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Conserved domains on  [gi|1953284729|ref|XP_038539107|]
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estradiol 17-beta-dehydrogenase 8 isoform X1 [Canis lupus familiaris]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 11-226 1.64e-97

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


The actual alignment was detected with superfamily member cd05333:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 240  Bit Score: 286.75  E-value: 1.64e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETV-------EEIKALGGNAAALEADVSDREAVEALVEKVEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05333    75 FG-PVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR-SGRIINISSVVGLIGNPGQANYAAS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:cd05333   153 KAGVIGFTKSLAKELAS-------RGITVNAVAPGFIDTDMTDALPEKVKEKILKQ 201
 
Name Accession Description Interval E-value
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 11-226 1.64e-97

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: 286.75  E-value: 1.64e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETV-------EEIKALGGNAAALEADVSDREAVEALVEKVEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05333    75 FG-PVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR-SGRIINISSVVGLIGNPGQANYAAS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:cd05333   153 KAGVIGFTKSLAKELAS-------RGITVNAVAPGFIDTDMTDALPEKVKEKILKQ 201
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
12-226 2.11e-80

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 243.53  E-value: 2.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05653    8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALA-------AELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05653   81 G-ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKAR-YGRIVNISSVSGVTGNPGQTNYSAAK 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:PRK05653  159 AGVIGFTKALALELA-------SRGITVNAVAPGFIDTDMTEGLPEEVKAEILKE 206
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 12-217 2.97e-74

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: 228.13  E-value: 2.97e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:COG1028     9 ALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELR-------AAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:COG1028    82 GRL-DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERG-GGRIVNISSIAGLRGSPGQAAYAASK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:COG1028   160 AAVVGLTRSLALELAP-------RGIRVNAVAPGPIDTPMTRALLG 198
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 12-223 3.79e-74

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 227.48  E-value: 3.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEV------VEELKALGVKALGVVLDVSDREDVKAVVEEIEEEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:TIGR01830  75 G-TIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQR-SGRIINISSVVGLMGNAGQANYAASK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:TIGR01830 153 AGVIGFTKSLAKELAS-------RNITVNAVAPGFIDTDMTDKLSEKVKKKI 197
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-220 1.34e-62

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 196.30  E-value: 1.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGK------AL-FIQGDVTDRAQVKALVEQAVERL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:pfam00106  76 GRL-DILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGS-GGRIVNISSVAGLVPYPGGSAYSASK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVL 220
Cdd:pfam00106 154 AAVIGFTRSLALELAP-------HGIRVNAVAPGGVDTDMTKELREDEG 195
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-169 5.79e-15

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 71.36  E-value: 5.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   13 LVTGAGSGIGRAVSVRLAKEGAT----VAACDLDRAAACETVWLLGGQGsekvapgGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlvlLSRSGPDAPGAAALLAELEAAG-------ARVTVVACDVADRDALAAVLAAIP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   89 ACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrgsIINISSIVGKVGNVGQTNYA 168
Cdd:smart00822  77 AVE-GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF-----FVLFSSIAGVLGSPGQANYA 150


                   .
gi 1953284729  169 A 169
Cdd:smart00822 151 A 151
 
Name Accession Description Interval E-value
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 11-226 1.64e-97

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: 286.75  E-value: 1.64e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETV-------EEIKALGGNAAALEADVSDREAVEALVEKVEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05333    75 FG-PVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR-SGRIINISSVVGLIGNPGQANYAAS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:cd05333   153 KAGVIGFTKSLAKELAS-------RGITVNAVAPGFIDTDMTDALPEKVKEKILKQ 201
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
12-226 2.11e-80

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 243.53  E-value: 2.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05653    8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALA-------AELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05653   81 G-ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKAR-YGRIVNISSVSGVTGNPGQTNYSAAK 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:PRK05653  159 AGVIGFTKALALELA-------SRGITVNAVAPGFIDTDMTEGLPEEVKAEILKE 206
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 12-227 3.09e-75

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 230.47  E-value: 3.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVA-ACDLDRAAACETVWLLGGQGsekvapGGAHtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK05557    8 ALVTGASRGIGRAIAERLAAQGANVViNYASSEAGAEALVAEIGALG------GKAL-AVQGDVSDAESVERAVDEAKAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK05557   81 FGGV-DILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRS-GRIINISSVVGLMGNPGQANYAAS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 171 KAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQMR 227
Cdd:PRK05557  159 KAGVIGFTKSLARELA-------SRGITVNAVAPGFIETDMTDALPEDVKEAILAQI 208
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 12-217 2.97e-74

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: 228.13  E-value: 2.97e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:COG1028     9 ALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELR-------AAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:COG1028    82 GRL-DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERG-GGRIVNISSIAGLRGSPGQAAYAASK 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:COG1028   160 AAVVGLTRSLALELAP-------RGIRVNAVAPGPIDTPMTRALLG 198
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 12-223 3.79e-74

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 227.48  E-value: 3.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEV------VEELKALGVKALGVVLDVSDREDVKAVVEEIEEEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:TIGR01830  75 G-TIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQR-SGRIINISSVVGLMGNAGQANYAASK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:TIGR01830 153 AGVIGFTKSLAKELAS-------RNITVNAVAPGFIDTDMTDKLSEKVKKKI 197
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 12-223 1.18e-63

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: 200.59  E-value: 1.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA--------AIEALGGNAVAVQADVSDEEDVEALVEEALEEF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05233    73 GRL-DILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQG-GGRIVNISSVAGLRPLPGQAAYAASK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:cd05233   151 AALEGLTRSLALELA-------PYGIRVNAVAPGLVDTPMLAKLGPEEAEKE 195
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-220 1.34e-62

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 196.30  E-value: 1.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGK------AL-FIQGDVTDRAQVKALVEQAVERL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:pfam00106  76 GRL-DILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGS-GGRIVNISSVAGLVPYPGGSAYSASK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVL 220
Cdd:pfam00106 154 AAVIGFTRSLALELAP-------HGIRVNAVAPGGVDTDMTKELREDEG 195
PRK12826 PRK12826
SDR family oxidoreductase;
6-217 3.75e-62

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 197.06  E-value: 3.75e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapGGAHtAFQADVSEAGAVRRLLE 85
Cdd:PRK12826    3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAG------GKAR-ARQVDVRDRAALKAAVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG-KVGNVGQ 164
Cdd:PRK12826   76 AGVEDFGR-LDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAG-GGRIVLTSSVAGpRVGYPGL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:PRK12826  154 AHYAASKAGLVGFTRALALELAA-------RNITVNSVHPGGVDTPMAGNLGD 199
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-226 7.08e-56

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 180.93  E-value: 7.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKvapggahTAFQADVSEAGAVRRLL 84
Cdd:PRK08217    1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEV-------RGYAANVTDEEDVEATF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSrPPSVVVSCAGLTRDEFLL---------RMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSI 155
Cdd:PRK08217   74 AQIAEDFG-QLNGLINNAGILRDGLLVkakdgkvtsKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGVIINISSI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 156 vGKVGNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:PRK08217  153 -ARAGNMGQTNYSASKAGVAAMTVTWAKELAR-------YGIRVAAIAPGVIETEMTAAMKPEALERLEKM 215
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 12-225 3.47e-54

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: 176.14  E-value: 3.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapggaHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:COG4221     8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGR----------ALAVPLDVTDEAAVEAAVAAAVAEF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:COG4221    78 GR-LDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARG-SGHIVNISSIAGLRPYPGGAVYAATK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQ 225
Cdd:COG4221   156 AAVRGLSESLRAELR-------PTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAA 202
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-226 4.85e-54

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 176.21  E-value: 4.85e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVA-ACDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK12825    9 ALVTGAARGLGRAIALRLARAGADVVvHYRSDEEAAEELVEAVEALGRRAQA-------VQADVTDKAALEAAVAAAVER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK12825   82 FGRI-DILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQR-GGRIVNISSVAGLPGWPGRSNYAAA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:PRK12825  160 KAGLVGLTKALARELAE-------YGITVNMVAPGDIDTDMKEATIEEAREAKDAE 208
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
6-223 1.59e-52

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 172.36  E-value: 1.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:COG0300     2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALA-------AELRAAGARVEVVALDVTDPDAVAALAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:COG0300    75 AVLARF-GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARG-RGRIVNVSSVAGLRGLPGMA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:COG0300   153 AYAASKAALEGFSESLRAELA-------PTGVRVTAVCPGPVDTPFTARAGAPAGRPL 203
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 12-217 4.60e-52

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 171.78  E-value: 4.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12829   14 VLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATA---------ARLPGAKVTATVADVADPAQVERVFDTAVERF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK12829   85 GGL-DVLVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAGRLGYPGRTPYAAS 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:PRK12829  164 KWAVVGLVKSLAIELGP-------LGIRVNAILPGIVRGPRMRRVIE 203
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 11-223 5.88e-51

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: 168.00  E-value: 5.88e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACEtvWLlggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:TIGR01829   2 IALVTGGMGGIGTAICQRLAKDGYRVAAnCGPNEERAEA--WL-----QEQGALGFDFRVVEGDVSSFESCKAAVAKVEA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAA 169
Cdd:TIGR01829  75 ELG-PVDVLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGW-GRIINISSVNGQKGQFGQTNYSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 170 SKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:TIGR01829 153 AKAGMIGFTKALAQEGAT-------KGVTVNTISPGYIATDMVMAMREDVLNSI 199
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 19-226 8.74e-49

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: 162.21  E-value: 8.74e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  19 SGIGRAVSVRLAKEGATVAACDLDRAAAcETVwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFSRPpSVV 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALA-KRV--------EELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRL-DIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  99 VSCAGLTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcRGSIINISSIVGKVGNVGQTNYAASKAGVIG 176
Cdd:pfam13561  76 VNNAGFAPKLKgpFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE---GGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 177 LTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVP--QKVLDKMSQM 226
Cdd:pfam13561 153 LTRYLAVELGP-------RGIRVNAISPGPIKTLAASGIPgfDELLAAAEAR 197
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
9-222 2.54e-48

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 161.47  E-value: 2.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   9 SALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQ 88
Cdd:PRK12824    2 KKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQV------RLKELDVTDTEECAEALAEIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 AcFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYA 168
Cdd:PRK12824   76 E-EEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQG-YGRIINISSVNGLKGQFGQTNYS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 169 ASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDK 222
Cdd:PRK12824  154 AAKAGMIGFTKALASEGAR-------YGITVNCIAPGYIATPMVEQMGPEVLQS 200
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 12-227 2.89e-47

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 158.98  E-value: 2.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12939   10 ALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELA-------AALEAAGGRAHAIAADLADPASVQRFFDAAAAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12939   83 GGL-DGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSG-RGRIVNLASDTALWGAPKLGAYVASK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVL-DKMSQMR 227
Cdd:PRK12939  161 GAVIGMTRSLARELG-------GRGITVNAIAPGLTATEATAYVPADERhAYYLKGR 210
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 12-233 3.28e-46

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: 156.29  E-value: 3.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsEKVAPGGAHTAF-QADVSEAGAVRRLLEQVQAC 90
Cdd:cd05371     5 AVVTGGASGLGLATVERLLAQGAKVVILDLPNSPG------------ETVAKLGDNCRFvPVDVTSEKDVKAALALAKAK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRM------SEDDWDRVIAVNLKGIFLVTQAAAQALV-----SSGCRGSIINISSIVGKV 159
Cdd:cd05371    73 FG-RLDIVVNCAGIAVAAKTYNKkgqqphSLELFQRVINVNLIGTFNVIRLAAGAMGknepdQGGERGVIINTASVAAFE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 160 GNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQMRSHSWRL 233
Cdd:cd05371   152 GQIGQAAYSASKGGIVGMTLPIARDLAP-------QGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFPSRL 218
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-216 1.16e-45

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 160.00  E-value: 1.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAAcetvwllgGQGSEKVAP--GGahTAFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK08261  213 ALVTGAARGIGAAIAEVLARDGAHVVC--LDVPAA--------GEALAAVANrvGG--TALALDITAPDAPARIAEHLAE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQA--AAQALVSSGcrgSIINISSIVGKVGNVGQTNY 167
Cdd:PRK08261  281 RHGGL-DIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEAllAAGALGDGG---RIVGVSSISGIAGNRGQTNY 356

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 168 AASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVP 216
Cdd:PRK08261  357 AASKAGVIGLVQALAPLLA-------ERGITINAVAPGFIETQMTAAIP 398
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-215 2.05e-45

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: 154.05  E-value: 2.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKvapggahTAFQADVSEAGAVRRLLEQ 86
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEA-------TAFTCDVSDEEAIKAAVEA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05347    76 IEEDF-GKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQG-HGKIINICSLLSELGGPPVPA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 167 YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:cd05347   154 YAASKGGVAGLTKALATEWAR-------HGIQVNAIAPGYFATEMTEAV 195
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 6-223 3.13e-45

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 153.62  E-value: 3.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLL 84
Cdd:PRK12935    3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGKEGHDVYA-------VQADVSKVEDANRLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK12935   76 EEAVNHFGKV-DILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAE-EGRIISISSIIGQAGGFGQ 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:PRK12935  154 TNYSAAKAGMLGFTKSLALELAKT-------NVTVNAICPGFIDTEMVAEVPEEVRQKI 205
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-217 6.53e-45

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 152.57  E-value: 6.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL----DRAAACETVWLLGGQGsekvapgGAHTAFQADVSEAGAVRR 82
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIhpmrGRAEADAVAAGIEAAG-------GKALGLAFDVRDFAATRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNV 162
Cdd:PRK12827   77 ALDAGVEEFGRL-DILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGGRIVNIASVAGVRGNR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:PRK12827  156 GQVNYAASKAGLIGLTKTLANELA-------PRGITVNAVAPGAINTPMADNAAP 203
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-210 1.77e-44

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: 151.77  E-value: 1.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAA---CDLDRAAacETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVnyrSKEDAAE--EVV-------EEIKAVGGKAIAVQADVSKEEDVVAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:cd05358    72 FQSAIKEFG-TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKGKIINMSSVHEKIPWPG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTP 210
Cdd:cd05358   151 HVNYAASKGGVKMMTKTLAQEYA-------PKGIRVNAIAPGAINTP 190
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 12-211 1.92e-44

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: 151.76  E-value: 1.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDR-AAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05366     5 AIITGAAQGIGRAIAERLAADGFNIVLADLNLeEAAKSTIQEISEAGYNAVA-------VGADVTDKDDVEALIDQAVEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05366    78 FGSF-DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSAS 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:cd05366   157 KFAVRGLTQTAAQELAP-------KGITVNAYAPGIVKTEM 190
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-226 2.16e-44

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 151.15  E-value: 2.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVA-ACDLDRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK05565    2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVViAYDINEEAAQELLEEIK-------EEGGDAIAVKADVSSEEDVENLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK05565   75 EQIVEKFG-KIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRK-SGVIVNISSIWGLIGASCE 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:PRK05565  153 VLYSASKGAVNAFTKALAKELAP-------SGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEE 207
FabG-like PRK07231
SDR family oxidoreductase;
5-213 3.54e-44

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 150.75  E-value: 3.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK07231    1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA--------GGRAIAVAADVSDEADVEAAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRpPSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG 163
Cdd:PRK07231   73 AAALERFGS-VDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG-GGAIVNVASTAGLRPRPG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGrlvrhPWghGIRCNSVLPGFITTPMTQ 213
Cdd:PRK07231  151 LGWYNASKGAVITLTKALAAELG-----PD--KIRVNAVAPVVVETGLLE 193
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 7-213 4.17e-44

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: 150.72  E-value: 4.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgsEKVAPGGAhtAFQADVSEAGAVRRLLEQ 86
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVV--------AQIAGGAL--ALRVDVTDEQQVAALFER 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:cd08944    71 AVEEFGGLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARG-GGSIVNLSSIAGQSGDPGYGA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 167 YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:cd08944   150 YGASKAAIRNLTRTLAAELRH-------AGIRCNALAPGLIDTPLLL 189
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 13-218 2.17e-42

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 146.01  E-value: 2.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACfs 92
Cdd:PRK07060   13 LVTGASSGIGRACAVALAQRGARVVAAARNAAAL------------DRLAGETGCEPLRLDVGDDAAIRAALAAAGAF-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 rppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK07060   79 ---DGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 173 GVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV---PQK 218
Cdd:PRK07060  156 ALDAITRVLCVELGP-------HGIRVNSVNPTVTLTPMAAEAwsdPQK 197
PRK06138 PRK06138
SDR family oxidoreductase;
5-214 1.15e-41

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 144.52  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK06138    1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA--------GGRAFARQGDVGSAEAVEALV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQ 164
Cdd:PRK06138   73 DFVAARWGR-LDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGG-GSIVNTASQLALAGGRGR 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQK 214
Cdd:PRK06138  151 AAYVASKGAIASLTRAMALDHAT-------DGIRVNAVAPGTIDTPYFRR 193
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-215 8.86e-41

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 143.77  E-value: 8.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRA-AACETVWLLGGQGSEKVAPGGahtafqaDVSEAGA 79
Cdd:PRK07792    4 TTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASAlDASDVLDEIRAAGAKAVAVAG-------DISQRAT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  80 VRRLLEQVQACFSRppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAA-----QALVSSG-CRGSIINIS 153
Cdd:PRK07792   77 ADELVATAVGLGGL--DIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywraKAKAAGGpVYGRIVNTS 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 154 SIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGfITTPMTQKV 215
Cdd:PRK07792  155 SEAGLVGPVGQANYGAAKAGITALTLSAARALGR-------YGVRANAICPR-ARTAMTADV 208
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 6-218 1.87e-40

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: 140.98  E-value: 1.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRLLE 85
Cdd:cd05341     2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAA----------RFFHLDVTDEDGWTAVVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:cd05341    72 TAREAFGRL-DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAG-GGSIINMSSIEGLVGDPALA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhPWGHGIRCNSVLPGFITTPMTQKVPQK 218
Cdd:cd05341   150 AYNASKGAVRGLTKSAALECA-----TQGYGIRVNSVHPGYIYTPMTDELLIA 197
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4-211 2.74e-40

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 140.93  E-value: 2.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRL 83
Cdd:PRK07067    1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAA----------IAVSLDVTRQDSIDRI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:PRK07067   71 VAAAVERFG-GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGGKIINMASQAGRRGEAL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:PRK07067  150 VSHYCATKAAVISYTQSAALALIR-------HGINVNAIAPGVVDTPM 190
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 12-214 3.75e-40

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 140.41  E-value: 3.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12429    7 ALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAA-------EALQKAGGKAIGVAMDVTDEEAINAGIDYAVETF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12429   80 GG-VDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGG-GRIINMASVHGLVGSAGKAAYVSAK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQK 214
Cdd:PRK12429  158 HGLIGLTKVVALEGAT-------HGVTVNAICPGYVDTPLVRK 193
PRK06114 PRK06114
SDR family oxidoreductase;
6-211 5.16e-40

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 140.30  E-value: 5.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK06114    5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLrTDDGLAETAEHIE-------AAGRRAIQIAADVTSKADLRAAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG- 163
Cdd:PRK06114   78 ARTEAELG-ALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENG-GGSIVNIASMSGIIVNRGl 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 164 -QTNYAASKAGVIGLTQTAARElgrlvrhpW-GHGIRCNSVLPGFITTPM 211
Cdd:PRK06114  156 lQAHYNASKAGVIHLSKSLAME--------WvGRGIRVNSISPGYTATPM 197
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 12-214 5.83e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 140.18  E-value: 5.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVwllggqgseKVAPGGAHT-AFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK06841   18 AVVTGGASGIGHAIAELFAAKGARVAL--LDRSEDVAEV---------AAQLLGGNAkGLVCDVSDSQSVEAAVAAVISA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK06841   87 FGRI-DILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAG-GGKIVNLASQAGVVALERHVAYCAS 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1953284729 171 KAGVIGLTQTAARElgrlvrhpWG-HGIRCNSVLPGFITTPMTQK 214
Cdd:PRK06841  165 KAGVVGMTKVLALE--------WGpYGITVNAISPTVVLTELGKK 201
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 12-211 5.28e-39

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 137.18  E-value: 5.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12937    8 AIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADEL------VAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvssGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12937   82 GR-IDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL---GQGGRIINLSTSVIALPLPGYGPYAASK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK12937  158 AAVEGLVHVLANELR-------GRGITVNAVAPGPVATEL 190
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 5-223 5.37e-39

(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: 137.45  E-value: 5.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL---------DRAAACETVwllggqgSEKVAPGGAHTAFQADVS 75
Cdd:cd05353     1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsgkSSSAADKVV-------DEIKAAGGKAVANYDSVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  76 EAGAvrrLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSI 155
Cdd:cd05353    74 DGEK---IVKTAIDAFGRV-DILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQK-FGRIINTSSA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 156 VGKVGNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGfITTPMTQKV-PQKVLDKM 223
Cdd:cd05353   149 AGLYGNFGQANYSAAKLGLLGLSNTLAIEGAK-------YNITCNTIAPA-AGSRMTETVmPEDLFDAL 209
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-226 6.38e-39

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: 137.08  E-value: 6.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtAFQADVSEAGAVRRLL 84
Cdd:cd05352     4 FSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTK------AYKCDVSSQESVEKTF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:cd05352    78 KQIQKDFG-KIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQG-KGSLIITASMSGTIVNRPQ 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 165 TN--YAASKAGVIGLTQTAARElgrlvrhpW-GHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:cd05352   156 PQaaYNASKAAVIHLAKSLAVE--------WaKYFIRVNSISPGYIDTDLTDFVDKELRKKWESY 212
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 12-211 7.38e-39

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: 136.64  E-value: 7.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05362     6 ALVTGASRGIGRAIAKRLARDGASVVVNYAsSKAAAEEVV-------AEIEAAGGKAIAVQADVSDPSQVARLFDAAEKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05362    79 FGGV-DILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG---GRIINISSSLTAAYTPNYGAYAGS 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1953284729 171 KAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:cd05362   155 KAAVEAFTRVLAKELG-------GRGITVNAVAPGPVDTDM 188
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
12-219 2.05e-38

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 136.01  E-value: 2.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08643    5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIA-------VKADVSDRDQVFAAVRQVVDTF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK08643   78 G-DLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGGKIINATSQAGVVGNPELAVYSSTK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 172 AGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQKVPQKV 219
Cdd:PRK08643  157 FAVRGLTQTAARDLASE-------GITVNAYAPGIVKTPMMFDIAHQV 197
PRK06172 PRK06172
SDR family oxidoreductase;
12-211 1.03e-37

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 134.11  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06172   10 ALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEAL-------FVACDVTRDAEVKALVEQTIAAY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDE-FLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK06172   83 GR-LDYAFNNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQG-GGAIVNTASVAGLGAAPKMSIYAAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:PRK06172  161 KHAVIGLTKSAAIEYAK-------KGIRVNAVCPAVIDTDM 194
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 11-216 6.14e-37

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: 131.60  E-value: 6.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHTaFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGK------VHY-YKCDVSKREEVYEAAKKIKKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05339    74 V-GDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERN-HGHIVTIASVAGLISPAGLADYCAS 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 171 KAGVIGLTQTAARELGRLVrHPwghGIRCNSVLPGFITTPMTQKVP 216
Cdd:cd05339   152 KAAAVGFHESLRLELKAYG-KP---GIKTTLVCPYFINTGMFQGVK 193
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 12-215 6.34e-37

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 132.87  E-value: 6.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACEtvwllGGQGS-------EKVAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK07791    9 VIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGS-----ASGGSaaqavvdEIVAAGGEAVANGDDIADWDGAANLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAA-----QALVSSGCRGSIINISSIVGKV 159
Cdd:PRK07791   84 DAAVETFGGL-DVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAaywraESKAGRAVDARIINTSSGAGLQ 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 160 GNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGfITTPMTQKV 215
Cdd:PRK07791  163 GSVGQGNYSAAKAGIAALTLVAAAELGR-------YGVTVNAIAPA-ARTRMTETV 210
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 12-226 9.95e-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: 128.93  E-value: 9.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05344     4 ALVTAASSGIGLAIARALAREGARVAICARNREN-------LERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05344    77 GR-VDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERG-WGRIVNISSLTVKEPEPNLVLSNVAR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQM 226
Cdd:cd05344   155 AGLIGLVKTLSRELA-------PDGVTVNSVLPGYIDTERVRRLLEARAEKEGIS 202
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
12-204 1.46e-35

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 135.36  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapgGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08324  425 ALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP--------DRALGVACDVTDEAAVQAAFEEAALAF 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrppSV--VVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISS---IVGKVGNVgqtN 166
Cdd:PRK08324  497 G---GVdiVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASknaVNPGPNFG---A 570

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953284729 167 YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLP 204
Cdd:PRK08324  571 YGAAKAAELHLVRQLALELGP-------DGIRVNGVNP 601
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 12-223 1.86e-35

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 128.11  E-value: 1.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdldRAAACETVWLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12936    9 ALVTGASGGIGEEIARLLHAQGAIVGL----HGTRVEKLEALAAELGERV------KIFPANLSDRDEVKALGQKAEADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12936   79 E-GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRR-YGRIINITSVVGVTGNPGQANYCASK 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:PRK12936  157 AGMIGFSKSLAQEIA-------TRNVTVNCVAPGFIESAMTGKLNDKQKEAI 201
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 6-211 1.21e-34

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 125.68  E-value: 1.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12828    4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTL---------PGVPADALRIGGIDLVDPQAARRAVD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK12828   75 EVNRQFGRL-DALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASG-GGRIVNIGAGAALKAGPGMG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:PRK12828  153 AYAAAKAGVARLTEALAAELLD-------RGITVNAVLPSIIDTPP 191
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 12-213 1.26e-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: 125.66  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACEtvwllggqgsekVAPGGAHTAFQADVSEAGAVRRLLEQVQACf 91
Cdd:cd05368     5 ALITAAAQGIGRAIALAFAREGANVIATDINEEKLKE------------LERGPGITTRVLDVTDKEQVAALAKEEGRI- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 srppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKV-GNVGQTNYAAS 170
Cdd:cd05368    72 ----DVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARK-DGSIINMSSVASSIkGVPNRFVYSTT 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953284729 171 KAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQ 213
Cdd:cd05368   147 KAAVIGLTKSVAADFA-------QQGIRCNAICPGTVDTPSLE 182
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-213 1.30e-34

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 131.51  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   8 RSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapggaHTAFQADVSEAGAVRRLLEQV 87
Cdd:PRK06484    4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPD----------HHALAMDVSDEAQIREGFEQL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  88 QACFSRPpSVVVSCAGLTrDEF---LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ 164
Cdd:PRK06484   74 HREFGRI-DVLVNNAGVT-DPTmtaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVNVASGAGLVALPKR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 165 TNYAASKAGVIGLTQTAARElgrlvrhpWGH-GIRCNSVLPGFITTPMTQ 213
Cdd:PRK06484  152 TAYSASKAAVISLTRSLACE--------WAAkGIRVNAVLPGYVRTQMVA 193
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 6-211 2.80e-34

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: 124.88  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggaHTafqaDVSEAGAVRRLLE 85
Cdd:cd05326     1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFV-----HC----DVTVEADVRAAVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPpSVVVSCAGL--TRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG 163
Cdd:cd05326    72 TAVARFGRL-DIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAK-KGSIVSVASVAGVVGGLG 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:cd05326   150 PHAYTASKHAVLGLTRSAATELGE-------HGIRVNCVSPYGVATPL 190
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
11-223 3.13e-34

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 124.74  E-value: 3.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATV-AACDLDRAAACEtvWLlggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK12938    5 IAYVTGGMGGIGTSICQRLHKDGFKVvAGCGPNSPRRVK--WL-----EDQKALGFDFIASEGNVGDWDSTKAAFDKVKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK12938   78 EVGEI-DVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGW-GRIINISSVNGQKGQFGQTNYST 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 170 SKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:PRK12938  156 AKAGIHGFTMSLAQEVAT-------KGVTVNTVSPGYIGTDMVKAIRPDVLEKI 202
PRK08589 PRK08589
SDR family oxidoreductase;
6-215 1.06e-33

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 124.12  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08589    3 RLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVS-ETV-------DKIKSNGGKAKAYHVDISDEQQVKDFAS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRpPSVVVSCAGLtrDEFLLRMSE---DDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNV 162
Cdd:PRK08589   75 EIKEQFGR-VDVLFNNAGV--DNAAGRIHEypvDVFDKIMAVDMRGTFLMTKMLLPLMMEQG--GSIINTSSFSGQAADL 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK08589  150 YRSGYNAAKGAVINFTKSIAIEYGR-------DGIRANAIAPGTIETPLVDKL 195
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 12-217 1.17e-33

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 123.61  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllgGQGSEKVAPG-----GAHTA--FQADVSEAGAVRRLL 84
Cdd:PRK12384    5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADIN------------SEKAANVAQEinaeyGEGMAygFGADATSEQSVLALS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPPSVVVScAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ 164
Cdd:PRK12384   73 RGVDEIFGRVDLLVYN-AGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQINSKSGKVGSKHN 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPG-FITTPMTQK-VPQ 217
Cdd:PRK12384  152 SGYSAAKFGGVGLTQSLALDLAE-------YGITVHSLMLGnLLKSPMFQSlLPQ 199
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 12-214 1.74e-33

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: 123.33  E-value: 1.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETV--WLLGGQGSeKVApggahtAFQADVSEAGAVRRLLEQVQA 89
Cdd:cd08940     5 ALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVraGLAAKHGV-KVL------YHGADLSKPAAIEDMVAYAQR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd08940    78 QFGGV-DILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGW-GRIINIASVHGLVASANKSAYVA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1953284729 170 SKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQK 214
Cdd:cd08940   156 AKHGVVGLTKVVALETA-------GTGVTCNAICPGWVLTPLVEK 193
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 12-217 4.15e-33

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: 121.69  E-value: 4.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVA---ACDLDRAAACETvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVinyRKSKDAAAEVAA---------EIEELGGKAVVVRADVSQPQDVEEMFAAVK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSRPPSVVV-SCAGLTRDefLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSiVGKVGnVGQTNY 167
Cdd:cd05359    72 ERFGRLDVLVSnAAAGAFRP--LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERG-GGRIVAISS-LGSIR-ALPNYL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 168 A--ASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:cd05359   147 AvgTAKAALEALVRYLAVELGP-------RGIRVNAVSPGVIDTDALAHFPN 191
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 11-218 4.31e-33

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: 122.19  E-value: 4.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINDLpDDDQATEVV-------AEVLAAGRRAIYFQADIGELSDHEALLDQAWE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRPpSVVVSCAGLT----RDefLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVS-----SGCRGSIINISSIVGKVG 160
Cdd:cd05337    76 DFGRL-DCLVNNAGIAvrprGD--LLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEqpdrfDGPHRSIIFVTSINAYLV 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 161 NVGQTNYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQKVPQK 218
Cdd:cd05337   153 SPNRGEYCISKAGLSMATRLLAYRLADE-------GIAVHEIRPGLIHTDMTAPVKEK 203
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-220 4.34e-33

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 121.72  E-value: 4.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVA-----ACDLDRAAacetvwllggqgsEKVAPGGAHTAFQ-ADVSEAGAV 80
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGllartEENLKAVA-------------EEVEAYGVKVVIAtADVSDYEEV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:PRK07666   72 TAAIEQLKNELGSI-DILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQ-SGDIINISSTAGQKG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 161 NVGQTNYAASKAGVIGLTQTAARElgrlVRHpwgHGIRCNSVLPGFITTPM------TQKVPQKVL 220
Cdd:PRK07666  150 AAVTSAYSASKFGVLGLTESLMQE----VRK---HNIRVTALTPSTVATDMavdlglTDGNPDKVM 208
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 12-228 4.34e-33

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: 121.32  E-value: 4.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwlLGGQGSEkvapggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd08932     3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS--ASGGDVE---------AVPYDARDPEDARALVDALRDRF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd08932    72 G-RIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAG-SGRVVFLNSLSGKRVLAGNAGYSASK 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELgrlvrhpWGHGIRCNSVLPGFITTPMTQK---VPQKVLDKMSQMRS 228
Cdd:cd08932   150 FALRALAHALRQEG-------WDHGVRVSAVCPGFVDTPMAQGltlVGAFPPEEMIQPKD 202
PRK05855 PRK05855
SDR family oxidoreductase;
11-227 5.86e-33

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 127.40  E-value: 5.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapGGAHtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK05855  317 LVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAG------AVAH-AYRVDVSDADAMEAFAEWVRAE 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK05855  390 HG-VPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTGGHIVNVASAAAYAPSRSLPAYATS 468

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 171 KAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMT------------QKVPQKVLDKMSQMR 227
Cdd:PRK05855  469 KAAVLMLSECLRAELA-------AAGIGVTAICPGFVDTNIVattrfagadaedEARRRGRADKLYQRR 530
PRK07774 PRK07774
SDR family oxidoreductase;
6-223 1.79e-32

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 120.23  E-value: 1.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK07774    3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGA-ERV------AKQIVADGGTAIAVQVDVSDPDSAKAMAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPPSVVVSCA--GLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKvgnVG 163
Cdd:PRK07774   76 ATVSAFGGIDYLVNNAAiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRG-GGAIVNQSSTAAW---LY 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKV-PQKVLDKM 223
Cdd:PRK07774  152 SNFYGLAKVGLNGLTQQLARELG-------GMNIRVNAIAPGPIDTEATRTVtPKEFVADM 205
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 12-211 2.87e-32

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 119.60  E-value: 2.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLdraaacetvwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08220   11 VWVTGAAQGIGYAVALAFVEAGAKVIGFDQ----------------AFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK08220   75 G-PLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQR-SGAIVTVGSNAAHVPRIGMAAYGASK 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK08220  153 AALTSLAKCVGLELA-------PYGVRCNVVSPGSTDTDM 185
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 12-224 3.88e-32

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 119.33  E-value: 3.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwLLGGQgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05323     3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAA--ELQAI-----NPKVKATFVQCDVTSWEQLAAAFKKAIEKF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLT--RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSS--GCRGSIINISSIVGKVGNVGQTNY 167
Cdd:cd05323    76 GR-VDILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNkgGKGGVIVNIGSVAGLYPAPQFPVY 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 168 AASKAGVIGLTQTAArelgrlVRHPWGHGIRCNSVLPGFITTPMTQKVPQKVLDKMS 224
Cdd:cd05323   155 SASKHGVVGFTRSLA------DLLEYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLP 205
PRK12743 PRK12743
SDR family oxidoreductase;
12-213 4.19e-32

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 119.37  E-value: 4.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAacdldraaaceTVWLLGGQGSEKVAP-----GGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK12743    5 AIVTASDSGIGKACALLLAQQGFDIG-----------ITWHSDEEGAKETAEevrshGVRAEIRQLDLSDLPEGAQALDK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK12743   74 LIQRLGRI-DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 167 YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK12743  153 YTAAKHALGGLTKAMALELVE-------HGILVNAVAPGAIATPMNG 192
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 12-220 5.08e-32

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 118.87  E-value: 5.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGgahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05374     3 VLITGCSSGIGLALALALAAQGYRVIATARNPDK-------LESLGELLNDNL---EVLELDVTDEESIKAAVKEVIERF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTrdEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05374    73 GRI-DVLVNNAGYG--LFgpLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQG-SGRIVNVSSVAGLVPTPFLGPYCA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 170 SKAGVIGLTQTAARELGrlvrhPWghGIRCNSVLPGFITTPMTQKVPQKVL 220
Cdd:cd05374   149 SKAALEALSESLRLELA-----PF--GIKVTIIEPGPVRTGFADNAAGSAL 192
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 4-210 8.45e-32

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 118.95  E-value: 8.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGAT-VAACDLDRAAacetvwllGGQGSEKVAPGGAHTAF-QADVSEAGAVR 81
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEK--------GEAQAAELEALGAKAVFvQADLSDVEDCR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  82 RLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGN 161
Cdd:PRK06198   73 RVVAAADEAFGRL-DALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTIVNIGSMSAHGGQ 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTP 210
Cdd:PRK06198  152 PFLAAYCASKGALATLTRNAAYALLR-------NRIRVNGLNIGWMATE 193
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 12-209 1.10e-31

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: 118.07  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDR-AAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05369     6 AFITGGGTGIGKAIAKAFAELGASVAIAgrKPEVlEAAAEEI---------SSATGGRAHPIQCDVRDPEAVEAAVDETL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSrPPSVVVSCAGltrDEFLL---RMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:cd05369    77 KEFG-KIDILINNAA---GNFLApaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITT 209
Cdd:cd05369   153 HSAAAKAGVDALTRSLAVEWGP-------YGIRVNAIAPGPIPT 189
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
6-224 1.23e-31

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 118.36  E-value: 1.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVaaCDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08226    3 KLTGKTALITGALQGIGEGIARVFARHGANL--ILLDISPEIEKL------ADELCGRGHRCTAVVADVRDPASVAAAIK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGK-VGNVGQ 164
Cdd:PRK08226   75 RAKEKEGRI-DILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARK-DGRIVMMSSVTGDmVADPGE 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV--------PQKVLDKMS 224
Cdd:PRK08226  153 TAYALTKAAIVGLTKSLAVEYAQ-------SGIRVNAICPGYVRTPMAESIarqsnpedPESVLTEMA 213
PRK07326 PRK07326
SDR family oxidoreductase;
12-241 2.57e-31

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 117.03  E-value: 2.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvAPGGAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK07326    9 ALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELN-------NKGNVL-GLAADVRDEADVQRAVDAIVAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07326   81 GG-LDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG--GYIINISSLAGTNFFAGGAAYNASK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELgrlvrHPwgHGIRCNSVLPGFITTPMTQKVPQKvldkmsqmrSHSWRLKTVDTSQA 241
Cdd:PRK07326  158 FGLVGFSEAAMLDL-----RQ--YGIKVSTIMPGSVATHFNGHTPSE---------KDAWKIQPEDIAQL 211
PRK07063 PRK07063
SDR family oxidoreductase;
6-212 3.48e-31

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 117.07  E-value: 3.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSekvapGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK07063    4 RLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVA-----GARVLAVPADVTDAASVAAAVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK07063   79 AAEEAFG-PLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERG-RGSIVNIASTHAFKIIPGCF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMT 212
Cdd:PRK07063  157 PYPVAKHGLLGLTRALGIEYAA-------RNVRVNAIAPGYIETQLT 196
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 6-216 4.25e-31

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 117.35  E-value: 4.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtafqaDVSEAGAVRRLLE 85
Cdd:PRK07825    2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVVGGPL-----------DVTDPASFAAFLD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK07825   71 AVEADL-GPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRG-RGHVVNVASLAGKIPVPGMA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVP 216
Cdd:PRK07825  149 TYCASKHAVVGFTDAARLELR-------GTGVHVSVVLPSFVNTELIAGTG 192
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 12-211 5.03e-31

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: 116.20  E-value: 5.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATV--AACDLDR-AAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd08939     4 VLITGGSSGIGKALAKELVKEGANViiVARSESKlEEAVEEI------EAEANASGQKVSYISADLSDYEEVEQAFAQAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYA 168
Cdd:cd08939    78 EKGG-PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQR-PGHIVFVSSQAALVGIYGYSAYC 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953284729 169 ASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:cd08939   156 PSKFALRGLAESLRQELK-------PYNIRVSVVYPPDTDTPG 191
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-218 6.14e-31

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 116.21  E-value: 6.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK12745    4 VALVTGGRRGIGLGIARALAAAGFDLAINDRpDDEELAATQQELRALGVEVIF-------FPADVADLSAHEAMLDAAQA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRPpSVVVSCAG---LTRDEfLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSS-----GCRGSIINISSIVGKVGN 161
Cdd:PRK12745   77 AWGRI-DCLVNNAGvgvKVRGD-LLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQpepeeLPHRSIVFVSSVNAIMVS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQK 218
Cdd:PRK12745  155 PNRGEYCISKAGLSMAAQLFAARLAE-------EGIGVYEVRPGLIKTDMTAPVTAK 204
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 12-215 6.58e-31

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: 116.48  E-value: 6.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvAPGGAhtafqADVSEAGAVRRLLEQVQACF 91
Cdd:cd08945     6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVE--ADGRT-----CDVRSVPEIEALVAAAVARY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQaaaQALVSSGCR----GSIINISSIVGKVGNVGQTNY 167
Cdd:cd08945    79 G-PIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTK---EVLKAGGMLergtGRIINIASTGGKQGVVHAAPY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 168 AASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQKV 215
Cdd:cd08945   155 SASKHGVVGFTKALGLELART-------GITVNAVCPGFVETPMAASV 195
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 7-214 7.81e-31

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 116.15  E-value: 7.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRA---AACETVWLLGGQGsekvapggAHTAfqADVSEAGAVRRL 83
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDganAVADEINKAGGKA--------IGVA--MDVTNEDAVNAG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:PRK13394   75 IDKVAERFG-SVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQK 214
Cdd:PRK13394  154 KSAYVTAKHGLLGLARVLAKEGA-------KHNVRSHVVCPGFVRTPLVDK 197
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 12-213 8.17e-31

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: 115.64  E-value: 8.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLdraaacetvwllggQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACf 91
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDL--------------PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAE- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05331    66 HGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRR-TGAIVTVASNAAHVPRISMAAYGASK 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQ 213
Cdd:cd05331   145 AALASLSKCLGLELA-------PYGVRCNVVSPGSTDTAMQR 179
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 6-211 9.09e-31

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 115.57  E-value: 9.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllgGQGSEKVA--PGGAHTAFQADVSEAGAVRRL 83
Cdd:cd05345     2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADIN------------ADGAERVAadIGEAAIAIQADVTKRADVEAM 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSRpPSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:cd05345    70 VEAALSKFGR-LDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQG-GGVIINIASTAGLRPRP 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:cd05345   148 GLTWYNASKGWVVTATKAMAVELAP-------RNIRVNCLCPVAGETPL 189
PRK05867 PRK05867
SDR family oxidoreductase;
7-213 3.25e-30

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 114.36  E-value: 3.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDA-------LEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ-- 164
Cdd:PRK05867   80 VTAELG-GIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASMSGHIINVPQqv 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK05867  159 SHYCASKAAVIHLTKAMAVELAP-------HKIRVNSVSPGYILTELVE 200
PRK07074 PRK07074
SDR family oxidoreductase;
11-210 3.36e-30

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 114.48  E-value: 3.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvapGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK07074    4 TALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALG---------DARFVPVACDLTDAASLAAALANAAAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGkVGNVGQTNYAAS 170
Cdd:PRK07074   75 RG-PVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRS-RGAVVNIGSVNG-MAALGHPAYSAA 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTP 210
Cdd:PRK07074  152 KAGLIHYTKLLAVEYGR-------FGIRANAVAPGTVKTQ 184
PRK07069 PRK07069
short chain dehydrogenase; Validated
 12-211 3.47e-30

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 114.42  E-value: 3.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQA--DVSEAGAVRRLLEQVQA 89
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAF------AAEINAAHGEGVAFAAvqDVTDEAQWQALLAQAAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK07069   76 AM-GGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQ-PASIVNISSVAAFKAEPDYTAYNA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953284729 170 SKAGVIGLTQTAARELGRLvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK07069  154 SKAAVASLTKSIALDCARR-----GLDVRCNSIHPTFIRTGI 190
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 6-213 1.04e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 113.29  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwllGGQGSEKVapGGahTAFQADVSEAGAVRRLLe 85
Cdd:PRK06057    4 RLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEA--------GKAAADEV--GG--LFVPTDVTDEDAVNALF- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 qvQACFSRPPSVVVSC--AGLT--RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:PRK06057   71 --DTAAETYGSVDIAFnnAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQG-KGSIINTASFVAVMGS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 162 -VGQTNYAASKAGVIGLTqtaaRELG-RLVRhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK06057  148 aTSQISYTASKGGVLAMS----RELGvQFAR----QGIRVNALCPGPVNTPLLQ 193
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 12-230 1.18e-29

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: 112.89  E-value: 1.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVAPggahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05364     6 AIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKI----LLVVADLTEEEGQDRIISTTLAKF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05364    82 GR-LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT--KGEIVNVSSVAGGRSFPGVLYYCISK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQK--VPQKVLDKMSQMRSHS 230
Cdd:cd05364   159 AALDQFTRCTALELAP-------KGVRVNSVSPGVIVTGFHRRmgMPEEQYIKFLSRAKET 212
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-211 1.26e-29

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 112.90  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVA-------EEIKKAGGEAIAVKGDVTVESDVVNLIQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08936   78 TAVKEFGTL-DVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKGNIINMSSVHEQIPWPLFV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:PRK08936  157 HYAASKGGVKLMTETLAMEYAP-------KGIRVNNIGPGAINTPI 195
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 11-217 1.47e-29

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: 112.94  E-value: 1.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllgGQGSEKVAP------GGAHTAFQADVSEAGAVRRLL 84
Cdd:cd05322     4 VAVVIGGGQTLGEFLCHGLAEAGYDVAVADIN------------SENAEKVADeinaeyGEKAYGFGADATNEQSVIALS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPPSVVVScAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ 164
Cdd:cd05322    72 KGVDEIFKRVDLLVYS-AGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQGRIIQINSKSGKVGSKHN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPG-FITTPMTQK-VPQ 217
Cdd:cd05322   151 SGYSAAKFGGVGLTQSLALDLAE-------HGITVNSLMLGnLLKSPMFQSlLPQ 198
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 1-211 3.07e-29

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 112.03  E-value: 3.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllggQGSEKvapGGAHTAFQADVSEAGAV 80
Cdd:PRK06171    1 MQDWLNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-------------GGDGQ---HENYQFVPTDVSSAEEV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSRPpSVVVSCAGLTRDEFLL---------RMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIIN 151
Cdd:PRK06171   65 NHTVAEIIEKFGRI-DGLVNNAGINIPRLLVdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQH-DGVIVN 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 152 ISSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFI-TTPM 211
Cdd:PRK06171  143 MSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGK-------HNIRVVGVAPGILeATGL 196
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 1-213 3.27e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 111.77  E-value: 3.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahTAFqaDVSEAGAV 80
Cdd:PRK08085    1 MNDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHA-----APF--NVTHKQEV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:PRK08085   74 EAAIEHIEKDIG-PIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQ-AGKIINICSMQSELG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 161 NVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK08085  152 RDTITPYAASKGAVKMLTRGMCVELAR-------HNIQVNGIAPGYFKTEMTK 197
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 6-223 4.69e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 111.58  E-value: 4.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAAcetvwLLGGQGSEKVApggahtaFQADVSEAGAV 80
Cdd:PRK08213    9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSarkaeELEEAAA-----HLEALGIDALW-------IAADVADEADI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVG 160
Cdd:PRK08213   77 ERLAEETLERFG-HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRGYGRIINVASVAGLGG 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 161 N----VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKM 223
Cdd:PRK08213  156 NppevMDTIAYNTSKGAVINFTRALAAEWGP-------HGIRVNAIAPGFFPTKMTRGTLERLGEDL 215
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 7-233 5.49e-29

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: 111.17  E-value: 5.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapggAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGP----------AACAISLDVTDQASIDRCVAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05363    71 LVDRWGSI-DILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGGKIINMASQAGRRGEALVGV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 167 YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQMRSHSWRL 233
Cdd:cd05363   150 YCATKAAVISLTQSAGLNLIR-------HGINVNAIAPGVVDGEHWDGVDAKFARYENRPRGEKKRL 209
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 13-232 7.73e-29

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: 111.07  E-value: 7.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllgGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:cd05330     7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAA-----KAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:cd05330    82 RIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGS-GMIVNTASVGGIRGVGNQSGYAAAKH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 173 GVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMtqkvpqkVLDKMSQMRSHSWR 232
Cdd:cd05330   161 GVVGLTRNSAVEYGQ-------YGIRINAIAPGAILTPM-------VEGSLKQLGPENPE 206
PRK07831 PRK07831
SDR family oxidoreductase;
7-224 7.77e-29

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 110.89  E-value: 7.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGA-GSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK07831   15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAAE-----LGLGRVEAVVCDVTSEAQVDALID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK07831   90 AAVERLGRL-DVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVNNASVLGWRAQHGQA 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKV-PQKVLDKMS 224
Cdd:PRK07831  169 HYAAAKAGVMALTRCSALEAA-------EYGVRINAVAPSIAMHPFLAKVtSAELLDELA 221
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 6-213 7.85e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 110.79  E-value: 7.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATV--AAcdlDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:PRK07478    3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVvvGA---RRQAELDQL------VAEIRAEGGEAVALAGDVRDEAYAKAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSRpPSVVVSCAGLTRDEF-LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG-KVGN 161
Cdd:PRK07478   74 VALAVERFGG-LDIAFNNAGTLGEMGpVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARG-GGSLIFTSTFVGhTAGF 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK07478  152 PGMAAYAASKAGLIGLTQVLAAEYGA-------QGIRVNALLPGGTDTPMGR 196
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-215 2.32e-28

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 109.82  E-value: 2.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGA----TVAACDLDraaacETVWLLGGQGsEKVapggahTAFQADVSEAGAVR 81
Cdd:PRK06935   12 SLDGKVAIVTGGNTGLGQGYAVALAKAGAdiiiTTHGTNWD-----ETRRLIEKEG-RKV------TFVQVDLTKPESAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  82 RLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:PRK06935   80 KVVKEALEEFGKI-DILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQG-SGKIINIASMLSFQGG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK06935  158 KFVPAYTASKHGVAGLTKAFANELAA-------YNIQVNAIAPGYIKTANTAPI 204
PRK06398 PRK06398
aldose dehydrogenase; Validated
 7-225 3.22e-28

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 109.15  E-value: 3.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRaaacetvwllggqgsekvaPGGAHTA-FQADVSEAGAVRRLLE 85
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKE-------------------PSYNDVDyFKVDVSNKEQVIKGID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK06398   65 YVISKYGR-IDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD-KGVIINIASVQSFAVTRNAA 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRLvrhpwghgIRCNSVLPGFITTPMTQKV--------PQKVLDKMSQ 225
Cdd:PRK06398  143 AYVTSKHAVLGLTRSIAVDYAPT--------IRCVAVCPGSIRTPLLEWAaelevgkdPEHVERKIRE 202
PRK06484 PRK06484
short chain dehydrogenase; Validated
 1-217 6.83e-28

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 112.64  E-value: 6.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapggaHTAFQADVSEAGAV 80
Cdd:PRK06484  261 APSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDE----------HLSVQADITDEAAV 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSrPPSVVVSCAGLTrDEFL--LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGK 158
Cdd:PRK06484  331 ESAFAQIQARWG-RLDVLVNNAGIA-EVFKpsLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG---GVIVNLGSIASL 405

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 159 VGNVGQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:PRK06484  406 LALPPRNAYCASKAAVTMLSRSLACEWA-------PAGIRVNTVAPGYIETPAVLALKA 457
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 12-204 1.62e-27

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: 107.09  E-value: 1.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggQGSEKVAPGGAHT-AFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd08943     4 ALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIA---------EKVAEAAQGGPRAlGVQCDVTSEAQVQSAFEQAVLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd08943    75 FG-GLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAA 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLP 204
Cdd:cd08943   154 KAAEAHLARCLALEGGE-------DGIRVNTVNP 180
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 6-217 1.86e-27

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: 107.38  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLD--RAAACETVWLLGGQGSEKVA-PGgahtafqaDVSEAGAVRR 82
Cdd:cd05355    23 KLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPeeEDDAEETKKLIEEEGRKCLLiPG--------DLGDESFCRD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSRpPSVVVSCAGLTRDEF-LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvssGCRGSIINISSIVGKVGN 161
Cdd:cd05355    95 LVKEVVKEFGK-LDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHL---KKGSSIINTTSVTAYKGS 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM------TQKVPQ 217
Cdd:cd05355   171 PHLLDYAATKGAIVAFTRGLSLQLAE-------KGIRVNAVAPGPIWTPLipssfpEEKVSE 225
PRK07832 PRK07832
SDR family oxidoreductase;
12-215 3.03e-27

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 107.05  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSeKVApggAHTAFqaDVSEAGAVRRLLEQVQACF 91
Cdd:PRK07832    3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGG-TVP---EHRAL--DISDYDAVAAFAADIHAAH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07832   77 G-SMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK07832  156 FGLRGLSEVLRFDLAR-------HGIGVSVVVPGAVKTPLVNTV 192
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-215 4.55e-27

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 106.11  E-value: 4.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLdrAAACETVwllggqgsEKV-APGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINI--VEPTETI--------EQVtALGRRFLSLTADLRKIDGIPALLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08993   78 RAVAEFGHI-DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVP 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK08993  157 SYTASKSGVMGVTRLMANEWAK-------HNINVNAIAPGYMATNNTQQL 199
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-212 4.67e-27

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 106.30  E-value: 4.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHTaFQADVSEAGAVRRLLEQ 86
Cdd:PRK07097    8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIE------AHG-YVCDVTDEDGVQAMVSQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK07097   81 IEKEVG-VIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKG-HGKIINICSMMSELGRETVSA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 167 YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMT 212
Cdd:PRK07097  159 YAAAKGGLKMLTKNIASEYGE-------ANIQCNGIGPGYIATPQT 197
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 11-207 5.62e-27

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: 105.88  E-value: 5.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd08930     4 IILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVI------ALELDITSKESIKELIESYLEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPpSVVVSCAGLT-RDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG----KVGNVG 163
Cdd:cd08930    78 FGRI-DILINNAYPSpKVWGsrFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQG-KGSIINIASIYGviapDFRIYE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 164 QTN------YAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFI 207
Cdd:cd08930   156 NTQmyspveYSVIKAGIIHLTKYLAKYYA-------DTGIRVNAISPGGI 198
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 10-222 5.97e-27

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: 105.05  E-value: 5.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  10 ALALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVwllggQGSEKVapGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVhYNRSEAEAQRLK-----DELNAL--RNSAVLVQADLSDFAACADLVAAAF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvSSGCRGSIINISSIVGKVGNVGQTNYA 168
Cdd:cd05357    74 RAFGRC-DVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRL-AGSRNGSIINIIDAMTDRPLTGYFAYC 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 169 ASKAGVIGLTQTAARELGRLvrhpwghgIRCNSVLPGFITTP--MTQKVPQKVLDK 222
Cdd:cd05357   152 MSKAALEGLTRSAALELAPN--------IRVNGIAPGLILLPedMDAEYRENALRK 199
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 5-218 9.10e-27

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: 104.86  E-value: 9.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDR-AAACETVwllggqgsekvapggahTAFQADVSEAG 78
Cdd:cd05351     3 LDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVsrtqaDLDSlVRECPGI-----------------EPVCVDLSDWD 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  79 AVRRLLEQVQacfsrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGK 158
Cdd:cd05351    66 ATEEALGSVG-----PVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQ 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 159 VGNVGQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKV---PQK 218
Cdd:cd05351   141 RALTNHTVYCSTKAALDMLTKVMALELG-------PHKIRVNSVNPTVVMTDMGRDNwsdPEK 196
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-214 2.16e-26

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 103.89  E-value: 2.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLdraaacetvwllggqgSEKVAPGGAHTAFQADVSEAgavrrlleqVQACFS 92
Cdd:PRK06550    9 LITGAASGIGLAQARAFLAQGAQVYGVDK----------------QDKPDLSGNFHFLQLDLSDD---------LEPLFD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPPSVVVSC--AGLTRD-EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK06550   64 WVPSVDILCntAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERK-SGIIINMCSIASFVAGGGGAAYTA 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1953284729 170 SKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQK 214
Cdd:PRK06550  143 SKHALAGFTKQLALDYAK-------DGIQVFGIAPGAVKTPMTAA 180
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-215 2.42e-26

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: 104.46  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVA-------KEITALGGRAIALAADVLDRASLERAREE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRpPSVVVSCAG------LTRDEFLLR--------MSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINI 152
Cdd:cd08935    76 IVAQFGT-VDILINGAGgnhpdaTTDPEHYEPeteqnffdLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQK-GGSIINI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 153 SSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKV 215
Cdd:cd08935   154 SSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFA-------TTGVRVNAIAPGFFVTPQNRKL 209
PRK08267 PRK08267
SDR family oxidoreductase;
13-241 2.54e-26

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 104.25  E-value: 2.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAfQADVSEAGAVRRLLEQvqacFS 92
Cdd:PRK08267    5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGA--------GNAWTG-ALDVTDRAAWDAALAD----FA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPPS----VVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQAL-VSSGCRgsIINISSIVGKVGNVGQTNY 167
Cdd:PRK08267   72 AATGgrldVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLkATPGAR--VINTSSASAIYGQPGLAVY 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 168 AASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVldKMSQMRSHSWRLKTVDTSQA 241
Cdd:PRK08267  150 SATKFAVRGLTEALDLEWRR-------HGIRVADVMPLFVDTAMLDGTSNEV--DAGSTKRLGVRLTPEDVAEA 214
PRK09730 PRK09730
SDR family oxidoreductase;
10-211 3.24e-26

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 103.78  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  10 ALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWllggqgSEKVAPGGAHTAFQADVSEAgavrrllEQVQA 89
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVV------NLITQAGGKAFVLQADISDE-------NQVVA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSR------PPSVVVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQ--ALVSSGCRGSIINISSIVGKVG 160
Cdd:PRK09730   69 MFTAidqhdePLAALVNNAGiLFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKrmALKHGGSGGAIVNVSSAASRLG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 161 NVGQ-TNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK09730  149 APGEyVDYAASKGAIDTLTTGLSLEVA-------AQGIRVNCVRPGFIYTEM 193
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-217 5.67e-26

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 103.26  E-value: 5.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA-ACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLE 85
Cdd:PRK06077    4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEeMNETLKMVKENGGEGI-------GVLADVSTREGCETLAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRpPSVVVSCAGLTRdeFLLRMSEDD--WDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGKVGNVG 163
Cdd:PRK06077   77 ATIDRYGV-ADILVNNAGLGL--FSPFLNVDDklIDKHISTDFKSVIYCSQELAKEMREG---GAIVNIASVAGIRPAYG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGRlvrhpwghGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:PRK06077  151 LSIYGAMKAAVINLTKYLALELAP--------KIRVNAIAPGFVKTKLGESLFK 196
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-212 1.29e-25

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 102.17  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVA---ACDLDRAaacetvwllggqgsEKVAPGGAHTaFQADVSEAGAVRR 82
Cdd:PRK06463    4 RFKGKVALITGGTRGIGRAIAEAFLREGAKVAvlyNSAENEA--------------KELREKGVFT-IKCDVGNRDQVKK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSRpPSVVVSCAG----LTRDEFllrmSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGk 158
Cdd:PRK06463   69 SKEVVEKEFGR-VDVLVNNAGimylMPFEEF----DEEKYNKMIKINLNGAIYTTYEFLPLLKLSK-NGAIVNIASNAG- 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 159 VGN--VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMT 212
Cdd:PRK06463  142 IGTaaEGTTFYAITKAGIIILTRRLAFELGK-------YGIRVNAVAPGWVETDMT 190
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-212 1.78e-25

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 101.91  E-value: 1.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETvwllggqgSEKV-APGGAHTAFQADVSEAGAVRR 82
Cdd:PRK12481    3 LFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVG--VGVAEAPET--------QAQVeALGRKFHFITADLIQQKDIDS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNV 162
Cdd:PRK12481   73 IVSQAVEVMGHI-DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGKIINIASMLSFQGGI 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMT 212
Cdd:PRK12481  152 RVPSYTASKSAVMGLTRALATELSQ-------YNINVNAIAPGYMATDNT 194
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 7-219 2.60e-25

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: 101.32  E-value: 2.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAAACETVWLLG--GQGSEKV-APGGAHTAFQADVSEAGAVR 81
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVvvAAKTASEGDNGSAKSLPGtiEETAEEIeAAGGQALPIVVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  82 RLLEQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:cd05338    81 ALVEATVDQFGR-LDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAG-QGHILNISPPLSLRPA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPG-FITTP-MTQKVPQKV 219
Cdd:cd05338   159 RGDVAYAAGKAGMSRLTLGLAAELRR-------HGIAVNSLWPStAIETPaATELSGGSD 211
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 14-213 3.25e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 101.19  E-value: 3.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  14 VTGAGSGIGRAVSVRLAKEGATVA-----ACDLDRAAAcetvwllggqgseKVAPGGAHT-AFQADVSEAGAVRRLLEQV 87
Cdd:PRK07890   10 VSGVGPGLGRTLAVRAARAGADVVlaartAERLDEVAA-------------EIDDLGRRAlAVPTDITDEDQCANLVALA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  88 QACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNY 167
Cdd:PRK07890   77 LERFGRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG--GSIVMINSMVLRHSQPKYGAY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 168 AASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK07890  155 KMAKGALLAASQSLATELGP-------QGIRVNSVAPGYIWGDPLK 193
PRK07454 PRK07454
SDR family oxidoreductase;
7-211 3.34e-25

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 100.80  E-value: 3.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVA--ACDLDRAAACetvwllggqgSEKVAPGGAHTAFQA-DVSEAGAVRRL 83
Cdd:PRK07454    4 NSMPRALITGASSGIGKATALAFAKAGWDLAlvARSQDALEAL----------AAELRSTGVKAAAYSiDLSNPEAIAPG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVG 163
Cdd:PRK07454   74 IAELLEQFG-CPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGG-GLIINVSSIAARNAFPQ 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 164 QTNYAASKAGVIGLTQTAARElgrlVRhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK07454  152 WGAYCVSKAALAAFTKCLAEE----ER---SHGIRVCTITLGAVNTPL 192
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 1-209 4.02e-25

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 101.52  E-value: 4.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAV 80
Cdd:PRK08277    2 MPNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVV-------AEIKAAGGEALAVKADVLDKESL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSRpPSVVVSCAG------LTRDEFLLR---------MSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGC 145
Cdd:PRK08277   75 EQARQQILEDFGP-CDILINGAGgnhpkaTTDNEFHELieptktffdLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 146 rGSIINISSIVG-----KVgnVGqtnYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITT 209
Cdd:PRK08277  154 -GNIINISSMNAftpltKV--PA---YSAAKAAISNFTQWLAVHFAKV-------GIRVNAIAPGFFLT 209
PRK07035 PRK07035
SDR family oxidoreductase;
7-209 5.57e-25

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 100.48  E-value: 5.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDlDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK07035    6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSS-RKLDGCQAV------ADAIVAAGGKAEALACHIGEMEQIDALFAH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRPPSVVVSCAglTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK07035   79 IRERHGRLDILVNNAA--ANPYFghILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQG-GGSIVNVASVNGVSPGDFQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITT 209
Cdd:PRK07035  156 GIYSITKAAVISMTKAFAKECA-------PFGIRVNALLPGLTDT 193
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 6-211 6.82e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 100.88  E-value: 6.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA-ACETVWLLGGQGSEKVAPGGahtafqaDVSEAGAVRRLL 84
Cdd:PRK06701   43 KLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLIPG-------DVSDEAFCKDAV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvSSGcrGSIINISSIVGKVGNVGQ 164
Cdd:PRK06701  116 EETVRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQG--SAIINTGSITGYEGNETL 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK06701  193 IDYSATKGAIHAFTRSLAQSLV-------QKGIRVNAVAPGPIWTPL 232
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 6-215 7.18e-25

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: 100.22  E-value: 7.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA--ACETVWllggqgSEKvapGGAHTAFQADVSEAGAVRRL 83
Cdd:cd05329     3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKEldECLTEW------REK---GFKVEGSVCDVSSRSERQEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVG 163
Cdd:cd05329    74 MDTVASHFGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGN-GNIVFISSVAGVIAVPS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 164 QTNYAASKAGVIGLTQTAARElgrlvrhpWGH-GIRCNSVLPGFITTPMTQKV 215
Cdd:cd05329   153 GAPYGATKGALNQLTRSLACE--------WAKdNIRVNAVAPWVIATPLVEPV 197
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 1-229 1.04e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 100.81  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAV 80
Cdd:PRK05872    1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGG--------DDRVLTVVADVTDLAAM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVG 160
Cdd:PRK05872   73 QAAAEEAVERFGG-IDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIER--RGYVLQVSSLAAFAA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 161 NVGQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKvLDKMSQMRSH 229
Cdd:PRK05872  150 APGMAAYCASKAGVEAFANALRLEVA-------HHGVTVGSAYLSWIDTDLVRDADAD-LPAFRELRAR 210
PRK09242 PRK09242
SDR family oxidoreductase;
6-215 1.16e-24

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 99.82  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAAACETVWLlggqgseKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:PRK09242    6 RLDGQTALITGASKGIGLAIAREFLGLGADVliVARDADALAQARDELA-------EEFPEREVHGLAADVSDDEDRRAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG 163
Cdd:PRK09242   79 LDWVEDHWDG-LHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHA-SSAIVNIGSVSGLTHVRS 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 164 QTNYAASKAGVIGLTQTAARElgrlvrhpW-GHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK09242  157 GAPYGMTKAALLQMTRNLAVE--------WaEDGIRVNAVAPWYIRTPLTSGP 201
PRK06500 PRK06500
SDR family oxidoreductase;
6-214 1.60e-24

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 99.26  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK06500    3 RLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAA----------RAELGESALVIRADAGDVAAQKALAQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPPSVVVScAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGKVGNVGQT 165
Cdd:PRK06500   73 ALAEAFGRLDAVFIN-AGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANP---ASIVLNGSINAHIGMPNSS 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 166 NYAASKAGVIGLTQTAARELgrlvrhpWGHGIRCNSVLPGFITTPMTQK 214
Cdd:PRK06500  149 VYAASKAALLSLAKTLSGEL-------LPRGIRVNAVSPGPVQTPLYGK 190
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 6-225 1.84e-24

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 99.31  E-value: 1.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwllggqGSEKVAPGGAHTAF-QADVSEAGAVRRLL 84
Cdd:PRK08265    3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADN-----------GAAVAASLGERARFiATDITDDAAIERAV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPpSVVVSCAGLTRDEFLlRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQ 164
Cdd:PRK08265   72 ATVVARFGRV-DILVNLACTYLDDGL-ASSRADWLAALDVNLVSAAMLAQAAHPHLARGG--GAIVNFTSISAKFAQTGR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPmtqkvpqkVLDKMSQ 225
Cdd:PRK08265  148 WLYPASKAAIRQLTRSMAMDLA-------PDGIRVNSVSPGWTWSR--------VMDELSG 193
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 12-213 7.37e-24

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 97.53  E-value: 7.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHT-AFqaDVSEAGAVRRLLEQVQAC 90
Cdd:PRK07523   13 ALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLS------AHAlAF--DVTDHDAVRAAIDAFEAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK07523   85 IG-PIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARG-AGKIINIASVQSALARPGIAPYTAT 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK07523  163 KGAVGNLTKGMATDWAK-------HGLQCNAIAPGYFDTPLNA 198
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 13-207 8.89e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 97.06  E-value: 8.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK07677    5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEA-------KLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPPSVVVSCAGltrdEFL---LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK07677   78 RIDALINNAAG----NFIcpaEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINMVATYAWDAGPGVIHSAA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 170 SKAGVIGLTQTAARElgrlvrhpWG--HGIRCNSVLPGFI 207
Cdd:PRK07677  154 AKAGVLAMTRTLAVE--------WGrkYGIRVNAIAPGPI 185
PRK06124 PRK06124
SDR family oxidoreductase;
1-209 2.39e-23

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 96.32  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLggqgsekVAPGGAHTAFQADVSEAGAV 80
Cdd:PRK06124    3 ILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAAL-------RAAGGAAEALAFDIADEEAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:PRK06124   76 AAAFARIDAEHGRL-DILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQG-YGRIIAITSIAGQVA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 161 NVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITT 209
Cdd:PRK06124  154 RAGDAVYPAAKQGLTGLMRALAAEFGP-------HGITSNAIAPGYFAT 195
PRK06947 PRK06947
SDR family oxidoreductase;
13-209 3.44e-23

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 95.64  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06947    6 LITGASRGIGRATAVLAAARGWSVGINYArDAAAAEETADAVR-------AAGGRACVVAGDVANEADVIAMFDAVQSAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSS--GCRGSIINISSIVGKVGNVGQ-TNYA 168
Cdd:PRK06947   79 GRLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrgGRGGAIVNVSSIASRLGSPNEyVDYA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1953284729 169 ASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITT 209
Cdd:PRK06947  159 GSKGAVDTLTLGLAKELGP-------HGVRVNAVRPGLIET 192
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 12-241 4.38e-23

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: 94.88  E-value: 4.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvapGGAHTAfQADVSEAGAVRRLLEQVQACF 91
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQEL---------EGVLGL-AGDVRDEADVRRAVDAMEEAF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd08929    73 GG-LDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRG-GGTIVNVGSLAGKNAFKGGAAYNASK 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELgrlvrHPWghGIRCNSVLPGFITTPMTQKVPQKvldkmsqmrshSWRLKTVDTSQA 241
Cdd:cd08929   151 FGLLGLSEAAMLDL-----REA--NIRVVNVMPGSVDTGFAGSPEGQ-----------AWKLAPEDVAQA 202
PRK08628 PRK08628
SDR family oxidoreductase;
5-214 5.43e-23

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 95.03  E-value: 5.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVWllggqgSEKVAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK08628    3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVI--FGRSAPDDEFA------EELRALQPRAEFVQVDLTDDAQCRDAV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPPSVVvSCAGlTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSivgKVGNVGQ 164
Cdd:PRK08628   75 EQTVAKFGRIDGLV-NNAG-VNDGVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKAS--RGAIVNISS---KTALTGQ 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 165 TN---YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQK 214
Cdd:PRK08628  148 GGtsgYAAAKGAQLALTREWAVALAK-------DGVRVNAVIPAEVMTPLYEN 193
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-240 6.13e-23

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 95.16  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRL 83
Cdd:PRK08642    1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRA----------IALQADVTDREQVQAM 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSRPPSVVVSCA-------GLTRDEFlLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIV 156
Cdd:PRK08642   71 FATATEHFGKPITTVVNNAladfsfdGDARKKA-DDITWEDFQQQLEGSVKGALNTIQAALPGMREQG-FGRIINIGTNL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 157 GKVGNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFI-TTPMTQKVPQKVLDKMSQMRShswrLKT 235
Cdd:PRK08642  149 FQNPVVPYHDYTTAKAALLGLTRNLAAELGP-------YGITVNMVSGGLLrTTDASAATPDEVFDLIAATTP----LRK 217


                  ....*
gi 1953284729 236 VDTSQ 240
Cdd:PRK08642  218 VTTPQ 222
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 7-227 7.03e-23

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: 94.53  E-value: 7.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVaacdldrAAACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAV-------AIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVER 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRpPSVVVSCAGLtrdeFLLRMSED----DWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:cd08934    74 TVEALGR-LDILVNNAGI----MLLGPVEDadttDWTRMIDTNLLGLMYTTHAALPHHLLRN-KGTIVNISSVAGRVAVR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQMR 227
Cdd:cd08934   148 NSAVYNATKFGVNAFSEGLRQEVTE-------RGVRVVVIEPGTVDTELRDHITHTITKEAYEER 205
PRK05650 PRK05650
SDR family oxidoreductase;
13-209 1.38e-22

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 94.34  E-value: 1.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapGGAHTAfQADVSEagaVRRLLEQVQACFS 92
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAG------GDGFYQ-RCDVRD---YSQLTALAQACEE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 R--PPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK05650   74 KwgGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQK-SGRIVNIASMAGLMQGPAMSSYNVA 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953284729 171 KAGVIGLTQTAARELgrlvrHPWGHGIRCnsVLPGFITT 209
Cdd:PRK05650  153 KAGVVALSETLLVEL-----ADDEIGVHV--VCPSFFQT 184
PRK06181 PRK06181
SDR family oxidoreductase;
11-209 1.58e-22

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 93.89  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK06181    3 VVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEAL-------VVPTDVSDAEACERLIEAAVAR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRpPSVVVSCAGLTRDEFLLRMSEDDW-DRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK06181   76 FGG-IDILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKAS--RGQIVVVSSLAGLTGVPTRSGYAA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 170 SKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITT 209
Cdd:PRK06181  153 SKHALHGFFDSLRIELA-------DDGVAVTVVCPGFVAT 185
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 1-207 2.76e-22

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 93.48  E-value: 2.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGA--TVAACDLDRAAAceTVWLLGgqgsekvAPGGAHTAFQADVSEAG 78
Cdd:PRK07576    1 MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGAnvAVASRSQEKVDA--AVAQLQ-------QAGPEGLGVSADVRDYA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  79 AVRRLLEQVQACFSrPPSVVVS-CAGltrdEFL---LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISS 154
Cdd:PRK07576   72 AVEAAFAQIADEFG-PIDVLVSgAAG----NFPapaAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG--ASIIQISA 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 155 IVGKVGNVGQTNYAASKAGVIGLTQTAARElgrlvrhpWG-HGIRCNSVLPGFI 207
Cdd:PRK07576  145 PQAFVPMPMQAHVCAAKAGVDMLTRTLALE--------WGpEGIRVNSIVPGPI 190
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 3-220 3.52e-22

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 92.99  E-value: 3.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   3 SPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllgGQGSEKV-APGGAHTAFQADVSEAGAVR 81
Cdd:PRK06113    5 DNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAA--------NHVVDEIqQLGGQAFACRCDITSEQELS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  82 RLLEQVQACFSRPPSVVVSCAGLTRDEFLLRMseDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:PRK06113   77 ALADFALSKLGKVDILVNNAGGGGPKPFDMPM--ADFRRAYELNVFSFFHLSQLVAPEMEKNG-GGVILTITSMAAENKN 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTP-----MTQKVPQKVL 220
Cdd:PRK06113  154 INMTSYASSKAAASHLVRNMAFDLGE-------KNIRVNGIAPGAILTDalksvITPEIEQKML 210
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-209 5.24e-22

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 92.96  E-value: 5.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   3 SPLRLRSALALVTGAGSGIGRAVsVRL-AKEGATVAACDLDRAAACETVWLLGGQgsEKVApggahtAFQADVSEAGAVR 81
Cdd:PLN02253   12 PSQRLLGKVALVTGGATGIGESI-VRLfHKHGAKVCIVDLQDDLGQNVCDSLGGE--PNVC------FFHCDVTVEDDVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  82 RLLEQVQACFSrPPSVVVSCAGLTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKV 159
Cdd:PLN02253   83 RAVDFTVDKFG-TLDIMVNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLK-KGSIVSLCSVASAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 160 GNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITT 209
Cdd:PLN02253  161 GGLGPHAYTGSKHAVLGLTRSVAAELGK-------HGIRVNCVSPYAVPT 203
PRK07856 PRK07856
SDR family oxidoreductase;
4-209 6.62e-22

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 92.30  E-value: 6.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACdldraaacetvwllGGQGSEKVAPGGAHTAfQADVSEAGAVRRL 83
Cdd:PRK07856    1 NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVC--------------GRRAPETVDGRPAEFH-AADVRDPDQVAAL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:PRK07856   66 VDAIVERHGR-LDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGGSIVNIGSVSGRRPSPG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 164 QTNYAASKAGVIGLTQTAARElgrlvrhpWGHGIRCNSVLPGFITT 209
Cdd:PRK07856  145 TAAYGAAKAGLLNLTRSLAVE--------WAPKVRVNAVVVGLVRT 182
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 12-215 1.01e-21

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: 91.24  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRaaacetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAarRTDR---------LDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05350    72 ELG-GLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKG-RGHLVLISSVAALRGLPGAAAYSA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 170 SKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:cd05350   150 SKAALSSLAESLRYDVKK-------RGIRVTVINPGFIDTPLTANM 188
PRK06194 PRK06194
hypothetical protein; Provisional
 12-225 1.27e-21

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 92.00  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06194    9 AVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVL-------GVRTDVSDAAQVEALADAALERF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQA-----AAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK06194   82 G-AVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAftplmLAAAEKDPAYEGHIVNTASMAGLLAPPAMGI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 167 YAASKAGVIGLTQTAARELgRLVrhpwGHGIRCNSVLPGFITTPMTQ---------------KVPQKVLDKMSQ 225
Cdd:PRK06194  161 YNVSKHAVVSLTETLYQDL-SLV----TDQVGASVLCPYFVPTGIWQsernrpadlantappTRSQLIAQAMSQ 229
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 6-241 2.81e-21

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: 90.26  E-value: 2.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACdldrAAACETVWLLGGQGSEkvAPGGAHTAFQADVSEAgavrrllE 85
Cdd:cd05343     3 RWRGRVALVTGASVGIGAAVARALVQHGMKVVGC----ARRVDKIEALAAECQS--AGYPTLFPYQCDLSNE-------E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPPS------VVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGC-RGSIINISSIVG- 157
Cdd:cd05343    70 QILSMFSAIRTqhqgvdVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVdDGHIININSMSGh 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 158 KVGNVGQTN-YAASKAGVIGLTQTAARELGRLVRHpwghgIRCNSVLPGFITTPMTQKVPQKVLDKMSQMRSHSWRLKTV 236
Cdd:cd05343   150 RVPPVSVFHfYAATKHAVTALTEGLRQELREAKTH-----IRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPE 224


                  ....*
gi 1953284729 237 DTSQA 241
Cdd:cd05343   225 DVANA 229
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 12-225 3.68e-21

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: 89.82  E-value: 3.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05349     3 VLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAG--------ERAI-AIQADVRDRDQVQAMIEEAKNHF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSED--DWDRV---IAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05349    74 GPVDTIVNNALIDFPFDPDQRKTFDtiDWEDYqqqLEGAVKGALNLLQAVLPDFKERG-SGRVINIGTNLFQNPVVPYHD 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 167 YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFI-TTPMTQKVPQKVLDKMSQ 225
Cdd:cd05349   153 YTTAKAALLGFTRNMAKELGP-------YGITVNMVSGGLLkVTDASAATPKEVFDAIAQ 205
PRK12746 PRK12746
SDR family oxidoreductase;
7-215 4.56e-21

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 90.09  E-value: 4.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12746    4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETI-------REIESNGGKAFLIEADLNSIDGVKKLVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACF-----SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQaaaQALVSSGCRGSIINISSIVGKVG 160
Cdd:PRK12746   77 QLKNELqirvgTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQ---QTLPLLRAEGRVINISSAEVRLG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 161 NVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK12746  154 FTGSIAYGLSKGALNTMTLPLAKHLGE-------RGITVNTIMPGYTKTDINAKL 201
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 12-224 6.66e-21

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: 87.96  E-value: 6.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGAtvaacdldraaacetvwllggqgsekvapggahtafqadvseagavrrllEQVQACF 91
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRGS--------------------------------------------------PKVLVVS 30

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAaQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd02266    31 RR--DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAA-RELMKAKRLGRFILISSVAGLFGAPGLGGYAASK 107

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 172 AGVIGLTQTAARELgrlvrhpWGHGIRCNSVLPGFITTPMTQKVPQKVLDKMS 224
Cdd:cd02266   108 AALDGLAQQWASEG-------WGNGLPATAVACGTWAGSGMAKGPVAPEEILG 153
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 12-209 6.75e-21

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: 89.26  E-value: 6.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDlDRAAACETVWL-LGGQGSEKVAPggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05346     3 VLITGASSGIGEATARRFAKAGAKLILTG-RRAERLQELADeLGAKFPVKVLP------LQLDVSDRESIEAALENLPEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRpPSVVVSCAGLTRD-EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05346    76 FRD-IDILVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARN-QGHIINLGSIAGRYPYAGGNVYCA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 170 SKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITT 209
Cdd:cd05346   154 TKAAVRQFSLNLRKDLI-------GTGIRVTNIEPGLVET 186
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 12-209 9.11e-21

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: 88.78  E-value: 9.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVA-------AAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05365    75 GGITILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAG-GGAILNISSMSSENKNVRIAAYGSSK 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953284729 172 AGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITT 209
Cdd:cd05365   154 AAVNHMTRNLAFDLGPK-------GIRVNAVAPGAVKT 184
PRK06123 PRK06123
SDR family oxidoreductase;
11-211 9.75e-21

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 89.07  E-value: 9.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK06123    4 VMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVV------QAIRRQGGEALAVAADVADEADVLRLFEAVDRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVS--SGCRGSIINISSIVGKVGNVGQ-TNY 167
Cdd:PRK06123   78 LGRLDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTrhGGRGGAIVNVSSMAARLGSPGEyIDY 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953284729 168 AASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK06123  158 AASKGAIDTMTIGLAKEVA-------AEGIRVNAVRPGVIYTEI 194
PRK06128 PRK06128
SDR family oxidoreductase;
6-217 2.27e-20

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 88.76  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL--DRAAACETVWLLGGQGSEKVA-PGgahtafqaDVSEAGAVRR 82
Cdd:PRK06128   52 RLQGRKALITGADSGIGRATAIAFAREGADIALNYLpeEEQDAAEVVQLIQAEGRKAVAlPG--------DLKDEAFCRQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGKVGNV 162
Cdd:PRK06128  124 LVERAVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG---ASIINTGSIQSYQPSP 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMT-------QKVPQ 217
Cdd:PRK06128  201 TLLDYASTKAAIVAFTKALAKQVA-------EKGIRVNAVAPGPVWTPLQpsggqppEKIPD 255
PRK09072 PRK09072
SDR family oxidoreductase;
5-185 2.34e-20

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 88.07  E-value: 2.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGGaHTAFQADVSEAGAVRRLL 84
Cdd:PRK09072    1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEK-------LEALAARLPYPGR-HRWVVADLTSEAGREAVL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQAcfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK09072   73 ARARE--MGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQP-SAMVVNVGSTFGSIGYPGY 149

                         170       180
                  ....*....|....*....|.
gi 1953284729 165 TNYAASKAGVIGLTQTAAREL 185
Cdd:PRK09072  150 ASYCASKFALRGFSEALRREL 170
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 12-211 4.46e-20

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 87.32  E-value: 4.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDrAAACETvwlLGGQGSEKVApggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06200    9 ALITGGGSGIGRALVERFLAEGARVAVLERS-AEKLAS---LRQRFGDHVL------VVEGDVTSYADNQRAVDQTVDAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTrdEFLLRMSEDDW-------DRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK06200   79 GK-LDCFVGNAGIW--DYNTSLVDIPAetldtafDEIFNVNVKGYLLGAKAALPALKAS--GGSMIFTLSNSSFYPGGGG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGrlvrhPwghGIRCNSVLPGFITTPM 211
Cdd:PRK06200  154 PLYTASKHAVVGLVRQLAYELA-----P---KIRVNGVAPGGTVTDL 192
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-211 7.03e-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: 7.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA--ACETVWLLGGQGSEKVAPggahtafqADVSEAG 78
Cdd:cd08933     1 MASGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAgqALESELNRAGPGSCKFVP--------CDVTKEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  79 AVRRLLEQVQACFSRPpSVVVSCAGL-----TRDEfllrMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINIS 153
Cdd:cd08933    73 DIKTLISVTVERFGRI-DCLVNNAGWhpphqTTDE----TSAQEFRDLLNLNLISYFLASKYALPHLRKS--QGNIINLS 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 154 SIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:cd08933   146 SLVGSIGQKQAAPYVATKGAITAMTKALAVDESR-------YGVRVNCISPGNIWTPL 196
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 12-212 1.28e-19

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 85.37  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGA---TVAACDLDRaaacetvwllGGQGSEKVAPGGAHTAF-QADVSEAGAVRRLLEQV 87
Cdd:cd05324     3 ALVTGANRGIGFEIVRQLAKSGPgtvILTARDVER----------GQAAVEKLRAEGLSVRFhQLDVTDDASIEAAADFV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  88 QACFSRpPSVVVSCAGLTRDEFL-LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVgnvgQTN 166
Cdd:cd05324    73 EEKYGG-LDILVNNAGIAFKGFDdSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPA-GRIVNVSSGLGSL----TSA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 167 YAASKAGVIGLTqtaaRELGRLVRHPwghGIRCNSVLPGFITTPMT 212
Cdd:cd05324   147 YGVSKAALNALT----RILAKELKET---GIKVNACCPGWVKTDMG 185
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 12-211 1.52e-19

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: 84.56  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVaacdldraaacetvwllggqgsekVAPGGAHTAFQADVSEAGAVRRLLEQVQACf 91
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEV------------------------ITAGRSSGDYQVDITDEASIKALFEKVGHF- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 srppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd11731    56 ----DAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND---GGSITLTSGILAQRPIPGGAAAATVN 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwghGIRCNSVLPGFITTPM 211
Cdd:cd11731   129 GALEGFVRAAAIELPR--------GIRINAVSPGVVEESL 160
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 12-211 3.16e-19

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 85.07  E-value: 3.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVA---PGGAHTaFQADVSEAGAVRRLLEQVQ 88
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDLCADDPAVGYPLATRAELDAVAaacPDQVLP-VIADVRDPAALAAAVALAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSRpPSVVVSCAGLTR-DEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVS----SGCRgsIINISSIVGKVGNVG 163
Cdd:TIGR04504  83 ERWGR-LDAAVAAAGVIAgGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLArpdpRGGR--FVAVASAAATRGLPH 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:TIGR04504 160 LAAYCAAKHAVVGLVRGLAADLG-------GTGVTANAVSPGSTRTAM 200
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 13-211 4.44e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 84.85  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAC--DLDR-AAACETVWLLGGQGSEKVAPggahtafqADVSEAGAVRRLLEQVQA 89
Cdd:PRK05875   11 LVTGGGSGIGKGVAAGLVAAGAAVMIVgrNPDKlAAAAEEIEALKGAGAVRYEP--------ADVTDEDQVARAVDAATA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK05875   83 WHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGG-GGSFVGISSIAASNTHRWFGAYGV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953284729 170 SKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK05875  162 TKSAVDHLMKLAADELG-------PSWVRVNSIRPGLIRTDL 196
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 12-215 7.08e-19

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: 83.68  E-value: 7.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDrAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQacf 91
Cdd:cd08942     9 VLVTGGSRGIGRMIAQGFLEAGARVIISARK-AEACADA-------AEELSAYGECIAIPADLSSEEGIEALVARVA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPS--VVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRG---SIINISSIVGKVGNVGQT- 165
Cdd:cd08942    78 ERSDRldVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAEnpaRVINIGSIAGIVVSGLENy 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKV 215
Cdd:cd08942   158 SYGASKAAVHQLTRKLAKELA-------GEHITVNAIAPGRFPSKMTAFL 200
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 12-186 9.60e-19

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 83.20  E-value: 9.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAacdldrAAACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05373     2 AAVVGAGDGLGAAIARRFAAEGFSVA------LAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05373    76 G-PLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARG-RGTIIFTGATASLRGRAGFAAFAGAK 153

                         170
                  ....*....|....*
gi 1953284729 172 AGVIGLTQTAARELG 186
Cdd:cd05373   154 FALRALAQSMARELG 168
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 12-214 1.22e-18

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 83.01  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd09761     4 AIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNL----------FFVHGDVADETLVKFVVYAMLEKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd09761    74 GR-IDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK--GRIINIASTRAFQSEPDSEAYAASK 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwghGIRCNSVLPGFITTPMTQK 214
Cdd:cd09761   151 GGLVALTHALAMSLGP--------DIRVNCISPGWINTTEQQE 185
PRK08264 PRK08264
SDR family oxidoreductase;
10-224 1.46e-18

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 82.63  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  10 ALALVTGAGSGIGRAVSVRLAKEGAT---VAACDLDRAAAcetvwllggqGSEKVAPggahtaFQADVSEAGAVRRLLEQ 86
Cdd:PRK08264    7 KVVLVTGANRGIGRAFVEQLLARGAAkvyAAARDPESVTD----------LGPRVVP------LQLDVTDPASVAAAAEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 vqacfSRPPSVVVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08264   71 -----ASDVTILVNNAGiFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANG-GGAIVNVLSVLSWVNFPNLG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPqkvLDKMS 224
Cdd:PRK08264  145 TYSASKAAAWSLTQALRAELA-------PQGTRVLGVHPGPIDTDMAAGLD---APKAS 193
PRK09134 PRK09134
SDR family oxidoreductase;
12-205 2.49e-18

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 82.28  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK09134   12 ALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALA-------AEIRALGRRAVALQADLADEAEVRALVARASAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvSSGCRGSIINIssIVGKVGNVGQ--TNYA 168
Cdd:PRK09134   85 LG-PITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARAL-PADARGLVVNM--IDQRVWNLNPdfLSYT 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1953284729 169 ASKAGVIGLTQTAARELGrlvrhPwghGIRCNSVLPG 205
Cdd:PRK09134  161 LSKAALWTATRTLAQALA-----P---RIRVNAIGPG 189
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 12-213 2.61e-18

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: 81.88  E-value: 2.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAacetvwllggqgSEKVAPGGAHT-AFQADVS-EAGAVRRLL 84
Cdd:cd05356     4 AVVTGATDGIGKAYAEELAKRGFNVILIsrtqeKLDAVA------------KEIEEKYGVETkTIAADFSaGDDIYERIE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQacfSRPPSVVVSCAGLTRD--EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:cd05356    72 KELE---GLDIGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRK-KGAIVNISSFAGLIPTP 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:cd05356   148 LLATYSASKAFLDFFSRALYEEYKS-------QGIDVQSLLPYLVATKMSK 191
PRK06949 PRK06949
SDR family oxidoreductase;
1-213 3.19e-18

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 82.12  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRaaacetvwlLGGQGSEKVAPGGAHTAFQADVSEAG 78
Cdd:PRK06949    1 MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVvlASRRVER---------LKELRAEIEAEGGAAHVVSLDVTDYQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  79 AVRRLLEQVQAcFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGC-------RGSIIN 151
Cdd:PRK06949   72 SIKAAVAHAET-EAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKgagntkpGGRIIN 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 152 ISSIVG-KVgnVGQTN-YAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQ 213
Cdd:PRK06949  151 IASVAGlRV--LPQIGlYCMSKAAVVHMTRAMALEWGR-------HGINVNAICPGYIDTEINH 205
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 6-209 3.65e-18

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 82.01  E-value: 3.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETvwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:cd05348     1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAV--LDRSAEKVA--------ELRADFGDAVVGVEGDVRSLADNERAVA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRpPSVVVSCAGLTrdEFLLRMSEDDWDR-------VIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGK 158
Cdd:cd05348    71 RCVERFGK-LDCFIGNAGIW--DYSTSLVDIPEEKldeafdeLFHINVKGYILGAKAALPALYAT--EGSVIFTVSNAGF 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 159 VGNVGQTNYAASKAGVIGLTQTAARElgrlvrhpWGHGIRCNSVLPGFITT 209
Cdd:cd05348   146 YPGGGGPLYTASKHAVVGLVKQLAYE--------LAPHIRVNGVAPGGMVT 188
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 1-205 5.95e-18

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 83.81  E-value: 5.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsEKVA--PGGAHTAFQADVSEAG 78
Cdd:COG3347   417 MPKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAA------------EAAAaeLGGGYGADAVDATDVD 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  79 AVRRllEQVQACFSRPPS------VVVSCAGL--TRDEFLLRMSedDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSII 150
Cdd:COG3347   485 VTAE--AAVAAAFGFAGLdiggsdIGVANAGIasSSPEEETRLS--FWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSV 560

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 151 NISSIVGKVGNVGQTNYAASKAgvigLTQTAARELGRLVRhpwGHGIRCNSVLPG 205
Cdd:COG3347   561 FAVSKNAAAAAYGAAAAATAKA----AAQHLLRALAAEGG---ANGINANRVNPD 608
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 7-215 8.48e-18

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 80.89  E-value: 8.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRA-AACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKeEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQAcfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGKVGNVGQT 165
Cdd:PRK12747   82 NRTG--STKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDN---SRIINISSAATRISLPDFI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK12747  157 AYSMTKGAINTMTFTLAKQLG-------ARGITVNAILPGFIKTDMNAEL 199
PRK12744 PRK12744
SDR family oxidoreductase;
7-210 1.27e-17

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 80.55  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAA----CDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRR 82
Cdd:PRK12744    6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynSAASKADAEETVAAVKAAGAKAVA-------FQADLTTAAAVEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINI-SSIVGKVGN 161
Cdd:PRK12744   79 LFDDAKAAFGR-PDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDN---GKIVTLvTSLLGAFTP 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 162 vGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTP 210
Cdd:PRK12744  155 -FYSAYAGSKAPVEHFTRAASKEFGA-------RGISVTAVGPGPMDTP 195
PRK09135 PRK09135
pteridine reductase; Provisional
 11-210 1.41e-17

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 80.36  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVA------ACDLDRAAAcetvwllggqGSEKVAPGGAHtAFQADVSEAGAVRRLL 84
Cdd:PRK09135    8 VALITGGARRIGAAIARTLHAAGYRVAihyhrsAAEADALAA----------ELNALRPGSAA-ALQADLLDPDALPELV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPPSVVVSCAGLTRDEfLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvsSGCRGSIINISSIVGKVGNVGQ 164
Cdd:PRK09135   77 AACVAAFGRLDALVNNASSFYPTP-LGSITEAQWDDLFASNLKAPFFLSQAAAPQL--RKQRGAIVNITDIHAERPLKGY 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGrlvrhPwghGIRCNSVLPGFITTP 210
Cdd:PRK09135  154 PVYCAAKAALEMLTRSLALELA-----P---EVRVNAVAPGAILWP 191
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 13-180 1.72e-17

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 79.82  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAAcetvwllggqgsekvAPGGAHTaFQADVSEAGAVRRLLEQV 87
Cdd:COG3967     9 LITGGTSGIGLALAKRLHARGNTVIITgrreeKLEEAAA---------------ANPGLHT-IVLDVADPASIAALAEQV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  88 QACFsrpPS--VVVSCAGLTRDEFLLRmSEDDWD---RVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:COG3967    73 TAEF---PDlnVLINNAGIMRAEDLLD-EAEDLAdaeREITTNLLGPIRLTAAFLPHLKAQP-EAAIVNVSSGLAFVPLA 147

                         170
                  ....*....|....*...
gi 1953284729 163 GQTNYAASKAGVIGLTQT 180
Cdd:COG3967   148 VTPTYSATKAALHSYTQS 165
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 14-211 2.69e-17

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 79.03  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  14 VTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACEtvwLLGGQGSEKVAPGgahtafQADVSEAGAVRRLLEQVQACFSR 93
Cdd:cd08931     5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAA---LAAELGAENVVAG------ALDVTDRAAWAAALADFAAATGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  94 PPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQAL-VSSGCRgsIINISSIVGKVGNVGQTNYAASKA 172
Cdd:cd08931    76 RLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLkATPGAR--VINTASSSAIYGQPDLAVYSATKF 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953284729 173 GVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:cd08931   154 AVRGLTEALDVEWAR-------HGIRVADVWPWFVDTPI 185
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 6-216 3.23e-17

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 79.22  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACdlDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12823    5 RFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLV--DRSELVHEV------AAELRAAGGEALALTADLETYAGAQAAMA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVgkVGNVGQT 165
Cdd:PRK12823   77 AAVEAFGRIDVLINNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQG-GGAIVNVSSIA--TRGINRV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPmTQKVP 216
Cdd:PRK12823  154 PYSAAKGGVNALTASLAFEYA-------EHGIRVNAVAPGGTEAP-PRRVP 196
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 13-169 3.87e-17

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 80.87  E-value: 3.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAK-EGATVAAcdLDRAAACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAcF 91
Cdd:cd08953   209 LVTGGAGGIGRALARALARrYGARLVL--LGRSPLPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRE-R 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVssgcrGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd08953   286 YGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPL-----DFFVLFSSVSAFFGGAGQADYAA 358
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 14-219 4.86e-17

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: 78.58  E-value: 4.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  14 VTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQACFSR 93
Cdd:cd05360     5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAI-------AVVADVADAAQVERAADTAVERFGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  94 pPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKAG 173
Cdd:cd05360    78 -IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRG-GGALINVGSLLGYRSAPLQAAYSASKHA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 174 VIGLTQTAARELgrlvRHPwGHGIRCNSVLPGFITTPMTQKVPQKV 219
Cdd:cd05360   156 VRGFTESLRAEL----AHD-GAPISVTLVQPTAMNTPFFGHARSYM 196
PRK07024 PRK07024
SDR family oxidoreductase;
11-216 5.40e-17

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 78.82  E-value: 5.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAVRRlleQVQAC 90
Cdd:PRK07024    4 KVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPK--------AARVSVYAADVRDADALAA---AAADF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRP--PSVVVSCAGLTRDEfLLRMSED--DWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK07024   73 IAAHglPDVVIANAGISVGT-LTEEREDlaVFREVMDTNYFGMVATFQPFIAPMRAAR-RGTLVGIASVAGVRGLPGAGA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 167 YAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVP 216
Cdd:PRK07024  151 YSASKAAAIKYLESLRVELR-------PAGVRVVTIAPGYIRTPMTAHNP 193
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 12-185 5.45e-17

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 79.23  E-value: 5.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05876    9 AVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFD------VH-GVMCDVRHREEVTHLADEAFRLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05876   82 GHV-DVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAK 160

                         170
                  ....*....|....
gi 1953284729 172 AGVIGLTQTAAREL 185
Cdd:PRK05876  161 YGVVGLAETLAREV 174
PRK09186 PRK09186
flagellin modification protein A; Provisional
 13-207 7.66e-17

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 78.11  E-value: 7.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLG-GQGSEKvapggaHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK09186    8 LITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGkEFKSKK------LSLVELDITDQESLEEFLSKSAEKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEF---LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG----KVGNVGQ 164
Cdd:PRK09186   82 GK-IDGAVNCAYPRNKDYgkkFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQG-GGNLVNISSIYGvvapKFEIYEG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 165 TN------YAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFI 207
Cdd:PRK09186  160 TSmtspveYAAIKAGIIHLTKYLAKYFK-------DSNIRVNCVSPGGI 201
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 6-210 7.81e-17

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: 78.34  E-value: 7.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacETVWLLGGqgsEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:cd08937     1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-----ELVHEVLA---EILAAGDAAHVHTADLETYAGAQGVVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRpPSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVgkVGNVGQ 164
Cdd:cd08937    73 AAVERFGR-VDVLINNVGGTiWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQ-QGVIVNVSSIA--TRGIYR 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 165 TNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTP 210
Cdd:cd08937   149 IPYSAAKGGVNALTASLAFEHAR-------DGIRVNAVAPGGTEAP 187
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 7-214 7.82e-17

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: 78.00  E-value: 7.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVaacdldraaacetvwLLGGQGSEKVAPGGAHTA---------FQADVSEA 77
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATV---------------ILLGRNEEKLRQVADHINeeggrqpqwFILDLLTC 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  78 GA--VRRLLEQVQACFSRPPSVVVScAGLTRDEF-LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISS 154
Cdd:cd05340    67 TSenCQQLAQRIAVNYPRLDGVLHN-AGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSD-AGSLVFTSS 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 155 IVGKVGNVGQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQK 214
Cdd:cd05340   145 SVGRQGRANWGAYAVSKFATEGL*QVLADEYQ-------QRNLRVNCINPGGTRTAMRAS 197
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
12-209 1.13e-16

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 77.84  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK08063    7 ALVTGSSRGIGKAIALRLAEEGYDIAVNYArSRKAAEETAEEIEALGRKAL-------AVKANVGDVEKIKEMFAQIDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGI-FLVTQAAAQALVSSGcrGSIINISSIvGKVGNVgqTNYAA 169
Cdd:PRK08063   80 FGR-LDVFVNNAASGVLRPAMELEESHWDWTMNINAKALlFCAQEAAKLMEKVGG--GKIISLSSL-GSIRYL--ENYTT 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953284729 170 ---SKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITT 209
Cdd:PRK08063  154 vgvSKAALEALTRYLAVELAP-------KGIAVNAVSGGAVDT 189
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 12-217 1.17e-16

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: 77.34  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGAT--VAAC-DLDRAAACETvwlLGGQGSEKVAPggahtafQADVSE-----AGAVRRL 83
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNtvIATCrDPSAATELAA---LGASHSRLHIL-------ELDVTDeiaesAEAVAER 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQvqacfsRPPSVVVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGCRGSIINISSIVGKVGNV 162
Cdd:cd05325    71 LGD------AGLDVLINNAGiLHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFL-PLLLKGARAKIINISSRVGSIGDN 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 163 ---GQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:cd05325   144 tsgGWYSYRASKAALNMLTKSLAVELKR-------DGITVVSLHPGWVRTDMGGPFAK 194
PRK07775 PRK07775
SDR family oxidoreductase;
12-241 2.06e-16

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 77.49  E-value: 2.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVaACDLDRAAACETVwllggqgSEKV-APGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPV-ALGARRVEKCEEL-------VDKIrADGGEAVAFPLDVTDPDSVKSFVAQAEEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK07775   85 LG-EIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERR-RGDLIFVGSDVALRQRPHMGAYGAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 171 KAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKM-------SQMRsHSWRLKTVDTSQA 241
Cdd:PRK07775  163 KAGLEAMVTNLQMELE-------GTGVRASIVHPGPTLTGMGWSLPAEVIGPMledwakwGQAR-HDYFLRASDLARA 232
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 13-169 2.81e-16

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 74.91  E-value: 2.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGAT----VAACDLDRAAACETVWLLGGQGSEKVAPggahtafQADVSEAGAVRRLLEQVQ 88
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhlvlLSRSAAPRPDAQALIAELEARGVEVVVV-------ACDVSDPDAVAALLAEIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 AcfsRPPSV--VVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVssgcrGSIINISSIVGKVGNVGQTN 166
Cdd:pfam08659  77 A---EGPPIrgVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPL-----DFFVLFSSIAGLLGSPGQAN 148


                  ...
gi 1953284729 167 YAA 169
Cdd:pfam08659 149 YAA 151
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 12-210 3.85e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 77.27  E-value: 3.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK07109   11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEAL-------AVVADVADAEAVQAAADRAEEEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07109   84 G-PIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRD-RGAIIQVGSALAYRSIPLQSAYCAAK 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953284729 172 AGVIGLTQTAARELgrlvRHPwGHGIRCNSVLPGFITTP 210
Cdd:PRK07109  162 HAIRGFTDSLRCEL----LHD-GSPVSVTMVQPPAVNTP 195
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 12-216 5.20e-16

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: 76.11  E-value: 5.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATV-AACdlDRAAACETVWllggqgSEKVAPGGAH--TAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05327     4 VVITGANSGIGKETARELAKRGAHViIAC--RNEEKGEEAA------AEIKKETGNAkvEVIQLDLSSLASVRQFAEEFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFsRPPSVVVSCAGLTRDEFllRMSEDDWDRVIAVNLKGIFLVTQAAAQALV-SSGCRgsIINISSIVGKVGNVGQTN- 166
Cdd:cd05327    76 ARF-PRLDILINNAGIMAPPR--RLTKDGFELQFAVNYLGHFLLTNLLLPVLKaSAPSR--IVNVSSIAHRAGPIDFNDl 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 167 -------------YAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVP 216
Cdd:cd05327   151 dlennkeyspykaYGQSKLANILFTRELARRLE-------GTGVTVNALHPGVVRTELLRRNG 206
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 11-241 5.86e-16

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: 75.40  E-value: 5.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQ------ELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPPSVVVScAG----LTRDEFLlrmSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05367    75 DGERDLLINN-AGslgpVSKIEFI---DLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKTVVNVSSGAAVNPFKGWGL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 167 YAASKAGVIGLTQTAARELgrlvrhpwgHGIRCNSVLPGFITTPMTQKV-----PQKVLDKMSQMRSHSWRLKTVDTSQA 241
Cdd:cd05367   151 YCSSKAARDMFFRVLAAEE---------PDVRVLSYAPGVVDTDMQREIretsaDPETRSRFRSLKEKGELLDPEQSAEK 221
PRK07201 PRK07201
SDR family oxidoreductase;
13-185 6.30e-16

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 78.07  E-value: 6.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK07201  375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELV-------AEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHG 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RpPSVVVSCAG--------LTRDEFllrmseDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIvgkvgnvG- 163
Cdd:PRK07201  448 H-VDYLVNNAGrsirrsveNSTDRF------HDYERTMAVNYFGAVRLILGLLPHMRERR-FGHVVNVSSI-------Gv 512

                         170       180
                  ....*....|....*....|....*...
gi 1953284729 164 QTN------YAASKAGVIGLTQTAAREL 185
Cdd:PRK07201  513 QTNaprfsaYVASKAALDAFSDVAASET 540
PRK07814 PRK07814
SDR family oxidoreductase;
6-209 6.68e-16

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 75.97  E-value: 6.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATV--AA---CDLDRAAacetvwllggqgsEKVAPGG--AHTAfQADVSEAG 78
Cdd:PRK07814    7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVliAArteSQLDEVA-------------EQIRAAGrrAHVV-AADLAHPE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  79 AVRRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGK 158
Cdd:PRK07814   73 ATAGLAGQAVEAFGRL-DIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGGGSVINISSTMGR 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 159 VGNVGQTNYAASKAGVIGLTQTAARELGrlvrhPwghGIRCNSVLPGFITT 209
Cdd:PRK07814  152 LAGRGFAAYGTAKAALAHYTRLAALDLC-----P---RIRVNAIAPGSILT 194
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 13-211 7.93e-16

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 75.29  E-value: 7.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVaacdldraaacetvwLLGGQGSEK--------VAPGGAHTA-FQADVSEAGA--VR 81
Cdd:PRK08945   16 LVTGAGDGIGREAALTYARHGATV---------------ILLGRTEEKleavydeiEAAGGPQPAiIPLDLLTATPqnYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  82 RLLEQVQACFSRPPSVVVScAGL--TRDEFLlRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKV 159
Cdd:PRK08945   81 QLADTIEEQFGRLDGVLHN-AGLlgELGPME-QQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPA-ASLVFTSSSVGRQ 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 160 GNVGQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK08945  158 GRANWGAYAVSKFATEGMMQVLADEYQ-------GTNLRVNCINPGGTRTAM 202
PRK05717 PRK05717
SDR family oxidoreductase;
11-207 9.81e-16

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 75.31  E-value: 9.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAaacetvwllggQGSEKVAPGGAHTAFQA-DVSEAGAVRRLLEQVQA 89
Cdd:PRK05717   12 VALVTGAARGIGLGIAAWLIAEGWQVVLADLDRE-----------RGSKVAKALGENAWFIAmDVADEAQVAAGVAEVLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRPPSVVVSCA-GLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvsSGCRGSIINISSIVGKVGNVGQTNYA 168
Cdd:PRK05717   81 QFGRLDALVCNAAiADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYL--RAHNGAIVNLASTRARQSEPDTEAYA 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953284729 169 ASKAGVIGLTQTAARELGRlvrhpwghGIRCNSVLPGFI 207
Cdd:PRK05717  159 ASKGGLLALTHALAISLGP--------EIRVNAVSPGWI 189
PRK07985 PRK07985
SDR family oxidoreductase;
6-217 1.24e-15

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 75.42  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL--DRAAACETVWLLGGQGSEKV-APGgahtafqaDVSEAGAVRR 82
Cdd:PRK07985   46 RLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLpvEEEDAQDVKKIIEECGRKAVlLPG--------DLSDEKFARS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGcrGSIINISSIVGKVGNV 162
Cdd:PRK07985  118 LVHEAHKALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAI-PLLPKG--ASIITTSSIQAYQPSP 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPMT-------QKVPQ 217
Cdd:PRK07985  195 HLLDYAATKAAILNYSRGLAKQVAE-------KGIRVNIVAPGPIWTALQisggqtqDKIPQ 249
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 13-224 1.72e-15

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: 74.45  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAaacetvwllggqgsekvapggahtAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTVIGIDLREA------------------------DVIADLSTPEGRAAAIADVLARCS 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPPSVVVSCAGLTRDEFLlrmseddwDRVIAVNLKGIFLVTQAAAQALvSSGCRGSIINISSIVG--------------- 157
Cdd:cd05328    59 GVLDGLVNCAGVGGTTVA--------GLVLKVNYFGLRALMEALLPRL-RKGHGPAAVVVSSIAGagwaqdklelakala 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 158 ------------KVGNVGQTNYAASKAGVIGLTQTAARELGrlvrhpWGHGIRCNSVLPGFITTPMTQKVPQKVLDKMS 224
Cdd:cd05328   130 agtearavalaeHAGQPGYLAYAGSKEALTVWTRRRAATWL------YGAGVRVNTVAPGPVETPILQAFLQDPRGGES 202
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 12-218 1.94e-15

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: 73.88  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggahtafQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05370     8 VLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIHTI-----------VLDVGDAESVEALAEALLSEY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSE--DDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05370    77 PN-LDILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQP-EATIVNVSSGLAFVPMAANPVYCA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284729 170 SKAGVIGLTQTaarelgrlVRHPW-GHGIRCNSVLPGFITTPMTQKVPQK 218
Cdd:cd05370   155 TKAALHSYTLA--------LRHQLkDTGVEVVEIVPPAVDTELHEERRNP 196
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 13-214 3.88e-15

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: 73.39  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:cd05332     7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSP------HVVPLDMSDLEDAEQVVEEALKLFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:cd05332    81 GL-DILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERS-QGSIVVVSSIAGKIGVPFRTAYAASKH 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953284729 173 GVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQK 214
Cdd:cd05332   159 ALQGFFDSLRAELSEP-------NISVTVVCPGLIDTNIAMN 193
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 1-210 4.60e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 73.40  E-value: 4.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACdldraaacetvwllgGQGSEKVAPGGAHtaF-QADVSEAGA 79
Cdd:PRK06523    1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTT---------------ARSRPDDLPEGVE--FvAADLTTAEG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  80 VRRLLEQVQACFSRpPSVVVSCAGLTR---DEFLLrMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIV 156
Cdd:PRK06523   64 CAAVARAVLERLGG-VDILVHVLGGSSapaGGFAA-LTDEEWQDELNLNLLAAVRLDRALLPGMIARG-SGVIIHVTSIQ 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 157 GKVGNVGQT-NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTP 210
Cdd:PRK06523  141 RRLPLPESTtAYAAAKAALSTYSKSLSKEVA-------PKGVRVNTVSPGWIETE 188
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-169 5.79e-15

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 71.36  E-value: 5.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   13 LVTGAGSGIGRAVSVRLAKEGAT----VAACDLDRAAACETVWLLGGQGsekvapgGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlvlLSRSGPDAPGAAALLAELEAAG-------ARVTVVACDVADRDALAAVLAAIP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   89 ACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrgsIINISSIVGKVGNVGQTNYA 168
Cdd:smart00822  77 AVE-GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF-----FVLFSSIAGVLGSPGQANYA 150


                   .
gi 1953284729  169 A 169
Cdd:smart00822 151 A 151
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 13-223 7.10e-15

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


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 73.08  E-value: 7.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdldraaACETVWLLGGQGSEKVAPGGAHTaFQADVSEAGAVRRLLEQVQAcfs 92
Cdd:cd09805     4 LITGCDSGFGNLLAKKLDSLGFTVLA-------GCLTKNGPGAKELRRVCSDRLRT-LQLDVTKPEQIKRAAQWVKE--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 rppSV-------VVSCAG---LTRDEFLLRMseDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNV 162
Cdd:cd09805    73 ---HVgekglwgLVNNAGilgFGGDEELLPM--DDYRKCMEVNLFGTVEVTKAFLPLLRRA--KGRVVNVSSMGGRVPFP 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELgrlvrHPWghGIRCNSVLPGFITTPMTQKVP--QKVLDKM 223
Cdd:cd09805   146 AGGAYCASKAAVEAFSDSLRREL-----QPW--GVKVSIIEPGNFKTGITGNSElwEKQAKKL 201
PRK08219 PRK08219
SDR family oxidoreductase;
10-215 1.01e-14

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 71.89  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  10 ALALVTGAGSGIGRAVSVRLAkEGATVaacdldraaacetvwLLGGQGSEKVAP-----GGAHTaFQADVSEAGAVRRLL 84
Cdd:PRK08219    4 PTALITGASRGIGAAIARELA-PTHTL---------------LLGGRPAERLDElaaelPGATP-FPVDLTDPEAIAAAV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVqacfsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK08219   67 EQL-----GRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAA--HGHVVFINSGAGLRANPGW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 165 TNYAASKagvigltqTAARELGRLVRHPWGHGIRCNSVLPGFITTPMTQKV 215
Cdd:PRK08219  140 GSYAASK--------FALRALADALREEEPGNVRVTSVHPGRTDTDMQRGL 182
PRK07577 PRK07577
SDR family oxidoreductase;
12-211 1.04e-14

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 72.07  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETvwllggqgsekvaPGgahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK07577    6 VLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDF-------------PG---ELFACDLADIEQTAATLAQINEIH 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 srPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIvGKVGNVGQTNYAASK 171
Cdd:PRK07577   68 --PVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLRE-QGRIVNICSR-AIFGALDRTSYSAAK 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTPM 211
Cdd:PRK07577  144 SALVGCTRTWALELAE-------YGITVNAVAPGPIETEL 176
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-227 1.80e-14

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 71.64  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGA--GSGIGRAVSVRLAKEGATVAA-------CDLDRAAACETVWLLGGqgsEKVAPGGAHTAFQADVS 75
Cdd:PRK12748    1 LPLMKKIALVTGAsrLNGIGAAVCRRLAAKGIDIFFtywspydKTMPWGMHDKEPVLLKE---EIESYGVRCEHMEIDLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  76 EAGAVRRLLEQVQACFSRPPSVVVSCAGLTRD---EFLLRMSEDDWdrviAVNLKGIFLVTQAAAQALvSSGCRGSIINI 152
Cdd:PRK12748   78 QPYAPNRVFYAVSERLGDPSILINNAAYSTHTrleELTAEQLDKHY----AVNVRATMLLSSAFAKQY-DGKAGGRIINL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284729 153 SS--IVGKVgnVGQTNYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFI-TTPMTQKVPQKVLDKMSQMR 227
Cdd:PRK12748  153 TSgqSLGPM--PDELAYAATKGAIEAFTKSLAPELAEK-------GITVNAVNPGPTdTGWITEELKHHLVPKFPQGR 221
PRK06914 PRK06914
SDR family oxidoreductase;
12-185 2.32e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 71.59  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAAcetvwlLGGQGSEKVAPGGAHTaFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK06914    6 AIVTGASSGFGLLTTLELAKKGYLVIATmrNPEKQEN------LLSQATQLNLQQNIKV-QQLDVTDQNSIHNFQLVLKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 cfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK06914   79 --IGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQK-SGKIINISSISGRVGFPGLSPYVS 155

                         170
                  ....*....|....*.
gi 1953284729 170 SKAGVIGLTQTAAREL 185
Cdd:PRK06914  156 SKYALEGFSESLRLEL 171
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 12-215 2.99e-14

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: 70.51  E-value: 2.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGAT---VAACDLDRAAacetvwllggqgsEKVAPGGAH-TAFQADVSEAGAVRRLLEQv 87
Cdd:cd05354     6 VLVTGANRGIGKAFVESLLAHGAKkvyAAVRDPGSAA-------------HLVAKYGDKvVPLRLDVTDPESIKAAAAQ- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  88 qacfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIA-VNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05354    72 ----AKDVDVVINNAGVLKPATLLEEGALEALKQEMdVNVFGLLRLAQAFAPVLKANG-GGAIVNLNSVASLKNFPAMGT 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 167 YAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKV 215
Cdd:cd05354   147 YSASKSAAYSLTQGLRAELA-------AQGTLVLSVHPGPIDTRMAAGA 188
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 7-263 3.57e-14

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: 70.94  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQ------LPGTAEEIEARGGKCIPVRCDHSDDDEVEALFER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRPPSVVVSCA-------GLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIvGKV 159
Cdd:cd09763    75 VAREQQGRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAG-KGLIVIISST-GGL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 160 GNVGQTNYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTpmtqkvpQKVLDKMSQMR-SHSWRLKTVdt 238
Cdd:cd09763   153 EYLFNVAYGVGKAAIDRMAADMAHELKP-------HGVAVVSLWPGFVRT-------ELVLEMPEDDEgSWHAKERDA-- 216

                         250       260
                  ....*....|....*....|....*....
gi 1953284729 239 sqAPQWKSLEvFTCNCLT----DPGLCSL 263
Cdd:cd09763   217 --FLNGETTE-YSGRCVValaaDPDLMEL 242
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-222 6.06e-14

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 70.20  E-value: 6.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAG--SGIGRAVSVRLAKEGATV---AACDLDRaaacETVWllGGQGSEKV-------APGGAHTAFQA 72
Cdd:PRK12859    2 NQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIfftYWTAYDK----EMPW--GVDQDEQIqlqeellKNGVKVSSMEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  73 DVSEAGAVRRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQaLVSSGCRGSIINI 152
Cdd:PRK12859   76 DLTQNDAPKELLNKVTEQLGYP-HILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFAR-GFDKKSGGRIINM 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 153 SSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTP-MTQKVPQKVLDK 222
Cdd:PRK12859  154 TSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHL-------GITVNAINPGPTDTGwMTEEIKQGLLPM 217
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 1-213 1.23e-13

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: 69.11  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKvapggahTAFQADVSEAGAV 80
Cdd:cd08936     2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSV-------TGTVCHVGKAEDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:cd08936    75 ERLVATAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRG-GGSVVIVSSVAAFHP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 161 NVGQTNYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQ 213
Cdd:cd08936   154 FPGLGPYNVSKTALLGLTKNLAPELAPR-------NIRVNCLAPGLIKTSFSS 199
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 12-217 1.74e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 69.16  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAACETVWLLggqgsekvapggahtafQADVSEAGAVRRLLEQVQA 89
Cdd:PRK06179    7 ALVTGASSGIGRATAEKLARAGYRVFGTsrNPARAAPIPGVELL-----------------ELDVTDDASVQAAVDEVIA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CFSRpPSVVVSCAGLT----RDEFllrmSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK06179   70 RAGR-IDVLVNNAGVGlagaAEES----SIAQAQALFDTNVFGILRMTRAVLPHMRAQG-SGRIINISSVLGFLPAPYMA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953284729 166 NYAASKAGVIGLTQTAARElgrlVRHpwgHGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:PRK06179  144 LYAASKHAVEGYSESLDHE----VRQ---FGIRVSLVEPAYTKTNFDANAPE 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 13-237 9.93e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 66.99  E-value: 9.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsEKVAPggahtaFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK08263    7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYG----DRLLP------LALDVTDRAAVFAAVETAVEHFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK08263   77 RL-DIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQR-SGHIIQISSIGGISAFPMSGIYHASKW 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 173 GVIGLTQTAARELGrlvrhpwGHGIRCNSVLPG-----FITTPMTQKVPQKVLDKMSQMRSHSWRLKTVD 237
Cdd:PRK08263  155 ALEGMSEALAQEVA-------EFGIKVTLVEPGgystdWAGTSAKRATPLDAYDTLREELAEQWSERSVD 217
PRK07062 PRK07062
SDR family oxidoreductase;
5-209 1.26e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 66.60  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAACETVwlLGGQgsekvAPGGAHTAFQADVSEAGAVRR 82
Cdd:PRK07062    4 IQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICgrDEERLASAEAR--LREK-----FPGARLLAARCDVLDEADVAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:PRK07062   77 FAAAVEARFG-GVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASA-AASIVCVNSLLALQPEP 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITT 209
Cdd:PRK07062  155 HMVATSAARAGLLNLVKSLATELA-------PKGVRVNSILLGLVES 194
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 12-215 1.35e-12

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: 65.62  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVApggahTAFQADVSEAGAVRRLLEQVQacf 91
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGA-------LAGLAAEVGA-----LARPADVAAELEVWALAQELG--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 srPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGCRGsiINISSIVGKVGNVGQTNYAASK 171
Cdd:cd11730    66 --PLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHAL-ALLAAGARL--VFLGAYPELVMLPGLSAYAAAK 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953284729 172 AGVIGLTQTAARELgrlvrhpwgHGIRCNSVLPGFITTPMTQKV 215
Cdd:cd11730   141 AALEAYVEVARKEV---------RGLRLTLVRPPAVDTGLWAPP 175
PRK08862 PRK08862
SDR family oxidoreductase;
7-204 1.58e-12

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 65.52  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLgGQGSEKVAPggahtaFQADVSEAGAVRRLLEQ 86
Cdd:PRK08862    3 IKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQC-SALTDNVYS------FQLKDFSQESIRHLFDA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 VQACFSRPPSVVVSC----------AGLTRDEFLLRMSEddwdrvIAVNLkgiFLVTQAAAQALVSSGCRGSIINissiV 156
Cdd:PRK08862   76 IEQQFNRAPDVLVNNwtssplpslfDEQPSESFIQQLSS------LASTL---FTYGQVAAERMRKRNKKGVIVN----V 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 157 GKVGNVGQ-TNYAASKAGVIGLTQTAARELgrlvrHPWghGIRCNSVLP 204
Cdd:PRK08862  143 ISHDDHQDlTGVESSNALVSGFTHSWAKEL-----TPF--NIRVGGVVP 184
PRK07102 PRK07102
SDR family oxidoreductase;
13-216 3.39e-12

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 64.95  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAAACEtvwllggqgSEKVAPGGAHTAFQA-DVSEAGAVRRLLEQVQA 89
Cdd:PRK07102    5 LIIGATSDIARACARRYAAAGARLylAARDVERLERLA---------DDLRARGAVAVSTHElDILDTASHAAFLDSLPA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 CfsrpPSVVVSCAGLTRDEfllRMSEDDWD---RVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNvgQTN 166
Cdd:PRK07102   76 L----PDIVLIAVGTLGDQ---AACEADPAlalREFRTNFEGPIALLTLLANRFEARG-SGTIVGISSVAGDRGR--ASN 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953284729 167 --YAASKAGVI----GLTQtaarelgRLVRhpwgHGIRCNSVLPGFITTPMTQKVP 216
Cdd:PRK07102  146 yvYGSAKAALTaflsGLRN-------RLFK----SGVHVLTVKPGFVRTPMTAGLK 190
PRK12742 PRK12742
SDR family oxidoreductase;
12-211 5.87e-12

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 64.01  E-value: 5.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAacdldraaaceTVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQvqacf 91
Cdd:PRK12742    9 VLVLGGSRGIGAAIVRRFVTDGANVR-----------FTYAGSKDAAERLAQETGATAVQTDSADRDAVIDVVRK----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVG-KVGNVGQTNYAAS 170
Cdd:PRK12742   73 SGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG---GRIIIIGSVNGdRMPVAGMAAYAAS 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1953284729 171 KAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPM 211
Cdd:PRK12742  150 KSALQGMARGLARDFG-------PRGITINVVQPGPIDTDA 183
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
13-228 5.98e-11

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 61.92  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAcfs 92
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGA------------ANLAALPGVEFVRGDLRDPEALAAALAGVDA--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 rppsvVVSCAGLTRDefllrmSEDDWDRVIAVNLKGiflvTQAAAQALVSSGCRgSIINISSI--VGKVGNV-------- 162
Cdd:COG0451    68 -----VVHLAAPAGV------GEEDPDETLEVNVEG----TLNLLEAARAAGVK-RFVYASSSsvYGDGEGPidedtplr 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284729 163 GQTNYAASKAGVIGLTQTAARELG---RLVRHPWGHGIRCNSVLPGFITTPMtQKVPQKVLDKMSQMRS 228
Cdd:COG0451   132 PVSPYGASKLAAELLARAYARRYGlpvTILRPGNVYGPGDRGVLPRLIRRAL-AGEPVPVFGDGDQRRD 199
PRK06482 PRK06482
SDR family oxidoreductase;
13-184 9.74e-11

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 61.28  E-value: 9.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdldraaaceTVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK06482    6 FITGASSGFGRGMTERLLARGDRVAA----------TVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK06482   76 R-IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQG-GGRIVQVSSEGGQIAYPGFSLYHATKW 153

                         170
                  ....*....|..
gi 1953284729 173 GVIGLTQTAARE 184
Cdd:PRK06482  154 GIEGFVEAVAQE 165
PRK06101 PRK06101
SDR family oxidoreductase;
13-214 2.07e-10

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 59.88  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllgGQGSEKVAPggahtaFQADVSEAGAVRRLLEQVQACfs 92
Cdd:PRK06101    5 LITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDEL-----HTQSANIFT------LAFDVTDHPGTKAALSQLPFI-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 rpPSVVVSCAGLTrdEFLlrmseDD-------WDRVIAVNLKGIFLVTQAAaQALVSSGCRgsIINISSIVGKVGNVGQT 165
Cdd:PRK06101   72 --PELWIFNAGDC--EYM-----DDgkvdatlMARVFNVNVLGVANCIEGI-QPHLSCGHR--VVIVGSIASELALPRAE 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQK 214
Cdd:PRK06101  140 AYGASKAAVAYFARTLQLDLRPK-------GIEVVTVFPGFVATPLTDK 181
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-208 3.94e-10

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 59.00  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVAPGgahtafqaDVSEAGAVRRLL 84
Cdd:PRK05786    1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYVVG--------DVSSTESARNVI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACFSRPPSVVVSCAGLTRDEFllrmsED--DWDRVIAVNLKGIFLVTQAAAQALVssgcRGSIINISSIVGKVGNV 162
Cdd:PRK05786   73 EKAAKVLNAIDGLVVTVGGYVEDTV-----EEfsGLEEMLTNHIKIPLYAVNASLRFLK----EGSSIVLVSSMSGIYKA 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 163 G--QTNYAASKAGVIGLTQTAARELgrlvrhpWGHGIRCNSVLPGFIT 208
Cdd:PRK05786  144 SpdQLSYAVAKAGLAKAVEILASEL-------LGRGIRVNGIAPTTIS 184
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 13-207 3.95e-10

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 60.09  E-value: 3.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGA---TVAACDLDRAAACETVWLLGGQGSEKVAPggahtafQADVSEAGAVRRLLEQVQA 89
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGArhlVLLSRRGPAPRAAARAALLRAGGARVSVV-------RCDVTDPAALAALLAELAA 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 cfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQalvSSGCRgsIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05274   227 --GGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPD---LPLDF--FVLFSSVAALLGGAGQAAYAA 299

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953284729 170 SKAGVIGLtqtaARELGRLvrhpwghGIRCNSVLPGFI 207
Cdd:cd05274   300 ANAFLDAL----AAQRRRR-------GLPATSVQWGAW 326
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 13-174 4.99e-10

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 58.61  E-value: 4.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDlDRAAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFs 92
Cdd:PRK10538    4 LVTGATAGFGECITRRFIQQGHKVIATG-RRQERLQEL---------KDELGDNLYIAQLDVRNRAAIEEMLASLPAEW- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPPSVVVSCAGLTRD-EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK10538   73 RNIDVLVNNAGLALGlEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERN-HGHIINIGSTAGSWPYAGGNVYGATK 151


                  ...
gi 1953284729 172 AGV 174
Cdd:PRK10538  152 AFV 154
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 13-214 1.33e-09

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 56.95  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDL---DRAAACETVwllggqgsekvaPGGAHTAFQADVSEAgAVRRLLEQVQA 89
Cdd:cd05334     5 LVYGGRGALGSAVVQAFKSRGWWVASIDLaenEEADASIIV------------LDSDSFTEQAKQVVA-SVARLSGKVDA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 cfsrppsvVVSCAG------LTRDEFLlrmseDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVGKVGNVG 163
Cdd:cd05334    72 --------LICVAGgwaggsAKSKSFV-----KNWDLMWKQNLWTSFIASHLATKHLLSGG---LLVLTGAKAALEPTPG 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 164 QTNYAASKAGVIGLTQTAARELGRLvrhpwGHGIRCNSVLPGFITTPMTQK 214
Cdd:cd05334   136 MIGYGAAKAAVHQLTQSLAAENSGL-----PAGSTANAILPVTLDTPANRK 181
PRK05866 PRK05866
SDR family oxidoreductase;
3-211 3.82e-09

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 56.67  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   3 SPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAAcetvwLLGGQGSEKVAPGGAHTAFQADVSEAGAVRR 82
Cdd:PRK05866   34 QPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVA--VARRED-----LLDAVADRITRAGGDAMAVPCDLSDLDAVDA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  83 LLEQVQACFSrPPSVVVSCAGLTRDEFLLRmSEDDW---DRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKV 159
Cdd:PRK05866  107 LVADVEKRIG-GVDILINNAGRSIRRPLAE-SLDRWhdvERTMVLNYYAPLRLIRGLAPGMLERG-DGHIINVATWGVLS 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 160 GNVGQ-TNYAASKAgvigltqtAARELGRLVRHPWGH-GIRCNSVLPGFITTPM 211
Cdd:PRK05866  184 EASPLfSVYNASKA--------ALSAVSRVIETEWGDrGVHSTTLYYPLVATPM 229
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 13-205 3.86e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 56.46  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggQGSEKVAPGGAHtAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK06180    8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAAR---------ADFEALHPDRAL-ARLLDVTDFDAIDAVVADAEATFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 rPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK06180   78 -PIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARR-RGHIVNITSMGGLITMPGIGYYCGSKF 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1953284729 173 GVIGLTQTAARELGRLvrhpwghGIRCNSVLPG 205
Cdd:PRK06180  156 ALEGISESLAKEVAPF-------GIHVTAVEPG 181
PRK05693 PRK05693
SDR family oxidoreductase;
12-234 1.29e-08

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 54.80  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACdldrAAACETVWLLGGQGsekvapggaHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05693    4 VLITGCSSGIGRALADAFKAAGYEVWAT----ARKAEDVEALAAAG---------FTAVQLDVNDGAALARLAEELEAEH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05693   71 GG-LDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRS--RGLVVNIGSVSGVLVTPFAGAYCASK 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 172 AGVIGLTQTAARELGrlvrhPWghGIRCNSVLPGFITTPMTQKVPQKVlDKMSQMRSHSWRLK 234
Cdd:PRK05693  148 AAVHALSDALRLELA-----PF--GVQVMEVQPGAIASQFASNASREA-EQLLAEQSPWWPLR 202
PRK06139 PRK06139
SDR family oxidoreductase;
6-210 1.42e-08

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 55.11  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   6 RLRSALALVTGAGSGIGRAVSVRLAKEGA--TVAACDldrAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:PRK06139    4 PLHGAVVVITGASSGIGQATAEAFARRGArlVLAARD---EEALQAV------AEECRALGAEVLVVPTDVTDADQVKAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQAcFSRPPSVVVSCAGL----TRDEFLLRMSEddwdRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKV 159
Cdd:PRK06139   75 ATQAAS-FGGRIDVWVNNVGVgavgRFEETPIEAHE----QVIQTNLIGYMRDAHAALPIFKKQG-HGIFINMISLGGFA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 160 GNVGQTNYAASKAGVIGLTQtAARelGRLVRHPwghGIRCNSVLPGFITTP 210
Cdd:PRK06139  149 AQPYAAAYSASKFGLRGFSE-ALR--GELADHP---DIHVCDVYPAFMDTP 193
PRK06182 PRK06182
short chain dehydrogenase; Validated
 8-210 2.50e-08

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 53.81  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   8 RSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAaacetvwllggqgsEKVAPGGAHtAFQADVSEAGAVRRLLE 85
Cdd:PRK06182    2 QKKVALVTGASSGIGKATARRLAAQGYTVygAARRVDKM--------------EDLASLGVH-PLSLDVTDEASIKAAVD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  86 QVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK06182   67 TIIAEEGR-IDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQR-SGRIINISSMGGKIYTPLGA 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1953284729 166 NYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTP 210
Cdd:PRK06182  145 WYHATKFALEGFSDALRLEVAP-------FGIDVVVIEPGGIKTE 182
PRK07041 PRK07041
SDR family oxidoreductase;
13-225 2.95e-08

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 53.12  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGA--TVAACDLDRAAAcetvwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLleqvqac 90
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGArvTIASRSRDRLAA----------AARALGGGAPVRTAALDITDEAAVDAF------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPPSV--VVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQAlvssgCRGSIINISSIVGKVGNVGQTNYA 168
Cdd:PRK07041   64 FAEAGPFdhVVITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAARIA-----PGGSLTFVSGFAAVRPSASGVLQG 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 169 ASKAGVIGLTQTAARELGrlvrhPwghgIRCNSVLPGFITTPMTQKVP----QKVLDKMSQ 225
Cdd:PRK07041  139 AINAALEALARGLALELA-----P----VRVNTVSPGLVDTPLWSKLAgdarEAMFAAAAE 190
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
11-211 5.95e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 52.76  E-value: 5.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVWLLGGQGSEkvapggaHTAFQADVSEAGAVRRLLEQV--Q 88
Cdd:PRK06924    3 YVIITGTSQGLGEAIANQLLEKGTHVIS--ISRTENKELTKLAEQYNSN-------LTFHSLDLQDVHELETNFNEIlsS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSRPPSV-VVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK06924   74 IQEDNVSSIhLINNAGmVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRVINISSGAAKNPYFGWSA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1953284729 167 YAASKAGVIGLTQTAARElGRLVRHPwghgIRCNSVLPGFITTPM 211
Cdd:PRK06924  154 YCSSKAGLDMFTQTVATE-QEEEEYP----VKIVAFSPGVMDTNM 193
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 13-185 8.64e-08

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: 52.08  E-value: 8.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGAT---VAACDLDRAAACETVWLLGGqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQa 89
Cdd:cd09806     4 LITGCSSGIGLHLAVRLASDPSKrfkVYATMRDLKKKGRLWEAAGA------LAGGTLETLQLDVCDSKSVAAAVERVT- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  90 cfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd09806    77 --ERHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRG-SGRILVTSSVGGLQGLPFNDVYCA 153

                         170
                  ....*....|....*.
gi 1953284729 170 SKAGVIGLTQTAAREL 185
Cdd:cd09806   154 SKFALEGLCESLAVQL 169
PRK08251 PRK08251
SDR family oxidoreductase;
13-217 1.04e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 51.86  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAACETVwLLGGQGSEKVApggahtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK08251    6 LITGASSGLGAGMAREFAAKGRDLALCarRTDRLEELKAE-LLARYPGIKVA------VAALDVNDHDQVFEVFAEFRDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPPSVVVScAGLTRDEfllRMSEDDWD---RVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG-QTN 166
Cdd:PRK08251   79 LGGLDRVIVN-AGIGKGA---RLGTGKFWankATAETNFVAALAQCEAAMEIFREQG-SGHLVLISSVSAVRGLPGvKAA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 167 YAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPMTQKVPQ 217
Cdd:PRK08251  154 YAASKAGVASLGEGLRAELAKT-------PIKVSTIEPGYIRSEMNAKAKS 197
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 13-211 1.98e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 50.58  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdldraaacetvwllggqgsekvapGGAHTAFQADVSEAGAVRRLLEQVqacfs 92
Cdd:PRK07578    4 LVIGASGTIGRAVVAELSKRHEVITA-------------------------GRSSGDVQVDITDPASIRALFEKV----- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  93 RPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKG-IFLVTqaAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07578   54 GKVDAVVSAAGKVHFAPLAEMTDEDFNVGLQSKLMGqVNLVL--IGQHYLNDG--GSFTLTSGILSDEPIPGGASAATVN 129

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 172 AGVIGLTQTAARELGRlvrhpwghGIRCNSVLPGFITTPM 211
Cdd:PRK07578  130 GALEGFVKAAALELPR--------GIRINVVSPTVLTESL 161
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 13-211 2.60e-07

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: 50.95  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVA--ACDLDRAAAcetvwllggqgSEKVAPGGAHtAFQADVSEAGAVRRLLEQVQAc 90
Cdd:cd08951    11 FITGSSDGLGLAAARTLLHQGHEVVlhARSQKRAAD-----------AKAACPGAAG-VLIGDLSSLAETRKLADQVNA- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRPPSVVVScAGLTRDEFLLRMSEDDwDRVIAVNLKGIF----LVTQAAAQALVSSGC-RGSIINISSIV-GKVGNVGQ 164
Cdd:cd08951    78 IGRFDAVIHN-AGILSGPNRKTPDTGI-PAMVAVNVLAPYvltaLIRRPKRLIYLSSGMhRGGNASLDDIDwFNRGENDS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284729 165 TNYAASKAGVIGLTQTAARelgrlvrhpWGHGIRCNSVLPGFITTPM 211
Cdd:cd08951   156 PAYSDSKLHVLTLAAAVAR---------RWKDVSSNAVHPGWVPTKM 193
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 7-209 2.67e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 50.62  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATV-----AACDLDRAaacetvwllggqgSEKV---APGGAHTaFQADVSEAG 78
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVillsrNEENLKKA-------------REKIkseSNVDVSY-IVADLTKRE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  79 AVRRLLEQVQACFSrpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGK 158
Cdd:PRK08339   72 DLERTVKELKNIGE--PDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGF-GRIIYSTSVAIK 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953284729 159 --VGNVGQTNYAasKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITT 209
Cdd:PRK08339  149 epIPNIALSNVV--RISMAGLVRTLAKELGP-------KGITVNGIMPGIIRT 192
PRK08017 PRK08017
SDR family oxidoreductase;
13-222 3.97e-07

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 50.08  E-value: 3.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATV-AACDldRAAACETVWLLGGQGSEkvapggahtafqADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08017    6 LITGCSSGIGLEAALELKRRGYRVlAACR--KPDDVARMNSLGFTGIL------------LDLDDPESVERAADEVIALT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK08017   72 DNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGE-GRIVMTSSVMGLISTPGRGAYAASK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284729 172 AGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDK 222
Cdd:PRK08017  151 YALEAWSDALRMELR-------HSGIKVSLIEPGPIRTRFTDNVNQTQSDK 194
PRK06196 PRK06196
oxidoreductase; Provisional
 7-231 4.37e-07

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 50.45  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAAACetvwLLGGQGSEKVApggahtafqADVSEAGAVRRLL 84
Cdd:PRK06196   24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVivPARRPDVAREA----LAGIDGVEVVM---------LDLADLESVRAFA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQACfSRPPSVVVSCAG-----LTRDefllrmsEDDWDRVIAVNLKGIF---------LVTQAAAQ--ALVSSGCRGS 148
Cdd:PRK06196   91 ERFLDS-GRRIDILINNAGvmacpETRV-------GDGWEAQFATNHLGHFalvnllwpaLAAGAGARvvALSSAGHRRS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 149 IINISSIVGKVGNVGQTNYAASKagvigltqTA----ARELGRLVRhpwGHGIRCNSVLPGFITTPMTQKVPQkvldkmS 224
Cdd:PRK06196  163 PIRWDDPHFTRGYDKWLAYGQSK--------TAnalfAVHLDKLGK---DQGVRAFSVHPGGILTPLQRHLPR------E 225


                  ....*..
gi 1953284729 225 QMRSHSW 231
Cdd:PRK06196  226 EQVALGW 232
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 12-234 6.19e-07

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: 49.93  E-value: 6.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwLLGGQGSEKvaPGGAHTAfQADVSEAGAV-RRLLEQVQAC 90
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAST--LAAELNARR--PNSAVTC-QADLSNSATLfSRCEAIIDAC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSR--PPSVVVSCAGLTRDEFLLRMSEDDWD-----------RVIAVNLKGIFLVTQAAAQALVSSG--CRG---SIINI 152
Cdd:TIGR02685  79 FRAfgRCDVLVNNASAFYPTPLLRGDAGEGVgdkkslevqvaELFGSNAIAPYFLIKAFAQRQAGTRaeQRStnlSIVNL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 153 SSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRLvrhpwghGIRCNSVLPGFITTPmtqkvpqkvlDKMSQMRSHSWR 232
Cdd:TIGR02685 159 CDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPL-------QIRVNGVAPGLSLLP----------DAMPFEVQEDYR 221


                  ..
gi 1953284729 233 LK 234
Cdd:TIGR02685 222 RK 223
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 5-209 6.25e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 49.66  E-value: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDR-AAACETVWLLGGQGSekvapggahTAFQADVSEAGAVR 81
Cdd:PRK06125    3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLhlVARDADAlEALAADLRAAHGVDV---------AVHALDLSSPEARE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  82 RLLEQVQacfsrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINIssivgkVGN 161
Cdd:PRK06125   74 QLAAEAG-----DIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARG-SGVIVNV------IGA 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953284729 162 VGQT---NY---AASKAGVIGLTQT-AARELgrlvrhpwGHGIRCNSVLPGFITT 209
Cdd:PRK06125  142 AGENpdaDYicgSAGNAALMAFTRAlGGKSL--------DDGVRVVGVNPGPVAT 188
PRK09291 PRK09291
SDR family oxidoreductase;
13-223 6.62e-07

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 49.61  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdldraaacetvwllGGQGSEKVapggahTAFQADVSEAGAVRR-----LLEQ- 86
Cdd:PRK09291    6 LITGAGSGFGREVALRLARKGHNVIA---------------GVQIAPQV------TALRAEAARRGLALRvekldLTDAi 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  87 -VQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG--KVGNVG 163
Cdd:PRK09291   65 dRAQAAEWDVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARG-KGKVVFTSSMAGliTGPFTG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729 164 QtnYAASKAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGF----------------------------ITTPMTQKV 215
Cdd:PRK09291  144 A--YCASKHALEAIAEAMHAELKP-------FGIQVATVNPGPyltgfndtmaetpkrwydparnftdpedLAFPLEQFD 214


                  ....*...
gi 1953284729 216 PQKVLDKM 223
Cdd:PRK09291  215 PQEMIDAM 222
PRK06720 PRK06720
hypothetical protein; Provisional
 5-125 6.66e-07

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 48.43  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK06720   12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATV-------EEITNLGGEALFVSYDMEKQGDWQRVI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953284729  85 EQVQACFSRpPSVVVSCAGLTR-DEFLLRMSEDDwDRVIAVN 125
Cdd:PRK06720   85 SITLNAFSR-IDMLFQNAGLYKiDSIFSRQQEND-SNVLCIN 124
PRK08703 PRK08703
SDR family oxidoreductase;
13-210 9.75e-07

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 48.77  E-value: 9.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAA-ACETVWllggqgSEKVAPGGAH-TAFQADVSEAG--AVRRLLEQVQ 88
Cdd:PRK08703   10 LVTGASQGLGEQVAKAYAAAGATVIL--VARHQkKLEKVY------DAIVEAGHPEpFAIRFDLMSAEekEFEQFAATIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSRPPSVVVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNY 167
Cdd:PRK08703   82 EATQGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSP-DASVIFVGESHGETPKAYWGGF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953284729 168 AASKAGVIGLTQTAARELGRLvrhpwgHGIRCNSVLPGFITTP 210
Cdd:PRK08703  161 GASKAALNYLCKVAADEWERF------GNLRANVLVPGPINSP 197
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 12-210 1.42e-06

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 48.34  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggQGSEKVAPGGAHTAFQADvseagavRRLLEQVQACF 91
Cdd:cd05361     4 ALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAER------QAFESENPGTKALSEQKP-------EELVDAVLQAG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVI-AVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05361    71 GAIDVLVSNDYIPRPMNPIDGTSEADIRQAFeALSIFPFALLQAAIAQMKKAGG--GSIIFITSAVPKKPLAYNSLYGPA 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284729 171 KAGVIGLTQTAARELGRlvrhpwgHGIRCNSVLPGFITTP 210
Cdd:cd05361   149 RAAAVALAESLAKELSR-------DNILVYAIGPNFFNSP 181
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 12-172 1.69e-06

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


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 49.09  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGAtvaacdldraaacETVWLLGGQGSEkvAPG-----------GAHTAFQA-DVSEAGA 79
Cdd:cd08952   233 VLVTGGTGALGAHVARWLARRGA-------------EHLVLTSRRGPD--APGaaelvaeltalGARVTVAAcDVADRDA 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  80 VRRLLEQVQAcfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVI------AVNLKGifLVTQAAAQALVSsgcrgsiinIS 153
Cdd:cd08952   298 LAALLAALPA--GHPLTAVVHAAGVLDDGPLDDLTPERLAEVLrakvagARHLDE--LTRDRDLDAFVL---------FS 364

                         170
                  ....*....|....*....
gi 1953284729 154 SIVGKVGNVGQTNYAASKA 172
Cdd:cd08952   365 SIAGVWGSGGQGAYAAANA 383
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 13-209 2.00e-06

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 48.23  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATV-AAC-DLDRA--AACEtvwLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd09807     5 IITGANTGIGKETARELARRGARViMACrDMAKCeeAAAE---IRRDTLNHEV------IVRHLDLASLKSIRAFAAEFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 ACFSRpPSVVVSCAGLTRDEFLLrmSEDDWDRVIAVNLKGIFLVTQAAAQAL-VSSGCRgsIINISSIVGKVGNVG---- 163
Cdd:cd09807    76 AEEDR-LDVLINNAGVMRCPYSK--TEDGFEMQFGVNHLGHFLLTNLLLDLLkKSAPSR--IVNVSSLAHKAGKINfddl 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284729 164 --------QTNYAASKAGVIGLTqtaaRELGRLVRhpwGHGIRCNSVLPGFITT 209
Cdd:cd09807   151 nseksyntGFAYCQSKLANVLFT----RELARRLQ---GTGVTVNALHPGVVRT 197
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 13-177 5.26e-06

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


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 47.28  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATvaacdldraaaceTVWLLGGQG---------SEKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:cd08955   153 LITGGLGGLGLLVAEWLVERGAR-------------HLVLTGRRApsaaarqaiAALEEAGAEVVVLAADVSDRDALAAA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  84 LEQVQAcfSRPP-SVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcrgSIINISSIVGKVGNV 162
Cdd:cd08955   220 LAQIRA--SLPPlRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLD-----FFVLFSSVASLLGSP 292

                         170
                  ....*....|....*
gi 1953284729 163 GQTNYAASKAGVIGL 177
Cdd:cd08955   293 GQANYAAANAFLDAL 307
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 13-154 5.46e-06

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 46.85  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsekvapggahtaFQADVSEAGAVRRLLEQVQacfs 92
Cdd:cd05254     3 LITGATGMLGRALVRLLKERGYEVIGTGRSRASL-----------------------FKLDLTDPDAVEEAIRDYK---- 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284729  93 rpPSVVVSCAGLTR-DEfllrmSEDDWDRVIAVNLKGIFLVTQAAAQAlvssGCRgsIINISS 154
Cdd:cd05254    56 --PDVIINCAAYTRvDK-----CESDPELAYRVNVLAPENLARAAKEV----GAR--LIHIST 105
PRK07806 PRK07806
SDR family oxidoreductase;
7-103 8.97e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 46.25  E-value: 8.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK07806    4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKV------VAEIEAAGGRASAVGADLTDEESVAALMDT 77

                          90
                  ....*....|....*..
gi 1953284729  87 VQACFSRPPSVVVSCAG 103
Cdd:PRK07806   78 AREEFGGLDALVLNASG 94
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 13-207 9.37e-06

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 46.08  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATV--------AACDLDRAAacetvwllggqgsekvapgGAhTAFQADVSEAGAVRRLL 84
Cdd:PRK06483    6 LITGAGQRIGLALAWHLLAQGQPVivsyrthyPAIDGLRQA-------------------GA-QCIQADFSTNAGIMAFI 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  85 EQVQacfSRPPSV--VVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGS-IINISSIVGKVGN 161
Cdd:PRK06483   66 DELK---QHTDGLraIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHAASdIIHITDYVVEKGS 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284729 162 VGQTNYAASKAGVIGLTQTAARELGRLVrhpwghgiRCNSVLPGFI 207
Cdd:PRK06483  143 DKHIAYAASKAALDNMTLSFAAKLAPEV--------KVNSIAPALI 180
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
13-154 2.91e-05

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 44.74  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllggqgsekvapggahtafQADVSEAGAVRRLLEQVQacfs 92
Cdd:COG1091     3 LVTGANGQLGRALVRLLAERGYEVVALDRS----------------------------ELDITDPEAVAALLEEVR---- 50

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284729  93 rpPSVVVSCAGLTR-DEfllrmSEDDWDRVIAVNLKGIFLVTQAAAQAlvssGCRgsIINISS 154
Cdd:COG1091    51 --PDVVINAAAYTAvDK-----AESEPELAYAVNATGPANLAEACAEL----GAR--LIHIST 100
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 12-184 7.38e-05

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 43.05  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVWLLGGQgsekvapggahTAFQADVSEAGAVRRLLEQVQacf 91
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIG--LDRLTSASNTARLADL-----------RFVEGDLTDRDALEKLLADVR--- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  92 srpPSVVVSCAGLTrdefLLRMSEDDWDRVIAVNLKGiflvTQAAAQALVSSGCRgSIINISS--IVGKVGNVGQTN--- 166
Cdd:pfam01370  65 ---PDAVIHLAAVG----GVGASIEDPEDFIEANVLG----TLNLLEAARKAGVK-RFLFASSseVYGDGAEIPQEEttl 132

                         170       180
                  ....*....|....*....|....*..
gi 1953284729 167 ---------YAASKAGVIGLTQTAARE 184
Cdd:pfam01370 133 tgplapnspYAAAKLAGEWLVLAYAAA 159
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 12-155 7.54e-05

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 43.43  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAAceTVWLLGGQGSEKVapggahtafQADVSEAGAVRRLLEQVQAcf 91
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRA--LVRSGS--DAVLLDGLPVEVV---------EGDLTDAASLAAAMKGCDR-- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284729  92 srppsvVVSCAGLTrdefllRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcrgSIINISSI 155
Cdd:cd05228    66 ------VFHLAAFT------SLWAKDRKELYRTNVEGTRNVLDAALEAGVR-----RVVHTSSI 112
PRK08340 PRK08340
SDR family oxidoreductase;
13-232 8.21e-05

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 43.25  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAacetvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQV 87
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKKGARVVISsrneeNLEKAL-------------KELKEYGEVYAVKADLSDKDDLKNLVKEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  88 QACFSRPPSVVVScAGLTRDE--FLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08340   71 WELLGGIDALVWN-AGNVRCEpcMLHEAGYSDWLEAALLHLVAPGYLTTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 166 NYAASKAGVIGLTQTAARELGrlvrhpwGHGIRCNSVLPGFITTPMTQKVPQKVLDKMSQMRSHSWR 232
Cdd:PRK08340  150 LADVTRAGLVQLAKGVSRTYG-------GKGIRAYTVLLGSFDTPGARENLARIAEERGVSFEETWE 209
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 1-89 4.98e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 41.14  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   1 MASPLRLRsaLALVTGAGSGIGRAVSVRLAKEGATV---------AACDLDRAaacETVwllgGQGSEKV-APGGAHTAF 70
Cdd:PRK08303    2 MMKPLRGK--VALVAGATRGAGRGIAVELGAAGATVyvtgrstraRRSEYDRP---ETI----EETAELVtAAGGRGIAV 72

                          90
                  ....*....|....*....
gi 1953284729  71 QADVSEAGAVRRLLEQVQA 89
Cdd:PRK08303   73 QVDHLVPEQVRALVERIDR 91
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 13-174 1.06e-03

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 39.44  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAAcetvwllggqgsekVAPGGAHTAfQADVSEAGAVRRLLEQVQAc 90
Cdd:COG0702     3 LVTGATGFIGRRVVRALLARGHPVRALvrDPEKAAA--------------LAAAGVEVV-QGDLDDPESLAAALAGVDA- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 fsrppsvVVSCAGltrdeflLRMSEDDWDRVIAvnlkgiflvTQAAAQALVSSGCRgSIINISSIVgkVGNVGQTNYAAS 170
Cdd:COG0702    67 -------VFLLVP-------SGPGGDFAVDVEG---------ARNLADAAKAAGVK-RIVYLSALG--ADRDSPSPYLRA 120


                  ....
gi 1953284729 171 KAGV 174
Cdd:COG0702   121 KAAV 124
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 13-172 1.08e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 40.33  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGAtvaacdldraaaCETVWLLGGQGSEkvAPG-----------GAHTAFQA-DVSEAGAV 80
Cdd:cd08956   197 LITGGTGTLGALLARHLVTEHG------------VRHLLLVSRRGPD--APGaaelvaelaalGAEVTVAAcDVADRAAL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  81 RRLLEQVQAcfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVI------AVNLKGIFLVTQAAAQALVssgcrgsiiniSS 154
Cdd:cd08956   263 AALLAAVPA--DHPLTAVVHAAGVLDDGVLTSLTPERLDAVLrpkvdaAWHLHELTRDLDLAAFVLF-----------SS 329

                         170
                  ....*....|....*...
gi 1953284729 155 IVGKVGNVGQTNYAASKA 172
Cdd:cd08956   330 AAGVLGSPGQANYAAANA 347
PRK06953 PRK06953
SDR family oxidoreductase;
9-211 1.12e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 39.67  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729   9 SALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLlggqgsekvapgGAHtAFQADVSEAGAVRRLLEQVQ 88
Cdd:PRK06953    1 MKTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQAL------------GAE-ALALDVADPASVAGLAWKLD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  89 AcfsRPPSVVVSCAGL--TRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK06953   68 G---EALDAAVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILL-PLVEAA-GGVLAVLSSRMGSIGDATGTT 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284729 167 ---YAASKAgvigltqtAARELGRLVRHPWGHGIrCNSVLPGFITTPM 211
Cdd:PRK06953  143 gwlYRASKA--------ALNDALRAASLQARHAT-CIALHPGWVRTDM 181
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 13-143 1.18e-03

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 39.14  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAAcetvwllggqGSEKVAPGGAhTAFQADVSEAGAVRRLLEqvqacfs 92
Cdd:cd05243     3 LVVGATGKVGRHVVRELLDRGYQVRA--LVRDPS----------QAEKLEAAGA-EVVVGDLTDAESLAAALE------- 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729  93 rPPSVVVSCAGltrdefllrMSEDDWDRVIAVNLKGIFLVTQAAAQA------LVSS 143
Cdd:cd05243    63 -GIDAVISAAG---------SGGKGGPRTEAVDYDGNINLIDAAKKAgvkrfvLVSS 109
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 13-213 1.40e-03

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 39.50  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqGSEKVAPGGAHTAFQ--ADVSEAGAVRRLLEQVQAC 90
Cdd:cd09808     5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEA-------RKEIETESGNQNIFLhiVDMSDPKQVWEFVEEFKEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  91 FSRpPSVVVSCAGLTRDEflLRMSEDDWDRVIAVNLKGIFLVTQAAAQAL----------VSSGcrGSII---NISSIVG 157
Cdd:cd09808    78 GKK-LHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLekeedprvitVSSG--GMLVqklNTNNLQS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284729 158 KVGNV-GQTNYAASKAGVIGLTQTAARelgrlvRHPwghGIRCNSVLPGFITTPMTQ 213
Cdd:cd09808   153 ERTAFdGTMVYAQNKRQQVIMTEQWAK------KHP---EIHFSVMHPGWADTPAVR 200
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 11-93 1.72e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 39.24  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  11 LALVTGAGSGIGRAVSVRLAKEGATV--AACDLDR-AAACETVwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQV 87
Cdd:PRK06197   18 VAVVTGANTGLGYETAAALAAKGAHVvlAVRNLDKgKAAAARI--------TAATPGADVTLQELDLTSLASVRAAADAL 89


                  ....*.
gi 1953284729  88 QACFSR 93
Cdd:PRK06197   90 RAAYPR 95
GatZ COG4573
Tagatose-1,6-bisphosphate aldolase non-catalytic subunit AgaZ/GatZ [Carbohydrate transport and ...
 34-124 5.73e-03

Tagatose-1,6-bisphosphate aldolase non-catalytic subunit AgaZ/GatZ [Carbohydrate transport and metabolism];


Pssm-ID: 443630  Cd Length: 423  Bit Score: 37.87  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284729  34 ATVA--ACDLdrAAACETVWLLGGQ-------GSEKVAPGGAHTAFQA-DVSEAGAVRRLLEQVQACFSRppsvvvscAG 103
Cdd:COG4573   141 EVVAerAARL--AAVAEAAAREAGGeapvyviGTEVPVPGGAQEALDElAVTTPEAARATLEAHRAAFAA--------AG 210

                          90       100
                  ....*....|....*....|.
gi 1953284729 104 LtrdefllrmsEDDWDRVIAV 124
Cdd:COG4573   211 L----------EDAWERVIAL 221
 
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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