGLTEALDLEWR---RHGIRVADVMPLFVDTAMLDG 189
PRK07774 PRK07774
SDR family oxidoreductase;
35-243 4.65e-21

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 90.57  E-value: 4.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsneetAEMAREIYRQLKPSTGSSDRVQelpllqpkvytymCDV 114
Cdd:PRK07774   5 DDKVAIVTGAAGGIGQAYAEALAREGASVVVADIN-------AEGAERVAKQIVADGGTAIAVQ-------------VDV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRH---LLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTvA 191
Cdd:PRK07774  65 SDPDSAKAMADATVSAFGGIDYLVNNAAIYGGMKldlLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVN-Q 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41152209  192 SSLGLFTTAGVedYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDT 243
Cdd:PRK07774 144 SSTAAWLYSNF--YGLAKVGLNGLTQQLARELGGM---NIRVNAIAPGPIDT 190
PRK06139 PRK06139
SDR family oxidoreductase;
30-243 5.24e-21

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 91.71  E-value: 5.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   30 REKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpstgssdrvqelplLQPKVYT 109
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRA--------------------LGAEVLV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  110 YMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVT 189
Cdd:PRK06139  61 VPTDVTDADQVKALATQAASFGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFIN 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  190 VASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkaADKDGIKMTLVCPFLVDT 243
Cdd:PRK06139 141 MISLGGFAAQPYAAAYSASKFGLRGFSEALRGEL--ADHPDIHVCDVYPAFMDT 192
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
35-248 5.99e-21

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 90.17  E-value: 5.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsnEETAEMAREiyrQLKPSTGSSDRVQelpllqpkvytymCDV 114
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYN----EETAQAAAD---KLSKDGGKAIAVK-------------ADV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVASS 193
Cdd:PRK08643  61 SDRDQVFAAVRQVVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQ 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEG 248
Cdd:PRK08643 141 AGVVGNPELAVYSSTKFAVRGLTQTAARDLA---SEGITVNAYAPGIVKTPMMFD 192
PRK05866 PRK05866
SDR family oxidoreductase;
28-304 9.72e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 90.57  E-value: 9.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   28 RPREKSVE--GQVCVITGAGSGLGRLFALEFARRRATLVLwdINRQSnEETAEMAREIyrqlkpsTGSSDRVQELPllqp 105
Cdd:PRK05866  30 RPPRQPVDltGKRILLTGASSGIGEAAAEQFARRGATVVA--VARRE-DLLDAVADRI-------TRAGGDAMAVP---- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  106 kvytymCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDEL--IERTMMVNCHAHFWTTKAFLPKMLELN 183
Cdd:PRK05866  96 ------CDLSDLDAVDALVADVEKRIGGVDILINNAGRSIRRPLAESLDRWhdVERTMVLNYYAPLRLIRGLAPGMLERG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  184 HGHIVTVAsSLGLFTTA----GVedYCASKFGAIGFHESLSHELkaADKdGIKMTLVCPFLVDTGMFEGCKIRKEMapff 259
Cdd:PRK05866 170 DGHIINVA-TWGVLSEAsplfSV--YNASKAALSAVSRVIETEW--GDR-GVHSTTLYYPLVATPMIAPTKAYDGL---- 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 41152209  260 PPLKPEYCVKQAMRAILTdQPMICTPRVMYMVTFMKTVLP--FDAIV 304
Cdd:PRK05866 240 PALTADEAAEWMVTAART-RPVRIAPRVAVAARALDSVAPraVNALM 285
PRK06484 PRK06484
short chain dehydrogenase; Validated
35-245 1.40e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 92.22  E-value: 1.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMareiyrqlkpstgssdrvqelplLQPKVYTYMCDV 114
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADS-----------------------LGPDHHALAMDV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVV--SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGH-IVTVA 191
Cdd:PRK06484  61 SDEAQIREGFEQLHREFGRIDVLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVA 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGM 245
Cdd:PRK06484 141 SGAGLVALPKRTAYSASKAAVISLTRSLACEWAA---KGIRVNAVLPGYVRTQM 191
PRK07063 PRK07063
SDR family oxidoreductase;
35-243 2.40e-20

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 88.57  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpsTGSSDRVQELPllqpkvytymCDV 114
Cdd:PRK07063   6 AGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIAR--------DVAGARVLAVP----------ADV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:PRK07063  68 TDAASVAAAVAAAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTH 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDT 243
Cdd:PRK07063 148 AFKIIPGCFPYPVAKHGLLGLTRALGIEYAA---RNVRVNAIAPGYIET 193
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-256 2.56e-20

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 88.10  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDInrqsneetaemareiyrqlkpstgssdrvQELPLLQPKVYTYMCDV 114
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVYGVDK-----------------------------QDKPDLSGNFHFLQLDL 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKresvylTAEKVRSEVGDIDLLINNAGVVSG-RHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:PRK06550  55 SD------DLEPLFDWVPSVDILCNTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSI 128
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152209  194 LGLFTTAGVEDYCASKFGAIGFHESLshelkAAD--KDGIKMTLVCPFLVDTGM----FEGCKIRKEMA 256
Cdd:PRK06550 129 ASFVAGGGGAAYTASKHALAGFTKQL-----ALDyaKDGIQVFGIAPGAVKTPMtaadFEPGGLADWVA 192
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
36-251 4.20e-20

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: 87.83  E-value: 4.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAReiyrqlkpstgssdrvqelplLQPKVYTYMCDVS 115
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ---------------------GGPRALGVQCDVT 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN-HGHIVTVASSL 194
Cdd:cd08943  60 SEAQVQSAFEQAVLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKN 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209 195 GLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPflvdTGMFEGCKI 251
Cdd:cd08943 140 AVAPGPNAAAYSAAKAAEAHLARCLALEGG---EDGIRVNTVNP----DAVFRGSKI 189
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
36-245 5.22e-20

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: 87.51  E-value: 5.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyRQLKPSTGSsdrvqelpllqpkvYTYmCDVS 115
Cdd:cd05326   4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVA-------AELGDPDIS--------------FVH-CDVT 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSG--RHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:cd05326  62 VEADVRAAVDTAVARFGRLDIMFNNAGVLGApcYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASV 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:cd05326 142 AGVVGGLGPHAYTASKHAVLGLTRSAATELGEH---GIRVNCVSPYGVATPL 190
PRK08263 PRK08263
short chain dehydrogenase; Provisional
36-265 5.71e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 88.17  E-value: 5.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFAlEFARRRATLVlwdinrqsneetAEMAREIYRQLKPSTGSSDRVQELPLlqpkvytymcDVS 115
Cdd:PRK08263   3 EKVWFITGASRGFGRAWT-EAALERGDRV------------VATARDTATLADLAEKYGDRLLPLAL----------DVT 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:PRK08263  60 DRAAVFAAVETAVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGG 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  196 LFTTAGVEDYCASKFGAIGFHESLSHElkaADKDGIKMTLVCPFLVDTGMFEGCKIRKEMAPFFPPLKPE 265
Cdd:PRK08263 140 ISAFPMSGIYHASKWALEGMSEALAQE---VAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREE 206
PRK09072 PRK09072
SDR family oxidoreductase;
35-245 1.17e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 86.92  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRQSNEETAEMAREIYrqlkpstgsSDRVQelpllqpKVYTYMCDV 114
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLL--VGRNAEKLEALAARLPY---------PGRHR-------WVVADLTSE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEkvrsEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:PRK09072  66 AGREAVLARAR----EMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTF 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:PRK09072 142 GSIGYPGYASYCASKFALRGFSEALRRELADT---GVRVLYLAPRATRTAM 189
PRK08589 PRK08589
SDR family oxidoreductase;
32-243 1.23e-19

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 87.14  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSnEETAEmareiyrQLKPSTGSSDrvqelpllqpkvyTYM 111
Cdd:PRK08589   2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAV-SETVD-------KIKSNGGKAK-------------AYH 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGV-VSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElNHGHIVTV 190
Cdd:PRK08589  61 VDISDEQQVKDFASEIKEQFGRVDVLFNNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINT 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDT 243
Cdd:PRK08589 140 SSFSGQAADLYRSGYNAAKGAVINFTKSIAIEYG---RDGIRANAIAPGTIET 189
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
35-270 1.41e-19

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 86.63  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQlkpstgssdrvqelpllqPKVYTYMCDV 114
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGE------------------GMAYGFGADA 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVASS 193
Cdd:PRK12384  63 TSEQSVLALSRGVDEIFGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIqGRIIQINSK 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152209  194 LGLFTTAGVEDYCASKFGAIGFHESLSHELkaADkDGIKMTLVCP-FLVDTGMFEGckirkemapffppLKPEYCVKQ 270
Cdd:PRK12384 143 SGKVGSKHNSGYSAAKFGGVGLTQSLALDL--AE-YGITVHSLMLgNLLKSPMFQS-------------LLPQYAKKL 204
PRK07454 PRK07454
SDR family oxidoreductase;
41-247 3.97e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 85.01  E-value: 3.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   41 ITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAReiyrqlkpSTGSsdrvqelpllqpKVYTYMCDVSKRESV 120
Cdd:PRK07454  11 ITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELR--------STGV------------KAAAYSIDLSNPEAI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  121 YLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTTA 200
Cdd:PRK07454  71 APGIAELLEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFP 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 41152209  201 GVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMFE 247
Cdd:PRK07454 151 QWGAYCVSKAALAAFTKCLAEEERS---HGIRVCTITLGAVNTPLWD 194
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-250 3.97e-19

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 85.01  E-value: 3.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETaemareiyrqlkpstgssdrVQELPLLQPKVYTYMCDV 114
Cdd:PRK08217   4 KDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEA--------------------VAECGALGTEVRGYAANV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMM---------VNCHAHFWTTKAFLPKMLEL-NH 184
Cdd:PRK08217  64 TDEEDVEATFAQIAEDFGQLNGLINNAGILRDGLLVKAKDGKVTSKMSleqfqsvidVNLTGVFLCGREAAAKMIESgSK 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209  185 GHIVTVaSSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCK 250
Cdd:PRK08217 144 GVIINI-SSIARAGNMGQTNYSASKAGVAAMTVTWAKELA---RYGIRVAAIAPGVIETEMTAAMK 205
PRK08219 PRK08219
SDR family oxidoreductase;
38-245 5.14e-19

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 84.21  E-value: 5.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   38 VCVITGAGSGLGRLFALEFARRRaTLVLwdinrqsneetaeMAReiyrqlkpstgSSDRVQELPLLQPKVYTYMCDVSKR 117
Cdd:PRK08219   5 TALITGASRGIGAAIARELAPTH-TLLL-------------GGR-----------PAERLDELAAELPGATPFPVDLTDP 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  118 ESVyltaEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKmLELNHGHIVTVASSLGLF 197
Cdd:PRK08219  60 EAI----AAAVEQLGRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPA-LRAAHGHVVFINSGAGLR 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 41152209  198 TTAGVEDYCASKFGAIGFHESLSHElkaaDKDGIKMTLVCPFLVDTGM 245
Cdd:PRK08219 135 ANPGWGSYAASKFALRALADALREE----EPGNVRVTSVHPGRTDTDM 178
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
37-294 9.73e-19

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 84.11  E-value: 9.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  37 QVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyrqlkpstgssdrvQELPLLQP--KVYTYMCDV 114
Cdd:cd05330   4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAK--------------------AALLEIAPdaEVLLIKADV 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGvVSGRHLL--DCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd05330  64 SDEAQVEAYVDATVEQFGRIDGFFNNAG-IEGKQNLteDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTAS 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCPFLVDTGMFEGCkiRKEMAPFFPplkpeycvKQAM 272
Cdd:cd05330 143 VGGIRGVGNQSGYAAAKHGVVGLTRNSAVEY---GQYGIRINAIAPGAILTPMVEGS--LKQLGPENP--------EEAG 209
                       250       260
                ....*....|....*....|....*
gi 41152209 273 RAILTDQPMIC---TPRVMYMVTFM 294
Cdd:cd05330 210 EEFVSVNPMKRfgePEEVAAVVAFL 234
PRK07326 PRK07326
SDR family oxidoreductase;
33-248 1.30e-18

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 83.52  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREIyrqlkpstGSSDRVQELPllqpkvytymC 112
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVA---ITARDQKELEEAAAEL--------NNKGNVLGLA----------A 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElNHGHIVTVAS 192
Cdd:PRK07326  62 DVRDEADVQRAVDAIVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKR-GGGYIINISS 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGmFEG 248
Cdd:PRK07326 141 LAGTNFFAGGAAYNASKFGLVGFSEAAMLDLR---QYGIKVSTIMPGSVATH-FNG 192
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
33-245 2.16e-18

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 83.52  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEEtaemareiyrqlkpstgssdrvqelpllqPKVYTYMC 112
Cdd:PRK06171   6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH-----------------------------ENYQFVPT 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPD-----ELIERT----MMVNCHAHFWTTKAFLPKMLELN 183
Cdd:PRK06171  57 DVSSAEEVNHTVAEIIEKFGRIDGLVNNAGINIPRLLVDEKDpagkyELNEAAfdkmFNINQKGVFLMSQAVARQMVKQH 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152209  184 HGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCPFLVD-TGM 245
Cdd:PRK06171 137 DGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKEL---GKHNIRVVGVAPGILEaTGL 196
PRK07074 PRK07074
SDR family oxidoreductase;
37-247 2.35e-18

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 83.28  E-value: 2.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyRQLkpstgSSDRVQELPllqpkvytymCDVSK 116
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFA-------DAL-----GDARFVPVA----------CDLTD 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:PRK07074  61 AASLAAALANAAAERGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGM 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41152209  197 fTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCPFLVDTGMFE 247
Cdd:PRK07074 141 -AALGHPAYSAAKAGLIHYTKLLAVEY---GRFGIRANAVAPGTVKTQAWE 187
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
33-247 2.48e-18

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 82.85  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEmarEIYRQLKPSTGSSDRVqelpllqpkvytyMC 112
Cdd:PRK06077   3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVV---VNAKKRAEEMN---ETLKMVKENGGEGIGV-------------LA 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnHGHIVTVAS 192
Cdd:PRK06077  64 DVSTREGCETLAKATIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMRE--GGAIVNIAS 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdgIKMTLVCPFLVDTGMFE 247
Cdd:PRK06077 142 VAGIRPAYGLSIYGAMKAAVINLTKYLALELAPK----IRVNAIAPGFVKTKLGE 192
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
35-244 2.90e-18

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: 82.84  E-value: 2.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQLKPstgssdrvqelPLLQPkvytymCDV 114
Cdd:cd05364   2 SGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKK-----------ILLVV------ADL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElNHGHIVTVASSL 194
Cdd:cd05364  65 TEEEGQDRIISTTLAKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIK-TKGEIVNVSSVA 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41152209 195 GLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTG 244
Cdd:cd05364 144 GGRSFPGVLYYCISKAALDQFTRCTALELA---PKGVRVNSVSPGVIVTG 190
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
36-265 3.32e-18

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


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 82.56  E-value: 3.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVlwdinrqSNEETAEMAREIYRQLKpSTGSsdrvqelpllqPKVYTYMCDVS 115
Cdd:cd05343   6 GRVALVTGASVGIGAAVARALVQHGMKVV-------GCARRVDKIEALAAECQ-SAGY-----------PTLFPYQCDLS 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN--HGHIVTVASS 193
Cdd:cd05343  67 NEEQILSMFSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSM 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 194 LG----LFTTAGVedYCASKFGAIGFHESLSHELKAAdKDGIKMTLVCPFLVDTGMFEGC-----KIRKEMAPFFPPLKP 264
Cdd:cd05343 147 SGhrvpPVSVFHF--YAATKHAVTALTEGLRQELREA-KTHIRATSISPGLVETEFAFKLhdndpEKAAATYESIPCLKP 223

                .
gi 41152209 265 E 265
Cdd:cd05343 224 E 224
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
35-245 5.50e-18

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 81.85  E-value: 5.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyrqlkpstgssdrvqelpllqpkVYTYMCDV 114
Cdd:PRK08220   7 SGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP-----------------------------FATFVLDV 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:PRK08220  58 SDAAAVAQVCQRLLAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNA 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:PRK08220 138 AHVPRIGMAAYGASKAALTSLAKCVGLELAPY---GVRCNVVSPGSTDTDM 185
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
40-248 6.34e-18

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: 81.40  E-value: 6.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  40 VITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAREiyrqlkpstgsSDRVQEL-PLLQPKVYTYMCDVSKRE 118
Cdd:cd08929   4 LVTGASRGIGEATARLLHAEGYRVGI-------------CARD-----------EARLAAAaAQELEGVLGLAGDVRDEA 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 119 SVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFT 198
Cdd:cd08929  60 DVRRAVDAMEEAFGGLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNA 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41152209 199 TAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGmFEG 248
Cdd:cd08929 140 FKGGAAYNASKFGLLGLSEAAMLDLR---EANIRVVNVMPGSVDTG-FAG 185
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
78-245 8.77e-18

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 81.50  E-value: 8.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   78 EMAREIYRQLKPSTGSSDRVQELPLLQP----KVYTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCP 153
Cdd:PRK12936  21 EIARLLHAQGAIVGLHGTRVEKLEALAAelgeRVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGITKDGLFVRMS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  154 DELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAADkdgIKM 233
Cdd:PRK12936 101 DEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLAQEIATRN---VTV 177
                        170
                 ....*....|..
gi 41152209  234 TLVCPFLVDTGM 245
Cdd:PRK12936 178 NCVAPGFIESAM 189
PRK06398 PRK06398
aldose dehydrogenase; Validated
36-247 1.29e-17

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 81.03  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsneetaemareiyrqlKPSTGSSDRVQelpllqpkvytymCDVS 115
Cdd:PRK06398   6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIK------------------EPSYNDVDYFK-------------VDVS 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:PRK06398  55 NKEQVIKGIDYVISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQS 134
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41152209  196 LFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdgIKMTLVCPFLVDTGMFE 247
Cdd:PRK06398 135 FAVTRNAAAYVTSKHAVLGLTRSIAVDYAPT----IRCVAVCPGSIRTPLLE 182
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
28-238 2.03e-17

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 81.37  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   28 RPREKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDInrQSNEETAEMAREIyrqlkPSTGSsdrvqelpllqpKV 107
Cdd:PRK07792   4 TTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDV--ASALDASDVLDEI-----RAAGA------------KA 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  108 YTYMCDVSKREsvylTA-EKVRS--EVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKA----FLPKML 180
Cdd:PRK07792  65 VAVAGDISQRA----TAdELVATavGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNaaayWRAKAK 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209  181 ELN---HGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLShelKAADKDGIKMTLVCP 238
Cdd:PRK07792 141 AAGgpvYGRIVNTSSEAGLVGPVGQANYGAAKAGITALTLSAA---RALGRYGVRANAICP 198
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
41-248 2.15e-17

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 79.80  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  41 ITGAGSGLGRLFALEFARRRATLVLWDINrqsneetAEMAREIYRQLKPSTGSSDRVqelpllqpkvytymcDVSKRESV 120
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDID-------EDGLAALAAELGAENVVAGAL---------------DVTDRAAW 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 121 YLT-AEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTT 199
Cdd:cd08931  63 AAAlADFAAATGGRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQ 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41152209 200 AGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEG 248
Cdd:cd08931 143 PDLAVYSATKFAVRGLTEALDVEWARH---GIRVADVWPWFVDTPILTK 188
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
41-266 4.69e-17

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


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 80.01  E-value: 4.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  41 ITGAGSGLGRLFALEFARRRATlVLWDINrQSNEETAEMAREIyrqlkpstgSSDRVQELPLlqpkvytymcDVSKRESV 120
Cdd:cd09805   5 ITGCDSGFGNLLAKKLDSLGFT-VLAGCL-TKNGPGAKELRRV---------CSDRLRTLQL----------DVTKPEQI 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 121 YLTAEKVRSEVGDIDL--LINNAGVVsgrhLLDCPDELIERTMMVNCHA-HFW----TTKAFLPkMLELNHGHIVTVASS 193
Cdd:cd09805  64 KRAAQWVKEHVGEKGLwgLVNNAGIL----GFGGDEELLPMDDYRKCMEvNLFgtveVTKAFLP-LLRRAKGRVVNVSSM 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 194 LG---LFTTAGvedYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCPFLVDTGMF----EGCKIRKEMAPFFPP-LKPE 265
Cdd:cd09805 139 GGrvpFPAGGA---YCASKAAVEAFSDSLRREL---QPWGVKVSIIEPGNFKTGITgnseLWEKQAKKLWERLPPeVKKD 212

                .
gi 41152209 266 Y 266
Cdd:cd09805 213 Y 213
PRK06179 PRK06179
short chain dehydrogenase; Provisional
35-247 6.55e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 79.18  E-value: 6.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVlwdinrqsneetaemareiyrqlkpstGSSDRVQELPLLQPkVYTYMCDV 114
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVF---------------------------GTSRNPARAAPIPG-VELLELDV 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGV-VSG----------RHLLDcpdeliertmmVNCHAHFWTTKAFLPKMLELN 183
Cdd:PRK06179  55 TDDASVQAAVDEVIARAGRIDVLVNNAGVgLAGaaeessiaqaQALFD-----------TNVFGILRMTRAVLPHMRAQG 123
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209  184 HGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGmFE 247
Cdd:PRK06179 124 SGRIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHEVRQF---GIRVSLVEPAYTKTN-FD 183
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
35-238 8.13e-17

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: 78.58  E-value: 8.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEmarEIYRQLKPSTGSSDRVQelpllqpkvytymCDV 114
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGANVV---VNYRSKEDAAE---EVVEEIKAVGGKAIAVQ-------------ADV 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN-HGHIVTVASS 193
Cdd:cd05358  63 SKEEDVVALFQSAIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSV 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCP 238
Cdd:cd05358 143 HEKIPWPGHVNYAASKGGVKMMTKTLAQEY--APK-GIRVNAIAP 184
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
33-243 1.15e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 78.40  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpsTGSsdrvqelpllqpKVYTYMC 112
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINK--------AGG------------KAIGVAM 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKML-ELNHGHIVTVA 191
Cdd:PRK13394  64 DVTNEDAVNAGIDKVAERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMG 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41152209  192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHElkaADKDGIKMTLVCPFLVDT 243
Cdd:PRK13394 144 SVHSHEASPLKSAYVTAKHGLLGLARVLAKE---GAKHNVRSHVVCPGFVRT 192
PRK06114 PRK06114
SDR family oxidoreductase;
33-256 2.44e-16

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 77.51  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDinrqsneetaemareiyrqLKPSTGSSDRVQELPLLQPKVYTYMC 112
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFD-------------------LRTDDGLAETAEHIEAAGRRAIQIAA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK06114  66 DVTSKADLRAAVARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIAS 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209  193 SLGLFTTAGVED--YCASKFGAIGFHESLSHELkaADKdGIKMTLVCPFLVDTGMfegcKIRKEMA 256
Cdd:PRK06114 146 MSGIIVNRGLLQahYNASKAGVIHLSKSLAMEW--VGR-GIRVNSISPGYTATPM----NTRPEMV 204
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
35-238 2.45e-16

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: 77.72  E-value: 2.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEEtaEMAREIyRQLKPSTGSSDRVQELPLLQPKvytyMCdv 114
Cdd:cd05355  25 KGKKALITGGDSGIGRAVAIAFAREGADVA---INYLPEEE--DDAEET-KKLIEEEGRKCLLIPGDLGDES----FC-- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 skRESVyltaEKVRSEVGDIDLLINNAGV-VSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnHGHIVTVASS 193
Cdd:cd05355  93 --RDLV----KEVVKEFGKLDILVNNAAYqHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSV 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 41152209 194 LGLFTTAGVEDYCASKfGAI-GFHESLSheLKAADKdGIKMTLVCP 238
Cdd:cd05355 165 TAYKGSPHLLDYAATK-GAIvAFTRGLS--LQLAEK-GIRVNAVAP 206
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
41-281 5.45e-16

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: 76.24  E-value: 5.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  41 ITGAGSGLGRLFALEFARRRATLVlwdIN-RQSNEETAEMAREIYRqlkpSTGSSDRVQelpllqpkvytymCDVSKRES 119
Cdd:cd05359   3 VTGGSRGIGKAIALRLAERGADVV---INyRKSKDAAAEVAAEIEE----LGGKAVVVR-------------ADVSQPQD 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 120 VYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDC-PDELiERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFT 198
Cdd:cd05359  63 VEEMFAAVKERFGRLDVLVSNAAAGAFRPLSELtPAHW-DAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 199 TAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTgmfegckirkEMAPFFP---PLKPEYCVKQAMRAI 275
Cdd:cd05359 142 LPNYLAVGTAKAALEALVRYLAVELGP---RGIRVNAVSPGVIDT----------DALAHFPnreDLLEAAAANTPAGRV 208

                ....*.
gi 41152209 276 LTDQPM 281
Cdd:cd05359 209 GTPQDV 214
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
38-223 5.91e-16

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 75.88  E-value: 5.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAREIYRQLKPstgssdRVQELPLLQPKVYTYMCDVSKR 117
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVAL-------------AARREAKLEAL------LVDIIRDAGGSAKAVPTDARDE 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLF 197
Cdd:cd05373  62 DEVIALFDLIEEEIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLR 141
                       170       180
                ....*....|....*....|....*.
gi 41152209 198 TTAGVEDYCASKFGAIGFHESLSHEL 223
Cdd:cd05373 142 GRAGFAAFAGAKFALRALAQSMAREL 167
PRK07060 PRK07060
short chain dehydrogenase; Provisional
33-245 6.24e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 75.91  E-value: 6.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQsneETAEMAREIyrqlkpstgsSDRVQELpllqpkvytymc 112
Cdd:PRK07060   6 DFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAA---ALDRLAGET----------GCEPLRL------------ 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAekvrSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVA 191
Cdd:PRK07060  61 DVGDDAAIRAAL----AAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVS 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGM 245
Cdd:PRK07060 137 SQAALVGLPDHLAYCASKAALDAITRVLCVELGP---HGIRVNSVNPTVTLTPM 187
PRK12827 PRK12827
short chain dehydrogenase; Provisional
33-245 7.65e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 75.91  E-value: 7.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDIN-RQSNEETAEMAREIyrqlkPSTGSSDRVQELpllqpkvytym 111
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHpMRGRAEADAVAAGI-----EAAGGKALGLAF----------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 cDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTV 190
Cdd:PRK12827  67 -DVRDFAATRAALDAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRgGRIVNI 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCPFLVDTGM 245
Cdd:PRK12827 146 ASVAGVRGNRGQVNYAASKAGLIGLTKTLANEL--APR-GITVNAVAPGAINTPM 197
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
35-238 8.53e-16

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: 75.83  E-value: 8.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEetaemareiyrQLKPSTGSSDRVQELPLlqpkvytyMCDV 114
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALE-----------QLKEELTNLYKNRVIAL--------ELDI 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVS---GRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:cd08930  62 TSKESIKELIESYLEKFGRIDILINNAYPSPkvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIA 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209 192 SSLGLF----------TTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCP 238
Cdd:cd08930 142 SIYGVIapdfriyentQMYSPVEYSVIKAGIIHLTKYLAKYY--ADT-GIRVNAISP 195
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
38-245 9.17e-16

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: 75.96  E-value: 9.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAreiyrqlkpstgssdrVQELPLLQPKVYTYMCDVSKR 117
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIA---INDLPDDDQATEV----------------VAEVLAAGRRAIYFQADIGEL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGV-VSGR-HLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLE------LNHGHIVT 189
Cdd:cd05337  64 SDHEALLDQAWEDFGRLDCLVNNAGIaVRPRgDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEqpdrfdGPHRSIIF 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41152209 190 VASSLGLFTTAGVEDYCASKFGAigfheSLSHELKAAD--KDGIKMTLVCPFLVDTGM 245
Cdd:cd05337 144 VTSINAYLVSPNRGEYCISKAGL-----SMATRLLAYRlaDEGIAVHEIRPGLIHTDM 196
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
37-245 1.04e-15

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: 75.65  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  37 QVCVITGAGSGLGrlfaLEFARRRATL---VLwdINRQSNEETAEMAREIYRQLKPSTGSSdrvqelpllqpkvytymCD 113
Cdd:cd08945   4 EVALVTGATSGIG----LAIARRLGKEglrVF--VCARGEEGLATTVKELREAGVEADGRT-----------------CD 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPK--MLELNHGHIVTVA 191
Cdd:cd08945  61 VRSVPEIEALVAAAVARYGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIA 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 41152209 192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM 245
Cdd:cd08945 141 STGGKQGVVHAAPYSASKHGVVGFTKALGLELA---RTGITVNAVCPGFVETPM 191
PRK12937 PRK12937
short chain dehydrogenase; Provisional
36-246 1.24e-15

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 75.16  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNeetAEMAREIYRQLKPSTGSSDRVQelpllqpkvytymCDVS 115
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVA---VNYAGS---AAAADELVAEIEAAGGRAIAVQ-------------ADVA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMleLNHGHIVTVASSLG 195
Cdd:PRK12937  66 DAAAVTRLFDAAETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVI 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41152209  196 LFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMF 246
Cdd:PRK12937 144 ALPLPGYGPYAASKAAVEGLVHVLANELRGR---GITVNAVAPGPVATELF 191
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
34-245 1.92e-15

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: 74.54  E-value: 1.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsneeTAEMAREIYRQLKPSTGSsdrvqelpllQPKVYTYMCD 113
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVIL--LGR-----NEEKLRQVADHINEEGGR----------QPQWFILDLL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRH-LLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd05340  65 TCTSENCQQLAQRIAVNYPRLDGVLHNAGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSS 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAADkdgIKMTLVCPFLVDTGM 245
Cdd:cd05340 145 SVGRQGRANWGAYAVSKFATEGL*QVLADEYQQRN---LRVNCINPGGTRTAM 194
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
33-225 3.18e-15

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 74.39  E-value: 3.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVL------WDinrqsneETaemareiyRQLKPSTGSsdrvqelpllqpK 106
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIItthgtnWD-------ET--------RRLIEKEGR------------K 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  107 VYTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGH 186
Cdd:PRK06935  65 VTFVQVDLTKPESAEKVVKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGK 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 41152209  187 IVTVASSL----GLFttagVEDYCASKFGAIGFHESLSHELKA 225
Cdd:PRK06935 145 IINIASMLsfqgGKF----VPAYTASKHGVAGLTKAFANELAA 183
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
34-254 8.09e-15

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: 72.82  E-value: 8.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaEMAREIyrqlkpstGSSDRVQELplLQPKVYTYMCD 113
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVY------------AAVRDP--------GSAAHLVAK--YGDKVVPLRLD 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRsevgDIDLLINNAGVVSGRHLLDCPD-ELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd05354  59 VTDPESIKAAAAQAK----DVDVVINNAGVLKPATLLEEGAlEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNS 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41152209 193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMFEGCKIRKE 254
Cdd:cd05354 135 VASLKNFPAMGTYSASKSAAYSLTQGLRAELAA---QGTLVLSVHPGPIDTRMAAGAGGPKE 193
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
41-245 8.95e-15

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 72.89  E-value: 8.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  41 ITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIyrqlkpstgssdrvqelPLlqpkvytymcDVSKRESV 120
Cdd:cd05331   3 VTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRLT-----------------PL----------DVADAAAV 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 121 YLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTTA 200
Cdd:cd05331  56 REVCSRLLAEHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRI 135
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 41152209 201 GVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:cd05331 136 SMAAYGASKAALASLSKCLGLELAPY---GVRCNVVSPGSTDTAM 177
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
29-224 8.96e-15

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 72.98  E-value: 8.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   29 PREKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsneeTAEMAREIYRQLKPSTGssdrvqelplLQPKVY 108
Cdd:PRK08945   5 PKPDLLKDRIILVTGAGDGIGREAALTYARHGATVIL--LGR-----TEEKLEAVYDEIEAAGG----------PQPAII 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  109 TymCD---VSKRESVYLtAEKVRSEVGDIDLLINNAGVVSGRHLLD-CPDELIERTMMVNCHAHFWTTKAFLPKMLELNH 184
Cdd:PRK08945  68 P--LDlltATPQNYQQL-ADTIEEQFGRLDGVLHNAGLLGELGPMEqQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPA 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 41152209  185 GHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELK 224
Cdd:PRK08945 145 ASLVFTSSSVGRQGRANWGAYAVSKFATEGMMQVLADEYQ 184
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
35-269 9.22e-15

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: 72.88  E-value: 9.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYrqlkpstgssdrvqelpllQPKVYTYMCDV 114
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEY-------------------GEKAYGFGADA 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN-HGHIVTVASS 193
Cdd:cd05322  62 TNEQSVIALSKGVDEIFKRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSK 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209 194 LGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKM-TLVCPFLVDTGMFEGckirkemapffppLKPEYCVK 269
Cdd:cd05322 142 SGKVGSKHNSGYSAAKFGGVGLTQSLALDLA---EHGITVnSLMLGNLLKSPMFQS-------------LLPQYAKK 202
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
35-238 1.21e-14

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: 72.56  E-value: 1.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDInrqsneetAEMAREIYRQLKPSTGssdrvqelpllqpKVYTYMCDV 114
Cdd:cd08937   3 EGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDR--------SELVHEVLAEILAAGD-------------AAHVHTADL 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAG-VVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASs 193
Cdd:cd08937  62 ETYAGAQGVVRAAVERFGRVDVLINNVGgTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSS- 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 41152209 194 lglFTTAGVED--YCASKFGAIGFHESLSHElkaADKDGIKMTLVCP 238
Cdd:cd08937 141 ---IATRGIYRipYSAAKGGVNALTASLAFE---HARDGIRVNAVAP 181
PRK07831 PRK07831
SDR family oxidoreductase;
35-215 1.92e-14

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 71.99  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGA-GSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrQLKPSTGssdrvqelpllQPKVYTYMCD 113
Cdd:PRK07831  16 AGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETAD-------ELAAELG-----------LGRVEAVVCD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVAS 192
Cdd:PRK07831  78 VTSEAQVDALIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHgGVIVNNAS 157
                        170       180
                 ....*....|....*....|...
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGF 215
Cdd:PRK07831 158 VLGWRAQHGQAHYAAAKAGVMAL 180
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
37-247 2.41e-14

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 71.72  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRATLVLwdiNRQSNEETAEMAREIYRQLKpstgssDRVQELPLlqpkvytymcDVSK 116
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIA---TYFSGNDCAKDWFEEYGFTE------DQVRLKEL----------DVTD 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:PRK12824  64 TEECAEALAEIEEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGL 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41152209  197 FTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFE 247
Cdd:PRK12824 144 KGQFGQTNYSAAKAGMIGFTKALASEGA---RYGITVNCIAPGYIATPMVE 191
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
38-263 2.57e-14

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: 71.55  E-value: 2.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEEtaemareiyRQLKPSTGSSDRVQelpllqpkvyTYMCDVSKR 117
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPL---------QELKEELRPGLRVT----------TVKADLSDA 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGV---VSGRHLLDcPDELIeRTMMVNCHAHFWTTKAFLPKMLELN-HGHIVTVASS 193
Cdd:cd05367  62 AGVEQLLEAIRKLDGERDLLINNAGSlgpVSKIEFID-LDELQ-KYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSG 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209 194 LGL--FTTAGVedYCASKFGAIGFHESLSHELKaadkdGIKMTLVCPFLVDTGMFEgcKIRKEMAP-----FFPPLK 263
Cdd:cd05367 140 AAVnpFKGWGL--YCSSKAARDMFFRVLAAEEP-----DVRVLSYAPGVVDTDMQR--EIRETSADpetrsRFRSLK 207
PRK06949 PRK06949
SDR family oxidoreductase;
35-245 4.85e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 70.95  E-value: 4.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLwdiNRQSNEETAEMAREIyrqlkPSTGSSDRVQELpllqpkvytymcDV 114
Cdd:PRK06949   8 EGKVALVTGASSGLGARFAQVLAQAGAKVVL---ASRRVERLKELRAEI-----EAEGGAAHVVSL------------DV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKML--------ELNHGH 186
Cdd:PRK06949  68 TDYQSIKAAVAHAETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIarakgagnTKPGGR 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 41152209  187 IVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCPFLVDTGM 245
Cdd:PRK06949 148 IINIASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEW---GRHGINVNAICPGYIDTEI 203
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
37-245 6.10e-14

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 70.76  E-value: 6.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRatlvlWDINRQSNEETAEMAREIyrqlkpstgssdrvQELPLLQPKVYTYMCDVSK 116
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAG-----FDLAINDRPDDEELAATQ--------------QELRALGVEVIFFPADVAD 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  117 RESVYLTAEKVRSEVGDIDLLINNAGV--VSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGH------IV 188
Cdd:PRK12745  64 LSAHEAMLDAAQAAWGRIDCLVNNAGVgvKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIV 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209  189 TVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:PRK12745 144 FVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAARLAEE---GIGVYEVRPGLIKTDM 197
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
36-248 6.47e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 70.36  E-value: 6.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdINRQSNEetAEMAREiyrqlkpstgssdrvqELPLLQPKVYTYMCDVS 115
Cdd:PRK08213  12 GKTALVTGGSRGLGLQIAEALGEAGARVVL--SARKAEE--LEEAAA----------------HLEALGIDALWIAADVA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPK-MLELNHGHIVTVASSL 194
Cdd:PRK08213  72 DEADIERLAEETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209  195 GL-------FTTAGvedYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEG 248
Cdd:PRK08213 152 GLggnppevMDTIA---YNTSKGAVINFTRALAAEWG---PHGIRVNAIAPGFFPTKMTRG 206
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
33-213 6.49e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 70.55  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsnEETAEMAreiyrqlkpstgssdrVQELPLLQPKVYTYMC 112
Cdd:PRK08085   6 SLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDIT----AERAELA----------------VAKLRQEGIKAHAAPF 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA- 191
Cdd:PRK08085  66 NVTHKQEVEAAIEHIEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICs 145
                        170       180
                 ....*....|....*....|....
gi 41152209  192 --SSLGLFTtagVEDYCASKfGAI 213
Cdd:PRK08085 146 mqSELGRDT---ITPYAASK-GAV 165
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
36-243 8.65e-14

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: 69.92  E-value: 8.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAReiyrqlkpstgssdrvqelpllqPKVYTYMCDVS 115
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEG-----------------------PNLFFVHGDVA 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElNHGHIVTVASSLG 195
Cdd:cd09761  58 DETLVKFVVYAMLEKLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIK-NKGRIINIASTRA 136
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 41152209 196 LFTTAGVEDYCASKFGAIgfheSLSHELKAADKDGIKMTLVCPFLVDT 243
Cdd:cd09761 137 FQSEPDSEAYAASKGGLV----ALTHALAMSLGPDIRVNCISPGWINT 180
PRK06484 PRK06484
short chain dehydrogenase; Validated
29-243 9.15e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 71.80  E-value: 9.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   29 PREKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDinrqSNEETAEMAREIyrqlkpstgssdrvqelplLQPKVY 108
Cdd:PRK06484 262 PSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIID----RDAEGAKKLAEA-------------------LGDEHL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  109 TYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSG-RHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnHGHI 187
Cdd:PRK06484 319 SVQADITDEAAVESAFAQIQARWGRLDVLVNNAGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQ--GGVI 396
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209  188 VTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDT 243
Cdd:PRK06484 397 VNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPA---GIRVNTVAPGYIET 449
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
41-278 1.30e-13

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 68.70  E-value: 1.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  41 ITGAGSGLGRLFALEFARRRATLVLwdINRQSnEETAEMAREIYRQLKPStgssdrvqelpllqpkvytymcDVSKRESV 120
Cdd:cd11730   3 ILGATGGIGRALARALAGRGWRLLL--SGRDA-GALAGLAAEVGALARPA----------------------DVAAELEV 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 121 YLTAEkvrsEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnHGHIVTVASSLGLFTTA 200
Cdd:cd11730  58 WALAQ----ELGPLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAA--GARLVFLGAYPELVMLP 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 201 GVEDYCASKFGAIGFHESLSHELKaadkdGIKMTLVCPFLVDTGMFEgckirkemAPFFPP---LKPEycvkQAMRAILT 277
Cdd:cd11730 132 GLSAYAAAKAALEAYVEVARKEVR-----GLRLTLVRPPAVDTGLWA--------PPGRLPkgaLSPE----DVAAAILE 194

                .
gi 41152209 278 D 278
Cdd:cd11730 195 A 195
PRK05867 PRK05867
SDR family oxidoreductase;
34-247 1.38e-13

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 69.68  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFArrratlvlwdinrQSNEETAEMAREiyrqlkpstgsSDRVQ----ELPLLQPKVYT 109
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYV-------------EAGAQVAIAARH-----------LDALEkladEIGTSGGKVVP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  110 YMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIV 188
Cdd:PRK05867  63 VCCDVSQHQQVTSMLDQVTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQgGVII 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209  189 TVASSLG--LFTTAGVEDYCASKFGAIGFHESLSHELKAADkdgIKMTLVCPFLVDTGMFE 247
Cdd:PRK05867 143 NTASMSGhiINVPQQVSHYCASKAAVIHLTKAMAVELAPHK---IRVNSVSPGYILTELVE 200
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
38-265 1.79e-13

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: 69.41  E-value: 1.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFAR---RRATLVLWDINRQSNEETAEMAREIYrqlkpstgssdrVQELPLLQpkvytymCDV 114
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLKKKGRLWEAAGALA------------GGTLETLQ-------LDV 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSevGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSL 194
Cdd:cd09806  63 CDSKSVAAAVERVTE--RHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVG 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209 195 GLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGmFEGCKIRKEMAPFFPPLKPE 265
Cdd:cd09806 141 GLQGLPFNDVYCASKFALEGLCESLAVQLL---PFNVHLSLIECGPVHTA-FMEKVLGSPEEVLDRTADDI 207
PRK06701 PRK06701
short chain dehydrogenase; Provisional
35-238 2.23e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 69.29  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRA--TLVLWDINRQSNEETAEMAREIYRQLKPSTGSSDRVQelpllqpkvytymC 112
Cdd:PRK06701  45 KGKVALITGGDSGIGRAVAVLFAKEGAdiAIVYLDEHEDANETKQRVEKEGVKCLLIPGDVSDEAF-------------C 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 dvskRESVyltaEKVRSEVGDIDLLINNAGV-VSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMleLNHGHIVTVA 191
Cdd:PRK06701 112 ----KDAV----EETVRELGRLDILVNNAAFqYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTG 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 41152209  192 SSLGLFTTAGVEDYCASKfGAI-GFHESLSHELKaadKDGIKMTLVCP 238
Cdd:PRK06701 182 SITGYEGNETLIDYSATK-GAIhAFTRSLAQSLV---QKGIRVNAVAP 225
PRK06057 PRK06057
short chain dehydrogenase; Provisional
34-243 2.38e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 68.99  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQlkpstgssdrvqelpllqpkvytymCD 113
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLFVP-------------------------TD 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVV--SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:PRK06057  60 VTDEDAVNALFDTAAETYGSVDIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTA 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  192 SSLGLFTTAGVE-DYCASKFGAIgfheSLSHELKAA-DKDGIKMTLVCPFLVDT 243
Cdd:PRK06057 140 SFVAVMGSATSQiSYTASKGGVL----AMSRELGVQfARQGIRVNALCPGPVNT 189
PLN02253 PLN02253
xanthoxin dehydrogenase
32-245 2.80e-13

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 69.08  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRqsneetaemarEIYRQLKPSTGSsdrvqelpllQPKVYTYM 111
Cdd:PLN02253  14 QRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQD-----------DLGQNVCDSLGG----------EPNVCFFH 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRhlldCPD------ELIERTMMVNCHAHFWTTKAFLPKMLELNHG 185
Cdd:PLN02253  73 CDVTVEDDVSRAVDFTVDKFGTLDIMVNNAGLTGPP----CPDirnvelSEFEKVFDVNVKGVFLGMKHAARIMIPLKKG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  186 HIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCPFLVDTGM 245
Cdd:PLN02253 149 SIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAEL---GKHGIRVNCVSPYAVPTAL 205
PRK07814 PRK07814
SDR family oxidoreductase;
33-220 3.04e-13

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 68.65  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQLKPstgssdrvqelpllqpkvytYMC 112
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHV--------------------VAA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN-HGHIVTVA 191
Cdd:PRK07814  67 DLAHPEATAGLAGQAVEAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINIS 146
                        170       180
                 ....*....|....*....|....*....
gi 41152209  192 SSLGLFTTAGVEDYCASKfGAIGFHESLS 220
Cdd:PRK07814 147 STMGRLAGRGFAAYGTAK-AALAHYTRLA 174
PRK06128 PRK06128
SDR family oxidoreductase;
36-264 3.30e-13

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 69.12  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdiNRQSNEETAemAREIYRQLKpstGSSDRVQELPllqpkvytymCDVS 115
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIAL---NYLPEEEQD--AAEVVQLIQ---AEGRKAVALP----------GDLK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAG-VVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnHGHIVTVASSL 194
Cdd:PRK06128 117 DEAFCRQLVERAVKELGGLDILVNIAGkQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPP--GASIINTGSIQ 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCPflvdtgmfegckirkemAPFFPPLKP 264
Cdd:PRK06128 195 SYQPSPTLLDYASTKAAIVAFTKALAKQV--AEK-GIRVNAVAP-----------------GPVWTPLQP 244
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
32-243 5.15e-13

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 67.83  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETaemAREIYRQLKPSTGSSDRVQelpllqpkvytym 111
Cdd:PRK08936   3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVV---INYRSDEEE---ANDVAEEIKKAGGEAIAVK------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 CDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN-HGHIVTV 190
Cdd:PRK08936  64 GDVTVESDVVNLIQTAVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINM 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDT 243
Cdd:PRK08936 144 SSVHEQIPWPLFVHYAASKGGVKLMTETLAMEYA---PKGIRVNNIGPGAINT 193
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
36-262 5.44e-13

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 68.26  E-value: 5.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyRQLKPSTGSSDrvqelpllqpkVYTYMCDVS 115
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAA-------AEIRRDTLNHE-----------VIVRHLDLA 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAGVvsgrhlLDCPDEL----IERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:cd09807  63 SLKSIRAFAAEFLAEEDRLDVLINNAGV------MRCPYSKtedgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVS 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 192 SSLGLFTTAGVED------------YCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKIRKEMA-PF 258
Cdd:cd09807 137 SLAHKAGKINFDDlnseksyntgfaYCQSKLANVLFTRELARRLQGT---GVTVNALHPGVVRTELGRHTGIHHLFLsTL 213

                ....
gi 41152209 259 FPPL 262
Cdd:cd09807 214 LNPL 217
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
35-263 5.46e-13

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: 67.70  E-value: 5.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssdrvqelplLQPKVYTYMCDV 114
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK------------------------LGDNCRFVPVDV 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGV------VSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLE---LNHG 185
Cdd:cd05371  57 TSEKDVKAALALAKAKFGRLDIVVNCAGIavaaktYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKnepDQGG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 186 H---IVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGC--KIRKEMAPFFP 260
Cdd:cd05371 137 ErgvIINTASVAAFEGQIGQAAYSASKGGIVGMTLPIARDLA---PQGIRVVTIAPGLFDTPLLAGLpeKVRDFLAKQVP 213

                ...
gi 41152209 261 PLK 263
Cdd:cd05371 214 FPS 216
PRK12743 PRK12743
SDR family oxidoreductase;
37-245 1.14e-12

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 66.98  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRATL-VLWDINRQSNEETAEMAREiyrqlkpsTGSSDRVQELpllqpkvytymcDVS 115
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRS--------HGVRAEIRQL------------DLS 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVASSL 194
Cdd:PRK12743  63 DLPEGAQALDKLIQRLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQgGRIINITSVH 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 41152209  195 GLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGM 245
Cdd:PRK12743 143 EHTPLPGASAYTAAKHALGGLTKAMALELV---EHGILVNAVAPGAIATPM 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
37-243 1.70e-12

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: 66.33  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  37 QVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREiyrqlkpstgssdrvqelpLLQPKVYTYMCDVSK 116
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVV---VNYYRSTESAEAVAA-------------------EAGERAIAIQADVRD 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 117 RESVYLTAEKVRSEVGDIDLLINNAgvvsgrhLLDCP-DELIERTMMV------------NCHAHFWTTKAFLPKMLELN 183
Cdd:cd05349  59 RDQVQAMIEEAKNHFGPVDTIVNNA-------LIDFPfDPDQRKTFDTidwedyqqqlegAVKGALNLLQAVLPDFKERG 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 184 HGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDT 243
Cdd:cd05349 132 SGRVINIGTNLFQNPVVPYHDYTTAKAALLGFTRNMAKELGP---YGITVNMVSGGLLKV 188
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
34-209 1.86e-12

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 66.41  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRqsneETAEMAREIYRQLKpstgssdrvqelpllqPKVYTYMCD 113
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINA----DAANHVVDEIQQLG----------------GQAFACRCD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGvVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASS 193
Cdd:PRK06113  69 ITSEQELSALADFALSKLGKVDILVNNAG-GGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSM 147
                        170
                 ....*....|....*.
gi 41152209  194 LGLFTTAGVEDYCASK 209
Cdd:PRK06113 148 AAENKNINMTSYASSK 163
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
38-244 2.44e-12

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: 65.67  E-value: 2.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyrqlkpstgssDRVQELpllQPKVYTYMCDVSKR 117
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVA-----------------AAIQQA---GGQAIGLECNVTSE 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 118 ESVYLTAEKVRSEVGDIDLLINNAGvVSGRHLLDCP--DELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLG 195
Cdd:cd05365  61 QDLEAVVKATVSQFGGITILVNNAG-GGGPKPFDMPmtEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSS 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41152209 196 LFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTG 244
Cdd:cd05365 140 ENKNVRIAAYGSSKAAVNHMTRNLAFDLGP---KGIRVNAVAPGAVKTD 185
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
33-248 3.67e-12

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: 65.56  E-value: 3.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyRQLKPSTGSSDRvqelpllqpkvytYMC 112
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVA-------KEITALGGRAIA-------------LAA 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAG--------------VVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPK 178
Cdd:cd08935  62 DVLDRASLERAREEIVAQFGTVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKD 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 179 MLELNHGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPflvdtGMFEG 248
Cdd:cd08935 142 MLEQKGGSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFA---TTGVRVNAIAP-----GFFVT 203
PRK07069 PRK07069
short chain dehydrogenase; Validated
41-248 4.35e-12

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 65.12  E-value: 4.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   41 ITGAGSGLGRLFALEFARRRATLVLWDINRQSNeeTAEMAREIYRQLKPSTGssdrvqelpllqpkvYTYMCDVSKRESV 120
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTDINDAAG--LDAFAAEINAAHGEGVA---------------FAAVQDVTDEAQW 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  121 YLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTTA 200
Cdd:PRK07069  67 QALLAQAADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEP 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 41152209  201 GVEDYCASKFGAIGFHESLSHELkAADKDGIKMTLVCPFLVDTGMFEG 248
Cdd:PRK07069 147 DYTAYNASKAAVASLTKSIALDC-ARRGLDVRCNSIHPTFIRTGIVDP 193
PRK08278 PRK08278
SDR family oxidoreductase;
32-227 8.27e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 64.54  E-value: 8.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdinrqsNEETAE-----------MAREIYRqlkpsTGssdrVQEL 100
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVI-------AAKTAEphpklpgtihtAAEEIEA-----AG----GQAL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  101 PLlqpkvytyMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKML 180
Cdd:PRK08278  66 PL--------VGDVRDEDQVAAAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLK 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  181 ELNHGHIVTVASSLGLFTT--AGVEDYCASKFG----AIGFHEslshELKAAD 227
Cdd:PRK08278 138 KSENPHILTLSPPLNLDPKwfAPHTAYTMAKYGmslcTLGLAE----EFRDDG 186
PRK05693 PRK05693
SDR family oxidoreductase;
38-223 9.35e-12

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 64.43  E-value: 9.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   38 VCVITGAGSGLGRLFALEFarRRATLVLWDINRQSnEETAEMAREIY--RQLkpstgssdrvqelpllqpkvytymcDVS 115
Cdd:PRK05693   3 VVLITGCSSGIGRALADAF--KAAGYEVWATARKA-EDVEALAAAGFtaVQL-------------------------DVN 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPkMLELNHGHIVTVASSLG 195
Cdd:PRK05693  55 DGAALARLAEELEAEHGGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGSVSG 133
                        170       180
                 ....*....|....*....|....*...
gi 41152209  196 LFTTAGVEDYCASKFGAIGFHESLSHEL 223
Cdd:PRK05693 134 VLVTPFAGAYCASKAAVHALSDALRLEL 161
PRK07478 PRK07478
short chain dehydrogenase; Provisional
35-246 1.39e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 63.80  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLwdiNRQSNEETAEMAREIYRQlkpsTGSSDRVQElpllqpkvytymcDV 114
Cdd:PRK07478   5 NGKVAIITGASSGIGRAAAKLFAREGAKVVV---GARRQAELDQLVAEIRAE----GGEAVALAG-------------DV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 skRESVYLTA--EKVRSEVGDIDLLINNAGVV-SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:PRK07478  65 --RDEAYAKAlvALAVERFGGLDIAFNNAGTLgEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTS 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41152209  192 SSLGlfTTA---GVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMF 246
Cdd:PRK07478 143 TFVG--HTAgfpGMAAYAASKAGLIGLTQVLAAEYGAQ---GIRVNALLPGGTDTPMG 195
PRK09242 PRK09242
SDR family oxidoreductase;
33-281 1.65e-11

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 63.61  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsNEETAEMAREIYRQLKPstgssdrvqelpllQPKVYTYMC 112
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLI--VAR--DADALAQARDELAEEFP--------------EREVHGLAA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK09242  68 DVSDDEDRRAILDWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTGMFEgckirkemapffPPLK-PEYcvkqa 271
Cdd:PRK09242 148 VSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAE---DGIRVNAVAPWYIRTPLTS------------GPLSdPDY----- 207
                        250
                 ....*....|
gi 41152209  272 MRAILTDQPM 281
Cdd:PRK09242 208 YEQVIERTPM 217
PRK06124 PRK06124
SDR family oxidoreductase;
33-223 2.86e-11

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 62.81  E-value: 2.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdinrqsNEETAEMAREIYRQLKPSTGSSDrvqELPLlqpkvytymc 112
Cdd:PRK06124   8 SLAGQVALVTGSARGLGFEIARALAGAGAHVLV-------NGRNAATLEAAVAALRAAGGAAE---ALAF---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK06124  68 DIADEEAVAAAFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITS 147
                        170       180       190
                 ....*....|....*....|....*....|.
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHEL 223
Cdd:PRK06124 148 IAGQVARAGDAVYPAAKQGLTGLMRALAAEF 178
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
33-241 4.21e-11

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 62.61  E-value: 4.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrQLKPSTGSSDRVQelpllqpkvytymC 112
Cdd:PRK08277   7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVA-------EIKAAGGEALAVK-------------A 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAG---------------VVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLP 177
Cdd:PRK08277  67 DVLDKESLEQARQQILEDFGPCDILINGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAK 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  178 KMLELNHGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCP-FLV 241
Cdd:PRK08277 147 DMVGRKGGNIINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFA---KVGIRVNAIAPgFFL 208
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
35-223 5.53e-11

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 61.89  E-value: 5.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRL----FALEFARRrATLVLwdinrqsNEETAEMAReiyrqlkpstgssdrvQELPllqPKVYTY 110
Cdd:PRK06200   5 HGQVALITGGGSGIGRAlverFLAEGARV-AVLER-------SAEKLASLR----------------QRFG---DHVLVV 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  111 MCDVSKRESvylTAEKVRSEV---GDIDLLINNAGVVS-GRHLLDCPDELIERT----MMVNCHAHFWTTKAFLPKmLEL 182
Cdd:PRK06200  58 EGDVTSYAD---NQRAVDQTVdafGKLDCFVGNAGIWDyNTSLVDIPAETLDTAfdeiFNVNVKGYLLGAKAALPA-LKA 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 41152209  183 NHGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHEL 223
Cdd:PRK06200 134 SGGSMIFTLSNSSFYPGGGGPLYTASKHAVVGLVRQLAYEL 174
PLN02780 PLN02780
ketoreductase/ oxidoreductase
7-285 6.53e-11

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 62.58  E-value: 6.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209    7 LFVVTFKIIWSFVLAGAKW----FIRPREKSVE-GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAR 81
Cdd:PLN02780  19 LFVLGSLSILKFFFTILNWvyvyFLRPAKNLKKyGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   82 EIYRQLKpstgssdrvqelplLQPKVYTYMCDVSkrESVYLTAEKVrsEVGDIDLLINNAGVV--SGRHLLDCPDELIER 159
Cdd:PLN02780  99 SKYSKTQ--------------IKTVVVDFSGDID--EGVKRIKETI--EGLDVGVLINNVGVSypYARFFHEVDEELLKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  160 TMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTTAG--VEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVC 237
Cdd:PLN02780 161 LIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDplYAVYAATKAYIDQFSRCLYVEYK---KSGIDVQCQV 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 41152209  238 PFLVDTGMfegCKIRKemAPFFPPLKPEYcVKQAMRAILTDQPmiCTP 285
Cdd:PLN02780 238 PLYVATKM---ASIRR--SSFLVPSSDGY-ARAALRWVGYEPR--CTP 277
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
35-243 8.05e-11

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 61.27  E-value: 8.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVL-WDINRQSNEETAEmareiyrqlkpstgssdrvqELPLLQPKVYTYMCD 113
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVnYARSRKAAEETAE--------------------EIEALGRKALAVKAN 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVaSS 193
Cdd:PRK08063  63 VGDVEKIKEMFAQIDEEFGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISL-SS 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209  194 LGL------FTTAGVedycaSKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDT 243
Cdd:PRK08063 142 LGSirylenYTTVGV-----SKAALEALTRYLAVELAP---KGIAVNAVSGGAVDT 189
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
31-245 9.18e-11

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 62.55  E-value: 9.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   31 EKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrQSNEETAEMAREIyrqlkpsTGSSdrvqeLPLlqpkvyty 110
Cdd:PRK08261 205 DRPLAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVP-AAGEALAAVANRV-------GGTA-----LAL-------- 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  111 mcDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTV 190
Cdd:PRK08261 264 --DITAPDAPARIAEHLAERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGV 341
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:PRK08261 342 SSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAER---GITINAVAPGFIETQM 393
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
35-185 9.85e-11

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: 61.06  E-value: 9.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrQLKPSTGSsdrvqelpllqpKVYTYMCDV 114
Cdd:cd05369   2 KGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAE-------EISSATGG------------RAHPIQCDV 62
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGvvsGRHLldCPDELIE----RTMM-VNCHAHFWTTKAFLPKMLELNHG 185
Cdd:cd05369  63 RDPEAVEAAVDETLKEFGKIDILINNAA---GNFL--APAESLSpngfKTVIdIDLNGTFNTTKAVGKRLIEAKHG 133
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
36-198 1.47e-10

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 60.69  E-value: 1.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsNEETAEMAReiyRQLKPSTGSSdrvqelpllqpKVYTYMCDVS 115
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHM--VCR--NQTRAEEAR---KEIETESGNQ-----------NIFLHIVDMS 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEVGDIDLLINNAG-VVSGRHLldcPDELIERTMMVNCHAHFWTTKAFLPkMLELNHGHIVTVASSL 194
Cdd:cd09808  63 DPKQVWEFVEEFKEEGKKLHVLINNAGcMVNKREL---TEDGLEKNFATNTLGTYILTTHLIP-VLEKEEDPRVITVSSG 138

                ....
gi 41152209 195 GLFT 198
Cdd:cd09808 139 GMLV 142
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
37-243 1.78e-10

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 60.49  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAE-MAREIyrqlkpstgsSDRVQELPllqpkvytymCDVS 115
Cdd:PRK08642   6 QTVLVTGGSRGLGAAIARAFAREGARVV---VNYHQSEDAAEaLADEL----------GDRAIALQ----------ADVT 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVG-DIDLLINNAGV------VSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIV 188
Cdd:PRK08642  63 DREQVQAMFATATEHFGkPITTVVNNALAdfsfdgDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRII 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  189 TVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDT 243
Cdd:PRK08642 143 NIGTNLFQNPVVPYHDYTTAKAALLGLTRNLAAELGP---YGITVNMVSGGLLRT 194
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
33-254 1.83e-10

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: 60.54  E-value: 1.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpstgssdrvQELpllqpKVYTYMC 112
Cdd:cd05329   3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWRE---------------KGF-----KVEGSVC 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEV-GDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:cd05329  63 DVSSRSERQELMDTVASHFgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFIS 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152209 192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMFEGCKIRKE 254
Cdd:cd05329 143 SVAGVIAVPSGAPYGATKGALNQLTRSLACEWA---KDNIRVNAVAPWVIATPLVEPVIQQKE 202
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
35-223 1.88e-10

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: 60.44  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREiyrqlkpstgssdrvqelpllqpKVYTYMCDV 114
Cdd:cd05348   3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGD-----------------------AVVGVEGDV 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVS-GRHLLDCPDELI----ERTMMVNCHAHFWTTKAFLPKMLELNhGHIVT 189
Cdd:cd05348  60 RSLADNERAVARCVERFGKLDCFIGNAGIWDySTSLVDIPEEKLdeafDELFHINVKGYILGAKAALPALYATE-GSVIF 138
                       170       180       190
                ....*....|....*....|....*....|....
gi 41152209 190 VASSLGLFTTAGVEDYCASKFGAIGFHESLSHEL 223
Cdd:cd05348 139 TVSNAGFYPGGGGPLYTASKHAVVGLVKQLAYEL 172
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
30-243 1.97e-10

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 60.25  E-value: 1.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  30 REKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLwDINRQSNEETAemareiyrqlkpstgssdrVQELPLLQPKVYT 109
Cdd:cd08936   4 RRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVV-SSRKQQNVDRA-------------------VATLQGEGLSVTG 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 110 YMCDVSK---RESVYLTAEKVRsevGDIDLLINNAGV--VSGRhLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH 184
Cdd:cd08936  64 TVCHVGKaedRERLVATAVNLH---GGVDILVSNAAVnpFFGN-ILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGG 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41152209 185 GHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAADkdgIKMTLVCPFLVDT 243
Cdd:cd08936 140 GSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRN---IRVNCLAPGLIKT 195
PRK08251 PRK08251
SDR family oxidoreductase;
37-273 2.03e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 60.33  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAREIYR--QLKpstgssdrvQELPLLQP--KVYTYMC 112
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLAL-------------CARRTDRleELK---------AELLARYPgiKVAVAAL 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK08251  61 DVNDHDQVFEVFAEFRDELGGLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  193 SLGLFTTAGVED-YCASKFGAIGFHESLSHELKaadKDGIKMTLV---------------CPFLVDTGmfEGCK-----I 251
Cdd:PRK08251 141 VSAVRGLPGVKAaYAASKAGVASLGEGLRAELA---KTPIKVSTIepgyirsemnakaksTPFMVDTE--TGVKalvkaI 215
                        250       260
                 ....*....|....*....|..
gi 41152209  252 RKEMAPFFPPLKPEYCVKQAMR 273
Cdd:PRK08251 216 EKEPGRAAVPWWPWAPLGALMR 237
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
35-238 2.09e-10

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 60.34  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDinrqsneeTAEMAREIyrqlkpstgssdrVQELPLLQPKVYTYMCDV 114
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVD--------RSELVHEV-------------AAELRAAGGEALALTADL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGvvsG-------RHLldCPDEL---IERTMMVNchahFWTTKAFLPKMLELNH 184
Cdd:PRK12823  66 ETYAGAQAAMAAAVEAFGRIDVLINNVG---GtiwakpfEEY--EEEQIeaeIRRSLFPT----LWCCRAVLPHMLAQGG 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41152209  185 GHIVTVASslglFTTAGVE--DYCASKFGAIGFHESLSHELKAadkDGIKMTLVCP 238
Cdd:PRK12823 137 GAIVNVSS----IATRGINrvPYSAAKGGVNALTASLAFEYAE---HGIRVNAVAP 185
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
33-238 2.22e-10

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 60.27  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVlwDINRQSNEETAEMAREIYRqlkpstgssdrvqelpllqpKVYTYMC 112
Cdd:PRK08993   7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIV--GINIVEPTETIEQVTALGR--------------------RFLSLTA 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNH-GHIVTVA 191
Cdd:PRK08993  65 DLRKIDGIPALLERAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIA 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 41152209  192 SSLGLFTTAGVEDYCASKFGAIGFHESLSHELKaadKDGIKMTLVCP 238
Cdd:PRK08993 145 SMLSFQGGIRVPSYTASKSGVMGVTRLMANEWA---KHNINVNAIAP 188
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
31-245 3.07e-10

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: 59.79  E-value: 3.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  31 EKSVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdinrqsneetaEMAREiYRQLKpstgssDRVQELPLLQPkvyty 110
Cdd:cd05351   2 ELDFAGKRALVTGAGKGIGRATVKALAKAGARVV-------------AVSRT-QADLD------SLVRECPGIEP----- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 111 MC-DVSKRESVyltaEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN-HGHIV 188
Cdd:cd05351  57 VCvDLSDWDAT----EEALGSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIV 132
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209 189 TVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAADkdgIKMTLVCPFLVDTGM 245
Cdd:cd05351 133 NVSSQASQRALTNHTVYCSTKAALDMLTKVMALELGPHK---IRVNSVNPTVVMTDM 186
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
36-290 3.42e-10

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: 59.77  E-value: 3.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdinrqsneetaeMAREIYRQLKpstGSSDRVQElplLQPKVYTYMCDVS 115
Cdd:cd09763   3 GKIALVTGASRGIGRGIALQLGEAGATVYI-------------TGRTILPQLP---GTAEEIEA---RGGKCIPVRCDHS 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESVYLTAEKVRSEV-GDIDLLINNA-GVVSGRHLLDCP-----DELIERTMM-VNCHAHFWTTKAFLPKMLELNHGHI 187
Cdd:cd09763  64 DDDEVEALFERVAREQqGRLDILVNNAyAAVQLILVGVAKpfweePPTIWDDINnVGLRAHYACSVYAAPLMVKAGKGLI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 188 VTVASSLG---LFTTAgvedYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDTGMF-------EGCKIRKEMAP 257
Cdd:cd09763 144 VIISSTGGleyLFNVA----YGVGKAAIDRMAADMAHELK---PHGVAVVSLWPGFVRTELVlempeddEGSWHAKERDA 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 41152209 258 FFPPLKPEYCVKqAMRAILTDqpmictPRVMYM 290
Cdd:cd09763 217 FLNGETTEYSGR-CVVALAAD------PDLMEL 242
PRK07791 PRK07791
short chain dehydrogenase; Provisional
34-211 4.33e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 59.69  E-value: 4.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDInRQSNEETAEmareiyrqlkPSTGSSDRVQELPLLQPKVYTYMCD 113
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDI-GVGLDGSAS----------GGSAAQAVVDEIVAAGGEAVANGDD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHF---------WTTKAflpKMLELNH 184
Cdd:PRK07791  73 IADWDGAANLVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFatlrhaaayWRAES---KAGRAVD 149
                        170       180
                 ....*....|....*....|....*..
gi 41152209  185 GHIVTVASSLGLFTTAGVEDYCASKFG 211
Cdd:PRK07791 150 ARIINTSSGAGLQGSVGQGNYSAAKAG 176
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
33-214 5.62e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 59.01  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdinrqsNEETAEMAREIYRQLKpstGSSDRVQELPLlqpkvytymc 112
Cdd:PRK07523   7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVIL-------NGRDPAKLAAAAESLK---GQGLSAHALAF---------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK07523  67 DVTDHDAVRAAIDAFEAEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIAS 146
                        170       180
                 ....*....|....*....|..
gi 41152209  193 SLGLFTTAGVEDYCASKfGAIG 214
Cdd:PRK07523 147 VQSALARPGIAPYTATK-GAVG 167
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-223 6.76e-10

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 58.76  E-value: 6.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVlwDINRQSNEETAEMAREIYRqlkpstgssdrvqelpllqpKVYTYMCD 113
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIV--GVGVAEAPETQAQVEALGR--------------------KFHFITAD 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKML-ELNHGHIVTVAS 192
Cdd:PRK12481  64 LIQQKDIDSIVSQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVkQGNGGKIINIAS 143
                        170       180       190
                 ....*....|....*....|....*....|.
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHEL 223
Cdd:PRK12481 144 MLSFQGGIRVPSYTASKSAVMGLTRALATEL 174
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
33-238 1.18e-09

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: 57.88  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREIYrqlKPSTgssdrVQELPllqpkvytymC 112
Cdd:cd08942   3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVI---ISARKAEACADAAEELS---AYGE-----CIAIP----------A 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPkMLEL-----NHGHI 187
Cdd:cd08942  62 DLSSEEGIEALVARVAERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLP-LLRAaataeNPARV 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 41152209 188 VTVASSLGLfTTAGVED--YCASKFGAIGFHESLSHELKAadkDGIKMTLVCP 238
Cdd:cd08942 141 INIGSIAGI-VVSGLENysYGASKAAVHQLTRKLAKELAG---EHITVNAIAP 189
PRK08628 PRK08628
SDR family oxidoreductase;
35-247 1.23e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 58.05  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEetaemareiyrqlkpstgssdRVQELPLLQPKVYTYMCDV 114
Cdd:PRK08628   6 KDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDE---------------------FAEELRALQPRAEFVQVDL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIeRTMMVNCHAHFWTTKAFLPkMLELNHGHIVTVASSL 194
Cdd:PRK08628  65 TDDAQCRDAVEQTVAKFGRIDGLVNNAGVNDGVGLEAGREAFV-ASLERNLIHYYVMAHYCLP-HLKASRGAIVNISSKT 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  195 GLFTTAGVEDYCASKfGAIgfhESLSHELKAA-DKDGIKMTLVCPFLVDTGMFE 247
Cdd:PRK08628 143 ALTGQGGTSGYAAAK-GAQ---LALTREWAVAlAKDGVRVNAVIPAEVMTPLYE 192
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
95-241 1.41e-09

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 57.84  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   95 DRVQELPL-LQPKVYTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSG---RHLLDCPDElieRTMM-VNCHAHF 169
Cdd:PRK10538  35 ERLQELKDeLGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGLALGlepAHKASVEDW---ETMIdTNNKGLV 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209  170 WTTKAFLPKMLELNHGHIVTVASSLGLFTTAGVEDYCASKfgaiGFHESLSHELKaADKDG--IKMTLVCPFLV 241
Cdd:PRK10538 112 YMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATK----AFVRQFSLNLR-TDLHGtaVRVTDIEPGLV 180
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
36-196 1.67e-09

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 57.46  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREIY---RQLKPSTGssdrvQELPLLqpkvytymC 112
Cdd:cd09762   3 GKTLFITGASRGIGKAIALKAARDGANVV---IAAKTAEPHPKLPGTIYtaaEEIEAAGG-----KALPCI--------V 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:cd09762  67 DIRDEDQVRAAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSP 146

                ....
gi 41152209 193 SLGL 196
Cdd:cd09762 147 PLNL 150
PRK06125 PRK06125
short chain dehydrogenase; Provisional
36-190 1.87e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 57.36  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAemareiyRQLKPSTGSSDRVQELpllqpkvytymcDVS 115
Cdd:PRK06125   7 GKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALA-------ADLRAAHGVDVAVHAL------------DLS 67
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  116 KRESVyltaEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTV 190
Cdd:PRK06125  68 SPEAR----EQLAAEAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV 138
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
113-255 1.91e-09

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 57.33  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVAS 192
Cdd:PRK12938  61 NVGDWDSTKAAFDKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISS 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152209  193 SLGLFTTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCPFLVDTGMFEGckIRKEM 255
Cdd:PRK12938 141 VNGQKGQFGQTNYSTAKAGIHGFTMSLAQEV--ATK-GVTVNTVSPGYIGTDMVKA--IRPDV 198
PRK06482 PRK06482
SDR family oxidoreductase;
41-244 5.11e-09

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 56.28  E-value: 5.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   41 ITGAGSGLGRLFA---LEFARRRATLVlwdinRQSNEetaemareiYRQLKPSTGSSDRVQELpllqpkvytymcDVSKR 117
Cdd:PRK06482   7 ITGASSGFGRGMTerlLARGDRVAATV-----RRPDA---------LDDLKARYGDRLWVLQL------------DVTDS 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLF 197
Cdd:PRK06482  61 AAVRAVVDRAFAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQI 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 41152209  198 TTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTG 244
Cdd:PRK06482 141 AYPGFSLYHATKWGIEGFVEAVAQEVAPF---GIEFTIVEPGPARTN 184
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
40-223 8.21e-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: 55.36  E-value: 8.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  40 VITGAGSGLGRLFALEFARRRATLVLWdinrqsneetaemareiYRQlkpSTGSSDR-VQELPLLQPKVYTYMCDVSKRE 118
Cdd:cd05357   4 LVTGAAKRIGRAIAEALAAEGYRVVVH-----------------YNR---SEAEAQRlKDELNALRNSAVLVQADLSDFA 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 119 SVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFT 198
Cdd:cd05357  64 ACADLVAAAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRP 143
                       170       180
                ....*....|....*....|....*
gi 41152209 199 TAGVEDYCASKFGAIGFHESLSHEL 223
Cdd:cd05357 144 LTGYFAYCMSKAALEGLTRSAALEL 168
PRK07577 PRK07577
SDR family oxidoreductase;
108-246 1.21e-08

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 54.73  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  108 YTYMCDVSKRESVYLTAEKVRSEvGDIDLLINNAGVVSGRHL--LDCPDelIERTMMVNCHAHFWTTKAFLPKMLELNHG 185
Cdd:PRK07577  44 ELFACDLADIEQTAATLAQINEI-HPVDAIVNNVGIALPQPLgkIDLAA--LQDVYDLNVRAAVQVTQAFLEGMKLREQG 120
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209  186 HIVTVASSlglfTTAGVED---YCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMF 246
Cdd:PRK07577 121 RIVNICSR----AIFGALDrtsYSAAKSALVGCTRTWALELAEY---GITVNAVAPGPIETELF 177
PRK07062 PRK07062
SDR family oxidoreductase;
34-244 1.25e-08

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 55.05  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLG----RLFALEFARrratlVLWdINRqsNEETAEMAREIYRQLKPstgssdrvqelpllQPKVYT 109
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGlatvELLLEAGAS-----VAI-CGR--DEERLASAEARLREKFP--------------GARLLA 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  110 YMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGvvSGR--HLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHI 187
Cdd:PRK07062  64 ARCDVLDEADVAAFAAAVEARFGGVDMLVNNAG--QGRvsTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASI 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152209  188 VTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDTG 244
Cdd:PRK07062 142 VCVNSLLALQPEPHMVATSAARAGLLNLVKSLATELAP---KGVRVNSILLGLVESG 195
PRK06197 PRK06197
short chain dehydrogenase; Provisional
36-192 1.40e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 55.42  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdinRQSNEETAEMAREIYRQLKPstGSSDRVQELpllqpkvytymcDVS 115
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVL----AVRNLDKGKAAAARITAATP--GADVTLQEL------------DLT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGV--------VSGrhlldcpdelIERTMMVNCHAHFWTTKAFLPKMLELNHGHI 187
Cdd:PRK06197  78 SLASVRAAADALRAAYPRIDLLINNAGVmytpkqttADG----------FELQFGTNHLGHFALTGLLLDRLLPVPGSRV 147

                 ....*
gi 41152209  188 VTVAS 192
Cdd:PRK06197 148 VTVSS 152
PRK09730 PRK09730
SDR family oxidoreductase;
38-245 1.93e-08

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 54.47  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   38 VCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEmarEIYRQLKPSTGSSDRVQelpllqpkvytymCDVSKR 117
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVA---VNYQQNLHAAQ---EVVNLITQAGGKAFVLQ-------------ADISDE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  118 ESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLD-CPDELIERTMMVNCHAHFWTTKAFLPKMlELNH----GHIVTVAS 192
Cdd:PRK09730  64 NQVVAMFTAIDQHDEPLAALVNNAGILFTQCTVEnLTAERINRVLSTNVTGYFLCCREAVKRM-ALKHggsgGAIVNVSS 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  193 SLGLFTTAG-VEDYCASKfGAI-GFHESLSHELKAadkDGIKMTLVCPFLVDTGM 245
Cdd:PRK09730 143 AASRLGAPGeYVDYAASK-GAIdTLTTGLSLEVAA---QGIRVNCVRPGFIYTEM 193
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
98-260 2.13e-08

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 54.41  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   98 QELPLLQPKVYTYMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFlP 177
Cdd:PRK12859  61 EELLKNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQF-A 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  178 KMLELNH-GHIVTVASSLGLFTTAGVEDYCASKfGAI-GFHESLSHELkaADKdGIKMTLVCPFLVDTG-MFEgcKIRKE 254
Cdd:PRK12859 140 RGFDKKSgGRIINMTSGQFQGPMVGELAYAATK-GAIdALTSSLAAEV--AHL-GITVNAINPGPTDTGwMTE--EIKQG 213

                 ....*.
gi 41152209  255 MAPFFP 260
Cdd:PRK12859 214 LLPMFP 219
PRK12746 PRK12746
SDR family oxidoreductase;
32-193 3.03e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 53.88  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVL-WDINRQSNEETAemareiyRQLKPSTGssdrvqelpllqpKVYTY 110
Cdd:PRK12746   2 KNLDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETI-------REIESNGG-------------KAFLI 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  111 MCDVSKRESVYLTAEKVRSEV------GDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPkmLELNH 184
Cdd:PRK12746  62 EADLNSIDGVKKLVEQLKNELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLP--LLRAE 139

                 ....*....
gi 41152209  185 GHIVTVASS 193
Cdd:PRK12746 140 GRVINISSA 148
PRK06198 PRK06198
short chain dehydrogenase; Provisional
35-209 3.51e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 53.86  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLWdINRqsNEETAEmareiyrqlkpstgssDRVQELPLLQPKVYTYMCDV 114
Cdd:PRK06198   5 DGKVALVTGGTQGLGAAIARAFAERGAAGLVI-CGR--NAEKGE----------------AQAAELEALGAKAVFVQADL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELN-HGHIVTVASS 193
Cdd:PRK06198  66 SDVEDCRRVVAAADEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSM 145
                        170       180
                 ....*....|....*....|
gi 41152209  194 LGL----FTTAgvedYCASK 209
Cdd:PRK06198 146 SAHggqpFLAA----YCASK 161
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
29-248 3.59e-08

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 54.92  E-value: 3.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  29 PREKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsNEETAEMAREIYRQLKPSTGSSDrvqelpllqpkvy 108
Cdd:COG3347 418 PKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLD---GEAAEAAAAELGGGYGADAVDAT------------- 481
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 109 tyMCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTK-AFLPKMLELNHGHI 187
Cdd:COG3347 482 --DVDVTAEAAVAAAFGFAGLDIGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARaAFQGTGGQGLGGSS 559
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209 188 VTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAADKDGIkmtLVCPFLVDTGMFEG 248
Cdd:COG3347 560 VFAVSKNAAAAAYGAAAAATAKAAAQHLLRALAAEGGANGINAN---RVNPDAVLDGSAIW 617
PRK06182 PRK06182
short chain dehydrogenase; Validated
38-244 3.73e-08

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 53.81  E-value: 3.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   38 VCVITGAGSGLGrlfalefarrratlvlwdinrqsnEETAE-MAREIYrQLKPSTGSSDRVQELPLLqpKVYTYMCDVSK 116
Cdd:PRK06182   5 VALVTGASSGIG------------------------KATARrLAAQGY-TVYGAARRVDKMEDLASL--GVHPLSLDVTD 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGL 196
Cdd:PRK06182  58 EASIKAAVDTIIAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGK 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 41152209  197 FTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTG 244
Cdd:PRK06182 138 IYTPLGAWYHATKFALEGFSDALRLEVAPF---GIDVVVIEPGGIKTE 182
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
35-207 6.61e-08

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: 53.53  E-value: 6.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  35 EGQVCVITGAGSGLGRLFALEFARR-RATLVLwdINRQSNEETAEMAREIYRQLKpstgssDRVQELPLLQpkvytymCD 113
Cdd:cd08953 204 PGGVYLVTGGAGGIGRALARALARRyGARLVL--LGRSPLPPEEEWKAQTLAALE------ALGARVLYIS-------AD 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 114 VSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTM------MVNCHAHFwttkaflpKMLELnhGHI 187
Cdd:cd08953 269 VTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLapkvdgLLNLAQAL--------ADEPL--DFF 338
                       170       180
                ....*....|....*....|
gi 41152209 188 VTVASSLGLFTTAGVEDYCA 207
Cdd:cd08953 339 VLFSSVSAFFGGAGQADYAA 358
PRK06123 PRK06123
SDR family oxidoreductase;
37-245 7.77e-08

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 52.47  E-value: 7.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMAREIYRQLKpstGSSDRVQelpllqpkvytymCDVSK 116
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVC---LNYLRNRDAAEAVVQAIRRQG---GEALAVA-------------ADVAD 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPD-ELIERTMMVNCHAHFWTTKAFLPKMLELNHGH---IVTVAS 192
Cdd:PRK06123  64 EADVLRLFEAVDRELGRLDALVNNAGILEAQMRLEQMDaARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSS 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152209  193 SLGLFTTAG-VEDYCASKfGAIgfhESLSHEL-KAADKDGIKMTLVCPFLVDTGM 245
Cdd:PRK06123 144 MAARLGSPGeYIDYAASK-GAI---DTMTIGLaKEVAAEGIRVNAVRPGVIYTEI 194
PRK07890 PRK07890
short chain dehydrogenase; Provisional
35-238 7.84e-08

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 52.65  E-value: 7.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLGRLFALEFARRRATLVLwdiNRQSNEETAEMAREIyrqlkpsTGSSDRVQelpllqpKVYTymcDV 114
Cdd:PRK07890   4 KGKVVVVSGVGPGLGRTLAVRAARAGADVVL---AARTAERLDEVAAEI-------DDLGRRAL-------AVPT---DI 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  115 SKRESVYLTAEKVRSEVGDIDLLINNAGVV-SGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElNHGHIVTVASS 193
Cdd:PRK07890  64 TDEDQCANLVALALERFGRVDALVNNAFRVpSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAE-SGGSIVMINSM 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 41152209  194 LGLFTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCP 238
Cdd:PRK07890 143 VLRHSQPKYGAYKMAKGALLAASQSLATEL---GPQGIRVNSVAP 184
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
36-261 9.11e-08

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 52.07  E-value: 9.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVlwdINRQSNEETAEMareiyrqlKPSTGSSDRVQELPllqpkvytymCDVS 115
Cdd:PRK05786   5 GKKVAIIGVSEGLGYAVAYFALKEGAQVC---INSRNENKLKRM--------KKTLSKYGNIHYVV----------GDVS 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLInnagVVSGRHLLDCPDELIERTMMVNCH--AHFWTTKAFLPKMLElnHGHIVTVASS 193
Cdd:PRK05786  64 STESARNVIEKAAKVLNAIDGLV----VTVGGYVEDTVEEFSGLEEMLTNHikIPLYAVNASLRFLKE--GSSIVLVSSM 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152209  194 LGLFTTAGVE-DYCASKFGAIGFHESLSHELkaADKdGIKMTLVCPFLVDtGMFE----GCKIRKEMAPFFPP 261
Cdd:PRK05786 138 SGIYKASPDQlSYAVAKAGLAKAVEILASEL--LGR-GIRVNGIAPTTIS-GDFEpernWKKLRKLGDDMAPP 206
PRK08017 PRK08017
SDR family oxidoreductase;
31-299 1.17e-07

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 52.01  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   31 EKSVegqvcVITGAGSGLGRLFALEFARRRatlvlwdinrqsneetaemareiYRQLKPSTGSSD--RVQELPLlqpkvY 108
Cdd:PRK08017   2 QKSV-----LITGCSSGIGLEAALELKRRG-----------------------YRVLAACRKPDDvaRMNSLGF-----T 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  109 TYMCDVSKRESVYLTAEKVrsevgdIDL-------LINNAGV-VSGrhlldcPDELIERTMM-----VNCHAHFWTTKAF 175
Cdd:PRK08017  49 GILLDLDDPESVERAADEV------IALtdnrlygLFNNAGFgVYG------PLSTISRQQMeqqfsTNFFGTHQLTMLL 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  176 LPKMLELNHGHIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGMFEGCKIRKEM 255
Cdd:PRK08017 117 LPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSDALRMELRHS---GIKVSLIEPGPIRTRFTDNVNQTQSD 193
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  256 APFFPP-------LKPEYCVKQAMRAILTDQPMICTP--RVMYMVTFMKTVLP 299
Cdd:PRK08017 194 KPVENPgiaarftLGPEAVVPKLRHALESPKPKLRYPvtLVTHAVMVLKRLLP 246
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
38-161 1.77e-07

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: 50.56  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209     38 VCVITGAGSGLGRLFALEFARRRA-TLVLwdinrqsneetaemareIYRQLKPSTGSSDRVQELPLLQPKVYTYMCDVSK 116
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVL-----------------LSRSGPDAPGAAALLAELEAAGARVTVVACDVAD 64
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 41152209    117 RESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTM 161
Cdd:smart00822  65 RDALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVL 109
PRK06947 PRK06947
SDR family oxidoreductase;
37-243 2.09e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 51.34  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   37 QVCVITGAGSGLGRLFALEFARRRatlvlWDI------NRQSNEETAEMAREIYRQLKPSTGssdrvqelpllqpkvyty 110
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARG-----WSVginyarDAAAAEETADAVRAAGGRACVVAG------------------ 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  111 mcDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVS-GRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGH--- 186
Cdd:PRK06947  60 --DVANEADVIAMFDAVQSAFGRLDALVNNAGIVApSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRgga 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152209  187 IVTV---ASSLGlfTTAGVEDYCASKfGAIgfhESLSHEL-KAADKDGIKMTLVCPFLVDT 243
Cdd:PRK06947 138 IVNVssiASRLG--SPNEYVDYAGSK-GAV---DTLTLGLaKELGPHGVRVNAVRPGLIET 192
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
36-260 2.69e-07

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 50.84  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGA--GSGLGRLFALEFARRRATLVLWDINRQSNEETAEMAREIYRQLKPSTGSS-DRVQELPLlqpkvytymc 112
Cdd:PRK12748   5 KKIALVTGAsrLNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWGMHDKEPVLLKEEIESYgVRCEHMEI---------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAgVVSGRHLLDCPD-ELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVA 191
Cdd:PRK12748  75 DLSQPYAPNRVFYAVSERLGDPSILINNA-AYSTHTRLEELTaEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLT 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  192 SSLGLFTTAGVEDYCASKfGAI-GFHESLSHELkaADKdGIKMTLVCPFLVDTGMFEGcKIRKEMAPFFP 260
Cdd:PRK12748 154 SGQSLGPMPDELAYAATK-GAIeAFTKSLAPEL--AEK-GITVNAVNPGPTDTGWITE-ELKHHLVPKFP 218
PRK07985 PRK07985
SDR family oxidoreductase;
34-238 3.84e-07

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 50.76  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVL--WDINRQSNEETAEMAREIYRQlkpstgssdrvqelPLLQPKvytym 111
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEECGRK--------------AVLLPG----- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 cDVSKRESVYLTAEKVRSEVGDIDLLINNAG-VVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPkmLELNHGHIVTV 190
Cdd:PRK07985 108 -DLSDEKFARSLVHEAHKALGGLDIMALVAGkQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIP--LLPKGASIITT 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkaADKdGIKMTLVCP 238
Cdd:PRK07985 185 SSIQAYQPSPHLLDYAATKAAILNYSRGLAKQV--AEK-GIRVNIVAP 229
PRK12744 PRK12744
SDR family oxidoreductase;
33-248 6.09e-07

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 50.12  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAEmareiyrqlkpstgssDRVQELPLLQPKVYTYMC 112
Cdd:PRK12744   5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAE----------------ETVAAVKAAGAKAVAFQA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWttkaFLP---KMLElNHGHIVT 189
Cdd:PRK12744  69 DLTTAAAVEKLFDDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFF----FIKeagRHLN-DNGKIVT 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209  190 VASS-LGLFtTAGVEDYCASKfgaigfhESLSHELKAADKD----GIKMTLVCPFLVDTGMFEG 248
Cdd:PRK12744 144 LVTSlLGAF-TPFYSAYAGSK-------APVEHFTRAASKEfgarGISVTAVGPGPMDTPFFYP 199
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
40-195 6.56e-07

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 50.21  E-value: 6.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  40 VITGAGSGLGRLFALEFARRRATLVLWDINrqsNEETAEMAReiyrqlkpstgssdrvQELPLLQPKVYTYMCDVSKRES 119
Cdd:cd09810   5 VITGASSGLGLAAAKALARRGEWHVVMACR---DFLKAEQAA----------------QEVGMPKDSYSVLHCDLASLDS 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 120 VYLTAEKVRSEVGDIDLLINNAGV--VSGRHLLDCPDELiERTMMVNCHAHFWTTKAFLP--KMLELNHGHIVTVASSLG 195
Cdd:cd09810  66 VRQFVDNFRRTGRPLDALVCNAAVylPTAKEPRFTADGF-ELTVGVNHLGHFLLTNLLLEdlQRSENASPRIVIVGSITH 144
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
135-248 1.67e-06

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 47.90  E-value: 1.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 135 DLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTTAGVEDYCASKFGAIG 214
Cdd:cd02266  33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDG 112
                        90       100       110
                ....*....|....*....|....*....|....*
gi 41152209 215 FHESLSHELKAadkDGIKMTLVCP-FLVDTGMFEG 248
Cdd:cd02266 113 LAQQWASEGWG---NGLPATAVACgTWAGSGMAKG 144
PRK06500 PRK06500
SDR family oxidoreductase;
35-243 2.33e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 48.03  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   35 EGQVCVITGAGSGLG----RLFALEFARRRATlvlwdinrQSNEETAEMAREIyrqlkpstgssdrvqelplLQPKVYTY 110
Cdd:PRK06500   5 QGKTALITGGTSGIGletaRQFLAEGARVAIT--------GRDPASLEAARAE-------------------LGESALVI 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  111 MCDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKmleLNHG----- 185
Cdd:PRK06500  58 RADAGDVAAQKALAQALAEAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPL---LANPasivl 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209  186 ------HIVTVASSLglfttagvedYCASKFGAIGFHESLSHELKaadKDGIKMTLVCPFLVDT 243
Cdd:PRK06500 135 ngsinaHIGMPNSSV----------YAASKAALLSLAKTLSGELL---PRGIRVNAVSPGPVQT 185
PRK12747 PRK12747
short chain dehydrogenase; Provisional
34-245 2.48e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 48.15  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   34 VEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQsneetaEMAREIYRQLKPSTGSSDRV-QELPLLQpkvytymc 112
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRK------EEAEETVYEIQSNGGSAFSIgANLESLH-------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnHGHIVTVAS 192
Cdd:PRK12747  68 GVEALYSSLDNELQNRTGSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRD--NSRIINISS 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152209  193 SLGLFTTAGVEDYCASKfGAIGFHE-SLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:PRK12747 146 AATRISLPDFIAYSMTK-GAINTMTfTLAKQLGAR---GITVNAILPGFIKTDM 195
PRK07677 PRK07677
short chain dehydrogenase; Provisional
36-155 8.24e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 46.60  E-value: 8.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLwdINRqsNEETAEMAReiyrqlkpstgssdrvQELPLLQPKVYTYMCDVS 115
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVI--TGR--TKEKLEEAK----------------LEIEQFPGQVLTVQMDVR 60
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAgvvSGRHLldCPDE 155
Cdd:PRK07677  61 NPEDVQKMVEQIDEKFGRIDALINNA---AGNFI--CPAE 95
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
36-193 9.79e-06

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 46.44  E-value: 9.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAE-MAREIYRQlkpstgssdRVQELPLlqpkvytymcDV 114
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSrILEEWHKA---------RVEAMTL----------DL 61
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152209 115 SKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDcpDELIERTMMVNCHAHFWTTKaFLPKMLELNHGHIVTVASS 193
Cdd:cd09809  62 ASLRSVQRFAEAFKAKNSPLHVLVCNAAVFALPWTLT--EDGLETTFQVNHLGHFYLVQ-LLEDVLRRSAPARVIVVSS 137
PRK07035 PRK07035
SDR family oxidoreductase;
33-243 3.32e-05

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 44.62  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdINRQsneetAEMAREIYRQLKPSTGSSDrvqelpllqpkvyTYMC 112
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIV--SSRK-----LDGCQAVADAIVAAGGKAE-------------ALAC 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGV--VSGrHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTV 190
Cdd:PRK07035  65 HIGEMEQIDALFAHIRERHGRLDILVNNAAAnpYFG-HILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNV 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  191 ASSLGLFTTAGVEDYCASKFGAIGFHESLSHELKAadkDGIKMTLVCPFLVDT 243
Cdd:PRK07035 144 ASVNGVSPGDFQGIYSITKAAVISMTKAFAKECAP---FGIRVNALLPGLTDT 193
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
40-207 3.47e-05

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 43.70  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209    40 VITGAGSGLGRLFALEFARRRA-TLVLwdinrqsneetaeMAREIYrqlkPSTGSSDRVQELPLLQPKVYTYMCDVSKRE 118
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVL-------------LSRSAA----PRPDAQALIAELEARGVEVVVVACDVSDPD 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   119 SVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLElnhgHIVTVASSLGLFT 198
Cdd:pfam08659  67 AVAALLAEIKAEGPPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLD----FFVLFSSIAGLLG 142

                  ....*....
gi 41152209   199 TAGVEDYCA 207
Cdd:pfam08659 143 SPGQANYAA 151
PRK06720 PRK06720
hypothetical protein; Provisional
36-78 3.53e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 43.81  E-value: 3.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETAE 78
Cdd:PRK06720  16 GKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVE 58
PRK06196 PRK06196
oxidoreductase; Provisional
36-195 4.31e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 44.67  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDINRqsneetaEMAREIYRQLkpstgssDRVQELPLlqpkvytymcDVS 115
Cdd:PRK06196  26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRP-------DVAREALAGI-------DGVEVVML----------DLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  116 KRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDelIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVaSSLG 195
Cdd:PRK06196  82 DLESVRAFAERFLDSGRRIDILINNAGVMACPETRVGDG--WEAQFATNHLGHFALVNLLWPALAAGAGARVVAL-SSAG 158
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
36-248 4.41e-05

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: 44.45  E-value: 4.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  36 GQVCVITGAGSGLGRLFALEFARRRATLVLWDinrQSNEETAEMAREIYRQLKPSTgssdrvqelpLLQPkvytymCDVS 115
Cdd:cd08933   9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCA---RGEAAGQALESELNRAGPGSC----------KFVP------CDVT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 116 KRESV-YLTAEKVRSeVGDIDLLINNAGvvsgrhlLDCPDELIERT--------MMVNCHAHFWTTKAFLPKmLELNHGH 186
Cdd:cd08933  70 KEEDIkTLISVTVER-FGRIDCLVNNAG-------WHPPHQTTDETsaqefrdlLNLNLISYFLASKYALPH-LRKSQGN 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152209 187 IVTVASSLGLFTTAGVEDYCASKFGAIGFHESLshelkAAD--KDGIKMTLVCPFLVDTGMFEG 248
Cdd:cd08933 141 IINLSSLVGSIGQKQAAPYVATKGAITAMTKAL-----AVDesRYGVRVNCISPGNIWTPLWEE 199
PRK05854 PRK05854
SDR family oxidoreductase;
36-143 5.37e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 44.29  E-value: 5.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   36 GQVCVITGAGSGLGrlfaLEFARRRATL---VLWDINrqsNEETAEMAREIYRQLKPstgssdrvqelpllQPKVYTYMC 112
Cdd:PRK05854  14 GKRAVVTGASDGLG----LGLARRLAAAgaeVILPVR---NRAKGEAAVAAIRTAVP--------------DAKLSLRAL 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGV 143
Cdd:PRK05854  73 DLSSLASVAALGEQLRAEGRPIHLLINNAGV 103
PRK09186 PRK09186
flagellin modification protein A; Provisional
33-195 8.83e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 43.44  E-value: 8.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   33 SVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINrqsneetaemaREIYRQLKPSTGSSDRVQELPLLQpkvytymC 112
Cdd:PRK09186   1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADID-----------KEALNELLESLGKEFKSKKLSLVE-------L 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKVRSEVGDIDLLINNA---GVVSGRHLLDC-PDELIERtmmVNCH--AHFWTTKAFLPKMLELNHGH 186
Cdd:PRK09186  63 DITDQESLEEFLSKSAEKYGKIDGAVNCAyprNKDYGKKFFDVsLDDFNEN---LSLHlgSSFLFSQQFAKYFKKQGGGN 139

                 ....*....
gi 41152209  187 IVTVASSLG 195
Cdd:PRK09186 140 LVNISSIYG 148
PRK08703 PRK08703
SDR family oxidoreductase;
32-211 5.09e-04

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 41.07  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   32 KSVEGQVCVITGAGSGLGRLFALEFARRRATLVLWDINRQSNEetaemarEIYRQLKPSTGSSDRVQELPLLqpkvytym 111
Cdd:PRK08703   2 ATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLE-------KVYDAIVEAGHPEPFAIRFDLM-------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  112 cDVSKRESVYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDcpDELIERTM---MVNCHAHFWTTKAFLPKMLELNHGHIV 188
Cdd:PRK08703  67 -SAEEKEFEQFAATIAEATQGKLDGIVHCAGYFYALSPLD--FQTVAEWVnqyRINTVAPMGLTRALFPLLKQSPDASVI 143
                        170       180
                 ....*....|....*....|...
gi 41152209  189 TVASSLGLFTTAGVEDYCASKFG 211
Cdd:PRK08703 144 FVGESHGETPKAYWGGFGASKAA 166
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
38-248 6.40e-04

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 40.83  E-value: 6.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  38 VCVITGAGSGLG-----RLFALEFARRRATLVLWDINRQSneetAEMAReiyRQLKPSTGSSDRVQELPLLqpkvytymc 112
Cdd:cd08941   3 VVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQR----AEAAC---RALLASHPDARVVFDYVLV--------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 113 DVSKRESVYLTAEKVRSEVGDIDLLINNAGV----------------VSGRHLLDCPDELIERTMMV------------- 163
Cdd:cd08941  67 DLSNMVSVFAAAKELKKRYPRLDYLYLNAGImpnpgidwigaikevlTNPLFAVTNPTYKIQAEGLLsqgdkatedglge 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209 164 ----NCHAHFWTTKAFLPKMLELNH-GHIVTVASSLGLFTTAGVED---------YCASKFGAIGFHESLsheLKAADKD 229
Cdd:cd08941 147 vfqtNVFGHYYLIRELEPLLCRSDGgSQIIWTSSLNASPKYFSLEDiqhlkgpapYSSSKYLVDLLSLAL---NRKFNKL 223
                       250
                ....*....|....*....
gi 41152209 230 GIKMTLVCPFLVDTGMFEG 248
Cdd:cd08941 224 GVYSYVVHPGICTTNLTYG 242
PRK07775 PRK07775
SDR family oxidoreductase;
40-245 9.71e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 40.12  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   40 VITGAGSGLGRLFALEFARRRATLVLwdiNRQSNEETAEMAREIyrqlkpsTGSSDRVQELPLlqpkvytymcDVSKRES 119
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVAL---GARRVEKCEELVDKI-------RADGGEAVAFPL----------DVTDPDS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  120 VYLTAEKVRSEVGDIDLLINNAGVVSGRHLLDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHGHIVTVASSLGLFTT 199
Cdd:PRK07775  74 VKSFVAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQR 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 41152209  200 AGVEDYCASKFGAIGFHESLSHELKAAdkdGIKMTLVCPFLVDTGM 245
Cdd:PRK07775 154 PHMGAYGAAKAGLEAMVTNLQMELEGT---GVRASIVHPGPTLTGM 196
PRK08416 PRK08416
enoyl-ACP reductase;
31-147 1.08e-03

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 40.14  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   31 EKSVEGQVCVITGAGSGLGRLFALEFARRRATLVLwdiNRQSNEETAEmarEIYRQLKPSTGSSDRVQELPLLQPKVYTY 110
Cdd:PRK08416   3 SNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAF---TYNSNVEEAN---KIAEDLEQKYGIKAKAYPLNILEPETYKE 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41152209  111 McdvskresvyltAEKVRSEVGDIDLLINNAgVVSGR 147
Cdd:PRK08416  77 L------------FKKIDEDFDRVDFFISNA-IISGR 100
PRK08862 PRK08862
SDR family oxidoreductase;
41-140 1.37e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 39.71  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   41 ITGAGSGLGRLFALEFARRRATLVLWDINRQSNEETaemareiYRQLKPSTGssdrvqelpllqpKVYTY-MCDVSKrES 119
Cdd:PRK08862  10 ITSAGSVLGRTISCHFARLGATLILCDQDQSALKDT-------YEQCSALTD-------------NVYSFqLKDFSQ-ES 68
                         90       100
                 ....*....|....*....|..
gi 41152209  120 VYLTAEKVRSEVGD-IDLLINN 140
Cdd:PRK08862  69 IRHLFDAIEQQFNRaPDVLVNN 90
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
39-161 2.18e-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: 39.67  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  39 CVITGAGSGLGRLFALEFARRRAT-LVLwdINRQSNEETAEMAREIYRQLkpstgsSDRVQELPllqpkvytymCDVSKR 117
Cdd:cd05274 153 YLITGGLGGLGLLVARWLAARGARhLVL--LSRRGPAPRAAARAALLRAG------GARVSVVR----------CDVTDP 214
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 41152209 118 ESVYLTAEKVRSEVGdIDLLINNAGVVSGRHLLDCPDELIERTM 161
Cdd:cd05274 215 AALAALLAELAAGGP-LAGVIHAAGVLRDALLAELTPAAFAAVL 257
PRK05993 PRK05993
SDR family oxidoreductase;
113-238 4.63e-03

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 38.08  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209  113 DVSKRESVYLTAEKV--RSEvGDIDLLINN-----AGVVSgrhllDCPDELIERTMMVNCHAHFWTTKAFLPKMLELNHG 185
Cdd:PRK05993  55 DYAEPESIAALVAQVleLSG-GRLDALFNNgaygqPGAVE-----DLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQG 128
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152209  186 HIVTVASSLGLFTTAGVEDYCASKFGAIGFHESLSHELkaaDKDGIKMTLVCP 238
Cdd:PRK05993 129 RIVQCSSILGLVPMKYRGAYNASKFAIEGLSLTLRMEL---QGSGIHVSLIEP 178
PRK08340 PRK08340
SDR family oxidoreductase;
40-145 7.71e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 37.48  E-value: 7.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152209   40 VITGAGSGLGRLFALEFARRRATLVLwdinRQSNEETAEMAreiYRQLKPSTGssdrvqelpllqpkVYTYMCDVSKRES 119
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVI----SSRNEENLEKA---LKELKEYGE--------------VYAVKADLSDKDD 62
                         90       100
                 ....*....|....*....|....*.
gi 41152209  120 VYLTAEKVRSEVGDIDLLINNAGVVS 145
Cdd:PRK08340  63 LKNLVKEAWELLGGIDALVWNAGNVR 88
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH