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Conserved domains on  [gi|446682265|ref|WP_000759611|]
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MULTISPECIES: elongation factor P 5-aminopentanone reductase [Bacillus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 11481119)

SDR family NAD(P)-dependent oxidoreductase is a short-chain dehydrogenase (SDR) family protein similar to Sinorhizobium meliloti 3-ketoacyl-ACP reductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-237 8.72e-117

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


:

Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 333.35  E-value: 8.72e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEeggdAIAVKADVSSEEDVENLVEQIVEkfgK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK05565  84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:PRK05565 164 AFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVDG 243

                 ....
gi 446682265 234 GWHC 237
Cdd:PRK05565 244 GWTC 247
 
Name Accession Description Interval E-value
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-237 8.72e-117

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 333.35  E-value: 8.72e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEeggdAIAVKADVSSEEDVENLVEQIVEkfgK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK05565  84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:PRK05565 164 AFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVDG 243

                 ....
gi 446682265 234 GWHC 237
Cdd:PRK05565 244 GWTC 247
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
20-236 4.07e-65

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: 202.32  E-value: 4.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSE---EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVT 93
Cdd:COG1028   24 RALAAEGARVVITDRDAEaleAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAafgRLDILVNNAGITPPGPLEELT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  94 NDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAV 173
Cdd:COG1028  104 EEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAV 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446682265 174 APGAIETEMLNVF--SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:COG1028  184 APGPIDTPMTRALlgAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLT 248
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
20-234 1.16e-55

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: 177.74  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSEEKVNELQKEWD---EVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVT 93
Cdd:cd05333   18 LRLAAEGAKVAVTDRSEEAAAETVEEIKAlggNAAALEADVSDREAVEALVEKVEAefgPVDILVNNAGITRDNLLMRMS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  94 NDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAV 173
Cdd:cd05333   98 EEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAV 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 174 APGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd05333  178 APGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGG 238
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
20-236 1.66e-48

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: 159.52  E-value: 1.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   20 KQLIQDGYTVYVHYNNSE--EKVNELQKEWDEVIpVQANLASTDGAEQLWKQIEH---PLDVIVYAAG--KSIFGLVTDV 92
Cdd:pfam13561  14 RALAEEGAEVVLTDLNEAlaKRVEELAEELGAAV-LPCDVTDEEQVEALVAAAVEkfgRLDILVNNAGfaPKLKGPFLDT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   93 TNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:pfam13561  93 SREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNA 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265  173 VAPGAIETEMLNVFSEEDK--NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:pfam13561 171 ISPGPIKTLAASGIPGFDEllAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
3-236 1.43e-42

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 144.50  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265    3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEK----VNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLD 75
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNEERaeawLQEQGALGFDFRVVEGDVSSFESCKAAVAKVEAelgPVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   76 VIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:TIGR01829  81 VLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  156 VKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:TIGR01829 161 TKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSINGGL 240

                  .
gi 446682265  236 H 236
Cdd:TIGR01829 241 Y 241
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
22-236 4.45e-29

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 109.24  E-value: 4.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVHYNNSEEKVNELQKEWDEV----IPVQANLASTDGAEQLWKQI-EH--PLDVIVYAAGKSIFGLVTDVTN 94
Cdd:NF012208  18 LAREGFDVAVHYRRSAEAAEQTAQEAEALgvkaITLQADLTDPEQARSLVEEAaEAlgGLSVLVNNVGNYLHKPLLETTD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  95 DELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQ--IGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:NF012208  98 EEWHEMLDSNLNATFYVTQAALPLMRAAGWGRIVNLGYAGAQnlLARPGITPYVIAKTGVIIYSKALAKELAGDGITVNV 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 173 VAPGAIEtemlNVFSEEDkneiaEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:NF012208 178 VSPGVAE----NSVSQPL-----PEIPAGRPATLEELADAVLFFVRPSSDYITGQVLEVAGGWN 232
 
Name Accession Description Interval E-value
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-237 8.72e-117

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 333.35  E-value: 8.72e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEeggdAIAVKADVSSEEDVENLVEQIVEkfgK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK05565  84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:PRK05565 164 AFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVDG 243

                 ....
gi 446682265 234 GWHC 237
Cdd:PRK05565 244 GWTC 247
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
20-236 4.07e-65

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: 202.32  E-value: 4.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSE---EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVT 93
Cdd:COG1028   24 RALAAEGARVVITDRDAEaleAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAafgRLDILVNNAGITPPGPLEELT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  94 NDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAV 173
Cdd:COG1028  104 EEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAV 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446682265 174 APGAIETEMLNVF--SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:COG1028  184 APGPIDTPMTRALlgAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLT 248
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
20-236 2.59e-59

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 187.29  E-value: 2.59e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVyVHYNNSEEKVNELQKEWD----EVIPVQANLASTDGAEQLWKQIE---HPLDVIVYAAGKSIFGLVTDV 92
Cdd:PRK05653  23 LRLAADGAKV-VIYDSNEEAAEALAAELRaaggEARVLVFDVSDEAAVRALIEAAVeafGALDILVNNAGITRDALLPRM 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:PRK05653 102 SEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNA 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 173 VAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:PRK05653 182 VAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNGGMY 245
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
20-236 2.03e-57

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 182.70  E-value: 2.03e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDV 92
Cdd:PRK05557  23 ERLAAQGANVVINYASSEAGAEALVAEIGAlggkALAVQGDVSDAESVERAVDEAKAefgGVDILVNNAGITRDNLLMRM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:PRK05557 103 KEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNA 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 173 VAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:PRK05557 183 VAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVNGGMV 246
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
20-234 1.16e-55

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: 177.74  E-value: 1.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSEEKVNELQKEWD---EVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVT 93
Cdd:cd05333   18 LRLAAEGAKVAVTDRSEEAAAETVEEIKAlggNAAALEADVSDREAVEALVEKVEAefgPVDILVNNAGITRDNLLMRMS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  94 NDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAV 173
Cdd:cd05333   98 EEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAV 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 174 APGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd05333  178 APGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGG 238
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-236 1.91e-55

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 177.75  E-value: 1.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEW----DEVIPVQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVealgRRAQAVQADVTDKAALEAAVAAAVErfgR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK12825  85 IDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:PRK12825 165 GLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEVTG 244

                 ...
gi 446682265 234 GWH 236
Cdd:PRK12825 245 GVD 247
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
22-232 4.21e-55

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: 176.32  E-value: 4.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVHYNNSE--EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDE 96
Cdd:cd05233   18 LAREGAKVVLADRNEEalAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEefgRLDILVNNAGIARPGPLEELTDED 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  97 LNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPG 176
Cdd:cd05233   98 WDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPG 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 177 AIETEML-NVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVN 232
Cdd:cd05233  178 LVDTPMLaKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
3-234 4.32e-49

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: 161.29  E-value: 4.32e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNS----EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLD 75
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVNYASSkaaaEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKafgGVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:cd05362   84 ILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 156 VKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd05362  162 TRVLAKELGGRGITVNAVAPGPVDTDMfYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRANGG 241
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-234 7.54e-49

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 160.70  E-value: 7.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTV----YVHYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRViatyFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEeegP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK12824  81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:PRK12824 161 GFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISING 240

                 .
gi 446682265 234 G 234
Cdd:PRK12824 241 G 241
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
20-236 1.66e-48

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: 159.52  E-value: 1.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   20 KQLIQDGYTVYVHYNNSE--EKVNELQKEWDEVIpVQANLASTDGAEQLWKQIEH---PLDVIVYAAG--KSIFGLVTDV 92
Cdd:pfam13561  14 RALAEEGAEVVLTDLNEAlaKRVEELAEELGAAV-LPCDVTDEEQVEALVAAAVEkfgRLDILVNNAGfaPKLKGPFLDT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   93 TNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:pfam13561  93 SREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNA 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265  173 VAPGAIETEMLNVFSEEDK--NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:pfam13561 171 ISPGPIKTLAASGIPGFDEllAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
3-234 8.77e-44

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: 147.60  E-value: 8.77e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEkVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEH----PL 74
Cdd:cd05329    7 KTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKE-LDECLTEWREkgfkVEGSVCDVSSRSERQELMDTVAShfggKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNS 154
Cdd:cd05329   86 NILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 155 YVKALAKEVSLSGIRVNAVAPGAIETEMLN--VFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVN 232
Cdd:cd05329  166 LTRSLACEWAKDNIRVNAVAPWVIATPLVEpvIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQIIAVD 245

                 ..
gi 446682265 233 GG 234
Cdd:cd05329  246 GG 247
PRK12826 PRK12826
SDR family oxidoreductase;
37-234 3.46e-43

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 146.21  E-value: 3.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLS 113
Cdd:PRK12826  44 AATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEdfgRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 114 MALPSMIQRRSGNIVLVSSIWGQIGA-SCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEEDK 191
Cdd:PRK12826 124 AALPALIRAGGGRIVLTSSVAGPRVGyPGLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAgNLGDAQWA 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446682265 192 NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK12826 204 EAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLPVDGG 246
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
3-236 1.43e-42

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 144.50  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265    3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEK----VNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLD 75
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNEERaeawLQEQGALGFDFRVVEGDVSSFESCKAAVAKVEAelgPVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   76 VIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:TIGR01829  81 VLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  156 VKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:TIGR01829 161 TKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSINGGL 240

                  .
gi 446682265  236 H 236
Cdd:TIGR01829 241 Y 241
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
22-235 5.36e-41

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: 140.18  E-value: 5.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVHYNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEHP---LDVIVYAAGKSIFGLVTDVTN 94
Cdd:cd05359   18 LAERGADVVINYRKSKDAAAEVAAEIEElggkAVVVRADVSQPQDVEEMFAAVKERfgrLDVLVSNAAAGAFRPLSELTP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  95 DELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSI--------WGQIGAScevlysmvKGAQNSYVKALAKEVSLS 166
Cdd:cd05359   98 AHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLgsiralpnYLAVGTA--------KAALEALVRYLAVELGPR 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 167 GIRVNAVAPGAIETEMLNVF--SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:cd05359  170 GIRVNAVSPGVIDTDALAHFpnREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDGGL 240
FabG-like PRK07231
SDR family oxidoreductase;
37-235 1.77e-38

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 133.80  E-value: 1.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEwDEVIPVQANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKS-IFGLVTDVTNDELNDMVELQVKSIYKLL 112
Cdd:PRK07231  43 ERVAAEILAG-GRAIAVAADVSDEADVEAAVAAaLERfgSVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWT 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 113 SMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKN 192
Cdd:PRK07231 122 QAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTP 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446682265 193 EIAEE----IPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK07231 202 ENRAKflatIPLGRLGTPEDIANAALFLASDEASWITGVTLVVDGGR 248
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
3-234 2.42e-37

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 130.89  E-value: 2.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEK----VNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLD 75
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAaenlVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNhfgKVD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:PRK12935  87 ILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGF 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 156 VKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGAsYITGQIIGVNGG 234
Cdd:PRK12935 167 TKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDGA-YITGQQLNINGG 244
PRK09135 PRK09135
pteridine reductase; Provisional
20-234 2.71e-37

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 130.82  E-value: 2.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSEEKVNELQKEW-----DEVIPVQANLASTDGAEQLWKQIEHP---LDVIVYAAgkSIF--GLV 89
Cdd:PRK09135  24 RTLHAAGYRVAIHYHRSAAEADALAAELnalrpGSAAALQADLLDPDALPELVAACVAAfgrLDALVNNA--SSFypTPL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  90 TDVTNDELNDMVELQVKSIYkLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSlSGIR 169
Cdd:PRK09135 102 GSITEAQWDDLFASNLKAPF-FLSQAAAPQLRKQRGAIVNITDIHAERPLKGYPVYCAAKAALEMLTRSLALELA-PEVR 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265 170 VNAVAPGAIE-TEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPgASYITGQIIGVNGG 234
Cdd:PRK09135 180 VNAVAPGAILwPEDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLLAD-ASFITGQILAVDGG 244
PRK12939 PRK12939
short chain dehydrogenase; Provisional
3-235 3.64e-37

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 130.48  E-value: 3.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNS---EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHPL---DV 76
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAaeaRELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALgglDG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSS---IWG--QIGAscevlYSMVKGA 151
Cdd:PRK12939  88 LVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASdtaLWGapKLGA-----YVASKGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 152 QNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIG 230
Cdd:PRK12939 163 VIGMTRSLARELGGRGITVNAIAPGLTATEAtAYVPADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLP 242

                 ....*
gi 446682265 231 VNGGW 235
Cdd:PRK12939 243 VNGGF 247
PRK07577 PRK07577
SDR family oxidoreductase;
54-234 2.72e-36

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 127.92  E-value: 2.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  54 QANLASTDGAEQLWKQI--EHPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVS 131
Cdd:PRK07577  47 ACDLADIEQTAATLAQIneIHPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNIC 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 132 SIWGQiGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLN----VFSEEDKnEIAEEIPLGRLGLPE 207
Cdd:PRK07577 127 SRAIF-GALDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRqtrpVGSEEEK-RVLASIPMRRLGTPE 204
                        170       180
                 ....*....|....*....|....*..
gi 446682265 208 EVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK07577 205 EVAAAIAFLLSDDAGFITGQVLGVDGG 231
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
20-236 3.00e-36

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: 128.16  E-value: 3.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSE---EKVNELQKEWDEVIPVQANLASTDG---AEQLWKQIEHPLDVIVYAAGKSIFGLVTDVT 93
Cdd:cd05344   19 RALAREGARVAICARNREnleRAASELRAGGAGVLAVVADLTDPEDidrLVEKAGDAFGRVDILVNNAGGPPPGPFAELT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  94 NDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAV 173
Cdd:cd05344   99 DEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSV 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 174 APGAIETEML----------NVFSEED-KNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:cd05344  179 LPGYIDTERVrrllearaekEGISVEEaEKEVASQIPLGRVGKPEELAALIAFLASEKASYITGQAILVDGGLT 252
PRK12827 PRK12827
short chain dehydrogenase; Provisional
1-235 1.07e-34

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 124.06  E-value: 1.07e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYV-------HYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH- 72
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVldihpmrGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEe 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 --PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQ-RRSGNIVLVSSIWGQIGASCEVLYSMVK 149
Cdd:PRK12827  85 fgRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYAASK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEEdknEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQI 228
Cdd:PRK12827 165 AGLIGLTKTLANELAPRGITVNAVAPGAINTPMAdNAAPTE---HLLNPVPVQRLGEPDEVAALVAFLVSDAASYVTGQV 241

                 ....*..
gi 446682265 229 IGVNGGW 235
Cdd:PRK12827 242 IPVDGGF 248
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
35-235 2.12e-34

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: 123.24  E-value: 2.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  35 NSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKL 111
Cdd:cd05347   41 KAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEdfgKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFV 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 112 LSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEED 190
Cdd:cd05347  121 SQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMtEAVVADPE 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446682265 191 KNE-IAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:cd05347  201 FNDdILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIFVDGGW 246
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
36-235 2.87e-34

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: 122.96  E-value: 2.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  36 SEEKVNELQKeWDEVIPVQANLASTDGAEQLWKQIEHpLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMA 115
Cdd:cd05368   35 NEEKLKELER-GPGITTRVLDVTDKEQVAALAKEEGR-IDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 116 LPSMIQRRSGNIVLVSSIWGQI-GASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML------NVFSE 188
Cdd:cd05368  113 LPKMLARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLeeriqaQPDPE 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446682265 189 EDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:cd05368  193 EALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGGW 239
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
49-236 8.91e-34

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: 121.75  E-value: 8.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  49 EVIPVQANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRsG 125
Cdd:cd05364   56 KILLVVADLTEEEGQDRIISTtLAKfgRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-G 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 126 NIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNV--FSEEDKNE----IAEEIP 199
Cdd:cd05364  135 EIVNVSSVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRmgMPEEQYIKflsrAKETHP 214
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446682265 200 LGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:cd05364  215 LGRPGTVDEVAEAIAFLASDASSFITGQLLPVDGGRH 251
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
20-213 1.29e-33

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 121.52  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNsEEKVNELQKE----WDEVIPVQANLASTDGAEQLWKQIE---HPLDVIVYAAGKSIFGLVTDV 92
Cdd:COG0300   23 RALAARGARVVLVARD-AERLEALAAElraaGARVEVVALDVTDPDAVAALAEAVLarfGPIDVLVNNAGVGGGGPFEEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:COG0300  102 DLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTA 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446682265 173 VAPGAIETEMLNVFSEEDKNEIAEeiplgrlglPEEVAKTV 213
Cdd:COG0300  182 VCPGPVDTPFTARAGAPAGRPLLS---------PEEVARAI 213
PRK12829 PRK12829
short chain dehydrogenase; Provisional
36-234 1.71e-33

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 121.32  E-value: 1.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  36 SEEKVNELQKEWDE--VIPVQANLASTDGAEQLWK-QIEH--PLDVIVYAAGksIFGL---VTDVTNDELNDMVELQVKS 107
Cdd:PRK12829  44 SEAALAATAARLPGakVTATVADVADPAQVERVFDtAVERfgGLDVLVNNAG--IAGPtggIDEITPEQWEQTLAVNLNG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 108 IYKLLSMALPSMIQRRSGN-IVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM---- 182
Cdd:PRK12829 122 QFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRmrrv 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 183 -------LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK12829 202 iearaqqLGIGLDEMEQEYLEKISLGRMVEPEDIAATALFLASPAARYITGQAISVDGN 260
PRK09242 PRK09242
SDR family oxidoreductase;
3-234 1.72e-33

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 121.39  E-value: 1.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEkVNELQKEWDEVIP------VQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLGADVLIVARDADA-LAQARDELAEEFPerevhgLAADVSDDEDRRAILDWVEDhwdG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK09242  89 LHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAALL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLN-VFSEEDK-NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:PRK09242 169 QMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSgPLSDPDYyEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQCIAV 248

                 ...
gi 446682265 232 NGG 234
Cdd:PRK09242 249 DGG 251
PRK12937 PRK12937
short chain dehydrogenase; Provisional
3-234 6.55e-33

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 119.46  E-value: 6.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNS----EEKVNELQKEWDEVIPVQANLAST-------DGAEQLWKQIe 71
Cdd:PRK12937   6 KVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSaaaaDELVAEIEAAGGRAIAVQADVADAaavtrlfDAAETAFGRI- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  72 hplDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSiwGQIGASCEV--LYSMVK 149
Cdd:PRK12937  85 ---DVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLST--SVIALPLPGygPYAASK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQI 228
Cdd:PRK12937 158 AAVEGLVHVLANELRGRGITVNAVAPGPVATELfFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQV 237

                 ....*.
gi 446682265 229 IGVNGG 234
Cdd:PRK12937 238 LRVNGG 243
PRK06500 PRK06500
SDR family oxidoreductase;
3-234 7.69e-33

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 119.29  E-value: 7.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVhYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQLWKQI-EH--PLDVIV 78
Cdd:PRK06500   7 KTALITGGTSGIGLETARQFLAEGARVAI-TGRDPASLEAARAELgESALVIRADAGDVAAQKALAQALaEAfgRLDAVF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  79 YAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPsmIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKA 158
Cdd:PRK06500  86 INAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP--LLANPASIVLNGSINAHIGMPNSSVYAASKAALLSLAKT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 159 LAKEVSLSGIRVNAVAPGAIETEMLNV--FSEEDKNEIAEEI----PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVN 232
Cdd:PRK06500 164 LSGELLPRGIRVNAVSPGPVQTPLYGKlgLPEATLDAVAAQIqalvPLGRFGTPEEIAKAVLYLASDESAFIVGSEIIVD 243

                 ..
gi 446682265 233 GG 234
Cdd:PRK06500 244 GG 245
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
5-235 1.14e-32

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 118.83  E-value: 1.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVHyNNSEEKVNELQKeWDEVIPVQANLASTDGAEQLWKQIEH--PLDVIVYA-A 81
Cdd:cd05361    4 ALVTHARHFAGPASAEALTEDGYTVVCH-DASFADAAERQA-FESENPGTKALSEQKPEELVDAVLQAggAIDVLVSNdY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  82 GKSIFGLVTDVTNDELNDMVE-LQVKSIyKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALA 160
Cdd:cd05361   82 IPRPMNPIDGTSEADIRQAFEaLSIFPF-ALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 161 KEVSLSGIRVNAVAPGAIETEMLNVFSE-----EDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:cd05361  161 KELSRDNILVYAIGPNFFNSPTYFPTSDwennpELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAGGY 240
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
20-218 1.37e-32

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: 118.36  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVhYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTND 95
Cdd:COG4221   23 RALAAAGARVVL-AARRAERLEALAAELgGRALAVPLDVTDEAAVEAAVAAAVAefgRLDVLVNNAGVALLGPLEELDPE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  96 ELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAP 175
Cdd:COG4221  102 DWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEP 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446682265 176 GAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVS 218
Cdd:COG4221  182 GAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALT 224
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
22-237 1.80e-32

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: 118.59  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVHYNNS---EEKVNELQKEWD-EVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTN 94
Cdd:cd05352   28 LAEAGADVAIIYNSApraEEKAEELAKKYGvKTKAYKCDVSSQESVEKTFKQIQKdfgKIDILIANAGITVHKPALDYTY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  95 DELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIG--ASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:cd05352  108 EQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVnrPQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNS 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446682265 173 VAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWHC 237
Cdd:cd05352  188 ISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDLIIDGGYTC 252
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
1-234 3.31e-32

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: 117.86  E-value: 3.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQ-IEH--P 73
Cdd:cd05366    1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEagynAVAVGADVTDKDDVEALIDQaVEKfgS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:cd05366   81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKkLGHGGKIINASSIAGVQGFPNLGAYSASKFAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEE-----------DKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGA 221
Cdd:cd05366  161 RGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEvgeiagkpegeGFAEFSSSIPLGRLSEPEDVAGLVSFLASEDS 240
                        250
                 ....*....|...
gi 446682265 222 SYITGQIIGVNGG 234
Cdd:cd05366  241 DYITGQTILVDGG 253
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
5-234 3.62e-32

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 117.71  E-value: 3.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVHyNNSEEKVNELQKEWDEVIPV-QANLASTDGAEQLWKQIEHPL---DVIVYA 80
Cdd:PRK12936   9 ALVTGASGGIGEEIARLLHAQGAIVGLH-GTRVEKLEALAAELGERVKIfPANLSDRDEVKALGQKAEADLegvDILVNN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  81 AGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALA 160
Cdd:PRK12936  88 AGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLA 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 161 KEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK12936 168 QEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVNGG 241
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
3-234 3.95e-32

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: 117.48  E-value: 3.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWD----EVIPVQANLASTDGAEQLWKQ-IEH--PLD 75
Cdd:cd05358    4 KVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKavggKAIAVQADVSKEEDVVALFQSaIKEfgTLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNS 154
Cdd:cd05358   84 ILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRkSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVKM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 155 YVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFS-EEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVN 232
Cdd:cd05358  164 MTKTLAQEYAPKGIRVNAIAPGAINTPInAEAWDdPEQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTTLFVD 243

                 ..
gi 446682265 233 GG 234
Cdd:cd05358  244 GG 245
PRK06523 PRK06523
short chain dehydrogenase; Provisional
53-234 4.01e-32

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 117.70  E-value: 4.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  53 VQANLASTDGAEQLWKQIEHPL---DVIVYAAGKSI--FGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNI 127
Cdd:PRK06523  54 VAADLTTAEGCAAVARAVLERLggvDILVHVLGGSSapAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 128 VLVSSIWGQIGASCEVL-YSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEedknEIAEE--------- 197
Cdd:PRK06523 134 IHVTSIQRRLPLPESTTaYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAE----RLAEAagtdyegak 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446682265 198 ---------IPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK06523 210 qiimdslggIPLGRPAEPEEVAELIAFLASDRAASITGTEYVIDGG 255
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
20-189 9.56e-32

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 115.02  E-value: 9.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   20 KQLIQDGYTVYVHYNNSE---EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVT 93
Cdd:pfam00106  18 KRLAKEGAKVVLVDRSEEkleAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVErlgRLDILVNNAGITGLGPFSELS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   94 NDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAV 173
Cdd:pfam00106  98 DEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAV 177
                         170
                  ....*....|....*.
gi 446682265  174 APGAIETEMLNVFSEE 189
Cdd:pfam00106 178 APGGVDTDMTKELRED 193
PRK12747 PRK12747
short chain dehydrogenase; Provisional
3-234 9.82e-32

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 116.71  E-value: 9.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNN----SEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHPL---- 74
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIHYGNrkeeAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELqnrt 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 -----DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVK 149
Cdd:PRK12747  85 gstkfDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAYSMTK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAEEI-PLGRLGLPEEVAKTVSFLVSPGASYITGQ 227
Cdd:PRK12747 163 GAINTMTFTLAKQLGARGITVNAILPGFIKTDMnAELLSDPMMKQYATTIsAFNRLGEVEDIADTAAFLASPDSRWVTGQ 242

                 ....*..
gi 446682265 228 IIGVNGG 234
Cdd:PRK12747 243 LIDVSGG 249
PRK07814 PRK07814
SDR family oxidoreductase;
52-234 1.36e-31

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 116.42  E-value: 1.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  52 PVQANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRR-SGNI 127
Cdd:PRK07814  63 VVAADLAHPEATAGLAGQaVEAfgRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSV 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 128 VLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSlSGIRVNAVAPGAIETEMLNVFSEED--KNEIAEEIPLGRLGL 205
Cdd:PRK07814 143 INISSTMGRLAGRGFAAYGTAKAALAHYTRLAALDLC-PRIRVNAIAPGSILTSALEVVAANDelRAPMEKATPLRRLGD 221
                        170       180
                 ....*....|....*....|....*....
gi 446682265 206 PEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK07814 222 PEDIAAAAVYLASPAGSYLTGKTLEVDGG 250
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
37-234 1.54e-31

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 116.20  E-value: 1.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIE---HPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYkLLS 113
Cdd:PRK08213  50 EEAAAHLEALGIDALWIAADVADEADIERLAEETLerfGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLF-LLS 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 114 MALP--SMIQRRSGNIVLVSSIWGQIGASCEVL----YSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFS 187
Cdd:PRK08213 129 QAVAkrSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTL 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446682265 188 EEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08213 209 ERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASKHITGQILAVDGG 255
PRK06138 PRK06138
SDR family oxidoreductase;
74-235 5.14e-31

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 114.86  E-value: 5.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK06138  82 LDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLN-VFSEEDKNEIAEEI-----PLGRLGLPEEVAKTVSFLVSPGASYITGQ 227
Cdd:PRK06138 162 SLTRAMALDHATDGIRVNAVAPGTIDTPYFRrIFARHADPEALREAlrarhPMNRFGTAEEVAQAALFLASDESSFATGT 241

                 ....*...
gi 446682265 228 IIGVNGGW 235
Cdd:PRK06138 242 TLVVDGGW 249
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
22-234 7.01e-31

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: 113.91  E-value: 7.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVHYNNSEEKVNELQKE----WDEVIPVQANLASTDGAEQLWKQIE---HPLDVIVYAAgkSIFGL--VTDV 92
Cdd:cd05357   20 LAAEGYRVVVHYNRSEAEAQRLKDElnalRNSAVLVQADLSDFAACADLVAAAFrafGRCDVLVNNA--SAFYPtpLGQG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMVELQVKSIYkLLSMAL-PSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSlSGIRVN 171
Cdd:cd05357   98 SEDAWAELFGINLKAPY-LLIQAFaRRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSAALELA-PNIRVN 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 172 AVAPGAIetemlnVFSEEDKNEIAE----EIPLGRLGLPEEVAKTVSFLVSPGasYITGQIIGVNGG 234
Cdd:cd05357  176 GIAPGLI------LLPEDMDAEYREnalrKVPLKRRPSAEEIADAVIFLLDSN--YITGQIIKVDGG 234
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
37-234 7.46e-31

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 114.51  E-value: 7.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWK---QIEHPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLS 113
Cdd:PRK08226  43 EKLADELCGRGHRCTAVVADVRDPASVAAAIKrakEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTK 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 114 MALPSMIQRRSGNIVLVSSIWGQIGASC-EVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDK- 191
Cdd:PRK08226 123 AVLPEMIARKDGRIVMMSSVTGDMVADPgETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSNp 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446682265 192 -------NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08226 203 edpesvlTEMAKAIPLRRLADPLEVGELAAFLASDESSYLTGTQNVIDGG 252
PRK06172 PRK06172
SDR family oxidoreductase;
87-234 9.32e-31

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 114.08  E-value: 9.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  87 GLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLS 166
Cdd:PRK06172  99 GRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKK 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446682265 167 GIRVNAVAPGAIETEMLNVFSEEDKnEIAEEI----PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK06172 179 GIRVNAVCPAVIDTDMFRRAYEADP-RKAEFAaamhPVGRIGKVEEVASAVLYLCSDGASFTTGHALMVDGG 249
PRK06484 PRK06484
short chain dehydrogenase; Validated
53-237 1.31e-30

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 118.03  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  53 VQANLASTDGAEQLWKQIEHP---LDVIVYAAGksIFG----LVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRS 124
Cdd:PRK06484  56 LAMDVSDEAQIREGFEQLHREfgrIDVLVNNAG--VTDptmtATLDTTLEEFARLQAINLTGAYLVAREALRLMIeQGHG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 125 GNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEE---DKNEIAEEIPLG 201
Cdd:PRK06484 134 AAIVNVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAgklDPSAVRSRIPLG 213
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446682265 202 RLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWHC 237
Cdd:PRK06484 214 RLGRPEEIAEAVFFLASDQASYITGSTLVVDGGWTV 249
PRK09730 PRK09730
SDR family oxidoreductase;
3-234 5.27e-30

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 111.87  E-value: 5.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHY----NNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLD 75
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYqqnlHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQhdePLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAGkSIFGLVT--DVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGN---IVLVSSIWGQIGASCE-VLYSMVK 149
Cdd:PRK09730  82 ALVNNAG-ILFTQCTveNLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGAPGEyVDYAASK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDK-NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQI 228
Cdd:PRK09730 161 GAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRvDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSF 240

                 ....*.
gi 446682265 229 IGVNGG 234
Cdd:PRK09730 241 IDLAGG 246
PRK06124 PRK06124
SDR family oxidoreductase;
74-234 9.65e-30

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 111.34  E-value: 9.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK06124  89 LDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLT 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPG--AIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:PRK06124 169 GLMRALAAEFGPHGITSNAIAPGyfATETNAAMAADPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAV 248

                 ...
gi 446682265 232 NGG 234
Cdd:PRK06124 249 DGG 251
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
3-236 1.23e-29

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: 111.09  E-value: 1.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYV---HYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWK---QIEHPLDV 76
Cdd:cd08936   11 KVALVTASTDGIGLAIARRLAQDGAHVVVssrKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAtavNLHGGVDI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVY-AAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:cd08936   91 LVSnAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLGL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 156 VKALAKEVSLSGIRVNAVAPGAIETEMLNVF--SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:cd08936  171 TKNLAPELAPRNIRVNCLAPGLIKTSFSSALwmDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVGG 250

                 ...
gi 446682265 234 GWH 236
Cdd:cd08936  251 GTP 253
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
5-234 3.55e-29

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: 109.94  E-value: 3.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE---EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIV 78
Cdd:cd08945    6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEglaTTVKELREAGVEADGRTCDVRSVPEIEALVAAAVArygPIDVLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  79 YAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLS--MALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYV 156
Cdd:cd08945   86 NNAGRSGGGATAELADELWLDVVETNLTGVFRVTKevLKAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVGFT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 157 KALAKEVSLSGIRVNAVAPGAIETEM-----------LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYIT 225
Cdd:cd08945  166 KALGLELARTGITVNAVCPGFVETPMaasvrehyadiWEVSTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAAAVT 245

                 ....*....
gi 446682265 226 GQIIGVNGG 234
Cdd:cd08945  246 AQALNVCGG 254
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
22-236 4.45e-29

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 109.24  E-value: 4.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVHYNNSEEKVNELQKEWDEV----IPVQANLASTDGAEQLWKQI-EH--PLDVIVYAAGKSIFGLVTDVTN 94
Cdd:NF012208  18 LAREGFDVAVHYRRSAEAAEQTAQEAEALgvkaITLQADLTDPEQARSLVEEAaEAlgGLSVLVNNVGNYLHKPLLETTD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  95 DELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQ--IGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNA 172
Cdd:NF012208  98 EEWHEMLDSNLNATFYVTQAALPLMRAAGWGRIVNLGYAGAQnlLARPGITPYVIAKTGVIIYSKALAKELAGDGITVNV 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 173 VAPGAIEtemlNVFSEEDkneiaEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:NF012208 178 VSPGVAE----NSVSQPL-----PEIPAGRPATLEELADAVLFFVRPSSDYITGQVLEVAGGWN 232
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
3-234 8.56e-29

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: 108.70  E-value: 8.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQLWKQI-EH--PLDVIV 78
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAgERAIAIQADVRDRDQVQAMIEEAkNHfgPVDTIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  79 YAA-GKSIFGLVTDVTNDEL-----NDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:cd05349   81 NNAlIDFPFDPDQRKTFDTIdwedyQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAI-ETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:cd05349  161 LGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNLVV 240

                 ...
gi 446682265 232 NGG 234
Cdd:cd05349  241 DGG 243
PRK06484 PRK06484
short chain dehydrogenase; Validated
26-235 1.08e-28

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 113.02  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  26 GYTVYVHYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAG-KSIFGLVTDVTNDELNDMV 101
Cdd:PRK06484 293 GDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQArwgRLDVLVNNAGiAEVFKPSLEQSAEDFTRVY 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 102 ELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETE 181
Cdd:PRK06484 373 DVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETP 450
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 182 MLNVF---SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK06484 451 AVLALkasGRADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGGW 507
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
3-234 3.06e-28

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: 107.18  E-value: 3.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE--EKVNELQKEWDEVIPVQANLASTDGAEQLWKQI---EHPLDVI 77
Cdd:cd08942    7 KIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEacADAAEELSAYGECIAIPADLSSEEGIEALVARVaerSDRLDVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  78 VYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGN------IVLVSSIWGQIGASCEVL-YSMVKG 150
Cdd:cd08942   87 VNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLL--RAAATaenparVINIGSIAGIVVSGLENYsYGASKA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 151 AQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSE--EDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQI 228
Cdd:cd08942  165 AVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNdpAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAYLTGAV 244

                 ....*.
gi 446682265 229 IGVNGG 234
Cdd:cd08942  245 IPVDGG 250
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
2-236 3.78e-28

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 107.02  E-value: 3.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   2 KKYALVTGGSGGIGSAISKQLIQDGYTVYVHYN-NSEEKVNELQKEWD---EVIPVQANLASTDGAEQLWKQIEHP---L 74
Cdd:PRK12938   3 QRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGpNSPRRVKWLEDQKAlgfDFIASEGNVGDWDSTKAAFDKVKAEvgeI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNS 154
Cdd:PRK12938  83 DVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIHG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 155 YVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK12938 163 FTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFSLNGG 242

                 ..
gi 446682265 235 WH 236
Cdd:PRK12938 243 LH 244
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
89-235 1.60e-27

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 105.04  E-value: 1.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  89 VTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGI 168
Cdd:PRK06550  84 LLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLALDYAKDGI 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 169 RVNAVAPGAIETEMLNVFSEEDK--NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK06550 164 QVFGIAPGAVKTPMTAADFEPGGlaDWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTIVPIDGGW 232
PRK12828 PRK12828
short chain dehydrogenase; Provisional
48-234 1.93e-27

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 104.88  E-value: 1.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  48 DEVIPVQANLASTDGAEQLWKqiehpLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNI 127
Cdd:PRK12828  62 DLVDPQAARRAVDEVNRQFGR-----LDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 128 VLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMlnvfseedkneIAEEIPLGRLG--- 204
Cdd:PRK12828 137 VNIGAGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPP-----------NRADMPDADFSrwv 205
                        170       180       190
                 ....*....|....*....|....*....|
gi 446682265 205 LPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK12828 206 TPEQIAAVIAFLLSDEAQAITGASIPVDGG 235
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
73-234 2.34e-27

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: 104.78  E-value: 2.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIF-GLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGA 151
Cdd:cd05345   79 RLDILVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGW 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 152 QNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEE----IPLGRLGLPEEVAKTVSFLVSPGASYITGQ 227
Cdd:cd05345  159 VVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGEDTPENRAKfratIPLGRLSTPDDIANAALYLASDEASFITGV 238

                 ....*..
gi 446682265 228 IIGVNGG 234
Cdd:cd05345  239 ALEVDGG 245
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-234 2.41e-27

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 104.80  E-value: 2.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNS----EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP--- 73
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSrkaaEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEfgr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIwgqigASCEVL--YSMV--- 148
Cdd:PRK08063  83 LDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSL-----GSIRYLenYTTVgvs 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 149 KGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFS--EEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITG 226
Cdd:PRK08063 158 KAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPnrEELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIRG 237

                 ....*...
gi 446682265 227 QIIGVNGG 234
Cdd:PRK08063 238 QTIIVDGG 245
PRK06123 PRK06123
SDR family oxidoreductase;
1-234 7.26e-27

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 103.71  E-value: 7.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHY----NNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLNYlrnrDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRelgR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKsifgLVTDVTNDELnDMVELQ------VKSIYKLLSMALPSMIQR---RSGNIVLVSSIWGQIGASCE-V 143
Cdd:PRK06123  81 LDALVNNAGI----LEAQMRLEQM-DAARLTrifatnVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGEyI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 144 LYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNE-IAEEIPLGRLGLPEEVAKTVSFLVSPGAS 222
Cdd:PRK06123 156 DYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDrVKAGIPMGRGGTAEEVARAILWLLSDEAS 235
                        250
                 ....*....|..
gi 446682265 223 YITGQIIGVNGG 234
Cdd:PRK06123 236 YTTGTFIDVSGG 247
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
74-234 1.80e-26

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: 103.14  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGL-VTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:cd05355  106 LDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKGAI 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:cd05355  184 VAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIpSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVLHV 263

                 ...
gi 446682265 232 NGG 234
Cdd:cd05355  264 NGG 266
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-234 2.32e-26

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 102.55  E-value: 2.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDEVIpvQANLASTDGAEQLWKQIEHPL---DVIVY 79
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGVFTI--KCDVGNRDQVKKSKEVVEKEFgrvDVLVN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  80 AAGKSIFGLVTDVTNDELNDMVELQVK-SIYKLLSmALPSMIQRRSGNIVLVSSIWGqIGASCE--VLYSMVKGAQNSYV 156
Cdd:PRK06463  86 NAGIMYLMPFEEFDEEKYNKMIKINLNgAIYTTYE-FLPLLKLSKNGAIVNIASNAG-IGTAAEgtTFYAITKAGIIILT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 157 KALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAE----EIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:PRK06463 164 RRLAFELGKYGIRVNAVAPGWVETDMtLSGKSQEEAEKLRElfrnKTVLKTTGKPEDIANIVLFLASDDARYITGQVIVA 243

                 ...
gi 446682265 232 NGG 234
Cdd:PRK06463 244 DGG 246
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-234 2.37e-26

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 102.50  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYV-HYN--NSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP---L 74
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIvDYNeeTAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTfgdL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSM-IQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK08643  81 NVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFkKLGHGGKIINATSQAGVVGNPELAVYSSTKFAVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEML-----NVFSEEDK------NEIAEEIPLGRLGLPEEVAKTVSFLVSPGAS 222
Cdd:PRK08643 161 GLTQTAARDLASEGITVNAYAPGIVKTPMMfdiahQVGENAGKpdewgmEQFAKDITLGRLSEPEDVANCVSFLAGPDSD 240
                        250
                 ....*....|..
gi 446682265 223 YITGQIIGVNGG 234
Cdd:PRK08643 241 YITGQTIIVDGG 252
PRK12743 PRK12743
SDR family oxidoreductase;
1-234 2.92e-26

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 102.42  E-value: 2.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEHPL-- 74
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRShgvrAEIRQLDLSDLPEGAQALDKLIQRLgr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 -DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSSI---WGQIGAScevLYSMVK 149
Cdd:PRK12743  81 iDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVkQGQGGRIINITSVhehTPLPGAS---AYTAAK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQII 229
Cdd:PRK12743 158 HALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSL 237

                 ....*
gi 446682265 230 GVNGG 234
Cdd:PRK12743 238 IVDGG 242
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
37-236 5.12e-26

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: 101.51  E-value: 5.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWD-EVIPVQANLASTDGAEQLWKQIEH---PLDVIVY-AAGKSI----------FGLVTD-VTNDELNdm 100
Cdd:cd05369   41 EAAAEEISSATGgRAHPIQCDVRDPEAVEAAVDETLKefgKIDILINnAAGNFLapaeslspngFKTVIDiDLNGTFN-- 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 101 velQVKSIYKLLsmalpsMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIET 180
Cdd:cd05369  119 ---TTKAVGKRL------IEAKHGGSILNISATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPT 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 181 E--MLNVFSEEDKN-EIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG-WH 236
Cdd:cd05369  190 TegMERLAPSGKSEkKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTTLVVDGGqWL 249
PRK12746 PRK12746
SDR family oxidoreductase;
3-235 5.75e-26

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 101.65  E-value: 5.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNN----SEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHPL---- 74
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIHYGRnkqaADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELqirv 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 -----DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVK 149
Cdd:PRK12746  87 gtseiDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAYGLSK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSE--EDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQ 227
Cdd:PRK12746 165 GALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDdpEIRNFATNSSVFGRIGQVEDIADAVAFLASSDSRWVTGQ 244

                 ....*...
gi 446682265 228 IIGVNGGW 235
Cdd:PRK12746 245 IIDVSGGF 252
PRK06701 PRK06701
short chain dehydrogenase; Provisional
74-234 6.11e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 102.03  E-value: 6.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAG-----KSIfglvTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMV 148
Cdd:PRK06701 125 LDILVNNAAfqypqQSL----EDITAEQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSAT 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 149 KGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEmLN--VFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITG 226
Cdd:PRK06701 199 KGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP-LIpsDFDEEKVSQFGSNTPMQRPGQPEELAPAYVFLASPDSSYITG 277

                 ....*...
gi 446682265 227 QIIGVNGG 234
Cdd:PRK06701 278 QMLHVNGG 285
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
20-234 9.11e-26

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 101.24  E-value: 9.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYvhynNSEEKVNELQKewDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTND- 95
Cdd:PRK06171  27 KELLANGANVV----NADIHGGDGQH--ENYQFVPTDVSSAEEVNHTVAEIIEkfgRIDGLVNNAGINIPRLLVDEKDPa 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  96 ---ELND-----MVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSG 167
Cdd:PRK06171 101 gkyELNEaafdkMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 168 IRVNAVAPGAIE-TEMLNVFSEED----KNEIAEE----------IPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVN 232
Cdd:PRK06171 181 IRVVGVAPGILEaTGLRTPEYEEAlaytRGITVEQlragytktstIPLGRSGKLSEVADLVCYLLSDRASYITGVTTNIA 260

                 ..
gi 446682265 233 GG 234
Cdd:PRK06171 261 GG 262
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
3-218 1.14e-25

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: 99.74  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNsEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVY 79
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRN-PEDLAALSASGGDVEAVPYDARDPEDARALVDALRDrfgRIDVLVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  80 AAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKAL 159
Cdd:cd08932   80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHAL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 160 AKEVSLSGIRVNAVAPGAIETEMLNVFSEEdkneiaEEIPLGRLGLPEEVAKTVSFLVS 218
Cdd:cd08932  160 RQEGWDHGVRVSAVCPGFVDTPMAQGLTLV------GAFPPEEMIQPKDIANLVRMVIE 212
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
36-234 1.41e-25

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: 100.34  E-value: 1.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  36 SEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHPL---DVIVYAAGKSIFG-LVTDVTNDELNDMVELQVKSIYKL 111
Cdd:cd05365   36 AEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFggiTILVNNAGGGGPKpFDMPMTEEDFEWAFKLNLFSAFRL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 112 LSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEED 190
Cdd:cd05365  116 SQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALaSVLTPEI 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446682265 191 KNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd05365  196 ERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
PRK07035 PRK07035
SDR family oxidoreductase;
3-234 2.10e-25

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 99.71  E-value: 2.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVhynnSEEKVNELQKEWDEVI-------PVQANLASTDGAEQLWKQIEHP-- 73
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLAQQGAHVIV----SSRKLDGCQAVADAIVaaggkaeALACHIGEMEQIDALFAHIRERhg 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 -LDVIVY-AAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGA 151
Cdd:PRK07035  85 rLDILVNnAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 152 QNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEED--KNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQII 229
Cdd:PRK07035 165 VISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDaiLKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECL 244

                 ....*
gi 446682265 230 GVNGG 234
Cdd:PRK07035 245 NVDGG 249
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
41-234 2.43e-25

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: 99.47  E-value: 2.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  41 NELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALP 117
Cdd:cd05331   33 VLLLEYGDPLRLTPLDVADAAAVREVCSRLLAehgPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAP 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 118 SMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEEDKNE--- 193
Cdd:cd05331  113 HMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQrTLWHDEDGAAqvi 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446682265 194 --IAEE----IPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd05331  193 agVPEQfrlgIPLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGG 239
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
37-234 5.48e-25

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 99.20  E-value: 5.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELN-------DMVELQVK 106
Cdd:PRK08277  48 EAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEdfgPCDILINGAGGNHPKATTDNEFHELIeptktffDLDEEGFE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 107 SIYKL--LSMALPS------MIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAI 178
Cdd:PRK08277 128 FVFDLnlLGTLLPTqvfakdMVGRKGGNIINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFF 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446682265 179 ETE-----MLNvfseED------KNEIAEEIPLGRLGLPEEVAKTVSFLVSP-GASYITGQIIGVNGG 234
Cdd:PRK08277 208 LTEqnralLFN----EDgslterANKILAHTPMGRFGKPEELLGTLLWLADEkASSFVTGVVLPVDGG 271
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
20-211 6.60e-25

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: 98.09  E-value: 6.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVhYNNSEEK----VNELQKEWDE----VIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGL 88
Cdd:cd08939   19 KELVKEGANVII-VARSESKleeaVEEIEAEANAsgqkVSYISADLSDYEEVEQAFAQAVEkggPPDLVVNCAGISIPGL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  89 VTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGI 168
Cdd:cd08939   98 FEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNI 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446682265 169 RVNAVAPGAIETEMlnvFSEEDKN--EIAEEIPLG-RLGLPEEVAK 211
Cdd:cd08939  178 RVSVVYPPDTDTPG---FEEENKTkpEETKAIEGSsGPITPEEAAR 220
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-237 7.22e-25

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 98.61  E-value: 7.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIG--SAISKQLIQDGYTVYVHY-----------NNSEEKV---NELQKEWDEVIPVQANLASTDGAE 64
Cdd:PRK12748   4 MKKIALVTGASRLNGigAAVCRRLAAKGIDIFFTYwspydktmpwgMHDKEPVllkEEIESYGVRCEHMEIDLSQPYAPN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  65 QLWKQIE----HPLDVIVYAAGKSIFGLVTdVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGAS 140
Cdd:PRK12748  84 RVFYAVSerlgDPSILINNAAYSTHTRLEE-LTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 141 CEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNvfsEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPG 220
Cdd:PRK12748 163 DELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWIT---EELKHHLVPKFPQGRVGEPVDAARLIAFLVSEE 239
                        250
                 ....*....|....*..
gi 446682265 221 ASYITGQIIGVNGGWHC 237
Cdd:PRK12748 240 AKWITGQVIHSEGGFSR 256
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-235 2.29e-24

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 97.11  E-value: 2.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYV--HYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQI--EHP-LDVI 77
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKAGADIIIttHGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEAleEFGkIDIL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  78 VYAAGKSIFGLVTDVTNDELNDMVELQVKSIYkLLSMALPS-MIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYV 156
Cdd:PRK06935  96 VNNAGTIRRAPLLEYKDEDWNAVMDINLNSVY-HLSQAVAKvMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVAGLT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 157 KALAKEVSLSGIRVNAVAPGAIETEmlN---VFSEEDKN-EIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVN 232
Cdd:PRK06935 175 KAFANELAAYNIQVNAIAPGYIKTA--NtapIRADKNRNdEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILAVD 252

                 ...
gi 446682265 233 GGW 235
Cdd:PRK06935 253 GGW 255
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-234 2.43e-24

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 97.08  E-value: 2.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQLWKQIE----HPLD 75
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADELgDRAIALQADVTDREQVQAMFATATehfgKPIT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAgksifgLV------------TDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEV 143
Cdd:PRK08642  84 TVVNNA------LAdfsfdgdarkkaDDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 144 LYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAI-ETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGAS 222
Cdd:PRK08642 158 DYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPWAR 237
                        250
                 ....*....|..
gi 446682265 223 YITGQIIGVNGG 234
Cdd:PRK08642 238 AVTGQNLVVDGG 249
PRK06947 PRK06947
SDR family oxidoreductase;
1-234 3.12e-24

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 96.80  E-value: 3.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNN----SEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP--- 73
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGINYARdaaaAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAfgr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGksIFGL---VTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGN---IVLVSSIWGQIGASCE-VLYS 146
Cdd:PRK06947  81 LDALVNNAG--IVAPsmpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGSPNEyVDYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 147 MVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNE-IAEEIPLGRLGLPEEVAKTVSFLVSPGASYIT 225
Cdd:PRK06947 159 GSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAArLGAQTPLGRAGEADEVAETIVWLLSDAASYVT 238

                 ....*....
gi 446682265 226 GQIIGVNGG 234
Cdd:PRK06947 239 GALLDVGGG 247
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
5-236 3.67e-24

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: 96.76  E-value: 3.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVHYN----NSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIE---HPLDVI 77
Cdd:cd05337    4 AIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWedfGRLDCL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  78 VYAAGKSIFGL--VTDVTNDELNDMVELQVKSIYKLLSMALPSMI------QRRSGNIVLVSSIWGQIGASCEVLYSMVK 149
Cdd:cd05337   84 VNNAGIAVRPRgdLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVeqpdrfDGPHRSIIFVTSINAYLVSPNRGEYCISK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAE-EIPLGRLGLPEEVAKTVSFLVSPGASYITGQI 228
Cdd:cd05337  164 AGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAgLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQP 243

                 ....*...
gi 446682265 229 IGVNGGWH 236
Cdd:cd05337  244 INIDGGLS 251
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
38-234 5.96e-24

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: 96.06  E-value: 5.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  38 EKVNELQKE----WDEVIPVQANLASTDGAEQLWKQIEHP---LDVIVYAAGKSIFGLVTDVTNDElndMVELQV-KSIY 109
Cdd:cd08937   38 ELVHEVLAEilaaGDAAHVHTADLETYAGAQGVVRAAVERfgrVDVLINNVGGTIWAKPYEHYEEE---QIEAEIrRSLF 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 110 KLL---SMALPSMIQRRSGNIVLVSSIWGQIGAscEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNV- 185
Cdd:cd08937  115 PTLwccRAVLPHMLERQQGVIVNVSSIATRGIY--RIPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIp 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 186 -----FSEEDK-------NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd08937  193 rnaapMSEQEKvwyqrivDQTLDSSLMGRYGTIDEQVRAILFLASDEASYITGTVLPVGGG 253
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
52-234 1.34e-23

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 94.95  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  52 PVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIV 128
Cdd:PRK08220  52 TFVLDVSDAAAVAQVCQRLLAetgPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIV 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 129 LVSSIWG-----QIGAscevlYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEED--KNEIA---EE 197
Cdd:PRK08220 132 TVGSNAAhvpriGMAA-----YGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQrTLWVDEDgeQQVIAgfpEQ 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446682265 198 ----IPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08220 207 fklgIPLGKIARPQEIANAVLFLASDLASHITLQDIVVDGG 247
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
102-234 2.37e-23

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 94.53  E-value: 2.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 102 ELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETE 181
Cdd:PRK06113 116 ELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446682265 182 ML-NVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK06113 196 ALkSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGG 249
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
3-235 3.87e-23

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: 93.69  E-value: 3.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVyVHYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIeHPLDVIVYAAG 82
Cdd:cd05351    8 KRALVTGAGKGIGRATVKALAKAGARV-VAVSRTQADLDSLVRECPGIEPVCVDLSDWDATEEALGSV-GPVDLLVNNAA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  83 KSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRR-SGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAK 161
Cdd:cd05351   86 VAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMAL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265 162 EVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNE-IAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:cd05351  166 ELGPHKIRVNSVNPTVVMTDMgRDNWSDPEKAKkMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGGF 241
PRK07890 PRK07890
short chain dehydrogenase; Provisional
74-234 1.09e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 92.71  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVY-AAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRsGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:PRK07890  83 VDALVNnAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKMAKGAL 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEMLN-----------VFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGA 221
Cdd:PRK07890 162 LAASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfrhqagkygVTVEQIYAETAANSDLKRLPTDDEVASAVLFLASDLA 241
                        170
                 ....*....|...
gi 446682265 222 SYITGQIIGVNGG 234
Cdd:PRK07890 242 RAITGQTLDVNCG 254
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
3-235 1.09e-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: 92.45  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVY 79
Cdd:cd05341    6 KVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREafgRLDVLVN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  80 AAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKAL 159
Cdd:cd05341   86 NAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKSA 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 160 AKEVSL--SGIRVNAVAPGAIETEML-NVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:cd05341  166 ALECATqgYGIRVNSVHPGYIYTPMTdELLIAQGEMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSELVVDGGY 244
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
24-234 1.38e-22

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 92.48  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  24 QDGYTVYVHYNNSEEK----VNELQKEWDEVIPVQANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDE 96
Cdd:PRK08936  29 KEKAKVVINYRSDEEEandvAEEIKKAGGEAIAVKGDVTVESDVVNLIQTaVKEfgTLDVMINNAGIENAVPSHEMSLED 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  97 LNDMVELQVKSIYKLLSMALPSMIQR-RSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAP 175
Cdd:PRK08936 109 WNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGP 188
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446682265 176 GAIETEmLNV--FSE-EDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08936 189 GAINTP-INAekFADpKQRADVESMIPMGYIGKPEEIAAVAAWLASSEASYVTGITLFADGG 249
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
48-234 1.93e-22

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 92.01  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  48 DEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGksIFGL--VTDVTNDELNDMVELQVKSIYKLLSMALPSMIQR 122
Cdd:PRK07067  52 PAAIAVSLDVTRQDSIDRIVAAAVErfgGIDILFNNAA--LFDMapILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQ 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 123 -RSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSE-----------ED 190
Cdd:PRK07067 130 gRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVDAlfaryenrppgEK 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446682265 191 KNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK07067 210 KRLVGEAVPLGRMGVPDDLTGMALFLASADADYIVAQTYNVDGG 253
PRK06398 PRK06398
aldose dehydrogenase; Validated
64-234 2.64e-22

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 91.82  E-value: 2.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  64 EQLWKQIEH------PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQI 137
Cdd:PRK06398  57 EQVIKGIDYviskygRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 138 GASCEVLYSMVKGAQNSYVKALAKEVSlSGIRVNAVAPGAIETEMLNVFSE----EDKNEIAEEI-------PLGRLGLP 206
Cdd:PRK06398 137 VTRNAAAYVTSKHAVLGLTRSIAVDYA-PTIRCVAVCPGSIRTPLLEWAAElevgKDPEHVERKIrewgemhPMKRVGKP 215
                        170       180
                 ....*....|....*....|....*...
gi 446682265 207 EEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK06398 216 EEVAYVVAFLASDLASFITGECVTVDGG 243
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
115-234 4.82e-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: 91.01  E-value: 4.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 115 ALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEI 194
Cdd:cd08944  120 AAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGAL 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446682265 195 AEEI-------PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd08944  200 GPGGfhllihqLQGRLGRPEDVAAAVVFLLSDDASFITGQVLCVDGG 246
PRK08589 PRK08589
SDR family oxidoreductase;
37-234 9.93e-22

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 90.61  E-value: 9.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP---LDVIVYAAG-KSIFGLVTDVTNDELNDMVELQVKSIYKLL 112
Cdd:PRK08589  43 SETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQfgrVDVLFNNAGvDNAAGRIHEYPVDVFDKIMAVDMRGTFLMT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 113 SMALPSMIQRrSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKN 192
Cdd:PRK08589 123 KMLLPLMMEQ-GGSIINTSSFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSED 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446682265 193 EIAEEI--------PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08589 202 EAGKTFrenqkwmtPLGRLGKPEEVAKLVVFLASDDSSFITGETIRIDGG 251
PRK07063 PRK07063
SDR family oxidoreductase;
48-234 1.69e-21

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 89.72  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  48 DEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRS 124
Cdd:PRK07063  58 ARVLAVPADVTDAASVAAAVAAAEEafgPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGR 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 125 GNIVLVSSIWG-QIGASCeVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML----NVFS--EEDKNEIAEE 197
Cdd:PRK07063 138 GSIVNIASTHAfKIIPGC-FPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTedwwNAQPdpAAARAETLAL 216
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446682265 198 IPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK07063 217 QPMKRIGRPEEVAMTAVFLASDEAPFINATCITIDGG 253
PRK07774 PRK07774
SDR family oxidoreductase;
115-235 1.79e-21

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 89.42  E-value: 1.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 115 ALPSMIQRRSGNIVLVSSI--WGQIGascevLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEED-K 191
Cdd:PRK07774 128 VYKHMAKRGGGAIVNQSSTaaWLYSN-----FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEfV 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446682265 192 NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK07774 203 ADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQIFNVDGGQ 246
PRK07856 PRK07856
SDR family oxidoreductase;
53-234 2.57e-21

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 88.84  E-value: 2.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  53 VQANLASTDGAEQLWKQI--EHP-LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGN-IV 128
Cdd:PRK07856  52 HAADVRDPDQVAALVDAIveRHGrLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGGsIV 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 129 LVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSlSGIRVNAVAPGAIETEMLNVF--SEEDKNEIAEEIPLGRLGLP 206
Cdd:PRK07856 132 NIGSVSGRRPSPGTAAYGAAKAGLLNLTRSLAVEWA-PKVRVNAVVVGLVRTEQSELHygDAEGIAAVAATVPLGRLATP 210
                        170       180
                 ....*....|....*....|....*...
gi 446682265 207 EEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK07856 211 ADIAWACLFLASDLASYVSGANLEVHGG 238
PRK08628 PRK08628
SDR family oxidoreductase;
38-235 7.10e-21

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 88.09  E-value: 7.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  38 EKVNELQKEWDEVIPVQANLASTDGAEQLWKQI--EH-PLDVIVYAAGKSIfGLVTDVTNDELNDMVELQVKSIYKLLSM 114
Cdd:PRK08628  45 EFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTvaKFgRIDGLVNNAGVND-GVGLEAGREAFVASLERNLIHYYVMAHY 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 115 ALPSMIQRRsGNIVLVSS---IWGQIGASCevlYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM----LNVFS 187
Cdd:PRK08628 124 CLPHLKASR-GAIVNISSktaLTGQGGTSG---YAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLyenwIATFD 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446682265 188 --EEDKNEIAEEIPLG-RLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK08628 200 dpEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHTTGQWLFVDGGY 250
PRK07060 PRK07060
short chain dehydrogenase; Provisional
73-235 8.40e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 87.46  E-value: 8.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSSIWGQIGASCEVLYSMVKGA 151
Cdd:PRK07060  77 AFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIaAGRGGSIVNVSSQAALVGLPDHLAYCASKAA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 152 QNSYVKALAKEVSLSGIRVNAVAPGAIETEMLN-VFSEEDKNEIA-EEIPLGRLGLPEEVAKTVSFLVSPGASYITGQII 229
Cdd:PRK07060 157 LDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAeAWSDPQKSGPMlAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSL 236

                 ....*.
gi 446682265 230 GVNGGW 235
Cdd:PRK07060 237 PVDGGY 242
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
111-235 9.42e-21

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 87.53  E-value: 9.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 111 LLSMALPSMIQRRSGN-IVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNvfsEE 189
Cdd:PRK12859 133 LLSSQFARGFDKKSGGrIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMT---EE 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446682265 190 DKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK12859 210 IKQGLLPMFPFGRIGEPKDAARLIKFLASEEAEWITGQIIHSEGGF 255
PRK05867 PRK05867
SDR family oxidoreductase;
3-237 1.55e-20

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 87.01  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYV---HYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHPL---DV 76
Cdd:PRK05867  10 KRALITGASTGIGKRVALAYVEAGAQVAIaarHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELggiDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSSIWGQIGASCEVL--YSMVKGAQN 153
Cdd:PRK05867  90 AVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVkQGQGGVIINTASMSGHIINVPQQVshYCASKAAVI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKnEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:PRK05867 170 HLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQP-LWEPKIPLGRLGRPEELAGLYLYLASEASSYMTGSDIVIDG 248

                 ....
gi 446682265 234 GWHC 237
Cdd:PRK05867 249 GYTC 252
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
33-234 1.80e-20

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: 86.62  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  33 YNNSEEKVNELQKEWD-EVIPVQANLASTDGAEQLWKQIEHPLDVI------VYAAGKSIFGLVTDVTNDELNDMVELQV 105
Cdd:cd08930   36 APALEQLKEELTNLYKnRVIALELDITSKESIKELIESYLEKFGRIdilinnAYPSPKVWGSRFEEFPYEQWNEVLNVNL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 106 KSiYKLLSMA-LPSMIQRRSGNIVLVSSIWGQIGASCEVL----------YSMVKGAQNSYVKALAKEVSLSGIRVNAVA 174
Cdd:cd08930  116 GG-AFLCSQAfIKLFKKQGKGSIINIASIYGVIAPDFRIYentqmyspveYSVIKAGIIHLTKYLAKYYADTGIRVNAIS 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 175 PGAIETEMLNVFSEEDKNEIaeeiPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd08930  195 PGGILNNQPSEFLEKYTKKC----PLKRMLNPEDLRGAIIFLLSDASSYVTGQNLVIDGG 250
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
91-234 2.09e-20

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: 86.82  E-value: 2.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  91 DVTNDELNDMVELQVKSIYKLLSMALPSMIQRRsGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRV 170
Cdd:cd08933  106 ETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRV 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 171 NAVAPGAIETEMLNVFSEEDKNEIA------EEIPLGRLGLPEEVAKTVSFLVSPgASYITGQIIGVNGG 234
Cdd:cd08933  185 NCISPGNIWTPLWEELAAQTPDTLAtikegeLAQLLGRMGTEAESGLAALFLAAE-ATFCTGIDLLLSGG 253
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
20-235 3.35e-20

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 86.19  E-value: 3.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVhYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTN-- 94
Cdd:cd05371   20 ERLLAQGAKVVI-LDLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALAKAkfgRLDIVVNCAGIAVAAKTYNKKGqq 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  95 ----DELNDMVELQVKSIYKLLSMALPSMI--------QRrsGNIVLVSSIW---GQIGascEVLYSMVKGAQNSYVKAL 159
Cdd:cd05371   99 phslELFQRVINVNLIGTFNVIRLAAGAMGknepdqggER--GVIINTASVAafeGQIG---QAAYSASKGGIVGMTLPI 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 160 AKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIP-LGRLGLPEEVAKTVSFLVSpgASYITGQIIGVNGGW 235
Cdd:cd05371  174 ARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPfPSRLGDPAEYAHLVQHIIE--NPYLNGEVIRLDGAI 248
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
115-234 4.49e-20

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 85.77  E-value: 4.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 115 ALPSMIQRRSGNIVLVSSIwgQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNV------FSE 188
Cdd:PRK12823 127 VLPHMLAQGGGAIVNVSSI--ATRGINRVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPPRRVprnaapQSE 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446682265 189 EDK---NEIAEEI----PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK12823 205 QEKawyQQIVDQTldssLMKRYGTIDEQVAAILFLASDEASYITGTVLPVGGG 257
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
74-235 7.03e-20

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: 85.19  E-value: 7.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:cd08940   82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVV 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEML-----------NVFSEEDKNE-IAEEIPLGRLGLPEEVAKTVSFLVSPGA 221
Cdd:cd08940  162 GLTKVVALETAGTGVTCNAICPGWVLTPLVekqisalaqknGVPQEQAARElLLEKQPSKQFVTPEQLGDTAVFLASDAA 241
                        170
                 ....*....|....
gi 446682265 222 SYITGQIIGVNGGW 235
Cdd:cd08940  242 SQITGTAVSVDGGW 255
PRK06128 PRK06128
SDR family oxidoreductase;
74-236 1.00e-19

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 85.68  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIF-GLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:PRK06128 135 LDILVNIAGKQTAvKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTGSIQSYQPSPTLLDYASTKAAI 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKN--EIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIG 230
Cdd:PRK06128 213 VAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKipDFGSETPMKRPGQPVEMAPLYVLLASQESSYVTGEVFG 292

                 ....*.
gi 446682265 231 VNGGWH 236
Cdd:PRK06128 293 VTGGLL 298
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
53-234 1.17e-19

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 84.47  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  53 VQANLASTDGAEQLWKQI----EHPLDVIVYAAGksifglVTDVTNdelndmVELQVKSIY----KLLSMALPSMIQRRS 124
Cdd:cd05328   36 VIADLSTPEGRAAAIADVlarcSGVLDGLVNCAG------VGGTTV------AGLVLKVNYfglrALMEALLPRLRKGHG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 125 GNIVLVSSI---------------------------WGQIGASCEVLYSMVKGAQNSYVKALAKE-VSLSGIRVNAVAPG 176
Cdd:cd05328  104 PAAVVVSSIagagwaqdklelakalaagtearavalAEHAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPG 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 177 AIETEMLNVF-SEEDKNEIAEEI--PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd05328  184 PVETPILQAFlQDPRGGESVDAFvtPMGRRAEPDEIAPVIAFLASDAASWINGANLFVDGG 244
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
74-234 1.34e-19

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: 84.43  E-value: 1.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKS--IFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGA 151
Cdd:cd05326   80 LDIMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHA 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 152 QNSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEEDknEIAEEI------PLGRLGLPEEVAKTVSFLVSPGASYI 224
Cdd:cd05326  160 VLGLTRSAATELGEHGIRVNCVSPYGVATPLLtAGFGVED--EAIEEAvrgaanLKGTALRPEDIAAAVLYLASDDSRYV 237
                        170
                 ....*....|
gi 446682265 225 TGQIIGVNGG 234
Cdd:cd05326  238 SGQNLVVDGG 247
PRK12742 PRK12742
SDR family oxidoreductase;
3-235 1.53e-19

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 84.04  E-value: 1.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEwDEVIPVQANLASTDGAEQLWKQiEHPLDVIVYAAG 82
Cdd:PRK12742   7 KKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQE-TGATAVQTDSADRDAVIDVVRK-SGALDILVVNAG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  83 KSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQI-----GAScevlYSMVKGAQNSYVK 157
Cdd:PRK12742  85 IAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIIIGSVNGDRmpvagMAA----YAASKSALQGMAR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446682265 158 ALAKEVSLSGIRVNAVAPGAIETEMlNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK12742 159 GLARDFGPRGITINVVQPGPIDTDA-NPANGPMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMHTIDGAF 235
PRK08416 PRK08416
enoyl-ACP reductase;
24-234 2.84e-19

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 83.67  E-value: 2.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  24 QDGYTVYVHYNNSEEKVNELQKEWDEVIPVQA-----NLASTDGAEQLWKQIEHPLD--------VIVYaaGKSI---FG 87
Cdd:PRK08416  30 QSGVNIAFTYNSNVEEANKIAEDLEQKYGIKAkayplNILEPETYKELFKKIDEDFDrvdffisnAIIS--GRAVvggYT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  88 LVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSG 167
Cdd:PRK08416 108 KFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNLVYIENYAGHGTSKAAVETMVKYAATELGEKN 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 168 IRVNAVAPGAIETEMLNVFS--EEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08416 188 IRVNAVSGGPIDTDALKAFTnyEEVKAKTEELSPLNRMGQPEDLAGACLFLCSEKASWLTGQTIVVDGG 256
PRK07576 PRK07576
short chain dehydrogenase; Provisional
36-235 2.98e-19

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 83.85  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  36 SEEKVN----ELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSI 108
Cdd:PRK07576  42 SQEKVDaavaQLQQAGPEGLGVSADVRDYAAVEAAFAQIADefgPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGT 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 109 YKLLSMALPSMiQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIE-TEMLNVF- 186
Cdd:PRK07576 122 FNVLKAAYPLL-RRPGASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgTEGMARLa 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446682265 187 -SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK07576 201 pSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVVLPVDGGW 250
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
3-234 3.11e-19

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: 83.66  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE---EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDV 76
Cdd:cd08935    6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEkgdKVAKEITALGGRAIALAADVLDRASLERAREEIVAqfgTVDI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVYAAGKSIFGLVTDVTNDELN------DMVELQVKSIYKL--LSMALPS------MIQRRSGNIVLVSSIWGQIGASCE 142
Cdd:cd08935   86 LINGAGGNHPDATTDPEHYEPEteqnffDLDEEGWEFVFDLnlNGSFLPSqvfgkdMLEQKGGSIINISSMNAFSPLTKV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 143 VLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEED------KNEIAEEIPLGRLGLPEEVAKTVSF 215
Cdd:cd08935  166 PAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQnRKLLINPDgsytdrSNKILGRTPMGRFGKPEELLGALLF 245
                        250       260
                 ....*....|....*....|
gi 446682265 216 LVSPGAS-YITGQIIGVNGG 234
Cdd:cd08935  246 LASEKASsFVTGVVIPVDGG 265
PRK07062 PRK07062
SDR family oxidoreductase;
73-234 3.95e-19

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 83.55  E-value: 3.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:PRK07062  87 GVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARAGL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIET-------EmlnvfSEEDKNEIAEE----------IPLGRLGLPEEVAKTVSF 215
Cdd:PRK07062 167 LNLVKSLATELAPKGVRVNSILLGLVESgqwrrryE-----ARADPGQSWEAwtaalarkkgIPLGRLGRPDEAARALFF 241
                        170
                 ....*....|....*....
gi 446682265 216 LVSPGASYITGQIIGVNGG 234
Cdd:PRK07062 242 LASPLSSYTTGSHIDVSGG 260
PRK08339 PRK08339
short chain dehydrogenase; Provisional
49-234 4.77e-19

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 82.98  E-value: 4.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  49 EVIPVQANLASTDGAEQLWKQ---IEHPlDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSG 125
Cdd:PRK08339  59 DVSYIVADLTKREDLERTVKElknIGEP-DIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFG 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 126 NIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFS-----------EEDKNEI 194
Cdd:PRK08339 138 RIIYSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAqdrakregksvEEALQEY 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446682265 195 AEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08339 218 AKPIPLGRLGEPEEIGYLVAFLASDLGSYINGAMIPVDGG 257
PRK07985 PRK07985
SDR family oxidoreductase;
74-236 5.94e-19

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 83.51  E-value: 5.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSI-FGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:PRK07985 129 LDIMALVAGKQVaIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSPHLLDYAATKAAI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEmLNVFSEEDKNEI---AEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQII 229
Cdd:PRK07985 207 LNYSRGLAKQVAEKGIRVNIVAPGPIWTA-LQISGGQTQDKIpqfGQQTPMKRAGQPAELAPVYVYLASQESSYVTAEVH 285

                 ....*..
gi 446682265 230 GVNGGWH 236
Cdd:PRK07985 286 GVCGGEH 292
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
37-236 6.78e-19

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 82.63  E-value: 6.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLS 113
Cdd:PRK12429  42 AAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVEtfgGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 114 MALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM----------- 182
Cdd:PRK12429 122 AALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLvrkqipdlake 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265 183 LNVfSEED--KNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:PRK12429 202 RGI-SEEEvlEDVLLPLVPQKRFTTVEEIADYALFLASFAAKGVTGQAWVVDGGWT 256
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
88-234 7.02e-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: 82.57  E-value: 7.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  88 LVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSG 167
Cdd:cd05330   98 LTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYG 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446682265 168 IRVNAVAPGAIETEM----LNVFSEEDKNEIAEEI----PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:cd05330  178 IRINAIAPGAILTPMvegsLKQLGPENPEEAGEEFvsvnPMKRFGEPEEVAAVVAFLLSDDAGYVNAAVVPIDGG 252
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
20-226 7.34e-19

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: 82.28  E-value: 7.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSEeKVNELQKEW-DEVIPVQANLASTD----GAEQLWKQiEHPLDVIVYAAGKSIFGLVTDVTN 94
Cdd:cd05374   18 LALAAQGYRVIATARNPD-KLESLGELLnDNLEVLELDVTDEEsikaAVKEVIER-FGRIDVLVNNAGYGLFGPLEETSI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  95 DELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVA 174
Cdd:cd05374   96 EEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIE 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 175 PGAIETEMLN--------VFSEEDKNEIAEEIPLGRLGL------PEEVAKTVSFLV---SPGASYITG 226
Cdd:cd05374  176 PGPVRTGFADnaagsaleDPEISPYAPERKEIKENAAGVgsnpgdPEKVADVIVKALtseSPPLRYFLG 244
PRK08265 PRK08265
short chain dehydrogenase; Provisional
111-235 7.93e-19

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 82.36  E-value: 7.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 111 LLSMALPSMIqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEED 190
Cdd:PRK08265 117 LAQAAHPHLA-RGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGGD 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446682265 191 KnEIAEEI-----PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK08265 196 R-AKADRVaapfhLLGRVGDPEEVAQVVAFLCSDAASFVTGADYAVDGGY 244
PRK06057 PRK06057
short chain dehydrogenase; Provisional
102-234 1.23e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 81.70  E-value: 1.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 102 ELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIG-ASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIET 180
Cdd:PRK06057 110 DVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGsATSQISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNT 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 181 EMLNVFSEEDKNEIAEE---IPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK06057 190 PLLQELFAKDPERAARRlvhVPMGRFAEPEEIAAAVAFLASDDASFITASTFLVDGG 246
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
37-218 1.24e-18

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: 81.82  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHPL---DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLS 113
Cdd:cd08934   41 EALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALgrlDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTH 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 114 MALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNE 193
Cdd:cd08934  121 AALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKE 200
                        170       180       190
                 ....*....|....*....|....*....|
gi 446682265 194 IAEE-----IPLGrlglPEEVAKTVSFLVS 218
Cdd:cd08934  201 AYEEristiRKLQ----AEDIAAAVRYAVT 226
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
74-234 1.48e-18

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 81.51  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:cd05363   78 IDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIaQGRGGKIINMASQAGRRGEALVGVYCATKAAV 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEMLN----VFSE-------EDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGA 221
Cdd:cd05363  158 ISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDgvdaKFARyenrprgEKKRLVGEAVPFGRMGRAEDLTGMAIFLASTDA 237
                        170
                 ....*....|...
gi 446682265 222 SYITGQIIGVNGG 234
Cdd:cd05363  238 DYIVAQTYNVDGG 250
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-235 1.83e-18

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 81.31  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDEV----IPVQANLASTDGAEQLWKQIEHP---LD 75
Cdd:PRK06077   7 KVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENggegIGVLADVSTREGCETLAKATIDRygvAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:PRK06077  87 ILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAAVINL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 156 VKALAKEVSlSGIRVNAVAPGAIETEM---LNVFSEEDKNEIAEEIPL-GRLGLPEEVAKTVSFLV-SPGasyITGQIIG 230
Cdd:PRK06077 165 TKYLALELA-PKIRVNAIAPGFVKTKLgesLFKVLGMSEKEFAEKFTLmGKILDPEEVAEFVAAILkIES---ITGQVFV 240

                 ....*
gi 446682265 231 VNGGW 235
Cdd:PRK06077 241 LDSGE 245
PRK06125 PRK06125
short chain dehydrogenase; Provisional
55-234 2.10e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 81.24  E-value: 2.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  55 ANLASTDGAEQLWKQIEhPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVssiw 134
Cdd:PRK06125  64 LDLSSPEAREQLAAEAG-DIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV---- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 135 gqIGASCE------VLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETE-MLNVFSEEDKNEIAEE---------I 198
Cdd:PRK06125 139 --IGAAGEnpdadyICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDrMLTLLKGRARAELGDEsrwqellagL 216
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446682265 199 PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK06125 217 PLGRPATPEEVADLVAFLASPRSGYTSGTVVTVDGG 252
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
53-235 4.62e-18

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 80.33  E-value: 4.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  53 VQANLASTDGAEQLWKQ---IEHPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYkLLSMALPSMIQRRS--GNI 127
Cdd:PRK12481  60 ITADLIQQKDIDSIVSQaveVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVF-FLSQAVAKQFVKQGngGKI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 128 VLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVF-SEEDKNE-IAEEIPLGRLGL 205
Cdd:PRK12481 139 INIASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALrADTARNEaILERIPASRWGT 218
                        170       180       190
                 ....*....|....*....|....*....|
gi 446682265 206 PEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK12481 219 PDDLAGPAIFLSSSASDYVTGYTLAVDGGW 248
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
119-234 5.30e-18

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 80.00  E-value: 5.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 119 MIQ-RRSGNIVLVSSI--WGQIGASCevlYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIA 195
Cdd:PRK08217 137 MIEsGSKGVIINISSIarAGNMGQTN---YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLE 213
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446682265 196 EEIPLGRLGLPEEVAKTVSFLVSpgASYITGQIIGVNGG 234
Cdd:PRK08217 214 KMIPVGRLGEPEEIAHTVRFIIE--NDYVTGRVLEIDGG 250
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
29-235 5.68e-18

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 79.92  E-value: 5.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  29 VYVHYNNSEEKVNELQKEWDEVIPVQANLASTDG----AEQLWKQIEHpLDVIVYAAGKSIFGLVTDVTNDELNDMVELQ 104
Cdd:PRK08993  38 VGINIVEPTETIEQVTALGRRFLSLTADLRKIDGipalLERAVAEFGH-IDILVNNAGLIRREDAIEFSEKDWDDVMNLN 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 105 VKSIYKLLSMALPSMI-QRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEML 183
Cdd:PRK08993 117 IKSVFFMSQAAAKHFIaQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNT 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446682265 184 NVF-SEEDKN-EIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK08993 197 QQLrADEQRSaEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAVDGGW 250
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
22-234 7.34e-18

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 79.42  E-value: 7.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVhYNNSEEKVNELQKE---WDEVIPVQANLASTDGAEQLW---KQIEHPLDVIVYAAGKSIFGLVTDVTnd 95
Cdd:PRK05786  25 ALKEGAQVCI-NSRNENKLKRMKKTlskYGNIHYVVGDVSSTESARNVIekaAKVLNAIDGLVVTVGGYVEDTVEEFS-- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  96 ELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGASC-EVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVA 174
Cdd:PRK05786 102 GLEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIYKASPdQLSYAVAKAGLAKAVEILASELLGRGIRVNGIA 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 175 PGAIETEMlnvfseEDKNEIAEEIPLGRLGLP-EEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK05786 180 PTTISGDF------EPERNWKKLRKLGDDMAPpEDFAKVIIWLLTDEADWVDGVVIPVDGG 234
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
20-236 8.69e-18

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 79.30  E-value: 8.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNN--SEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQI-EH--PLDVIVYAAGKS----IFGLVT 90
Cdd:COG0623   25 KALHEEGAELAFTYQGeaLKKRVEPLAEELGSALVLPCDVTDDEQIDALFDEIkEKwgKLDFLVHSIAFApkeeLGGRFL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  91 DVTNDELNDMVELqvkSIYKLLSM---ALPSMiqRRSGNIVLVSSIwgqiGAScEVL--Y---SMVKGAQNSYVKALAKE 162
Cdd:COG0623  105 DTSREGFLLAMDI---SAYSLVALakaAEPLM--NEGGSIVTLTYL----GAE-RVVpnYnvmGVAKAALEASVRYLAAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 163 VSLSGIRVNAVAPGAIET----------EMLNvfseedknEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVN 232
Cdd:COG0623  175 LGPKGIRVNAISAGPIKTlaasgipgfdKLLD--------YAEERAPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVD 246

                 ....
gi 446682265 233 GGWH 236
Cdd:COG0623  247 GGYH 250
PRK07074 PRK07074
SDR family oxidoreductase;
73-234 1.99e-17

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 78.66  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGqIGASCEVLYSMVKGAQ 152
Cdd:PRK07074  77 PVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNG-MAALGHPAYSAAKAGL 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEML--------NVFSEEDKneiaeEIPLGRLGLPEEVAKTVSFLVSPGASYI 224
Cdd:PRK07074 156 IHYTKLLAVEYGRFGIRANAVAPGTVKTQAWearvaanpQVFEELKK-----WYPLQDFATPDDVANAVLFLASPAARAI 230
                        170
                 ....*....|
gi 446682265 225 TGQIIGVNGG 234
Cdd:PRK07074 231 TGVCLPVDGG 240
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
5-234 2.64e-17

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 78.43  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265    5 ALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDE-----VIPVQANLASTDgaeQLWKQIEHPLDVIVY 79
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNArrpnsAVTCQADLSNSA---TLFSRCEAIIDACFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   80 AAGK--------SIFGLVTDVTNDELNDM-----VELQVKSIYKLLSMA----LPSMIQR--------RSGNIVLVSSIW 134
Cdd:TIGR02685  81 AFGRcdvlvnnaSAFYPTPLLRGDAGEGVgdkksLEVQVAELFGSNAIApyflIKAFAQRqagtraeqRSTNLSIVNLCD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  135 GQIGASCE--VLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAieTEMLNVFSEEDKNEIAEEIPLG-RLGLPEEVAK 211
Cdd:TIGR02685 161 AMTDQPLLgfTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL--SLLPDAMPFEVQEDYRRKVPLGqREASAEQIAD 238
                         250       260
                  ....*....|....*....|...
gi 446682265  212 TVSFLVSPGASYITGQIIGVNGG 234
Cdd:TIGR02685 239 VVIFLVSPKAKYITGTCIKVDGG 261
PRK07677 PRK07677
short chain dehydrogenase; Provisional
167-236 3.13e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 77.80  E-value: 3.13e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 167 GIRVNAVAPGAIE----TEMLnVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:PRK07677 174 GIRVNAIAPGPIErtggADKL-WESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCITMDGGQW 246
PRK07069 PRK07069
short chain dehydrogenase; Validated
74-234 3.82e-17

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 77.83  E-value: 3.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAqn 153
Cdd:PRK07069  80 LSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAA-- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 syVKALAKEVSLS------GIRVNAVAPGAIETEMLNVFS-----EEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGAS 222
Cdd:PRK07069 158 --VASLTKSIALDcarrglDVRCNSIHPTFIRTGIVDPIFqrlgeEEATRKLARGVPLGRLGEPDDVAHAVLYLASDESR 235
                        170
                 ....*....|..
gi 446682265 223 YITGQIIGVNGG 234
Cdd:PRK07069 236 FVTGAELVIDGG 247
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
35-234 5.46e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 77.49  E-value: 5.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  35 NSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYkL 111
Cdd:PRK08085  45 RAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKdigPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVF-L 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 112 LSMALPS-MIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEED 190
Cdd:PRK08085 124 VSQAVARyMVKRQAGKIINICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDE 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446682265 191 K--NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK08085 204 AftAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVDGG 249
PRK06198 PRK06198
short chain dehydrogenase; Provisional
37-229 7.68e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 76.97  E-value: 7.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLS 113
Cdd:PRK06198  45 EAQAAELEALGAKAVFVQADLSDVEDCRRVVAAaDEAfgRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQ 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 114 MALPSMIQRRS-GNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETE----MLNVFSE 188
Cdd:PRK06198 125 EAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEgedrIQREFHG 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446682265 189 EDKN---EIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQII 229
Cdd:PRK06198 205 APDDwleKAAATQPFGRLLDPDEVARAVAFLLSDESGLMTGSVI 248
PRK06841 PRK06841
short chain dehydrogenase; Provisional
52-235 8.19e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 77.01  E-value: 8.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  52 PVQANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIV 128
Cdd:PRK06841  65 GLVCDVSDSQSVEAAVAAvISAfgRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 129 LVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAEEIPLGRLGLPE 207
Cdd:PRK06841 145 NLASQAGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELgKKAWAGEKGERAKKLIPAGRFAYPE 224
                        170       180
                 ....*....|....*....|....*...
gi 446682265 208 EVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK06841 225 EIAAAALFLASDAAAMITGENLVIDGGY 252
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-236 1.75e-16

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 76.15  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVH----YNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---P 73
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINdrpdDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAawgR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIF--GLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGN------IVLVSSIwGQIGASCEVL- 144
Cdd:PRK12745  81 IDCLVNNAGVGVKvrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSV-NAIMVSPNRGe 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 145 YSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEI-PLGRLGLPEEVAKTVSFLVSPGASY 223
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYDALIAKGLvPMPRWGEPEDVARAVAALASGDLPY 239
                        250
                 ....*....|...
gi 446682265 224 ITGQIIGVNGGWH 236
Cdd:PRK12745 240 STGQAIHVDGGLS 252
PRK12744 PRK12744
SDR family oxidoreductase;
29-235 2.42e-16

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 75.55  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  29 VYVHYN------NSEEKVNELQKEWDEVIPVQANLASTDGAEQLW-KQIEH--PLDVIVYAAGKSIFGLVTDVTNDELND 99
Cdd:PRK12744  36 VAIHYNsaaskaDAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFdDAKAAfgRPDIAINTVGKVLKKPIVEISEAEYDE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 100 MVELQVKSIYKLLSMALPSMiqRRSGNIV-LVSSIWGQIGAscevLYSMVKGAQ---NSYVKALAKEVSLSGIRVNAVAP 175
Cdd:PRK12744 116 MFAVNSKSAFFFIKEAGRHL--NDNGKIVtLVTSLLGAFTP----FYSAYAGSKapvEHFTRAASKEFGARGISVTAVGP 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446682265 176 GAIETEMLnvFSEEDKNEIAEEI------PLGRLGL--PEEVAKTVSFLVSPGAsYITGQIIGVNGGW 235
Cdd:PRK12744 190 GPMDTPFF--YPQEGAEAVAYHKtaaalsPFSKTGLtdIEDIVPFIRFLVTDGW-WITGQTILINGGY 254
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
122-233 3.54e-16

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 76.80  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 122 RRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMlnvfseedkneiAEEIPLG 201
Cdd:PRK08261 333 GDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM------------TAAIPFA 400
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446682265 202 ------RL------GLPEEVAKTVSFLVSPGASYITGQIIGVNG 233
Cdd:PRK08261 401 treagrRMnslqqgGLPVDVAETIAWLASPASGGVTGNVVRVCG 444
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
37-213 3.55e-16

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: 75.32  E-value: 3.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWD-EVIPVQANLASTDGAEQLWKQIEHP---LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLL 112
Cdd:cd05332   41 EEVKSECLELGApSPHVVPLDMSDLEDAEQVVEEALKLfggLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALT 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 113 SMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKN 192
Cdd:cd05332  121 KAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGS 200
                        170       180
                 ....*....|....*....|..
gi 446682265 193 EIAEEIPLGRLGL-PEEVAKTV 213
Cdd:cd05332  201 MSAKMDDTTANGMsPEECALEI 222
PRK07041 PRK07041
SDR family oxidoreductase;
124-234 4.12e-16

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 74.69  E-value: 4.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 124 SGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEvsLSGIRVNAVAPGAIETEMLNVFSEEDKNEI----AEEIP 199
Cdd:PRK07041 116 GGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALE--LAPVRVNTVSPGLVDTPLWSKLAGDAREAMfaaaAERLP 193
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446682265 200 LGRLGLPEEVAKTVSFLVSPGasYITGQIIGVNGG 234
Cdd:PRK07041 194 ARRVGQPEDVANAILFLAANG--FTTGSTVLVDGG 226
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
3-234 5.23e-16

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: 74.74  E-value: 5.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE--EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP---LDVI 77
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEiaEKVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEfggLDIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  78 VYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSS---IWGQIGASCevlYSMVKGAQN 153
Cdd:cd08943   82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKsQGIGGNIVFNASknaVAPGPNAAA---YSAAKAAEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAP-----GAIETEMLNVFSEEDKNEIAEEI-----PLGRLGLPEEVAKTVSFLVSPGASY 223
Cdd:cd08943  159 HLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWRAARAKAYGLLEEEyrtrnLLKREVLPEDVAEAVVAMASEDFGK 238
                        250
                 ....*....|.
gi 446682265 224 ITGQIIGVNGG 234
Cdd:cd08943  239 TTGAIVTVDGG 249
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
74-235 8.79e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 74.16  E-value: 8.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQ-RRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:PRK13394  85 VDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTAKHGL 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEMLNV----------FSEED--KNEIAEEIPLGRLGLPEEVAKTVSFLVSPG 220
Cdd:PRK13394 165 LGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqipeqakelgISEEEvvKKVMLGKTVDGVFTTVEDVAQTVLFLSSFP 244
                        170
                 ....*....|....*
gi 446682265 221 ASYITGQIIGVNGGW 235
Cdd:PRK13394 245 SAALTGQSFVVSHGW 259
PRK09072 PRK09072
SDR family oxidoreductase;
36-182 1.28e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 73.82  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  36 SEEKVNELQKEW---DEVIPVQANLASTDGAEQLWKQIEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYK 110
Cdd:PRK09072  38 NAEKLEALAARLpypGRHRWVVADLTSEAGREAVLARAREmgGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQ 117
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446682265 111 LLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:PRK09072 118 LTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
20-182 1.69e-15

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: 73.02  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVhYNNSEEKVNELQKEWDEVIPVQANLASTD--GAEQLWKQIEHPL-----DVIVYAAGKS--IFGLVT 90
Cdd:cd05356   19 EELAKRGFNVIL-ISRTQEKLDAVAKEIEEKYGVETKTIAADfsAGDDIYERIEKELegldiGILVNNVGIShsIPEYFL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  91 DVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRV 170
Cdd:cd05356   98 ETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFSRALYEEYKSQGIDV 177
                        170
                 ....*....|..
gi 446682265 171 NAVAPGAIETEM 182
Cdd:cd05356  178 QSLLPYLVATKM 189
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
36-182 1.83e-15

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 72.80  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  36 SEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEHPL---DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSI 108
Cdd:PRK07666  40 TEENLKAVAEEVEAygvkVVIATADVSDYEEVTAAIEQLKNELgsiDILINNAGISKFGKFLELDPAEWEKIIQVNLMGV 119
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 109 YKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:PRK07666 120 YYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
148-236 2.01e-15

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 73.05  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 148 VKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDK--NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYIT 225
Cdd:PRK07533 165 VKAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDFDAllEDAAERAPLRRLVDIDDVGAVAAFLASDAARRLT 244
                         90
                 ....*....|.
gi 446682265 226 GQIIGVNGGWH 236
Cdd:PRK07533 245 GNTLYIDGGYH 255
PRK05875 PRK05875
short chain dehydrogenase; Provisional
2-234 2.35e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 73.30  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   2 KKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE------EKVNELQKEwDEVIPVQANLASTDGAEQL------WKQ 69
Cdd:PRK05875   7 DRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDklaaaaEEIEALKGA-GAVRYEPADVTDEDQVARAvdaataWHG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  70 iehPLDVIVYAAGKS-IFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSI-------WgqIGAsc 141
Cdd:PRK05875  86 ---RLHGVVHCAGGSeTIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIaasnthrW--FGA-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 142 evlYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVF--SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSP 219
Cdd:PRK05875 159 ---YGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPIteSPELSADYRACTPLPRVGEVEDVANLAMFLLSD 235
                        250
                 ....*....|....*
gi 446682265 220 GASYITGQIIGVNGG 234
Cdd:PRK05875 236 AASWITGQVINVDGG 250
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
3-234 3.23e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 72.79  E-value: 3.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHyNNSEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQIEH---PLD 75
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVFN-DINQELVDKGLAAYRElgieAHGYVCDVTDEDGVQAMVSQIEKevgVID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAG--KSIfgLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK07097  90 ILVNNAGiiKRI--PMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGLK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIET-------EMLNVFSEEDKNE-IAEEIPLGRLGLPEEVAKTVSFLVSPGASYIT 225
Cdd:PRK07097 168 MLTKNIASEYGEANIQCNGIGPGYIATpqtaplrELQADGSRHPFDQfIIAKTPAARWGDPEDLAGPAVFLASDASNFVN 247

                 ....*....
gi 446682265 226 GQIIGVNGG 234
Cdd:PRK07097 248 GHILYVDGG 256
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
74-220 3.86e-15

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: 71.01  E-value: 3.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:cd02266   32 RDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALD 111
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPG 220
Cdd:cd02266  112 GLAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDRP 178
PRK07478 PRK07478
short chain dehydrogenase; Provisional
87-234 4.94e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 71.88  E-value: 4.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  87 GLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWG------QIGAscevlYSMVKGAQNSYVKALA 160
Cdd:PRK07478  98 GPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGhtagfpGMAA-----YAASKAGLIGLTQVLA 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265 161 KEVSLSGIRVNAVAPGAIETEMLNVFSE-EDKNEIAEEI-PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK07478 173 AEYGAQGIRVNALLPGGTDTPMGRAMGDtPEALAFVAGLhALKRMAQPEEIAQAALFLASDAASFVTGTALLVDGG 248
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
1-234 5.25e-15

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 71.99  E-value: 5.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE------EKVNELQKEwDEVIPVQANLASTDGAEQLWKQIE--- 71
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEkaanvaQEINAEYGE-GMAYGFGADATSEQSVLALSRGVDeif 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  72 HPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRR-SGNIVLVSSIWGQIGASCEVLYSMVKG 150
Cdd:PRK12384  80 GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 151 AQNSYVKALAKEVSLSGIRVNAVAPG-AIETEM-----------LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVS 218
Cdd:PRK12384 160 GGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMfqsllpqyakkLGIKPDEVEQYYIDKVPLKRGCDYQDVLNMLLFYAS 239
                        250
                 ....*....|....*.
gi 446682265 219 PGASYITGQIIGVNGG 234
Cdd:PRK12384 240 PKASYCTGQSINVTGG 255
PRK09186 PRK09186
flagellin modification protein A; Provisional
82-235 7.55e-15

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 71.56  E-value: 7.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  82 GKSIFglvtDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGqIGA-----------SCEVLYSMVKG 150
Cdd:PRK09186  99 GKKFF----DVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYG-VVApkfeiyegtsmTSPVEYAAIKA 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 151 AQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEiplGRLGlPEEVAKTVSFLVSPGASYITGQIIG 230
Cdd:PRK09186 174 GIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFLNAYKKCCNGK---GMLD-PDDICGTLVFLLSDQSKYITGQNII 249

                 ....*
gi 446682265 231 VNGGW 235
Cdd:PRK09186 250 VDDGF 254
PRK06114 PRK06114
SDR family oxidoreductase;
73-237 1.02e-14

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 70.97  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQI---GAScEVLYSMVK 149
Cdd:PRK06114  86 ALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIvnrGLL-QAHYNASK 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMlNVFSE--EDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQ 227
Cdd:PRK06114 165 AGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM-NTRPEmvHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGV 243
                        170
                 ....*....|
gi 446682265 228 IIGVNGGWHC 237
Cdd:PRK06114 244 DLLVDGGFVC 253
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
1-234 1.93e-14

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 70.57  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDEV----IPVQANLASTDGAEQLWKQIE---HP 73
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYgekaYGFGADATNEQSVIALSKGVDeifKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRS-GNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGA-IETEM-----------LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPG 220
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGNlLKSPMfqsllpqyakkLGIKESEVEQYYIDKVPLKRGCDYQDVLNMLLFYASPK 240
                        250
                 ....*....|....
gi 446682265 221 ASYITGQIIGVNGG 234
Cdd:cd05322  241 ASYCTGQSINITGG 254
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
167-234 2.86e-14

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 69.65  E-value: 2.86e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 167 GIRVNAVAPGAIETEMLNVFSEEDKNEIAEEI--PLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK12428 160 GIRVNCVAPGPVFTPILGDFRSMLGQERVDSDakRMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGG 229
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
91-237 2.90e-14

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 69.92  E-value: 2.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  91 DVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIwgqigASCEVLY-----SMVKGAQNSYVKALAKEVSL 165
Cdd:cd05372  102 DTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYL-----GSERVVPgynvmGVAKAALESSVRYLAYELGR 174
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265 166 SGIRVNAVAPGAIET-EMLNV-FSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGWHC 237
Cdd:cd05372  175 KGIRVNAISAGPIKTlAASGItGFDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDLSSGITGEIIYVDGGYHI 248
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-234 3.85e-14

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 71.03  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE--EKVNELQKEWDEVIPVQANLASTDGAEQLWKQ-IEH--PLDVI 77
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEaaEAAAAELGGPDRALGVACDVTDEAAVQAAFEEaALAfgGVDIV 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  78 VYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMI-QRRSGNIVLVSSIWGQI-GASCeVLYSMVKGAQNSY 155
Cdd:PRK08324 503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKaQGLGGSIVFIASKNAVNpGPNF-GAYGAAKAAELHL 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 156 VKALAKEVSLSGIRVNAVAPGAI-------ETEML-------NVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGA 221
Cdd:PRK08324 582 VRQLALELGPDGIRVNGVNPDAVvrgsgiwTGEWIearaaayGLSEEELEEFYRARNLLKREVTPEDVAEAVVFLASGLL 661
                        250
                 ....*....|...
gi 446682265 222 SYITGQIIGVNGG 234
Cdd:PRK08324 662 SKTTGAIITVDGG 674
PRK07831 PRK07831
SDR family oxidoreductase;
37-231 4.34e-14

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 69.29  E-value: 4.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEW--DEVIPVQANLASTDGAEQLWKQIEHPL---DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKL 111
Cdd:PRK07831  56 GETADELAAELglGRVEAVVCDVTSEAQVDALIDAAVERLgrlDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 112 LSMALPSMIQR-RSGNIVLVSSIWG---QIGAScevLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPG-AIETEMLNVF 186
Cdd:PRK07831 136 TRAALRYMRARgHGGVIVNNASVLGwraQHGQA---HYAAAKAGVMALTRCSALEAAEYGVRINAVAPSiAMHPFLAKVT 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446682265 187 SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:PRK07831 213 SAELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTGEVVSV 257
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
3-215 6.75e-14

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: 68.42  E-value: 6.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDG-YTVYVHYNNSE---EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP---LD 75
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVErgqAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKyggLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAGKSIFGLVTDVTNDE-LNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGAScevlYSMVKGAQNS 154
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTREqARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVSKAALNA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446682265 155 YVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPlgRL-GLPEEVAKTVSF 215
Cdd:cd05324  157 LTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEEGAETPV--YLaLLPPDGEPTGKF 216
PRK08263 PRK08263
short chain dehydrogenase; Provisional
38-181 8.24e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 68.91  E-value: 8.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  38 EKVNELQKEW-DEVIPVQANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLS 113
Cdd:PRK08263  38 ATLADLAEKYgDRLLPLALDVTDRAAVFAAVETaVEHfgRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQ 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446682265 114 MALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETE 181
Cdd:PRK08263 118 AVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTD 185
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
60-182 2.50e-13

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: 66.97  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  60 TDgAEQLWKQIEH------PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSI 133
Cdd:cd05350   57 TD-EERNQLVIAEleaelgGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSV 135
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446682265 134 WGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:cd05350  136 AALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPL 184
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
5-234 2.79e-13

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 66.99  E-value: 2.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVhYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYA 80
Cdd:cd05348    7 ALITGGGSGLGRALVERFVAEGAKVAV-LDRSAEKVAELRADFgDAVVGVEGDVRSLADNERAVARCVErfgKLDCFIGN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  81 AG-----KSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRsGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:cd05348   86 AGiwdysTSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGGGPLYTASKHAVVGL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 156 VKALAKEVSlSGIRVNAVAPGAIETEMLNVFSEEDKNE----------IAEEIPLGRLGLPEEVAKTVSFLVSPGAS-YI 224
Cdd:cd05348  165 VKQLAYELA-PHIRVNGVAPGGMVTDLRGPASLGQGETsistpplddmLKSILPLGFAPEPEDYTGAYVFLASRGDNrPA 243
                        250
                 ....*....|
gi 446682265 225 TGQIIGVNGG 234
Cdd:cd05348  244 TGTVINYDGG 253
PRK08219 PRK08219
SDR family oxidoreductase;
1-221 3.78e-13

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 66.50  E-value: 3.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLiQDGYTVYVHYNNSEEkVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHpLDVIVYA 80
Cdd:PRK08219   2 ERPTALITGASRGIGAAIAREL-APTHTLLLGGRPAER-LDELAAELPGATPFPVDLTDPEAIAAAVEQLGR-LDVLVHN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  81 AGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSmIQRRSGNIVLVSSIWGqIGASCE-VLYSMVKGAQNSYVKAL 159
Cdd:PRK08219  79 AGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPA-LRAAHGHVVFINSGAG-LRANPGwGSYAASKFALRALADAL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446682265 160 AKEvSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGrlglPEEVAKTVSFLVSPGA 221
Cdd:PRK08219 157 REE-EPGNVRVTSVHPGRTDTDMQRGLVAQEGGEYDPERYLR----PETVAKAVRFAVDAPP 213
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
37-218 3.79e-13

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: 66.53  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWD-----EVIPVQA---NLASTDGA-EQL---WKQIehplDVIVYAAGKSIfGL--VTDVTNDELNDMVE 102
Cdd:cd05346   34 AERLQELADELGakfpvKVLPLQLdvsDRESIEAAlENLpeeFRDI----DILVNNAGLAL-GLdpAQEADLEDWETMID 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 103 LQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQ---IGAScevLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIE 179
Cdd:cd05346  109 TNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRypyAGGN---VYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVE 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446682265 180 TEMLNVFSEEDKnEIAEEIPLGRLGL-PEEVAKTVSFLVS 218
Cdd:cd05346  186 TEFSLVRFHGDK-EKADKVYEGVEPLtPEDIAETILWVAS 224
PRK06182 PRK06182
short chain dehydrogenase; Validated
2-181 4.55e-13

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 66.91  E-value: 4.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   2 KKYALVTGGSGGIGSAISKQLIQDGYTVYVHyNNSEEKVNELQKewDEVIPVQANLASTDGAEQLWKQI---EHPLDVIV 78
Cdd:PRK06182   3 KKVALVTGASSGIGKATARRLAAQGYTVYGA-ARRVDKMEDLAS--LGVHPLSLDVTDEASIKAAVDTIiaeEGRIDVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  79 YAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKA 158
Cdd:PRK06182  80 NNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDA 159
                        170       180
                 ....*....|....*....|...
gi 446682265 159 LAKEVSLSGIRVNAVAPGAIETE 181
Cdd:PRK06182 160 LRLEVAPFGIDVVVIEPGGIKTE 182
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
2-180 1.02e-12

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: 65.49  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   2 KKYALVTGGSGGIGSAISKQLIQDGYTVYV---HYNNS------------EEKVNELQKEWDEVIPVQANLASTDGAEQL 66
Cdd:cd05338    3 GKVAFVTGASRGIGRAIALRLAKAGATVVVaakTASEGdngsakslpgtiEETAEEIEAAGGQALPIVVDVRDEDQVRAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  67 WKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEV 143
Cdd:cd05338   83 VEAtVDQfgRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDV 162
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446682265 144 LYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPG-AIET 180
Cdd:cd05338  163 AYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIET 200
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
73-234 1.03e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 65.56  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:PRK07523  87 PIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAV 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEmLN---VFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQII 229
Cdd:PRK07523 167 GNLTKGMATDWAKHGLQCNAIAPGYFDTP-LNaalVADPEFSAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHVL 245

                 ....*
gi 446682265 230 GVNGG 234
Cdd:PRK07523 246 YVDGG 250
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
4-229 1.78e-12

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: 64.61  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   4 YALVTGGSGGIGSAISKQLIQDGYTVYVH-YNNSEEKVNELQKEW---DEVIPVQANLASTDGAEQLW---KQIEHPLDV 76
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVlLARSEEPLQELKEELrpgLRVTTVKADLSDAAGVEQLLeaiRKLDGERDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVYAAGkSI--FGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRS-GNIVLVSSI--------WGqigascevLY 145
Cdd:cd05367   81 LINNAG-SLgpVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGaavnpfkgWG--------LY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 146 SMVKGAQNSYVKALAKEvsLSGIRVNAVAPGAIETEMLNVFSEEDKNEIA-----EEIPLGRLGLPEEVAKTVSFLVsPG 220
Cdd:cd05367  152 CSSKAARDMFFRVLAAE--EPDVRVLSYAPGVVDTDMQREIRETSADPETrsrfrSLKEKGELLDPEQSAEKLANLL-EK 228

                 ....*....
gi 446682265 221 ASYITGQII 229
Cdd:cd05367  229 DKFESGAHV 237
PRK06180 PRK06180
short chain dehydrogenase; Provisional
20-181 3.28e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 64.17  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVyVHYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTND 95
Cdd:PRK06180  22 QAALAAGHRV-VGTVRSEAARADFEALHpDRALARLLDVTDFDAIDAVVADAEAtfgPIDVLVNNAGYGHEGAIEESPLA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  96 ELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAP 175
Cdd:PRK06180 101 EMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEP 180

                 ....*.
gi 446682265 176 GAIETE 181
Cdd:PRK06180 181 GSFRTD 186
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
37-235 8.01e-12

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 63.06  E-value: 8.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQL-------WKQIEHPLDVIVYAAGKSIFGLVTD-VTNDELNDMVELQVKSI 108
Cdd:PRK08690  45 EERVRKMAAELDSELVFRCDVASDDEINQVfadlgkhWDGLDGLVHSIGFAPKEALSGDFLDsISREAFNTAHEISAYSL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 109 YKLLSMALPsMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSE 188
Cdd:PRK08690 125 PALAKAARP-MMRGRNSAIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIAD 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446682265 189 EDK--NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK08690 204 FGKllGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGGY 252
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
149-236 8.10e-12

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 63.21  E-value: 8.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 149 KGAQNSYVKALAKEVSLSGIRVNAVAPGAIETemLNVFSEEDKNEIAEEI----PLGRLGLPEEVAKTVSFLVSPGASYI 224
Cdd:PRK08594 165 KASLEASVKYLANDLGKDGIRVNAISAGPIRT--LSAKGVGGFNSILKEIeeraPLRRTTTQEEVGDTAAFLFSDLSRGV 242
                         90
                 ....*....|..
gi 446682265 225 TGQIIGVNGGWH 236
Cdd:PRK08594 243 TGENIHVDSGYH 254
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
5-235 1.16e-11

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 62.67  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVhYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQLWKQIEHP---LDVIVYA 80
Cdd:PRK06200   9 ALITGGGSGIGRALVERFLAEGARVAV-LERSAEKLASLRQRFgDHVLVVEGDVTSYADNQRAVDQTVDAfgkLDCFVGN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  81 AG-----KSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRsGNIVLVSSIWGQIGASCEVLYSMVKGAQNSY 155
Cdd:PRK06200  88 AGiwdynTSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGGGGPLYTASKHAVVGL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 156 VKALAKEVSlSGIRVNAVAPGAIETEM-------LNVFSEEDKNEIAEEI----PLGRLGLPEEVAKTVSFLVSPGAS-Y 223
Cdd:PRK06200 167 VRQLAYELA-PKIRVNGVAPGGTVTDLrgpaslgQGETSISDSPGLADMIaaitPLQFAPQPEDHTGPYVLLASRRNSrA 245
                        250
                 ....*....|..
gi 446682265 224 ITGQIIGVNGGW 235
Cdd:PRK06200 246 LTGVVINADGGL 257
PLN02253 PLN02253
xanthoxin dehydrogenase
74-237 1.79e-11

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 62.15  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSiFGLVTDVTNDELND---MVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKG 150
Cdd:PLN02253  95 LDIMVNNAGLT-GPPCPDIRNVELSEfekVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKH 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 151 AQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNE---------IAEEIPL-GRLGLPEEVAKTVSFLVSP 219
Cdd:PLN02253 174 AVLGLTRSVAAELGKHGIRVNCVSPYAVPTALaLAHLPEDERTEdalagfrafAGKNANLkGVELTVDDVANAVLFLASD 253
                        170
                 ....*....|....*...
gi 446682265 220 GASYITGQIIGVNGGWHC 237
Cdd:PLN02253 254 EARYISGLNLMIDGGFTC 271
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
74-234 1.91e-11

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: 61.83  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:cd09761   76 IDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSEAYAASKGGLV 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAkeVSLS-GIRVNAVAPGAIETEMLNVFSEEDKNEI-AEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:cd09761  155 ALTHALA--MSLGpDIRVNCISPGWINTTEQQEFTAAPLTQEdHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIV 232

                 ...
gi 446682265 232 NGG 234
Cdd:cd09761  233 DGG 235
PRK06949 PRK06949
SDR family oxidoreductase;
3-234 4.72e-11

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 60.93  E-value: 4.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVyVHYNNSEEKVNELQKEWdEVIPVQANLASTDGAEQ--LWKQIEH------PL 74
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKV-VLASRRVERLKELRAEI-EAEGGAAHVVSLDVTDYqsIKAAVAHaeteagTI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQR--------RSGNIVLVSSIWG-----QIGasc 141
Cdd:PRK06949  88 DILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARakgagntkPGGRIINIASVAGlrvlpQIG--- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 142 evLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPG 220
Cdd:PRK06949 165 --LYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEInHHHWETEQGQKLVSMLPRKRVGKPEDLDGLLLLLAADE 242
                        250
                 ....*....|....
gi 446682265 221 ASYITGQIIGVNGG 234
Cdd:PRK06949 243 SQFINGAIISADDG 256
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
20-236 6.59e-11

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 60.33  E-value: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSEEKVNELQKewDEVIPVQANLASTDG----AEQLwKQIEHPLDVIVYAAGKSIFGLVTDVTND 95
Cdd:PRK06483  20 WHLLAQGQPVIVSYRTHYPAIDGLRQ--AGAQCIQADFSTNAGimafIDEL-KQHTDGLRAIIHNASDWLAEKPGAPLAD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  96 ELNDMVELQVKSIYkLLSMALPSMIQRRS---GNIVLVSSIWGQIGASCEVLYSMVKGA-QN---SYVKALAKEVslsgi 168
Cdd:PRK06483  97 VLARMMQIHVNAPY-LLNLALEDLLRGHGhaaSDIIHITDYVVEKGSDKHIAYAASKAAlDNmtlSFAAKLAPEV----- 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446682265 169 RVNAVAPGAIetemlnVFSEED-----KNEIAEEIpLGRLGLPEEVAKTVSFLVSpgASYITGQIIGVNGGWH 236
Cdd:PRK06483 171 KVNSIAPALI------LFNEGDdaayrQKALAKSL-LKIEPGEEEIIDLVDYLLT--SCYVTGRSLPVDGGRH 234
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
40-235 6.69e-11

(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: 60.41  E-value: 6.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  40 VNELQKEWDEVIpvqANLASTDGAEQLWKQ-IEH--PLDVIVYAAGksifgLVTDV----TNDELNDMV-ELQVKSIYKL 111
Cdd:cd05353   55 VDEIKAAGGKAV---ANYDSVEDGEKIVKTaIDAfgRVDILVNNAG-----ILRDRsfakMSEEDWDLVmRVHLKGSFKV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 112 LSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAiETEM-LNVFSEED 190
Cdd:cd05353  127 TRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA-GSRMtETVMPEDL 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446682265 191 KNEIAeeiplgrlglPEEVAKTVSFLVSPgASYITGQIIGVNGGW 235
Cdd:cd05353  206 FDALK----------PEYVAPLVLYLCHE-SCEVTGGLFEVGAGW 239
PRK09134 PRK09134
SDR family oxidoreductase;
22-236 7.36e-11

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 60.33  E-value: 7.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  22 LIQDGYTVYVHYNNS----EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAgkSIF--GLVTDV 92
Cdd:PRK09134  29 LAAHGFDVAVHYNRSrdeaEALAAEIRALGRRAVALQADLADEAEVRALVARASAalgPITLLVNNA--SLFeyDSAASF 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMVELQVK-------SIYKLLSMALPSMI-----QR-RSGNIVLVSsiwgqigascevlYSMVKGAQNSYVKAL 159
Cdd:PRK09134 107 TRASWDRHMATNLRapfvlaqAFARALPADARGLVvnmidQRvWNLNPDFLS-------------YTLSKAALWTATRTL 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446682265 160 AKEVSlSGIRVNAVAPGAIeteMLNVF-SEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSpgASYITGQIIGVNGGWH 236
Cdd:PRK09134 174 AQALA-PRIRVNAIGPGPT---LPSGRqSPEDFARQHAATPLGRGSTPEEIAAAVRYLLD--APSVTGQMIAVDGGQH 245
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
37-235 8.49e-11

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 60.11  E-value: 8.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP---LDVIVYA---AGKS-IFGLVTDVTNDELNDMVELQVKSIY 109
Cdd:PRK07370  48 EKKVRELTEPLNPSLFLPCDVQDDAQIEETFETIKQKwgkLDILVHClafAGKEeLIGDFSATSREGFARALEISAYSLA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 110 KLLSMALPSMiqRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIET--------- 180
Cdd:PRK07370 128 PLCKAAKPLM--SEGGSIVTLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTlassavggi 205
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265 181 -EMLNvfseedknEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK07370 206 lDMIH--------HVEEKAPLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAGY 253
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
20-236 1.55e-10

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 59.35  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSEEKvNELQKEWDEVIP-VQANLASTDGAEQLWKQIEH---PLDVIVYA---AGKSifGLVTDV 92
Cdd:PRK06079  27 QAIKDQGATVIYTYQNDRMK-KSLQKLVDEEDLlVECDVASDESIERAFATIKErvgKIDGIVHAiayAKKE--ELGGNV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMVELQVKSIYKLLSMA-LPSMIQRRSGNIVLVSsiwgQIGASCEVL-YSMV---KGAQNSYVKALAKEVSLSG 167
Cdd:PRK06079 104 TDTSRDGYALAQDISAYSLIAVAkYARPLLNPGASIVTLT----YFGSERAIPnYNVMgiaKAALESSVRYLARDLGKKG 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 168 IRVNAVAPGAIET-EMLNVFSEEDKNEIAEEIPLGRLGLP-EEVAKTVSFLVSPGASYITGQIIGVNGGWH 236
Cdd:PRK06079 180 IRVNAISAGAVKTlAVTGIKGHKDLLKESDSRTVDGVGVTiEEVGNTAAFLLSDLSTGVTGDIIYVDKGVH 250
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
15-231 2.39e-10

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 57.98  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  15 GSAISKQLIQDGYTVYVHYNNSEEkvnelqkewdevipVQANLASTDGAEQLWKQIEHpLDVIVYAAGKSIFGLVTDVTN 94
Cdd:cd11731   11 GLAVAQLLSAHGHEVITAGRSSGD--------------YQVDITDEASIKALFEKVGH-FDAIVSTAGDAEFAPLAELTD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  95 DELNDMVELQVKSIYKLLSMALPSMIQRrsGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVsLSGIRVNAVA 174
Cdd:cd11731   76 ADFQRGLNSKLLGQINLVRHGLPYLNDG--GSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIEL-PRGIRINAVS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 175 PGAIETEMlnvfsEEDKNEIAEEIPlgrlGLPEEVAKTVSFLVSpgaSYITGQIIGV 231
Cdd:cd11731  153 PGVVEESL-----EAYGDFFPGFEP----VPAEDVAKAYVRSVE---GAFTGQVLHV 197
PRK07326 PRK07326
SDR family oxidoreductase;
1-218 2.93e-10

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 58.48  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYV---HYNNSEEKVNELQKEwDEVIPVQANLASTDGAEQLWKQIEHP---L 74
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAItarDQKELEEAAAELNNK-GNVLGLAADVRDEADVQRAVDAIVAAfggL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiQRRSGNIVLVSSIWGQ----IGAScevlYSMVKG 150
Cdd:PRK07326  84 DVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTnffaGGAA----YNASKF 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 151 AQNSYVKALAKEVSLSGIRVNAVAPGAIETEML-NVFSEEDKNEIAeeiplgrlglPEEVAKTVSFLVS 218
Cdd:PRK07326 159 GLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNgHTPSEKDAWKIQ----------PEDIAQLVLDLLK 217
PRK06482 PRK06482
SDR family oxidoreductase;
74-181 4.01e-10

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 58.20  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQI---GAScevLYSMVKG 150
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIaypGFS---LYHATKW 153
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446682265 151 AQNSYVKALAKEVSLSGIRVNAVAPGAIETE 181
Cdd:PRK06482 154 GIEGFVEAVAQEVAPFGIEFTIVEPGPARTN 184
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
2-233 4.83e-10

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: 58.00  E-value: 4.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   2 KKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNN---SEEKVNELQKEWD----EVIPVQ-ANLASTDGAEQLWKQIEHP 73
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNeekGEEAAAEIKKETGnakvEVIQLDlSSLASVRQFAEEFLARFPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGksIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSI---WGQIGA----------- 139
Cdd:cd05327   81 LDILINNAG--IMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIahrAGPIDFndldlennkey 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 140 SCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMLNvfseedKNEIAEEI-PLGRLGL---PEEVAKTVSF 215
Cdd:cd05327  159 SPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLR------RNGSFFLLyKLLRPFLkksPEQGAQTALY 232
                        250
                 ....*....|....*....
gi 446682265 216 LV-SPGASYITGQIIGVNG 233
Cdd:cd05327  233 AAtSPELEGVSGKYFSDCK 251
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
63-182 5.52e-10

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: 57.64  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  63 AEQLWKQIEHPlDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCE 142
Cdd:cd05339   67 AKKIKKEVGDV-TILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGL 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446682265 143 VLYSMVKGAQNSYVKALAKEVSLS---GIRVNAVAPGAIETEM 182
Cdd:cd05339  146 ADYCASKAAAVGFHESLRLELKAYgkpGIKTTLVCPYFINTGM 188
PRK08340 PRK08340
SDR family oxidoreductase;
20-233 5.89e-10

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 57.89  E-value: 5.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHYNNSE--EKVNELQKEWDEVIPVQANLASTDGAEQLWKQ---IEHPLDVIVYAAG--KSIFGLVTDV 92
Cdd:PRK08340  18 RELLKKGARVVISSRNEEnlEKALKELKEYGEVYAVKADLSDKDDLKNLVKEaweLLGGIDALVWNAGnvRCEPCMLHEA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMVELQVKSIYKLLSMALPSMIQRR-SGNIVLVSSIwgqigascEVLYSMVKGAQNSYVKA----LAKEVSLS- 166
Cdd:PRK08340  98 GYSDWLEAALLHLVAPGYLTTLLIQAWLEKKmKGVLVYLSSV--------SVKEPMPPLVLADVTRAglvqLAKGVSRTy 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 167 ---GIRVNAV------APGAIET------EMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGV 231
Cdd:PRK08340 170 ggkGIRAYTVllgsfdTPGARENlariaeERGVSFEETWEREVLERTPLKRTGRWEELGSLIAFLLSENAEYMLGSTIVF 249

                 ..
gi 446682265 232 NG 233
Cdd:PRK08340 250 DG 251
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
3-234 6.69e-10

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: 57.31  E-value: 6.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYV-HYNNSEEKVNELQKEW--DEVIPVQANLASTDGAEQLWKQ-IEH--PLDV 76
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAIlDRNENPGAAAELQAINpkVKATFVQCDVTSWEQLAAAFKKaIEKfgRVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVYAAG----KSIFGLVTDVTNDElnDMVELQVKSIYKLLSMALPSM---IQRRSGNIVLVSSIWGQIGASCEVLYSMVK 149
Cdd:cd05323   81 LINNAGildeKSYLFAGKLPPPWE--KTIDVNLTGVINTTYLALHYMdknKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 150 GAQNSYVKALAKEVSL-SGIRVNAVAPGAIETEMLnvfsEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGASyiTGQI 228
Cdd:cd05323  159 HGVVGFTRSLADLLEYkTGVRVNAICPGFTNTPLL----PDLVAKEAEMLPSAPTQSPEVVAKAIVYLIEDDEK--NGAI 232

                 ....*.
gi 446682265 229 IGVNGG 234
Cdd:cd05323  233 WIVDGG 238
PRK07454 PRK07454
SDR family oxidoreductase;
72-182 7.34e-10

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 57.28  E-value: 7.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  72 HPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWG-----QIGAscevlYS 146
Cdd:PRK07454  82 GCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAArnafpQWGA-----YC 156
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446682265 147 MVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:PRK07454 157 VSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
26-227 7.49e-10

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 57.20  E-value: 7.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  26 GYTVYVHYNNSE------EKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP---LDVIVYAAGksIFGLVTDV---T 93
Cdd:cd05340   28 GATVILLGRNEEklrqvaDHINEEGGRQPQWFILDLLTCTSENCQQLAQRIAVNyprLDGVLHNAG--LLGDVCPLseqN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  94 NDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAV 173
Cdd:cd05340  106 PQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCI 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446682265 174 APGAIETEM-LNVFSEEDkneiaeeiPLgRLGLPEEVAKTVSFLVSPGASYITGQ 227
Cdd:cd05340  186 NPGGTRTAMrASAFPTED--------PQ-KLKTPADIMPLYLWLMGDDSRRKTGM 231
PRK07775 PRK07775
SDR family oxidoreductase;
73-182 1.03e-09

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 57.07  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWG-----QIGAscevlYSM 147
Cdd:PRK07775  87 EIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVAlrqrpHMGA-----YGA 161
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446682265 148 VKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:PRK07775 162 AKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
PRK06940 PRK06940
short chain dehydrogenase; Provisional
145-234 1.37e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 56.95  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 145 YSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM----LNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPG 220
Cdd:PRK06940 169 YQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLaqdeLNGPRGDGYRNMFAKSPAGRPGTPDEIAALAEFLMGPR 248
                         90
                 ....*....|....
gi 446682265 221 ASYITGQIIGVNGG 234
Cdd:PRK06940 249 GSFITGSDFLVDGG 262
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
37-180 3.88e-09

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: 55.08  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  37 EEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQ-VKSIYKLL 112
Cdd:cd05360   38 HELAREVRELGGEAIAVVADVADAAQVERAADTAVErfgRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNyLGHVYGTL 117
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 113 SmALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSG--IRVNAVAPGAIET 180
Cdd:cd05360  118 A-ALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHDGapISVTLVQPTAMNT 186
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
20-182 5.05e-09

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: 54.61  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGY-TVY--VHYNNSEEKVNELQKEWDEVIPVQANLAST--DGAEQL-WKQIEHPLDVIVYAAG-KSIFGLVTDV 92
Cdd:cd05325   16 RQLLARGNnTVIatCRDPSAATELAALGASHSRLHILELDVTDEiaESAEAVaERLGDAGLDVLINNAGiLHSYGPASEV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  93 TNDELNDMveLQVKSIYKLLSM--ALPSMIQRRSGNIVLVSSIWGQIGA---SCEVLYSMVKGAQNSYVKALAKEVSLSG 167
Cdd:cd05325   96 DSEDLLEV--FQVNVLGPLLLTqaFLPLLLKGARAKIINISSRVGSIGDntsGGWYSYRASKAALNMLTKSLAVELKRDG 173
                        170
                 ....*....|....*
gi 446682265 168 IRVNAVAPGAIETEM 182
Cdd:cd05325  174 ITVVSLHPGWVRTDM 188
PRK06179 PRK06179
short chain dehydrogenase; Provisional
74-213 2.16e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 53.37  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:PRK06179  74 IDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVE 153
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMlnvfseeDKNEIAEEIPLG-----RLGL-------------PEEVAKTV 213
Cdd:PRK06179 154 GYSESLDHEVRQFGIRVSLVEPAYTKTNF-------DANAPEPDSPLAeydreRAVVskavakavkkadaPEVVADTV 224
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
74-234 3.35e-08

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 52.86  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYkLLSMALPSMIQRRS--------GNIVLVSSIWGQIGASCEVLY 145
Cdd:PRK07792  90 LDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHF-LLTRNAAAYWRAKAkaaggpvyGRIVNTSSEAGLVGPVGQANY 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 146 SMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAiETEML-NVFSEEDKNEIAEEIPLGrlglPEEVAKTVSFLVSPGASYI 224
Cdd:PRK07792 169 GAAKAGITALTLSAARALGRYGVRANAICPRA-RTAMTaDVFGDAPDVEAGGIDPLS----PEHVVPLVQFLASPAAAEV 243
                        170
                 ....*....|
gi 446682265 225 TGQIIGVNGG 234
Cdd:PRK07792 244 NGQVFIVYGP 253
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
2-218 3.86e-08

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: 52.51  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   2 KKYALVTGGSGGIGSAISKQLIQDGYTVyVHYNNSEEKVNELQKE-----WDEVIPVQANLASTDGAEQLWKQIE---HP 73
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKV-VGCARRVDKIEALAAEcqsagYPTLFPYQCDLSNEEQILSMFSAIRtqhQG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRR--SGNIVLVSSIWGQIGASCEVL--YSMVK 149
Cdd:cd05343   85 VDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGHRVPPVSVFhfYAATK 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 150 GAQNSYVKALAKEVSL--SGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVS 218
Cdd:cd05343  165 HAVTALTEGLRQELREakTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYVLS 235
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
74-213 4.13e-08

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: 52.07  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  74 LDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQN 153
Cdd:cd08931   77 LDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVR 156
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDkneiAEEIPLGRLGLPEEVAKTV 213
Cdd:cd08931  157 GLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGA----APKKGLGRVLPVSDVAKVV 212
PRK05717 PRK05717
SDR family oxidoreductase;
111-234 6.77e-08

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 51.81  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 111 LLSMALPSMIQRRSGNIV-LVSSIWGQIGASCEVlYSMVKGAQNSYVKALAkeVSLS-GIRVNAVAPGAIETEMLNVFSE 188
Cdd:PRK05717 123 LLAKHCAPYLRAHNGAIVnLASTRARQSEPDTEA-YAASKGGLLALTHALA--ISLGpEIRVNAVSPGWIDARDPSQRRA 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446682265 189 EDKNEIAE-EIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGG 234
Cdd:PRK05717 200 EPLSEADHaQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVVDGG 246
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
3-218 7.77e-08

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: 51.35  E-value: 7.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP---LDVIVY 79
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAfggLDALVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  80 AAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKAL 159
Cdd:cd08929   81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446682265 160 AKEVSLSGIRVNAVAPGAIETEmLNVFSEEDKNEIAeeiplgrlglPEEVAKTVSFLVS 218
Cdd:cd08929  161 MLDLREANIRVVNVMPGSVDTG-FAGSPEGQAWKLA----------PEDVAQAVLFALE 208
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
75-193 1.07e-07

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: 51.31  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 DVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNS 154
Cdd:cd09806   81 DVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446682265 155 YVKALAKEVSLSGIRVNAVAPGAIETE-MLNVFSEEDKNE 193
Cdd:cd09806  161 LCESLAVQLLPFNVHLSLIECGPVHTAfMEKVLGSPEEVL 200
PRK08267 PRK08267
SDR family oxidoreductase;
24-213 2.49e-07

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 49.94  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  24 QDGYTVYVhYNNSEEKVNELQKEWDEVIPVQANLASTDGAEqlWKQI-----EHP---LDVIVYAAGKSIFGLVTDVTND 95
Cdd:PRK08267  23 AEGWRVGA-YDINEAGLAALAAELGAGNAWTGALDVTDRAA--WDAAladfaAATggrLDVLFNNAGILRGGPFEDIPLE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  96 ELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLV-----SSIWGQIGAScevLYSMVKGAQNSYVKALAKEVSLSGIRV 170
Cdd:PRK08267 100 AHDRVIDINVKGVLNGAHAALPYL--KATPGARVIntssaSAIYGQPGLA---VYSATKFAVRGLTEALDLEWRRHGIRV 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446682265 171 NAVAPGAIETEMLNVFSEEDKNEIaeeipLGRLGL---PEEVAKTV 213
Cdd:PRK08267 175 ADVMPLFVDTAMLDGTSNEVDAGS-----TKRLGVrltPEDVAEAV 215
PRK06914 PRK06914
SDR family oxidoreductase;
73-213 2.75e-07

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 50.02  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  73 PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQ 152
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIPLGRL---------------GLPEEVAKTV 213
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIWEVGKQLAENQSETTSPYKEYmkkiqkhinsgsdtfGNPIDVANLI 236
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
5-184 3.08e-07

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: 49.61  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVHyNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQI--EHP-LDVIVYAA 81
Cdd:cd05370    8 VLITGGTSGIGLALARKFLEAGNTVIIT-GRREERLAEAKKELPNIHTIVLDVGDAESVEALAEALlsEYPnLDILINNA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  82 G--KSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKAL 159
Cdd:cd05370   87 GiqRPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHSYTLAL 166
                        170       180
                 ....*....|....*....|....*
gi 446682265 160 AKEVSLSGIRVNAVAPGAIETEMLN 184
Cdd:cd05370  167 RHQLKDTGVEVVEIVPPAVDTELHE 191
PRK08017 PRK08017
SDR family oxidoreductase;
1-219 4.20e-07

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 49.31  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSE--EKVNELQKEwdeviPVQANLASTDGAEQLWKQIEHPLDVIV 78
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDdvARMNSLGFT-----GILLDLDDPESVERAADEVIALTDNRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  79 YA----AGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNS 154
Cdd:PRK08017  76 YGlfnnAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446682265 155 YVKALAKEVSLSGIRVNAVAPGAIETEmlnvFSeEDKNEIAEEIPL------GRLGLPEE--VAKTVSFLVSP 219
Cdd:PRK08017 156 WSDALRMELRHSGIKVSLIEPGPIRTR----FT-DNVNQTQSDKPVenpgiaARFTLGPEavVPKLRHALESP 223
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
63-229 5.38e-07

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 49.10  E-value: 5.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  63 AEQLWKQIEHpLDVIVYAAGksIFGLVTDVTN---DELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQIGA 139
Cdd:PRK08945  83 ADTIEEQFGR-LDGVLHNAG--LLGELGPMEQqdpEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGR 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 140 SCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEiaeeiplgrLGLPEEVAKTVSFLVS 218
Cdd:PRK08945 160 ANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMrASAFPGEDPQK---------LKTPEDIMPLYLYLMG 230
                        170
                 ....*....|.
gi 446682265 219 PGASYITGQII 229
Cdd:PRK08945 231 DDSRRKNGQSF 241
PRK07109 PRK07109
short chain dehydrogenase; Provisional
49-180 1.14e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 48.38  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  49 EVIPVQANLASTDGAEQLWKQIEH---PLDVIVYAAGKSIFGLVTDVTNDELNDMVEL----QVKSiykllSM-ALPSMI 120
Cdd:PRK07109  58 EALAVVADVADAEAVQAAADRAEEelgPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVtylgVVHG-----TLaALRHMR 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446682265 121 QRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEV--SLSGIRVNAVAPGAIET 180
Cdd:PRK07109 133 PRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTDSLRCELlhDGSPVSVTMVQPPAVNT 194
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
3-229 1.20e-06

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: 48.21  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYV----HYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIEHP----L 74
Cdd:cd09763    4 KIALVTGASRGIGRGIALQLGEAGATVYItgrtILPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREqqgrL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  75 DVIV---YAAGKSIFGLVT------DVTNdeLNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIwGQIGASCEVLY 145
Cdd:cd09763   84 DILVnnaYAAVQLILVGVAkpfweePPTI--WDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISST-GGLEYLFNVAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 146 SMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM-LNVFSEEDKNEIAEEIPLGRLG-LPEEVAKTVSFLVS-PGAS 222
Cdd:cd09763  161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELvLEMPEDDEGSWHAKERDAFLNGeTTEYSGRCVVALAAdPDLM 240

                 ....*..
gi 446682265 223 YITGQII 229
Cdd:cd09763  241 ELSGRVL 247
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
149-236 1.43e-06

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 48.01  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 149 KGAQNSYVKALAKEVSLSGIRVNAVAPGAIET---------EMLNvfseedkNEIAEEIPLG-RLGLPEEVAKTVSFLVS 218
Cdd:PRK07889 162 KAALESTNRYLARDLGPRGIRVNLVAAGPIRTlaakaipgfELLE-------EGWDERAPLGwDVKDPTPVARAVVALLS 234
                         90
                 ....*....|....*...
gi 446682265 219 PGASYITGQIIGVNGGWH 236
Cdd:PRK07889 235 DWFPATTGEIVHVDGGAH 252
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
3-198 2.24e-06

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: 47.02  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYT-VYVHYNNSEEKVNELQKEWDEVIPVQANLASTDGAEQLWKQIeHPLDVIVYAA 81
Cdd:cd05354    4 KTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQA-KDVDVVINNA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  82 G-KSIFGLVTDvtNDELNDMVELQVkSIYKLLSMA---LPSMIQRRSGNIVLVSSIwGQIGASCEV-LYSMVKGAQNSYV 156
Cdd:cd05354   83 GvLKPATLLEE--GALEALKQEMDV-NVFGLLRLAqafAPVLKANGGGAIVNLNSV-ASLKNFPAMgTYSASKSAAYSLT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446682265 157 KALAKEVSLSGIRVNAVAPGAIETEMLNV--FSEEDKNEIAEEI 198
Cdd:cd05354  159 QGLRAELAAQGTLVLSVHPGPIDTRMAAGagGPKESPETVAEAV 202
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
77-236 4.13e-06

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 46.66  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqrRSGNIVLVSSIWGqiGASCEVLYSMV---KGAQN 153
Cdd:PRK08415  91 VAFAPKEALEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL---NDGASVLTLSYLG--GVKYVPHYNVMgvaKAALE 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 154 SYVKALAKEVSLSGIRVNAVAPGAIET----------EMLNVfseedkNEIaeEIPLGRLGLPEEVAKTVSFLVSPGASY 223
Cdd:PRK08415 166 SSVRYLAVDLGKKGIRVNAISAGPIKTlaasgigdfrMILKW------NEI--NAPLKKNVSIEEVGNSGMYLLSDLSSG 237
                        170
                 ....*....|...
gi 446682265 224 ITGQIIGVNGGWH 236
Cdd:PRK08415 238 VTGEIHYVDAGYN 250
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
147-235 5.73e-06

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 45.97  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 147 MVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIET---EMLNVFSEEDKNeIAEEIPLGRLGLPEEVAKTVSFLVSPGASY 223
Cdd:PRK06997 161 LAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaaSGIKDFGKILDF-VESNAPLRRNVTIEEVGNVAAFLLSDLASG 239
                         90
                 ....*....|..
gi 446682265 224 ITGQIIGVNGGW 235
Cdd:PRK06997 240 VTGEITHVDSGF 251
PRK07832 PRK07832
SDR family oxidoreductase;
3-184 9.32e-06

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 45.42  E-value: 9.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVY---VHYNNSEEKVNELQKEWDEVIPVQA-NLASTDGAEQLWKQI--EHP-LD 75
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFltdRDADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIhaAHGsMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  76 VIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQ-RRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNS 154
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAaGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRG 160
                        170       180       190
                 ....*....|....*....|....*....|
gi 446682265 155 YVKALAKEVSLSGIRVNAVAPGAIETEMLN 184
Cdd:PRK07832 161 LSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK09291 PRK09291
SDR family oxidoreductase;
71-180 1.26e-05

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 44.99  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  71 EHPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQI-----GAscevlY 145
Cdd:PRK09291  71 EWDVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLItgpftGA-----Y 145
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446682265 146 SMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIET 180
Cdd:PRK09291 146 CASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK07984 PRK07984
enoyl-ACP reductase FabI;
33-235 1.49e-05

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 44.89  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  33 YNNSEEK--VNELQKEWDEVIPVQANLASTDGAEQL-------WKQIEHPLDVIVYAAGKSIFG-LVTDVTNDELNDMVE 102
Cdd:PRK07984  39 YQNDKLKgrVEEFAAQLGSDIVLPCDVAEDASIDAMfaelgkvWPKFDGFVHSIGFAPGDQLDGdYVNAVTREGFKIAHD 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 103 LqvkSIYKLLSMALP--SMIQRRSGNIVLvssiwGQIGASCEV----LYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPG 176
Cdd:PRK07984 119 I---SSYSFVAMAKAcrSMLNPGSALLTL-----SYLGAERAIpnynVMGLAKASLEANVRYMANAMGPEGVRVNAISAG 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446682265 177 AIETEMLNVFSEEDK--NEIAEEIPLGRLGLPEEVAKTVSFLVSPGASYITGQIIGVNGGW 235
Cdd:PRK07984 191 PIRTLAASGIKDFRKmlAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGF 251
PRK07578 PRK07578
short chain dehydrogenase; Provisional
26-182 1.76e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 44.03  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  26 GYTVyvhynnseekVNELQKEwDEVIPV-------QANLASTDGAEQLWKQIEHpLDVIVYAAGKSIFGLVTDVTNDE-- 96
Cdd:PRK07578  13 GRAV----------VAELSKR-HEVITAgrssgdvQVDITDPASIRALFEKVGK-VDAVVSAAGKVHFAPLAEMTDEDfn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  97 --LNDMVELQVksiyKLLSMALPSMiqRRSGNIVLVSSIWGQ----IGAScevlYSMVKGAQNSYVKALAKEVSlSGIRV 170
Cdd:PRK07578  81 vgLQSKLMGQV----NLVLIGQHYL--NDGGSFTLTSGILSDepipGGAS----AATVNGALEGFVKAAALELP-RGIRI 149
                        170
                 ....*....|..
gi 446682265 171 NAVAPGAIETEM 182
Cdd:PRK07578 150 NVVSPTVLTESL 161
PRK07024 PRK07024
SDR family oxidoreductase;
116-182 2.79e-05

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 44.15  E-value: 2.79e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446682265 116 LPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:PRK07024 122 IAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPM 188
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
3-213 3.51e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 43.52  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEKVNELQKEWDE-VIPVQANLASTDGAEQLWKQIEHPLDVivyAA 81
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSnLTFHSLDLQDVHELETNFNEILSSIQE---DN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  82 GKSIF-----GLVTDV------TNDELNDMVELQVksiykLLSMALPSMIQRRSGN------IVLVSSIWGQ---IGASC 141
Cdd:PRK06924  79 VSSIHlinnaGMVAPIkpiekaESEELITNVHLNL-----LAPMILTSTFMKHTKDwkvdkrVINISSGAAKnpyFGWSA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 142 evlYSMVKGAQNSYVKALA---KEVSLsGIRVNAVAPGAIETEMLNVF---SEEDKNEIAEEIPL---GRLGLPEEVAKT 212
Cdd:PRK06924 154 ---YCSSKAGLDMFTQTVAteqEEEEY-PVKIVAFSPGVMDTNMQAQIrssSKEDFTNLDRFITLkeeGKLLSPEYVAKA 229

                 .
gi 446682265 213 V 213
Cdd:PRK06924 230 L 230
PRK07791 PRK07791
short chain dehydrogenase; Provisional
55-236 4.86e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 43.51  E-value: 4.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  55 ANLASTDGAEQLWKQ-IEH--PLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPS-MIQRRSGN---- 126
Cdd:PRK07791  71 DDIADWDGAANLVDAaVETfgGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYwRAESKAGRavda 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 127 -IVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAiETEMlnvfSEEDKNEIAEEIPLGRLGL 205
Cdd:PRK07791 151 rIINTSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAA-RTRM----TETVFAEMMAKPEEGEFDA 225
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446682265 206 --PEEVAKTVSFLVSPGASYITGQIIGVNG-------GWH 236
Cdd:PRK07791 226 maPENVSPLVVWLGSAESRDVTGKVFEVEGgkisvaeGWR 265
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
61-236 5.26e-05

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 43.07  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  61 DGAEQLWKQIEHPLDVIVYAAGKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiqRRSGNIVLVSSIWGQIGAS 140
Cdd:PRK06603  78 DDIKEKWGSFDFLLHGMAFADKNELKGRYVDTSLENFHNSLHISCYSLLELSRSAEALM--HDGGSIVTLTYYGAEKVIP 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 141 CEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIET---EMLNVFSEEDKNEiAEEIPLGRLGLPEEVAKTVSFLV 217
Cdd:PRK06603 156 NYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTlasSAIGDFSTMLKSH-AATAPLKRNTTQEDVGGAAVYLF 234
                        170
                 ....*....|....*....
gi 446682265 218 SPGASYITGQIIGVNGGWH 236
Cdd:PRK06603 235 SELSKGVTGEIHYVDCGYN 253
PRK05693 PRK05693
SDR family oxidoreductase;
5-199 1.08e-04

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 42.47  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEkVNELQKEwdEVIPVQANLASTDGAEQLWKQIEHP---LDVIVYAA 81
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAED-VEALAAA--GFTAVQLDVNDGAALARLAEELEAEhggLDVLINNA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  82 GKSIFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMiQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAK 161
Cdd:PRK05693  81 GYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRL 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446682265 162 EVSLSGIRVNAVAPGAIETEMLNVFSEEDKNEIAEEIP 199
Cdd:PRK05693 160 ELAPFGVQVMEVQPGAIASQFASNASREAEQLLAEQSP 197
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
146-236 1.26e-04

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 42.11  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 146 SMVKGAQNSYVKALAKEVSLS-GIRVNAVAPGAIETEMLNV--FSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGAS 222
Cdd:PRK06300 193 SSAKAALESDTKVLAWEAGRRwGIRVNTISAGPLASRAGKAigFIERMVDYYQDWAPLPEPMEAEQVGAAAAFLVSPLAS 272
                         90
                 ....*....|....
gi 446682265 223 YITGQIIGVNGGWH 236
Cdd:PRK06300 273 AITGETLYVDHGAN 286
PRK05884 PRK05884
SDR family oxidoreductase;
146-234 1.83e-04

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 41.33  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 146 SMVKGAQNSYVKALAKEVSLSGIRVNAVAPG-AIETEMLNVFSEEDknEIAEEIplGRLGLpeevaktvsFLVSPGASYI 224
Cdd:PRK05884 141 AAIKAALSNWTAGQAAVFGTRGITINAVACGrSVQPGYDGLSRTPP--PVAAEI--ARLAL---------FLTTPAARHI 207
                         90
                 ....*....|
gi 446682265 225 TGQIIGVNGG 234
Cdd:PRK05884 208 TGQTLHVSHG 217
PRK07102 PRK07102
SDR family oxidoreductase;
111-213 2.46e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 41.06  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 111 LLSMALPSMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEMlnvfseed 190
Cdd:PRK07102 114 LLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPM-------- 185
                         90       100
                 ....*....|....*....|....*
gi 446682265 191 kneiAEEIPL-GRL-GLPEEVAKTV 213
Cdd:PRK07102 186 ----TAGLKLpGPLtAQPEEVAKDI 206
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
149-236 2.75e-04

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 41.27  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 149 KGAQNSYVKALAKEVSLSGIRVNAVAPGAIET-------EMLNVFSEEDKNEiaeeiPLGRLGLPEEVAKTVSFLVSPGA 221
Cdd:PRK06505 163 KAALEASVRYLAADYGPQGIRVNAISAGPVRTlagagigDARAIFSYQQRNS-----PLRRTVTIDEVGGSALYLLSDLS 237
                         90
                 ....*....|....*
gi 446682265 222 SYITGQIIGVNGGWH 236
Cdd:PRK06505 238 SGVTGEIHFVDSGYN 252
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
146-236 3.96e-04

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 40.91  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265 146 SMVKGAQNSYVKALAKEVSLS-GIRVNAVAPGAIETEMLNV--FSEEDKNEIAEEIPLGRLGLPEEVAKTVSFLVSPGAS 222
Cdd:PLN02730 194 SSAKAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKAigFIDDMIEYSYANAPLQKELTADEVGNAAAFLASPLAS 273
                         90
                 ....*....|....
gi 446682265 223 YITGQIIGVNGGWH 236
Cdd:PLN02730 274 AITGATIYVDNGLN 287
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
6-213 1.29e-03

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 38.97  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   6 LVTGGSGGIGSAISKQLIQDGYTVyVHYNNSEEKVNELQKEW-DEVIPVQANLASTDGAEQL-------WKQIehplDVI 77
Cdd:PRK10538   4 LVTGATAGFGECITRRFIQQGHKV-IATGRRQERLQELKDELgDNLYIAQLDVRNRAAIEEMlaslpaeWRNI----DVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  78 VYAAGKSIfGL--VTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSI---WGQIGAScevlysmVKGAQ 152
Cdd:PRK10538  79 VNNAGLAL-GLepAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTagsWPYAGGN-------VYGAT 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446682265 153 NSYVK--ALAKEVSLSG--IRVNAVAPGAIE-TEMLNVFSEEDKNEIAEEIPLGRLGLPEEVAKTV 213
Cdd:PRK10538 151 KAFVRqfSLNLRTDLHGtaVRVTDIEPGLVGgTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAV 216
PRK07201 PRK07201
SDR family oxidoreductase;
3-133 1.98e-03

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 38.78  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   3 KYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNsEEKVNELQKEWDE----VIPVQANLASTDGAEQLWKQI--EHP-LD 75
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARN-GEALDELVAEIRAkggtAHAYTCDLTDSAAVDHTVKDIlaEHGhVD 450
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446682265  76 VIVYAAGKSIFGLVTDVTnDELND----MvelQVKSIYKL-LSMA-LPSMIQRRSGNIVLVSSI 133
Cdd:PRK07201 451 YLVNNAGRSIRRSVENST-DRFHDyertM---AVNYFGAVrLILGlLPHMRERRFGHVVNVSSI 510
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
20-182 3.84e-03

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 37.47  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  20 KQLIQDGYTVYVHyNNSEEKVNELQKEWDEV-IPVQANLASTDGAEQLWKQIEH--PLDVIVYAAGkSIFGLVTDVTNDE 96
Cdd:cd08951   25 RTLLHQGHEVVLH-ARSQKRAADAKAACPGAaGVLIGDLSSLAETRKLADQVNAigRFDAVIHNAG-ILSGPNRKTPDTG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  97 LNDMVELQVKSIYKLLSMALP-------SMIQRRSGNIVLVSSIWGQIGASCEVLYSMVKgaqnSYVKALAKEVS--LSG 167
Cdd:cd08951  103 IPAMVAVNVLAPYVLTALIRRpkrliylSSGMHRGGNASLDDIDWFNRGENDSPAYSDSK----LHVLTLAAAVArrWKD 178
                        170
                 ....*....|....*
gi 446682265 168 IRVNAVAPGAIETEM 182
Cdd:cd08951  179 VSSNAVHPGWVPTKM 193
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
5-206 5.88e-03

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: 36.73  E-value: 5.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   5 ALVTGGSGGIGSAISKQLIQDGYTVYVHYNNsEEKVNELQKEWDEVIpVQANLASTDGAEQLWKQIEhPLDVIVYAAGKS 84
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRD-AGALAGLAAEVGALA-RPADVAAELEVWALAQELG-PLDLLVYAAGAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  85 IFGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQrrSGNIVLvssiwgqIGASCEVL-------YSMVKGAQNSYVK 157
Cdd:cd11730   78 LGKPLARTKPAAWRRILDANLTGAALVLKHALALLAA--GARLVF-------LGAYPELVmlpglsaYAAAKAALEAYVE 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446682265 158 ALAKEVslSGIRVNAVAPGAIETEMLNVFSEEDKN-----EIAEEIPLGRLGLP 206
Cdd:cd11730  149 VARKEV--RGLRLTLVRPPAVDTGLWAPPGRLPKGalspeDVAAAILEAHQGEP 200
PRK08177 PRK08177
SDR family oxidoreductase;
2-182 7.52e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 36.55  E-value: 7.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   2 KKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNSEEkvNELQKEWDEVIPVQANLASTDGAEQLWKQI-EHPLDVIVYA 80
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQ--DTALQALPGVHIEKLDMNDPASLDQLLQRLqGQRFDLLFVN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  81 AGksIFG----LVTDVTNDELNDMveLQVKSIYKL-LSMALPSMIQRRSGNIVLVSSIWG--QIGASCEV-LYSMVKGAQ 152
Cdd:PRK08177  79 AG--ISGpahqSAADATAAEIGQL--FLTNAIAPIrLARRLLGQVRPGQGVLAFMSSQLGsvELPDGGEMpLYKASKAAL 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 446682265 153 NSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:PRK08177 155 NSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK05993 PRK05993
SDR family oxidoreductase;
1-181 8.02e-03

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 36.54  E-value: 8.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265   1 MKKYALVTGGSGGIGSAISKQLIQDGYTVYVHYNNsEEKVNELQKEWDEVIpvQANLASTD----GAEQLWKQIEHPLDV 76
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRK-EEDVAALEAEGLEAF--QLDYAEPEsiaaLVAQVLELSGGRLDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446682265  77 IVY--AAGKSifGLVTDVTNDELNDMVELQVKSIYKLLSMALPSMIQRRSGNIVLVSSIWGQI-----GAscevlYSMVK 149
Cdd:PRK05993  80 LFNngAYGQP--GAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVpmkyrGA-----YNASK 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446682265 150 GAQNSYVKALAKEVSLSGIRVNAVAPGAIETE 181
Cdd:PRK05993 153 FAIEGLSLTLRMELQGSGIHVSLIEPGPIETR 184
PRK08251 PRK08251
SDR family oxidoreductase;
121-182 8.73e-03

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 36.45  E-value: 8.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446682265 121 QRRSGNIVLVSSIWGQIGA-SCEVLYSMVKGAQNSYVKALAKEVSLSGIRVNAVAPGAIETEM 182
Cdd:PRK08251 129 EQGSGHLVLISSVSAVRGLpGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEM 191
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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