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Conserved domains on  [gi|1953284735|ref|XP_038539110|]
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estradiol 17-beta-dehydrogenase 8 isoform X4 [Canis lupus familiaris]

Protein Classification

beta-ketoacyl-ACP reductase( domain architecture ID 10143190)

3-oxoacyl-[acyl-carrier-protein] reductase catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis

Graphical summary

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List of domain hits

 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; ...
 11-258 6.22e-121

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: 344.53  E-value: 6.22e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETV-------EEIKALGGNAAALEADVSDREAVEALVEKVEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05333    75 FG-PVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR-SGRIINISSVVGLIGNPGQANYAAS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:cd05333   153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQV 232


                  ....*...
gi 1953284735 251 VEVTGGLY 258
Cdd:cd05333   233 LHVNGGMY 240
 
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; ...
 11-258 6.22e-121

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: 344.53  E-value: 6.22e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETV-------EEIKALGGNAAALEADVSDREAVEALVEKVEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05333    75 FG-PVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR-SGRIINISSVVGLIGNPGQANYAAS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:cd05333   153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQV 232


                  ....*...
gi 1953284735 251 VEVTGGLY 258
Cdd:cd05333   233 LHVNGGMY 240
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
12-259 5.73e-101

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 293.99  E-value: 5.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05653    8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALA-------AELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05653   81 G-ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKAR-YGRIVNISSVSGVTGNPGQTNYSAAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASV 251
Cdd:PRK05653  159 AGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVI 238


                  ....*...
gi 1953284735 252 EVTGGLYM 259
Cdd:PRK05653  239 PVNGGMYM 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 12-259 1.59e-93

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: 275.51  E-value: 1.59e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:COG1028     9 ALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELR-------AAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:COG1028    82 GRL-DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERG-GGRIVNISSIAGLRGSPGQAAYAASK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGA 249
Cdd:COG1028   160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLgaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQ 239

                         250
                  ....*....|
gi 1953284735 250 SVEVTGGLYM 259
Cdd:COG1028   240 VLAVDGGLTA 249
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 12-258 2.04e-93

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: 274.86  E-value: 2.04e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEV------VEELKALGVKALGVVLDVSDREDVKAVVEEIEEEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:TIGR01830  75 G-TIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQR-SGRIINISSVVGLMGNAGQANYAASK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASV 251
Cdd:TIGR01830 153 AGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVI 232


                  ....*..
gi 1953284735 252 EVTGGLY 258
Cdd:TIGR01830 233 HVDGGMY 239
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 19-257 3.07e-68

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: 210.75  E-value: 3.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  19 SGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFSRPpSVV 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRV---------EELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRL-DIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  99 VSCAGLTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcRGSIINISSIVGKVGNVGQTNYAASKAGVIG 176
Cdd:pfam13561  76 VNNAGFAPKLKgpFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE---GGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 177 LTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASVEVT 254
Cdd:pfam13561 153 LTRYLAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVD 232


                  ...
gi 1953284735 255 GGL 257
Cdd:pfam13561 233 GGY 235
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-169 6.29e-14

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: 67.89  E-value: 6.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   13 LVTGAGSGIGRAVSVRLAKEGAT----VAACDLDRAAACETVWLLGGQGsekvapgGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlvlLSRSGPDAPGAAALLAELEAAG-------ARVTVVACDVADRDALAAVLAAIP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   89 ACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrgsIINISSIVGKVGNVGQTNYA 168
Cdd:smart00822  77 AVE-GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF-----FVLFSSIAGVLGSPGQANYA 150


                   .
gi 1953284735  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; ...
 11-258 6.22e-121

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: 344.53  E-value: 6.22e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05333     2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETV-------EEIKALGGNAAALEADVSDREAVEALVEKVEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05333    75 FG-PVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR-SGRIINISSVVGLIGNPGQANYAAS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:cd05333   153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQV 232


                  ....*...
gi 1953284735 251 VEVTGGLY 258
Cdd:cd05333   233 LHVNGGMY 240
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
12-259 5.73e-101

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 293.99  E-value: 5.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05653    8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALA-------AELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05653   81 G-ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKAR-YGRIVNISSVSGVTGNPGQTNYSAAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASV 251
Cdd:PRK05653  159 AGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVI 238


                  ....*...
gi 1953284735 252 EVTGGLYM 259
Cdd:PRK05653  239 PVNGGMYM 246
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 12-259 8.09e-95

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 278.62  E-value: 8.09e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVA-ACDLDRAAACETVWLLGGQGsekvapGGAHtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK05557    8 ALVTGASRGIGRAIAERLAAQGANVViNYASSEAGAEALVAEIGALG------GKAL-AVQGDVSDAESVERAVDEAKAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK05557   81 FGGV-DILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRS-GRIINISSVVGLMGNPGQANYAAS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:PRK05557  159 KAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQT 238


                  ....*....
gi 1953284735 251 VEVTGGLYM 259
Cdd:PRK05557  239 LHVNGGMVM 247
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 12-259 1.59e-93

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: 275.51  E-value: 1.59e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:COG1028     9 ALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELR-------AAGGRALAVAADVTDEAAVEALVAAAVAAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:COG1028    82 GRL-DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERG-GGRIVNISSIAGLRGSPGQAAYAASK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGA 249
Cdd:COG1028   160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLgaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQ 239

                         250
                  ....*....|
gi 1953284735 250 SVEVTGGLYM 259
Cdd:COG1028   240 VLAVDGGLTA 249
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 12-258 2.04e-93

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: 274.86  E-value: 2.04e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEV------VEELKALGVKALGVVLDVSDREDVKAVVEEIEEEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:TIGR01830  75 G-TIDILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQR-SGRIINISSVVGLMGNAGQANYAASK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASV 251
Cdd:TIGR01830 153 AGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVI 232


                  ....*..
gi 1953284735 252 EVTGGLY 258
Cdd:TIGR01830 233 HVDGGMY 239
PRK12826 PRK12826
SDR family oxidoreductase;
6-259 2.35e-77

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 234.43  E-value: 2.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapGGAHtAFQADVSEAGAVRRLLE 85
Cdd:PRK12826    3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAG------GKAR-ARQVDVRDRAALKAAVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG-KVGNVGQ 164
Cdd:PRK12826   76 AGVEDFGRL-DILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAG-GGRIVLTSSVAGpRVGYPGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIG-MIPMGHLGDPEDVADAVTFLASEDS 243
Cdd:PRK12826  154 AHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAaAIPLGRLGEPEDIAAAVLFLASDEA 233

                         250
                  ....*....|....*.
gi 1953284735 244 GYITGASVEVTGGLYM 259
Cdd:PRK12826  234 RYITGQTLPVDGGATL 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 12-254 5.43e-77

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: 232.94  E-value: 5.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA--------AIEALGGNAVAVQADVSDEEDVEALVEEALEEF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05233    73 GRL-DILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQG-GGRIVNISSVAGLRPLPGQAAYAASK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDK-VIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:cd05233   151 AALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKeLAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQV 230


                  ....
gi 1953284735 251 VEVT 254
Cdd:cd05233   231 IPVD 234
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-259 8.38e-76

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 230.53  E-value: 8.38e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVA-ACDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK12825    9 ALVTGAARGLGRAIALRLARAGADVVvHYRSDEEAAEELVEAVEALGRRAQA-------VQADVTDKAALEAAVAAAVER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK12825   82 FGRI-DILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQR-GGRIVNISSVAGLPGWPGRSNYAAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:PRK12825  160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQV 239


                  ....*....
gi 1953284735 251 VEVTGGLYM 259
Cdd:PRK12825  240 IEVTGGVDV 248
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 11-259 1.71e-74

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: 226.93  E-value: 1.71e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAA---CDLDRAAACEtvwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQV 87
Cdd:TIGR01829   2 IALVTGGMGGIGTAICQRLAKDGYRVAAncgPNEERAEAWL---------QEQGALGFDFRVVEGDVSSFESCKAAVAKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  88 QACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNY 167
Cdd:TIGR01829  73 EAELG-PVDVLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGW-GRIINISSVNGQKGQFGQTNY 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 168 AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYIT 247
Cdd:TIGR01829 151 SAAKAGMIGFTKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYIT 230

                         250
                  ....*....|..
gi 1953284735 248 GASVEVTGGLYM 259
Cdd:TIGR01829 231 GATLSINGGLYM 242
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
9-259 8.86e-72

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 220.02  E-value: 8.86e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   9 SALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQ 88
Cdd:PRK12824    2 KKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQV------RLKELDVTDTEECAEALAEIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 AcFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYA 168
Cdd:PRK12824   76 E-EEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQG-YGRIINISSVNGLKGQFGQTNYS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITG 248
Cdd:PRK12824  154 AAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITG 233

                         250
                  ....*....|.
gi 1953284735 249 ASVEVTGGLYM 259
Cdd:PRK12824  234 ETISINGGLYM 244
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 19-257 3.07e-68

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: 210.75  E-value: 3.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  19 SGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFSRPpSVV 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRV---------EELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRL-DIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  99 VSCAGLTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcRGSIINISSIVGKVGNVGQTNYAASKAGVIG 176
Cdd:pfam13561  76 VNNAGFAPKLKgpFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE---GGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 177 LTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASVEVT 254
Cdd:pfam13561 153 LTRYLAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVD 232


                  ...
gi 1953284735 255 GGL 257
Cdd:pfam13561 233 GGY 235
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-259 1.18e-66

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 207.12  E-value: 1.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKvapggahTAFQADVSEAGAVRRLL 84
Cdd:PRK08217    1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEV-------RGYAANVTDEEDVEATF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSrPPSVVVSCAGLTRDEFLL---------RMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSI 155
Cdd:PRK08217   74 AQIAEDFG-QLNGLINNAGILRDGLLVkakdgkvtsKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGVIINISSI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 156 vGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAV 235
Cdd:PRK08217  153 -ARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTV 231

                         250       260
                  ....*....|....*....|....
gi 1953284735 236 TFLASEDsgYITGASVEVTGGLYM 259
Cdd:PRK08217  232 RFIIEND--YVTGRVLEIDGGLRL 253
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-258 4.31e-64

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 200.45  E-value: 4.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVA-ACDLDRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK05565    2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVViAYDINEEAAQELLEEIK-------EEGGDAIAVKADVSSEEDVENLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK05565   75 EQIVEKFG-KIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRK-SGVIVNISSIWGLIGASCE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSG 244
Cdd:PRK05565  153 VLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDAS 232

                         250
                  ....*....|....
gi 1953284735 245 YITGASVEVTGGLY 258
Cdd:PRK05565  233 YITGQIITVDGGWT 246
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 12-257 2.39e-63

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 199.13  E-value: 2.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12829   14 VLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATA---------ARLPGAKVTATVADVADPAQVERVFDTAVERF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK12829   85 GGL-DVLVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAGRLGYPGRTPYAAS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ-----------KVLDKVIGMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK12829  164 KWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEaraqqlgigldEMEQEYLEKISLGRMVEPEDIAATALFLA 243

                         250
                  ....*....|....*...
gi 1953284735 240 SEDSGYITGASVEVTGGL 257
Cdd:PRK12829  244 SPAARYITGQAISVDGNV 261
FabG-like PRK07231
SDR family oxidoreductase;
5-257 3.65e-62

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 195.82  E-value: 3.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK07231    1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA--------GGRAIAVAADVSDEADVEAAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPpSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG 163
Cdd:PRK07231   73 AAALERFGSV-DILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG-GGAIVNVASTAGLRPRPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVL----DKVIGMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK07231  151 LGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTpenrAKFLATIPLGRLGTPEDIANAALFLA 230

                         250
                  ....*....|....*...
gi 1953284735 240 SEDSGYITGASVEVTGGL 257
Cdd:PRK07231  231 SDEASWITGVTLVVDGGR 248
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-257 9.15e-62

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: 194.91  E-value: 9.15e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAA---CDLDRAAacETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVnyrSKEDAAE--EVV-------EEIKAVGGKAIAVQADVSKEEDVVAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:cd05358    72 FQSAIKEFG-TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKGKIINMSSVHEKIPWPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV---PQKvLDKVIGMIPMGHLGDPEDVADAVTFLAS 240
Cdd:cd05358   151 HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAwddPEQ-RADLLSLIPMGRIGEPEEIAAAAAWLAS 229

                         250
                  ....*....|....*..
gi 1953284735 241 EDSGYITGASVEVTGGL 257
Cdd:cd05358   230 DEASYVTGTTLFVDGGM 246
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-213 3.94e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 188.59  E-value: 3.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGK------AL-FIQGDVTDRAQVKALVEQAVERL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:pfam00106  76 GRL-DILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGS-GGRIVNISSVAGLVPYPGGSAYSASK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVL 213
Cdd:pfam00106 154 AAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 12-259 4.00e-60

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: 190.67  E-value: 4.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDR-AAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05366     5 AIITGAAQGIGRAIAERLAADGFNIVLADLNLeEAAKSTIQEISEAGYNAVA-------VGADVTDKDDVEALIDQAVEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05366    78 FGSF-DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSAS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKV---LDKVIG--------MIPMGHLGDPEDVADAVTFLA 239
Cdd:cd05366   157 KFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVgeiAGKPEGegfaefssSIPLGRLSEPEDVAGLVSFLA 236

                         250       260
                  ....*....|....*....|
gi 1953284735 240 SEDSGYITGASVEVTGGLYM 259
Cdd:cd05366   237 SEDSDYITGQTILVDGGMVY 256
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 6-259 1.32e-58

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 186.36  E-value: 1.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLL 84
Cdd:PRK12935    3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGKEGHDVYA-------VQADVSKVEDANRLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK12935   76 EEAVNHFGKV-DILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAE-EGRIISISSIIGQAGGFGQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLAsEDSG 244
Cdd:PRK12935  154 TNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLC-RDGA 232

                         250
                  ....*....|....*
gi 1953284735 245 YITGASVEVTGGLYM 259
Cdd:PRK12935  233 YITGQQLNINGGLYM 247
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 12-240 1.36e-58

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: 186.16  E-value: 1.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapggaHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:COG4221     8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGR----------ALAVPLDVTDEAAVEAAVAAAVAEF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:COG4221    78 GRL-DVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARG-SGHIVNISSIAGLRPYPGGAVYAATK 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLAS 240
Cdd:COG4221   156 AAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALT 224
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-256 1.92e-58

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: 186.02  E-value: 1.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKvapggahTAFQADVSEAGAVRRLLEQ 86
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEA-------TAFTCDVSDEEAIKAAVEA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05347    76 IEEDF-GKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQG-HGKIINICSLLSELGGPPVPA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSG 244
Cdd:cd05347   154 YAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVvaDPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASD 233

                         250
                  ....*....|..
gi 1953284735 245 YITGASVEVTGG 256
Cdd:cd05347   234 YVNGQIIFVDGG 245
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 12-259 1.78e-57

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 183.63  E-value: 1.78e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12939   10 ALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELA-------AALEAAGGRAHAIAADLADPASVQRFFDAAAAAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12939   83 GGL-DGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSG-RGRIVNLASDTALWGAPKLGAYVASK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVL-DKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:PRK12939  161 GAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERhAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQL 240


                  ....*....
gi 1953284735 251 VEVTGGLYM 259
Cdd:PRK12939  241 LPVNGGFVM 249
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 11-257 1.29e-56

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 181.50  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:TIGR02415   2 VALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEINQAGGKAVA-------YKLDVSDKDQVFSAIDQAAEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:TIGR02415  75 FGGF-DVMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHGGKIINAASIAGHEGNPILSAYSST 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVL---DKVIG--------MIPMGHLGDPEDVADAVTFLA 239
Cdd:TIGR02415 154 KFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETSeiaGKPIGegfeefssEIALGRPSEPEDVAGLVSFLA 233

                         250
                  ....*....|....*...
gi 1953284735 240 SEDSGYITGASVEVTGGL 257
Cdd:TIGR02415 234 SEDSDYITGQSILVDGGM 251
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-257 1.35e-55

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 178.76  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL----DRAAACETVWLLGGQGsekvapgGAHTAFQADVSEAGAVRR 82
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIhpmrGRAEADAVAAGIEAAG-------GKALGLAFDVRDFAATRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNV 162
Cdd:PRK12827   77 ALDAGVEEFGRL-DILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGGRIVNIASVAGVRGNR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKvlDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:PRK12827  156 GQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPT--EHLLNPVPVQRLGEPDEVAALVAFLVSDA 233

                         250
                  ....*....|....*
gi 1953284735 243 SGYITGASVEVTGGL 257
Cdd:PRK12827  234 ASYVTGQVIPVDGGF 248
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
11-259 4.34e-54

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 174.82  E-value: 4.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATV-AACDLDRAAACEtvWLlggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK12938    5 IAYVTGGMGGIGTSICQRLHKDGFKVvAGCGPNSPRRVK--WL-----EDQKALGFDFIASEGNVGDWDSTKAAFDKVKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK12938   78 EVGEI-DVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGW-GRIINISSVNGQKGQFGQTNYST 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGA 249
Cdd:PRK12938  156 AKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGA 235

                         250
                  ....*....|
gi 1953284735 250 SVEVTGGLYM 259
Cdd:PRK12938  236 DFSLNGGLHM 245
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
6-235 8.30e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 174.29  E-value: 8.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:COG0300     2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALA-------AELRAAGARVEVVALDVTDPDAVAALAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:COG0300    75 AVLARF-GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARG-RGRIVNVSSVAGLRGLPGMA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIgmipmghlgDPEDVADAV 235
Cdd:COG0300   153 AYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL---------SPEEVARAI 213
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 12-258 1.72e-53

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: 173.61  E-value: 1.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05344     4 ALVTAASSGIGLAIARALAREGARVAICARNREN-------LERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05344    77 GRV-DILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERG-WGRIVNISSLTVKEPEPNLVLSNVAR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-----------PQKVLDKVIGMIPMGHLGDPEDVADAVTFLAS 240
Cdd:cd05344   155 AGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLlearaekegisVEEAEKEVASQIPLGRVGKPEELAALIAFLAS 234

                         250
                  ....*....|....*...
gi 1953284735 241 EDSGYITGASVEVTGGLY 258
Cdd:cd05344   235 EKASYITGQAILVDGGLT 252
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-255 1.14e-52

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 176.95  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAAcetvwllgGQGSEKVAP--GGahTAFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK08261  213 ALVTGAARGIGAAIAEVLARDGAHVVC--LDVPAA--------GEALAAVANrvGG--TALALDITAPDAPARIAEHLAE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQA--AAQALVSSGcrgSIINISSIVGKVGNVGQTNY 167
Cdd:PRK08261  281 RHGGL-DIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEAllAAGALGDGG---RIVGVSSISGIAGNRGQTNY 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 168 AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPqkVLDKVIG--MIPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:PRK08261  357 AASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTAAIP--FATREAGrrMNSLQQGGLPVDVAETIAWLASPASGG 434

                         250
                  ....*....|
gi 1953284735 246 ITGASVEVTG 255
Cdd:PRK08261  435 VTGNVVRVCG 444
PRK06138 PRK06138
SDR family oxidoreductase;
5-257 1.86e-52

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 170.72  E-value: 1.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK06138    1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA--------GGRAFARQGDVGSAEAVEALV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQ 164
Cdd:PRK06138   73 DFVAARWGR-LDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGG-GSIVNTASQLALAGGRGR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV------PQKVLDKVIGMIPMGHLGDPEDVADAVTFL 238
Cdd:PRK06138  151 AAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIfarhadPEALREALRARHPMNRFGTAEEVAQAALFL 230

                         250
                  ....*....|....*....
gi 1953284735 239 ASEDSGYITGASVEVTGGL 257
Cdd:PRK06138  231 ASDESSFATGTTLVVDGGW 249
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 12-259 2.74e-52

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 170.10  E-value: 2.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdldRAAACETVWLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12936    9 ALVTGASGGIGEEIARLLHAQGAIVGL----HGTRVEKLEALAAELGERV------KIFPANLSDRDEVKALGQKAEADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12936   79 E-GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRR-YGRIINITSVVGVTGNPGQANYCASK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASV 251
Cdd:PRK12936  157 AGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTI 236


                  ....*...
gi 1953284735 252 EVTGGLYM 259
Cdd:PRK12936  237 HVNGGMAM 244
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
12-257 3.38e-52

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 170.29  E-value: 3.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08643    5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIA-------VKADVSDRDQVFAAVRQVVDTF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK08643   78 G-DLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGGKIINATSQAGVVGNPELAVYSSTK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKV-----IGM------IPMGHLGDPEDVADAVTFLAS 240
Cdd:PRK08643  157 FAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGENAgkpdeWGMeqfakdITLGRLSEPEDVANCVSFLAG 236

                         250
                  ....*....|....*..
gi 1953284735 241 EDSGYITGASVEVTGGL 257
Cdd:PRK08643  237 PDSDYITGQTIIVDGGM 253
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 6-256 9.26e-52

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: 169.10  E-value: 9.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRLLE 85
Cdd:cd05341     2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAA----------RFFHLDVTDEDGWTAVVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:cd05341    72 TAREAFGRL-DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAG-GGSIINMSSIEGLVGDPALA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRH--GIRCNSVLPGFITTPMTQKVPQKVLDK-VIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:cd05341   150 AYNASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEMgNYPNTPMGRAGEPDEIAYAVVYLASDE 229

                         250
                  ....*....|....
gi 1953284735 243 SGYITGASVEVTGG 256
Cdd:cd05341   230 SSFVTGSELVVDGG 243
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 13-256 9.47e-52

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 168.74  E-value: 9.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACfs 92
Cdd:PRK07060   13 LVTGASSGIGRACAVALAQRGARVVAAARNAAAL------------DRLAGETGCEPLRLDVGDDAAIRAALAAAGAF-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 rppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK07060   79 ---DGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 173 GVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV---PQKVlDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGA 249
Cdd:PRK07060  156 ALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAwsdPQKS-GPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGV 234


                  ....*..
gi 1953284735 250 SVEVTGG 256
Cdd:PRK07060  235 SLPVDGG 241
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 12-256 9.80e-52

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: 168.61  E-value: 9.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05362     6 ALVTGASRGIGRAIAKRLARDGASVVVNYAsSKAAAEEVV-------AEIEAAGGKAIAVQADVSDPSQVARLFDAAEKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05362    79 FGGV-DILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGG---RIINISSSLTAAYTPNYGAYAGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM--TQKVPQKVlDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITG 248
Cdd:cd05362   155 KAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMfyAGKTEEAV-EGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNG 233


                  ....*...
gi 1953284735 249 ASVEVTGG 256
Cdd:cd05362   234 QVIRANGG 241
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 7-256 1.13e-51

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: 168.82  E-value: 1.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSekvapggahtAFQADVSEAGAVRRLLEQ 86
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGAL----------ALRVDVTDEQQVAALFER 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:cd08944    71 AVEEFGGLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARG-GGSIVNLSSIAGQSGDPGYGA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPM-------GHLGDPEDVADAVTFLA 239
Cdd:cd08944   150 YGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPGGFHllihqlqGRLGRPEDVAAAVVFLL 229

                         250
                  ....*....|....*..
gi 1953284735 240 SEDSGYITGASVEVTGG 256
Cdd:cd08944   230 SDDASFITGQVLCVDGG 246
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 12-259 1.48e-51

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 168.53  E-value: 1.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12429    7 ALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAA-------EALQKAGGKAIGVAMDVTDEEAINAGIDYAVETF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12429   80 GGV-DILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGG-GRIINMASVHGLVGSAGKAAYVSAK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQK-----------VPQKVLDKVI-GMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK12429  158 HGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKqipdlakergiSEEEVLEDVLlPLVPQKRFTTVEEIADYALFLA 237

                         250       260
                  ....*....|....*....|
gi 1953284735 240 SEDSGYITGASVEVTGGLYM 259
Cdd:PRK12429  238 SFAAKGVTGQAWVVDGGWTA 257
PRK06172 PRK06172
SDR family oxidoreductase;
12-257 1.99e-51

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 168.39  E-value: 1.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06172   10 ALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALF-------VACDVTRDAEVKALVEQTIAAY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDE-FLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK06172   83 GRL-DYAFNNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQG-GGAIVNTASVAGLGAAPKMSIYAAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV---PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYIT 247
Cdd:PRK06172  161 KHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAyeaDPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGASFTT 240

                         250
                  ....*....|
gi 1953284735 248 GASVEVTGGL 257
Cdd:PRK06172  241 GHALMVDGGA 250
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-256 2.83e-51

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: 167.89  E-value: 2.83e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtAFQADVSEAGAVRRLL 84
Cdd:cd05352     4 FSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTK------AYKCDVSSQESVEKTF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:cd05352    78 KQIQKDFG-KIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQG-KGSLIITASMSGTIVNRPQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TN--YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:cd05352   156 PQaaYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDA 235

                         250
                  ....*....|....
gi 1953284735 243 SGYITGASVEVTGG 256
Cdd:cd05352   236 SSYTTGSDLIIDGG 249
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 12-259 1.04e-50

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: 166.31  E-value: 1.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsEKVAPGGAHTAF-QADVSEAGAVRRLLEQVQAC 90
Cdd:cd05371     5 AVVTGGASGLGLATVERLLAQGAKVVILDLPNSPG------------ETVAKLGDNCRFvPVDVTSEKDVKAALALAKAK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRM------SEDDWDRVIAVNLKGIFLVTQAAAQALV-----SSGCRGSIINISSIVGKV 159
Cdd:cd05371    73 FG-RLDIVVNCAGIAVAAKTYNKkgqqphSLELFQRVINVNLIGTFNVIRLAAGAMGknepdQGGERGVIINTASVAAFE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 160 GNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPM-GHLGDPEDVADAVTFL 238
Cdd:cd05371   152 GQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFpSRLGDPAEYAHLVQHI 231

                         250       260
                  ....*....|....*....|.
gi 1953284735 239 ASEDsgYITGASVEVTGGLYM 259
Cdd:cd05371   232 IENP--YLNGEVIRLDGAIRM 250
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
4-259 6.33e-50

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 164.43  E-value: 6.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRL 83
Cdd:PRK07067    1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAA----------IAVSLDVTRQDSIDRI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:PRK07067   71 VAAAVERFG-GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGGKIINMASQAGRRGEAL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-----------PQKVLDKVIGMIPMGHLGDPEDVA 232
Cdd:PRK07067  150 VSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVdalfaryenrpPGEKKRLVGEAVPLGRMGVPDDLT 229

                         250       260
                  ....*....|....*....|....*..
gi 1953284735 233 DAVTFLASEDSGYITGASVEVTGGLYM 259
Cdd:PRK07067  230 GMALFLASADADYIVAQTYNVDGGNWM 256
PRK08589 PRK08589
SDR family oxidoreductase;
6-257 2.23e-49

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 163.41  E-value: 2.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08589    3 RLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVS-ETV-------DKIKSNGGKAKAYHVDISDEQQVKDFAS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLtrDEFLLRMSE---DDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNV 162
Cdd:PRK08589   75 EIKEQFGRV-DVLFNNAGV--DNAAGRIHEypvDVFDKIMAVDMRGTFLMTKMLLPLMMEQG--GSIINTSSFSGQAADL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--------QKVLDKVIGMIPMGHLGDPEDVADA 234
Cdd:PRK08589  150 YRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTgtsedeagKTFRENQKWMTPLGRLGKPEEVAKL 229

                         250       260
                  ....*....|....*....|...
gi 1953284735 235 VTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK08589  230 VVFLASDDSSFITGETIRIDGGV 252
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 12-257 3.02e-49

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 162.22  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK12937    8 AIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADEL------VAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvssGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK12937   82 GRI-DVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL---GQGGRIINLSTSVIALPLPGYGPYAASK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPM-TQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:PRK12937  158 AAVEGLVHVLANELRGRGITVNAVAPGPVATELfFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQV 237


                  ....*..
gi 1953284735 251 VEVTGGL 257
Cdd:PRK12937  238 LRVNGGF 244
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-256 3.76e-49

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 169.26  E-value: 3.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   8 RSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapggaHTAFQADVSEAGAVRRLLEQV 87
Cdd:PRK06484    4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPD----------HHALAMDVSDEAQIREGFEQL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  88 QACFSRPpSVVVSCAGLTrDEF---LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ 164
Cdd:PRK06484   74 HREFGRI-DVLVNNAGVT-DPTmtaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVNVASGAGLVALPKR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQK-VLDK--VIGMIPMGHLGDPEDVADAVTFLASE 241
Cdd:PRK06484  152 TAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAgKLDPsaVRSRIPLGRLGRPEEIAEAVFFLASD 231

                         250
                  ....*....|....*
gi 1953284735 242 DSGYITGASVEVTGG 256
Cdd:PRK06484  232 QASYITGSTLVVDGG 246
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 12-259 3.01e-48

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 160.20  E-value: 3.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllgGQGSEKVAPG-----GAHTA--FQADVSEAGAVRRLL 84
Cdd:PRK12384    5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADIN------------SEKAANVAQEinaeyGEGMAygFGADATSEQSVLALS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPPSVVVScAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ 164
Cdd:PRK12384   73 RGVDEIFGRVDLLVYN-AGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQINSKSGKVGSKHN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPG-FITTPMTQ---------------KVPQKVLDKVigmiPMGHLGDP 228
Cdd:PRK12384  152 SGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQsllpqyakklgikpdEVEQYYIDKV----PLKRGCDY 227

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953284735 229 EDVADAVTFLASEDSGYITGASVEVTGGLYM 259
Cdd:PRK12384  228 QDVLNMLLFYASPKASYCTGQSINVTGGQVM 258
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-257 5.34e-48

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 159.51  E-value: 5.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVA-------EEIKKAGGEAIAVKGDVTVESDVVNLIQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08936   78 TAVKEFGTL-DVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKGNIINMSSVHEQIPWPLFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT-QKVPQKVL-DKVIGMIPMGHLGDPEDVADAVTFLASEDS 243
Cdd:PRK08936  157 HYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINaEKFADPKQrADVESMIPMGYIGKPEEIAAVAAWLASSEA 236

                         250
                  ....*....|....
gi 1953284735 244 GYITGASVEVTGGL 257
Cdd:PRK08936  237 SYVTGITLFADGGM 250
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 12-256 7.95e-48

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 159.05  E-value: 7.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVwllggqgseKVAPGGAHT-AFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK06841   18 AVVTGGASGIGHAIAELFAAKGARVAL--LDRSEDVAEV---------AAQLLGGNAkGLVCDVSDSQSVEAAVAAVISA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK06841   87 FGRI-DILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAG-GGKIVNLASQAGVVALERHVAYCAS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGA 249
Cdd:PRK06841  165 KAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAwAGEKGERAKKLIPAGRFAYPEEIAAAALFLASDAAAMITGE 244


                  ....*..
gi 1953284735 250 SVEVTGG 256
Cdd:PRK06841  245 NLVIDGG 251
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 12-257 8.40e-48

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: 158.67  E-value: 8.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVA---ACDLDRAAACETvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVinyRKSKDAAAEVAA---------EIEELGGKAVVVRADVSQPQDVEEMFAAVK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYA 168
Cdd:cd05359    72 ERFGRL-DVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERG-GGRIVAISSLGSIRALPNYLAVG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ--KVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYI 246
Cdd:cd05359   150 TAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNreDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMI 229

                         250
                  ....*....|.
gi 1953284735 247 TGASVEVTGGL 257
Cdd:cd05359   230 TGQTLVVDGGL 240
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 12-256 1.25e-47

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: 158.02  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACEtvwllggqgsekVAPGGAHTAFQADVSEAGAVRRLLEQVQACf 91
Cdd:cd05368     5 ALITAAAQGIGRAIALAFAREGANVIATDINEEKLKE------------LERGPGITTRVLDVTDKEQVAALAKEEGRI- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 srppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKV-GNVGQTNYAAS 170
Cdd:cd05368    72 ----DVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARK-DGSIINMSSVASSIkGVPNRFVYSTT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV------PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSG 244
Cdd:cd05368   147 KAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERiqaqpdPEEALKAFAARQPLGRLATPEEVAALAVYLASDESA 226

                         250
                  ....*....|..
gi 1953284735 245 YITGASVEVTGG 256
Cdd:cd05368   227 YVTGTAVVIDGG 238
PRK12743 PRK12743
SDR family oxidoreductase;
12-257 4.23e-47

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 157.12  E-value: 4.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAacdldraaaceTVWLLGGQGSEKVAP-----GGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK12743    5 AIVTASDSGIGKACALLLAQQGFDIG-----------ITWHSDEEGAKETAEevrshGVRAEIRQLDLSDLPEGAQALDK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK12743   74 LIQRLGRI-DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYI 246
Cdd:PRK12743  153 YTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYT 232

                         250
                  ....*....|.
gi 1953284735 247 TGASVEVTGGL 257
Cdd:PRK12743  233 TGQSLIVDGGF 243
PRK06114 PRK06114
SDR family oxidoreductase;
6-256 1.19e-46

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 156.10  E-value: 1.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK06114    5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLrTDDGLAETAEHIE-------AAGRRAIQIAADVTSKADLRAAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG- 163
Cdd:PRK06114   78 ARTEAELG-ALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENG-GGSIVNIASMSGIIVNRGl 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 -QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVI-GMIPMGHLGDPEDVADAVTFLASE 241
Cdd:PRK06114  156 lQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVHQTKLFeEQTPMQRMAKVDEMVGPAVFLLSD 235

                         250
                  ....*....|....*
gi 1953284735 242 DSGYITGASVEVTGG 256
Cdd:PRK06114  236 AASFCTGVDLLVDGG 250
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 6-256 1.34e-46

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: 155.63  E-value: 1.34e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllgGQGSEKVA--PGGAHTAFQADVSEAGAVRRL 83
Cdd:cd05345     2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADIN------------ADGAERVAadIGEAAIAIQADVTKRADVEAM 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSRPpSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:cd05345    70 VEAALSKFGRL-DILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQG-GGVIINIASTAGLRPRP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLP-----GFITTPMTQKVPQKvLDKVIGMIPMGHLGDPEDVADAVTF 237
Cdd:cd05345   148 GLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPvagetPLLSMFMGEDTPEN-RAKFRATIPLGRLSTPDDIANAALY 226

                         250
                  ....*....|....*....
gi 1953284735 238 LASEDSGYITGASVEVTGG 256
Cdd:cd05345   227 LASDEASFITGVALEVDGG 245
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 12-256 2.29e-46

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: 155.05  E-value: 2.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDR-AAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05369     6 AFITGGGTGIGKAIAKAFAELGASVAIAgrKPEVlEAAAEEI---------SSATGGRAHPIQCDVRDPEAVEAAVDETL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSrPPSVVVSCAGltrDEFLL---RMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:cd05369    77 KEFG-KIDILINNAA---GNFLApaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFI--TTPMTQKVPQKVL-DKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:cd05369   153 HSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIptTEGMERLAPSGKSeKKMIERVPLGRLGTPEEIANLALFLLSDA 232

                         250
                  ....*....|....
gi 1953284735 243 SGYITGASVEVTGG 256
Cdd:cd05369   233 ASYINGTTLVVDGG 246
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 12-256 4.40e-46

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: 154.49  E-value: 4.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVAPggahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05364     6 AIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKI----LLVVADLTEEEGQDRIISTTLAKF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05364    82 GRL-DILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT--KGEIVNVSSVAGGRSFPGVLYYCISK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTP------MTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:cd05364   159 AALDQFTRCTALELAPKGVRVNSVSPGVIVTGfhrrmgMPEEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASSF 238

                         250
                  ....*....|.
gi 1953284735 246 ITGASVEVTGG 256
Cdd:cd05364   239 ITGQLLPVDGG 249
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 4-251 6.35e-46

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 154.39  E-value: 6.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGAT-VAACDLDRAAacetvwllGGQGSEKVAPGGAHTAF-QADVSEAGAVR 81
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEK--------GEAQAAELEALGAKAVFvQADLSDVEDCR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  82 RLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGN 161
Cdd:PRK06198   73 RVVAAADEAFGRL-DALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTIVNIGSMSAHGGQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 VGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTP---MTQK----VPQKVLDKVIGMIPMGHLGDPEDVADA 234
Cdd:PRK06198  152 PFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEgedRIQRefhgAPDDWLEKAAATQPFGRLLDPDEVARA 231

                         250
                  ....*....|....*..
gi 1953284735 235 VTFLASEDSGYITGASV 251
Cdd:PRK06198  232 VAFLLSDESGLMTGSVI 248
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
6-256 1.16e-45

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 153.80  E-value: 1.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVaaCDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08226    3 KLTGKTALITGALQGIGEGIARVFARHGANL--ILLDISPEIEKL------ADELCGRGHRCTAVVADVRDPASVAAAIK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGK-VGNVGQ 164
Cdd:PRK08226   75 RAKEKEGRI-DILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARK-DGRIVMMSSVTGDmVADPGE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--------PQKVLDKVIGMIPMGHLGDPEDVADAVT 236
Cdd:PRK08226  153 TAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIarqsnpedPESVLTEMAKAIPLRRLADPLEVGELAA 232

                         250       260
                  ....*....|....*....|
gi 1953284735 237 FLASEDSGYITGASVEVTGG 256
Cdd:PRK08226  233 FLASDESSYLTGTQNVIDGG 252
PRK07069 PRK07069
short chain dehydrogenase; Validated
 12-257 3.60e-45

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 152.17  E-value: 3.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQA--DVSEAGAVRRLLEQVQA 89
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAF------AAEINAAHGEGVAFAAvqDVTDEAQWQALLAQAAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK07069   76 AM-GGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQ-PASIVNISSVAAFKAEPDYTAYNA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHG--IRCNSVLPGFITTPMTQKVPQ-----KVLDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:PRK07069  154 SKAAVASLTKSIALDCARRGldVRCNSIHPTFIRTGIVDPIFQrlgeeEATRKLARGVPLGRLGEPDDVAHAVLYLASDE 233

                         250
                  ....*....|....*
gi 1953284735 243 SGYITGASVEVTGGL 257
Cdd:PRK07069  234 SRFVTGAELVIDGGI 248
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 11-259 7.91e-45

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: 151.46  E-value: 7.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINDLpDDDQATEVV-------AEVLAAGRRAIYFQADIGELSDHEALLDQAWE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRPpSVVVSCAGLT----RDefLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVS-----SGCRGSIINISSIVGKVG 160
Cdd:cd05337    76 DFGRL-DCLVNNAGIAvrprGD--LLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEqpdrfDGPHRSIIFVTSINAYLV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVI-GMIPMGHLGDPEDVADAVTFLA 239
Cdd:cd05337   153 SPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAaGLVPIRRWGQPEDIAKAVRTLA 232

                         250       260
                  ....*....|....*....|
gi 1953284735 240 SEDSGYITGASVEVTGGLYM 259
Cdd:cd05337   233 SGLLPYSTGQPINIDGGLSM 252
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 6-257 1.36e-44

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 150.33  E-value: 1.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12828    4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTL---------PGVPADALRIGGIDLVDPQAARRAVD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK12828   75 EVNRQFGRL-DALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASG-GGRIVNIGAGAALKAGPGMG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVpqkvldkvigmIPMGHLG---DPEDVADAVTFLASED 242
Cdd:PRK12828  153 AYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRAD-----------MPDADFSrwvTPEQIAAVIAFLLSDE 221

                         250
                  ....*....|....*
gi 1953284735 243 SGYITGASVEVTGGL 257
Cdd:PRK12828  222 AQAITGASIPVDGGV 236
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-256 1.54e-44

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 150.66  E-value: 1.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGA----TVAACDLDraaacETVWLLGGQGsEKVapggahTAFQADVSEAGAVR 81
Cdd:PRK06935   12 SLDGKVAIVTGGNTGLGQGYAVALAKAGAdiiiTTHGTNWD-----ETRRLIEKEG-RKV------TFVQVDLTKPESAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  82 RLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:PRK06935   80 KVVKEALEEFGKI-DILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQG-SGKIINIASMLSFQGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 VGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK06935  158 KFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIraDKNRNDEILKRIPAGRWGEPDDLMGAAVFLA 237

                         250
                  ....*....|....*..
gi 1953284735 240 SEDSGYITGASVEVTGG 256
Cdd:PRK06935  238 SRASDYVNGHILAVDGG 254
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 6-257 2.23e-44

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 150.10  E-value: 2.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAAcetvwLLGGQGSEKVApggahtaFQADVSEAGAV 80
Cdd:PRK08213    9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSarkaeELEEAAA-----HLEALGIDALW-------IAADVADEADI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVG 160
Cdd:PRK08213   77 ERLAEETLERFG-HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRGYGRIINVASVAGLGG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 N----VGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVT 236
Cdd:PRK08213  156 NppevMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAAL 235

                         250       260
                  ....*....|....*....|.
gi 1953284735 237 FLASEDSGYITGASVEVTGGL 257
Cdd:PRK08213  236 LLASDASKHITGQILAVDGGV 256
PRK06484 PRK06484
short chain dehydrogenase; Validated
 1-257 3.75e-44

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 155.78  E-value: 3.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapggaHTAFQADVSEAGAV 80
Cdd:PRK06484  261 APSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDE----------HLSVQADITDEAAV 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSrPPSVVVSCAGLTrDEFL--LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVGK 158
Cdd:PRK06484  331 ESAFAQIQARWG-RLDVLVNNAGIA-EVFKpsLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGG---VIVNLGSIASL 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 159 VGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKV---LDKVIGMIPMGHLGDPEDVADAV 235
Cdd:PRK06484  406 LALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALKASGradFDSIRRRIPLGRLGDPEEVAEAI 485

                         250       260
                  ....*....|....*....|..
gi 1953284735 236 TFLASEDSGYITGASVEVTGGL 257
Cdd:PRK06484  486 AFLASPAASYVNGATLTVDGGW 507
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 6-257 6.72e-44

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: 148.76  E-value: 6.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggaHTafqaDVSEAGAVRRLLE 85
Cdd:cd05326     1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFV-----HC----DVTVEADVRAAVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGL--TRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG 163
Cdd:cd05326    72 TAVARFGRL-DIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAK-KGSIVSVASVAGVVGGLG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP---QKVLDKVI--GMIPMGHLGDPEDVADAVTFL 238
Cdd:cd05326   150 PHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFgveDEAIEEAVrgAANLKGTALRPEDIAAAVLYL 229

                         250
                  ....*....|....*....
gi 1953284735 239 ASEDSGYITGASVEVTGGL 257
Cdd:cd05326   230 ASDDSRYVSGQNLVVDGGL 248
PRK06398 PRK06398
aldose dehydrogenase; Validated
 7-257 2.52e-43

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 147.67  E-value: 2.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRaaacetvwllggqgsekvaPGGAHTA-FQADVSEAGAVRRLLE 85
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKE-------------------PSYNDVDyFKVDVSNKEQVIKGID 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK06398   65 YVISKYGR-IDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD-KGVIINIASVQSFAVTRNAA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRhGIRCNSVLPGFITTPMTQKV--------PQKVLDKVI---GMIPMGHLGDPEDVADA 234
Cdd:PRK06398  143 AYVTSKHAVLGLTRSIAVDYAP-TIRCVAVCPGSIRTPLLEWAaelevgkdPEHVERKIRewgEMHPMKRVGKPEEVAYV 221

                         250       260
                  ....*....|....*....|...
gi 1953284735 235 VTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK06398  222 VAFLASDLASFITGECVTVDGGL 244
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 6-257 2.96e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 147.18  E-value: 2.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapggahTAFQADVSEAGAVRRLLe 85
Cdd:PRK06057    4 RLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGG------------LFVPTDVTDEDAVNALF- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 qvQACFSRPPSVVVSC--AGLT--RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:PRK06057   71 --DTAAETYGSVDIAFnnAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQG-KGSIINTASFVAVMGS 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 -VGQTNYAASKAGVIGLTqtaaRELG----RHGIRCNSVLPGFITTPMTQ----KVPQKVLDKVIgMIPMGHLGDPEDVA 232
Cdd:PRK06057  148 aTSQISYTASKGGVLAMS----RELGvqfaRQGIRVNALCPGPVNTPLLQelfaKDPERAARRLV-HVPMGRFAEPEEIA 222

                         250       260
                  ....*....|....*....|....*
gi 1953284735 233 DAVTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK06057  223 AAVAFLASDDASFITASTFLVDGGI 247
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 6-256 4.37e-43

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: 147.44  E-value: 4.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLD--RAAACETVWLLGGQGSEKVAPGGahtafqaDVSEAGAVRRL 83
Cdd:cd05355    23 KLKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPeeEDDAEETKKLIEEEGRKCLLIPG-------DLGDESFCRDL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSRPpSVVVSCAGLTRDEF-LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvssGCRGSIINISSIVGKVGNV 162
Cdd:cd05355    96 VKEVVKEFGKL-DILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHL---KKGSSIINTTSVTAYKGSP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM-TQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASE 241
Cdd:cd05355   172 HLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLiPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQ 251

                         250
                  ....*....|....*
gi 1953284735 242 DSGYITGASVEVTGG 256
Cdd:cd05355   252 DSSYVTGQVLHVNGG 266
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 5-256 4.75e-43

(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: 146.70  E-value: 4.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL---------DRAAACETVwllggqgSEKVAPGGAHTAFQADVS 75
Cdd:cd05353     1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsgkSSSAADKVV-------DEIKAAGGKAVANYDSVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  76 EAGAvrrLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSI 155
Cdd:cd05353    74 DGEK---IVKTAIDAFGRV-DILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQK-FGRIINTSSA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 156 VGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGfITTPMTQKV-PQKVLDKVigmipmghlgDPEDVADA 234
Cdd:cd05353   149 AGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRMTETVmPEDLFDAL----------KPEYVAPL 217

                         250       260
                  ....*....|....*....|..
gi 1953284735 235 VTFLASEDSgYITGASVEVTGG 256
Cdd:cd05353   218 VLYLCHESC-EVTGGLFEVGAG 238
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-256 1.62e-42

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 146.85  E-value: 1.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAV 80
Cdd:PRK07792    4 TTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDV------LDEIRAAGAKAVAVAGDISQRATA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAA-----QALVSSG-CRGSIINISS 154
Cdd:PRK07792   78 DELVATAVGLGGL--DIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywraKAKAAGGpVYGRIVNTSS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 155 IVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGfITTPMTQKVPQKVLDKVIGMI-PMGhlgdPEDVAD 233
Cdd:PRK07792  156 EAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICPR-ARTAMTADVFGDAPDVEAGGIdPLS----PEHVVP 230

                         250       260
                  ....*....|....*....|...
gi 1953284735 234 AVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK07792  231 LVQFLASPAAAEVNGQVFIVYGP 253
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-259 1.64e-42

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 145.49  E-value: 1.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK12745    4 VALVTGGRRGIGLGIARALAAAGFDLAINDRpDDEELAATQQELRALGVEVIF-------FPADVADLSAHEAMLDAAQA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRPpSVVVSCAG---LTRDEfLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSS-----GCRGSIINISSIVGKVGN 161
Cdd:PRK12745   77 AWGRI-DCLVNNAGvgvKVRGD-LLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQpepeeLPHRSIVFVSSVNAIMVS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 VGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKvLDKVI--GMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK12745  155 PNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAK-YDALIakGLVPMPRWGEPEDVARAVAALA 233

                         250       260
                  ....*....|....*....|
gi 1953284735 240 SEDSGYITGASVEVTGGLYM 259
Cdd:PRK12745  234 SGDLPYSTGQAIHVDGGLSI 253
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 12-256 1.94e-42

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 145.97  E-value: 1.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACEtvwllGGQGS-------EKVAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK07791    9 VIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGS-----ASGGSaaqavvdEIVAAGGEAVANGDDIADWDGAANLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAA-----QALVSSGCRGSIINISSIVGKV 159
Cdd:PRK07791   84 DAAVETFGGL-DVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAaywraESKAGRAVDARIINTSSGAGLQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 160 GNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGfITTPMTQKVPQKVLDKVigmiPMGHLG--DPEDVADAVTF 237
Cdd:PRK07791  163 GSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-ARTRMTETVFAEMMAKP----EEGEFDamAPENVSPLVVW 237

                         250
                  ....*....|....*....
gi 1953284735 238 LASEDSGYITGASVEVTGG 256
Cdd:PRK07791  238 LGSAESRDVTGKVFEVEGG 256
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 11-256 2.16e-42

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: 144.78  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd08930     4 IILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVI------ALELDITSKESIKELIESYLEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLT-RDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG----NVG 163
Cdd:cd08930    78 FGRI-DILINNAYPSpKVWGsrFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQG-KGSIINIASIYGVIApdfrIYE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTN------YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMtqkvPQKVLDKVIGMIPMGHLGDPEDVADAVTF 237
Cdd:cd08930   156 NTQmyspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQ----PSEFLEKYTKKCPLKRMLNPEDLRGAIIF 231

                         250
                  ....*....|....*....
gi 1953284735 238 LASEDSGYITGASVEVTGG 256
Cdd:cd08930   232 LLSDASSYVTGQNLVIDGG 250
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 6-257 6.46e-42

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: 143.74  E-value: 6.46e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA--ACETVWllggqgSEKvapGGAHTAFQADVSEAGAVRRL 83
Cdd:cd05329     3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKEldECLTEW------REK---GFKVEGSVCDVSSRSERQEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVG 163
Cdd:cd05329    74 MDTVASHFGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGN-GNIVFISSVAGVIAVPS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ--KVLDKVIGMIPMGHLGDPEDVADAVTFLASE 241
Cdd:cd05329   153 GAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQqkENLDKVIERTPLKRFGEPEEVAALVAFLCMP 232

                         250
                  ....*....|....*.
gi 1953284735 242 DSGYITGASVEVTGGL 257
Cdd:cd05329   233 AASYITGQIIAVDGGL 248
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 11-259 9.57e-42

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: 143.37  E-value: 9.57e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllgGQGSEKVAP------GGAHTAFQADVSEAGAVRRLL 84
Cdd:cd05322     4 VAVVIGGGQTLGEFLCHGLAEAGYDVAVADIN------------SENAEKVADeinaeyGEKAYGFGADATNEQSVIALS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPPSVVVScAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ 164
Cdd:cd05322    72 KGVDEIFKRVDLLVYS-AGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQGRIIQINSKSGKVGSKHN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPG-FITTPMTQ---------------KVPQKVLDKVigmiPMGHLGDP 228
Cdd:cd05322   151 SGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQsllpqyakklgikesEVEQYYIDKV----PLKRGCDY 226

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953284735 229 EDVADAVTFLASEDSGYITGASVEVTGGLYM 259
Cdd:cd05322   227 QDVLNMLLFYASPKASYCTGQSINITGGQVM 257
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
12-257 1.33e-41

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 150.77  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvapgGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08324  425 ALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP--------DRALGVACDVTDEAAVQAAFEEAALAF 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISS---IVGKVGNVgqtNYA 168
Cdd:PRK08324  497 G-GVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASknaVNPGPNFG---AYG 572

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRHGIRCNSVLPgfittpmtQKVPQ--KVLDKVIG-------MIPMGHLGD------------ 227
Cdd:PRK08324  573 AAKAAELHLVRQLALELGPDGIRVNGVNP--------DAVVRgsGIWTGEWIearaaayGLSEEELEEfyrarnllkrev 644

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953284735 228 -PEDVADAVTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK08324  645 tPEDVAEAVVFLASGLLSKTTGAIITVDGGN 675
PRK07074 PRK07074
SDR family oxidoreductase;
11-257 1.35e-41

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 142.99  E-value: 1.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapgGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK07074    4 TALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGD---------ARFVPVACDLTDAASLAAALANAAAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGkVGNVGQTNYAAS 170
Cdd:PRK07074   75 RG-PVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRS-RGAVVNIGSVNG-MAALGHPAYSAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQ----KVPQkVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYI 246
Cdd:PRK07074  152 KAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEarvaANPQ-VFEELKKWYPLQDFATPDDVANAVLFLASPAARAI 230

                         250
                  ....*....|.
gi 1953284735 247 TGASVEVTGGL 257
Cdd:PRK07074  231 TGVCLPVDGGL 241
PRK07774 PRK07774
SDR family oxidoreductase;
6-256 1.63e-41

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 142.58  E-value: 1.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK07774    3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGA-ERV------AKQIVADGGTAIAVQVDVSDPDSAKAMAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPPSVVVSCA--GLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGnvg 163
Cdd:PRK07774   76 ATVSAFGGIDYLVNNAAiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRG-GGAIVNQSSTAAWLY--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:PRK07774  152 SNFYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVtPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDE 231

                         250
                  ....*....|....
gi 1953284735 243 SGYITGASVEVTGG 256
Cdd:PRK07774  232 ASWITGQIFNVDGG 245
PRK07063 PRK07063
SDR family oxidoreductase;
6-257 3.22e-41

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 142.11  E-value: 3.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSekvapGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK07063    4 RLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVA-----GARVLAVPADVTDAASVAAAVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK07063   79 AAEEAFG-PLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERG-RGSIVNIASTHAFKIIPGCF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT------QKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK07063  157 PYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTedwwnaQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLA 236

                         250
                  ....*....|....*...
gi 1953284735 240 SEDSGYITGASVEVTGGL 257
Cdd:PRK07063  237 SDEAPFINATCITIDGGR 254
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 12-256 4.31e-41

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 141.56  E-value: 4.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLdraaacetvwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08220   11 VWVTGAAQGIGYAVALAFVEAGAKVIGFDQ----------------AFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK08220   75 G-PLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQR-SGAIVTVGSNAAHVPRIGMAAYGASK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPM----------TQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASE 241
Cdd:PRK08220  153 AALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMqrtlwvdedgEQQVIAGFPEQFKLGIPLGKIARPQEIANAVLFLASD 232

                         250
                  ....*....|....*
gi 1953284735 242 DSGYITGASVEVTGG 256
Cdd:PRK08220  233 LASHITLQDIVVDGG 247
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 12-256 9.93e-41

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: 140.66  E-value: 9.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLdRAAACETVWLLGGQGSEKVAPGgahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd08940     5 ALVTGSTSGIGLGIARALAAAGANIVLNGF-GDAAEIEAVRAGLAAKHGVKVL----YHGADLSKPAAIEDMVAYAQRQF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd08940    80 GGV-DILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGW-GRIINIASVHGLVASANKSAYVAAK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQK----------VPQ-KVLDKVIG-MIPMGHLGDPEDVADAVTFLA 239
Cdd:cd08940   158 HGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKqisalaqkngVPQeQAARELLLeKQPSKQFVTPEQLGDTAVFLA 237

                         250
                  ....*....|....*..
gi 1953284735 240 SEDSGYITGASVEVTGG 256
Cdd:cd08940   238 SDAASQITGTAVSVDGG 254
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 12-256 9.96e-41

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: 140.30  E-value: 9.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLdraaacetvwllggQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACf 91
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDL--------------PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAE- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05331    66 HGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRR-TGAIVTVASNAAHVPRISMAAYGASK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPM-----------TQKVPQKVLDKVIGmIPMGHLGDPEDVADAVTFLAS 240
Cdd:cd05331   145 AALASLSKCLGLELAPYGVRCNVVSPGSTDTAMqrtlwhdedgaAQVIAGVPEQFRLG-IPLGKIAQPADIANAVLFLAS 223

                         250
                  ....*....|....*.
gi 1953284735 241 EDSGYITGASVEVTGG 256
Cdd:cd05331   224 DQAGHITMHDLVVDGG 239
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 6-259 1.08e-40

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 141.71  E-value: 1.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA-ACETVWLLGGQGSEKVAPGGahtafqaDVSEAGAVRRLL 84
Cdd:PRK06701   43 KLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLIPG-------DVSDEAFCKDAV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvSSGcrGSIINISSIVGKVGNVGQ 164
Cdd:PRK06701  116 EETVRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQG--SAIINTGSITGYEGNETL 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM--TQKVPQKVlDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:PRK06701  193 IDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLipSDFDEEKV-SQFGSNTPMQRPGQPEELAPAYVFLASPD 271

                         250
                  ....*....|....*..
gi 1953284735 243 SGYITGASVEVTGGLYM 259
Cdd:PRK06701  272 SSYITGQMLHVNGGVIV 288
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 12-257 1.77e-40

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: 140.37  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvAPGGAhtafqADVSEAGAVRRLLEQVQACF 91
Cdd:cd08945     6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVE--ADGRT-----CDVRSVPEIEALVAAAVARY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQA--AAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd08945    79 G-PIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEvlKAGGMLERG-TGRIINIASTGGKQGVVHAAPYSA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-----------PQKVLDKVIGMIPMGHLGDPEDVADAVTFL 238
Cdd:cd08945   157 SKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYL 236

                         250
                  ....*....|....*....
gi 1953284735 239 ASEDSGYITGASVEVTGGL 257
Cdd:cd08945   237 IGDGAAAVTAQALNVCGGL 255
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 1-256 2.40e-40

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 140.15  E-value: 2.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllggQGSEKvapGGAHTAFQADVSEAGAV 80
Cdd:PRK06171    1 MQDWLNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-------------GGDGQ---HENYQFVPTDVSSAEEV 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRPpSVVVSCAGLTRDEFLL---------RMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIIN 151
Cdd:PRK06171   65 NHTVAEIIEKFGRI-DGLVNNAGINIPRLLVdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQH-DGVIVN 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 152 ISSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFI-TTPM-------------TQKVPQKVLD-KV 216
Cdd:PRK06171  143 MSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILeATGLrtpeyeealaytrGITVEQLRAGyTK 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1953284735 217 IGMIPMGHLGDPEDVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK06171  223 TSTIPLGRSGKLSEVADLVCYLLSDRASYITGVTTNIAGG 262
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 13-256 2.57e-40

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: 139.58  E-value: 2.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllgGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:cd05330     7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAA-----KAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:cd05330    82 RIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGS-GMIVNTASVGGIRGVGNQSGYAAAKH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 173 GVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--------PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSG 244
Cdd:cd05330   161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkqlgpenPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAG 240

                         250
                  ....*....|..
gi 1953284735 245 YITGASVEVTGG 256
Cdd:cd05330   241 YVNAAVVPIDGG 252
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-257 5.60e-40

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 139.04  E-value: 5.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHTaFQADVSEAGAVRRLLEQ 86
Cdd:PRK07097    8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIE------AHG-YVCDVTDEDGVQAMVSQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK07097   81 IEKEVG-VIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKG-HGKIINICSMMSELGRETVSA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQ--KVPQKVLDK------VIGMIPMGHLGDPEDVADAVTFL 238
Cdd:PRK07097  159 YAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAplRELQADGSRhpfdqfIIAKTPAARWGDPEDLAGPAVFL 238

                         250
                  ....*....|....*....
gi 1953284735 239 ASEDSGYITGASVEVTGGL 257
Cdd:PRK07097  239 ASDASNFVNGHILYVDGGI 257
PRK09242 PRK09242
SDR family oxidoreductase;
6-257 5.80e-40

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 138.73  E-value: 5.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAAACETVWLlggqgseKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:PRK09242    6 RLDGQTALITGASKGIGLAIAREFLGLGADVliVARDADALAQARDELA-------EEFPEREVHGLAADVSDDEDRRAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG 163
Cdd:PRK09242   79 LDWVEDHWDGL-HILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHA-SSAIVNIGSVSGLTHVRS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASE 241
Cdd:PRK09242  157 GAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlsDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMP 236

                         250
                  ....*....|....*.
gi 1953284735 242 DSGYITGASVEVTGGL 257
Cdd:PRK09242  237 AASYITGQCIAVDGGF 252
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 10-256 7.12e-40

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: 137.79  E-value: 7.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  10 ALALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVwllggQGSEKVapGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVhYNRSEAEAQRLK-----DELNAL--RNSAVLVQADLSDFAACADLVAAAF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvSSGCRGSIINISSIVGKVGNVGQTNYA 168
Cdd:cd05357    74 RAFGRC-DVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRL-AGSRNGSIINIIDAMTDRPLTGYFAYC 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRHgIRCNSVLPGFITTPMTQkvPQKVLDKVIGMIPMGHLGDPEDVADAVTFLAseDSGYITG 248
Cdd:cd05357   152 MSKAALEGLTRSAALELAPN-IRVNGIAPGLILLPEDM--DAEYRENALRKVPLKRRPSAEEIADAVIFLL--DSNYITG 226


                  ....*...
gi 1953284735 249 ASVEVTGG 256
Cdd:cd05357   227 QIIKVDGG 234
PRK09730 PRK09730
SDR family oxidoreductase;
10-256 9.50e-40

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 138.06  E-value: 9.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  10 ALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVV------NLITQAGGKAFVLQADISDENQVVAMFTAIDQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 cFSRPPSVVVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQ--ALVSSGCRGSIINISSIVGKVGNVGQ-T 165
Cdd:PRK09730   76 -HDEPLAALVNNAGiLFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKrmALKHGGSGGAIVNVSSAASRLGAPGEyV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM--TQKVPQKVlDKVIGMIPMGHLGDPEDVADAVTFLASEDS 243
Cdd:PRK09730  155 DYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMhaSGGEPGRV-DRVKSNIPMQRGGQPEEVAQAIVWLLSDKA 233

                         250
                  ....*....|...
gi 1953284735 244 GYITGASVEVTGG 256
Cdd:PRK09730  234 SYVTGSFIDLAGG 246
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-256 1.30e-39

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 137.70  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLdrAAACETVwllggqgsEKV-APGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINI--VEPTETI--------EQVtALGRRFLSLTADLRKIDGIPALLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08993   78 RAVAEFGHI-DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV------PQKVLDKvigmIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK08993  157 SYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLradeqrSAEILDR----IPAGRWGLPSDLMGPVVFLA 232

                         250
                  ....*....|....*..
gi 1953284735 240 SEDSGYITGASVEVTGG 256
Cdd:PRK08993  233 SSASDYINGYTIAVDGG 249
PRK05867 PRK05867
SDR family oxidoreductase;
7-256 1.38e-39

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 137.86  E-value: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDA-------LEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQ-- 164
Cdd:PRK05867   80 VTAELG-GIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASMSGHIINVPQqv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVpQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSG 244
Cdd:PRK05867  159 SHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPY-TEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASS 237

                         250
                  ....*....|..
gi 1953284735 245 YITGASVEVTGG 256
Cdd:PRK05867  238 YMTGSDIVIDGG 249
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-256 1.64e-39

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: 137.97  E-value: 1.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVA-------KEITALGGRAIALAADVLDRASLERAREE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPpSVVVSCAG------LTRDEFLLR--------MSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINI 152
Cdd:cd08935    76 IVAQFGTV-DILINGAGgnhpdaTTDPEHYEPeteqnffdLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQK-GGSIINI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 153 SSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-------PQKVLDKVIGMIPMGHL 225
Cdd:cd08935   154 SSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLlinpdgsYTDRSNKILGRTPMGRF 233

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1953284735 226 GDPEDVADAVTFLASED-SGYITGASVEVTGG 256
Cdd:cd08935   234 GKPEELLGALLFLASEKaSSFVTGVVIPVDGG 265
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 7-259 3.54e-39

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: 136.59  E-value: 3.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapggAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGP----------AACAISLDVTDQASIDRCVAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05363    71 LVDRWGSI-DILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGGKIINMASQAGRRGEALVGV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLD----------KVIG-MIPMGHLGDPEDVADAV 235
Cdd:cd05363   150 YCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFARyenrprgekkRLVGeAVPFGRMGRAEDLTGMA 229

                         250       260
                  ....*....|....*....|....
gi 1953284735 236 TFLASEDSGYITGASVEVTGGLYM 259
Cdd:cd05363   230 IFLASTDADYIVAQTYNVDGGNWM 253
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-256 3.88e-39

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 136.45  E-value: 3.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVA---ACDLDRAaacetvwllggqgsEKVAPGGAHTaFQADVSEAGAVRR 82
Cdd:PRK06463    4 RFKGKVALITGGTRGIGRAIAEAFLREGAKVAvlyNSAENEA--------------KELREKGVFT-IKCDVGNRDQVKK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSRPpSVVVSCAG----LTRDEFllrmSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGk 158
Cdd:PRK06463   69 SKEVVEKEFGRV-DVLVNNAGimylMPFEEF----DEEKYNKMIKINLNGAIYTTYEFLPLLKLSK-NGAIVNIASNAG- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 159 VGN--VGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT--QKVPQ---KVLDKVIGMIPMGHLGDPEDV 231
Cdd:PRK06463  142 IGTaaEGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsGKSQEeaeKLRELFRNKTVLKTTGKPEDI 221

                         250       260
                  ....*....|....*....|....*
gi 1953284735 232 ADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK06463  222 ANIVLFLASDDARYITGQVIVADGG 246
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 12-259 6.66e-39

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: 135.66  E-value: 6.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05349     3 VLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAG--------ERAI-AIQADVRDRDQVQAMIEEAKNHF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSED--DWDRV---IAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:cd05349    74 GPVDTIVNNALIDFPFDPDQRKTFDtiDWEDYqqqLEGAVKGALNLLQAVLPDFKERG-SGRVINIGTNLFQNPVVPYHD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFI-TTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:cd05349   153 YTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARA 232

                         250
                  ....*....|....
gi 1953284735 246 ITGASVEVTGGLYM 259
Cdd:cd05349   233 VTGQNLVVDGGLVM 246
PRK07035 PRK07035
SDR family oxidoreductase;
7-257 7.35e-39

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 135.91  E-value: 7.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDlDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK07035    6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSS-RKLDGCQAV------ADAIVAAGGKAEALACHIGEMEQIDALFAH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPPSVVVSCAglTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK07035   79 IRERHGRLDILVNNAA--ANPYFghILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQG-GGSIVNVASVNGVSPGDFQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ--KVLDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:PRK07035  156 GIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKndAILKQALAHIPLRRHAEPSEMAGAVLYLASDA 235

                         250
                  ....*....|....*
gi 1953284735 243 SGYITGASVEVTGGL 257
Cdd:PRK07035  236 SSYTTGECLNVDGGY 250
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 11-235 4.90e-38

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: 133.52  E-value: 4.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHTaFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGK------VHY-YKCDVSKREEVYEAAKKIKKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05339    74 V-GDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERN-HGHIVTIASVAGLISPAGLADYCAS 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAAREL---GRHGIRCNSVLPGFITTPMTQ--KVPQKVLDKVIgmipmghlgDPEDVADAV 235
Cdd:cd05339   152 KAAAVGFHESLRLELkayGKPGIKTTLVCPYFINTGMFQgvKTPRPLLAPIL---------EPEYVAEKI 212
PRK06500 PRK06500
SDR family oxidoreductase;
6-256 5.51e-38

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 133.54  E-value: 5.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK06500    3 RLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAA----------RAELGESALVIRADAGDVAAQKALAQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPPSVVVScAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVGKVGNVGQT 165
Cdd:PRK06500   73 ALAEAFGRLDAVFIN-AGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPA---SIVLNGSINAHIGMPNSS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP------QKVLDKVIGMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK06500  149 VYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGlpeatlDAVAAQIQALVPLGRFGTPEEIAKAVLYLA 228

                         250
                  ....*....|....*..
gi 1953284735 240 SEDSGYITGASVEVTGG 256
Cdd:PRK06500  229 SDESAFIVGSEIIVDGG 245
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 5-256 5.60e-38

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: 133.36  E-value: 5.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDR-AAACETVwllggqgsekvapggahTAFQADVSEAG 78
Cdd:cd05351     3 LDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVsrtqaDLDSlVRECPGI-----------------EPVCVDLSDWD 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  79 AVRRLLEQVQacfsrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGK 158
Cdd:cd05351    66 ATEEALGSVG-----PVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 159 VGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV---PQKVlDKVIGMIPMGHLGDPEDVADAV 235
Cdd:cd05351   141 RALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNwsdPEKA-KKMLNRIPLGKFAEVEDVVNAI 219

                         250       260
                  ....*....|....*....|.
gi 1953284735 236 TFLASEDSGYITGASVEVTGG 256
Cdd:cd05351   220 LFLLSDKSSMTTGSTLPVDGG 240
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 6-256 5.61e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 133.52  E-value: 5.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK07478    3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVV-GARRQAELDQL------VAEIRAEGGEAVALAGDVRDEAYAKALVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG-KVGNVGQ 164
Cdd:PRK07478   76 LAVERFGGLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARG-GGSLIFTSTFVGhTAGFPGM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:PRK07478  155 AAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMgdTPEALAFVAGLHALKRMAQPEEIAQAALFLASDA 234

                         250
                  ....*....|....
gi 1953284735 243 SGYITGASVEVTGG 256
Cdd:PRK07478  235 ASFVTGTALLVDGG 248
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 14-259 9.53e-38

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 133.16  E-value: 9.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  14 VTGAGSGIGRAVSVRLAKEGATVA-----ACDLDRAAAcetvwllggqgseKVAPGGAHT-AFQADVSEAGAVRRLLEQV 87
Cdd:PRK07890   10 VSGVGPGLGRTLAVRAARAGADVVlaartAERLDEVAA-------------EIDDLGRRAlAVPTDITDEDQCANLVALA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  88 QACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNY 167
Cdd:PRK07890   77 LERFGRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG--GSIVMINSMVLRHSQPKYGAY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 168 AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQ-----------KVPQKVLDKVIGMIPMGHLGDPEDVADAVT 236
Cdd:PRK07890  155 KMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfrhqagkygVTVEQIYAETAANSDLKRLPTDDEVASAVL 234

                         250       260
                  ....*....|....*....|...
gi 1953284735 237 FLASEDSGYITGASVEVTGGLYM 259
Cdd:PRK07890  235 FLASDLARAITGQTLDVNCGEYH 257
PRK07831 PRK07831
SDR family oxidoreductase;
7-254 2.22e-37

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 132.08  E-value: 2.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGA-GSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsekvAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK07831   15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAAE-----LGLGRVEAVVCDVTSEAQVDALID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK07831   90 AAVERLGRL-DVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVNNASVLGWRAQHGQA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSG 244
Cdd:PRK07831  169 HYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVtSAELLDELAAREAFGRAAEPWEVANVIAFLASDYSS 248

                         250
                  ....*....|
gi 1953284735 245 YITGASVEVT 254
Cdd:PRK07831  249 YLTGEVVSVS 258
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 7-259 2.75e-37

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 131.94  E-value: 2.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRA---AACETVWLLGGQGsekvapggAHTAfqADVSEAGAVRRL 83
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDganAVADEINKAGGKA--------IGVA--MDVTNEDAVNAG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:PRK13394   75 IDKVAERFG-SVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQK-VPQK----------VLDKVI-GMIPMGHLGDPEDV 231
Cdd:PRK13394  154 KSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqIPEQakelgiseeeVVKKVMlGKTVDGVFTTVEDV 233

                         250       260
                  ....*....|....*....|....*...
gi 1953284735 232 ADAVTFLASEDSGYITGASVEVTGGLYM 259
Cdd:PRK13394  234 AQTVLFLSSFPSAALTGQSFVVSHGWFM 261
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 1-257 5.64e-37

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 131.03  E-value: 5.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahTAFqaDVSEAGAV 80
Cdd:PRK08085    1 MNDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHA-----APF--NVTHKQEV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:PRK08085   74 EAAIEHIEKDIG-PIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQ-AGKIINICSMQSELG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFL 238
Cdd:PRK08085  152 RDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALveDEAFTAWLCKRTPAARWGDPQELIGAAVFL 231

                         250
                  ....*....|....*....
gi 1953284735 239 ASEDSGYITGASVEVTGGL 257
Cdd:PRK08085  232 SSKASDFVNGHLLFVDGGM 250
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-259 1.24e-36

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 130.21  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRL 83
Cdd:PRK08642    1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRA----------IALQADVTDREQVQAM 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSRPPSVVVSCA-------GLTRDEFLlRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIV 156
Cdd:PRK08642   71 FATATEHFGKPITTVVNNAladfsfdGDARKKAD-DITWEDFQQQLEGSVKGALNTIQAALPGMREQG-FGRIINIGTNL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 157 GKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFI-TTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAV 235
Cdd:PRK08642  149 FQNPVVPYHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAV 228

                         250       260
                  ....*....|....*....|....
gi 1953284735 236 TFLASEDSGYITGASVEVTGGLYM 259
Cdd:PRK08642  229 LFFASPWARAVTGQNLVVDGGLVM 252
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 6-256 1.38e-36

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 130.13  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwllggqGSEKVAPGGAHTAF-QADVSEAGAVRRLL 84
Cdd:PRK08265    3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADN-----------GAAVAASLGERARFiATDITDDAAIERAV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPpSVVVSCAGLTRDEFLlRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQ 164
Cdd:PRK08265   72 ATVVARFGRV-DILVNLACTYLDDGL-ASSRADWLAALDVNLVSAAMLAQAAHPHLARGG--GAIVNFTSISAKFAQTGR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP---QKVLDKVIG-MIPMGHLGDPEDVADAVTFLAS 240
Cdd:PRK08265  148 WLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSggdRAKADRVAApFHLLGRVGDPEEVAQVVAFLCS 227

                         250
                  ....*....|....*.
gi 1953284735 241 EDSGYITGASVEVTGG 256
Cdd:PRK08265  228 DAASFVTGADYAVDGG 243
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-256 2.24e-36

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 128.93  E-value: 2.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLdraaacetvwllggqgSEKVAPGGAHTAFQADVSEAgavrrlleqVQACFS 92
Cdd:PRK06550    9 LITGAASGIGLAQARAFLAQGAQVYGVDK----------------QDKPDLSGNFHFLQLDLSDD---------LEPLFD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPSVVVSC--AGLTRD-EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK06550   64 WVPSVDILCntAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERK-SGIIINMCSIASFVAGGGGAAYTA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQK--VPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYIT 247
Cdd:PRK06550  143 SKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAAdfEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQ 222


                  ....*....
gi 1953284735 248 GASVEVTGG 256
Cdd:PRK06550  223 GTIVPIDGG 231
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 1-256 5.16e-36

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 129.25  E-value: 5.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAV 80
Cdd:PRK08277    2 MPNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVV-------AEIKAAGGEALAVKADVLDKESL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRPpSVVVSCAG------LTRDEFLLR---------MSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGC 145
Cdd:PRK08277   75 EQARQQILEDFGPC-DILINGAGgnhpkaTTDNEFHELieptktffdLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 146 rGSIINISSIVG-----KVgnVGqtnYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-------PQKVL 213
Cdd:PRK08277  154 -GNIINISSMNAftpltKV--PA---YSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALlfnedgsLTERA 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1953284735 214 DKVIGMIPMGHLGDPEDVADAVTFLASED-SGYITGASVEVTGG 256
Cdd:PRK08277  228 NKILAHTPMGRFGKPEELLGTLLWLADEKaSSFVTGVVLPVDGG 271
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 13-256 5.18e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 128.26  E-value: 5.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK07677    5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEA-------KLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPSVVVSCAGltrdEFL---LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK07677   78 RIDALINNAAG----NFIcpaEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINMVATYAWDAGPGVIHSAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGR-HGIRCNSVLPGFITTP-------MTQKVPQKVLDKVigmiPMGHLGDPEDVADAVTFLASE 241
Cdd:PRK07677  154 AKAGVLAMTRTLAVEWGRkYGIRVNAIAPGPIERTggadklwESEEAAKRTIQSV----PLGRLGTPEEIAGLAYFLLSD 229

                         250
                  ....*....|....*
gi 1953284735 242 DSGYITGASVEVTGG 256
Cdd:PRK07677  230 EAAYINGTCITMDGG 244
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-256 5.52e-36

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 128.48  E-value: 5.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETvwllggqgSEKV-APGGAHTAFQADVSEAGAVRR 82
Cdd:PRK12481    3 LFDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVG--VGVAEAPET--------QAQVeALGRKFHFITADLIQQKDIDS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNV 162
Cdd:PRK12481   73 IVSQAVEVMGHI-DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGKIINIASMLSFQGGI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQ--KVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLAS 240
Cdd:PRK12481  152 RVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAalRADTARNEAILERIPASRWGTPDDLAGPAIFLSS 231

                         250
                  ....*....|....*.
gi 1953284735 241 EDSGYITGASVEVTGG 256
Cdd:PRK12481  232 SASDYVTGYTLAVDGG 247
PRK06123 PRK06123
SDR family oxidoreductase;
11-256 2.09e-35

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 126.82  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK06123    4 VMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVV------QAIRRQGGEALAVAADVADEADVLRLFEAVDRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVS--SGCRGSIINISSIVGKVGNVGQ-TNY 167
Cdd:PRK06123   78 LGRLDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTrhGGRGGAIVNVSSMAARLGSPGEyIDY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 168 AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM--TQKVPQKVlDKVIGMIPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:PRK06123  158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIhaSGGEPGRV-DRVKAGIPMGRGGTAEEVARAILWLLSDEASY 236

                         250
                  ....*....|.
gi 1953284735 246 ITGASVEVTGG 256
Cdd:PRK06123  237 TTGTFIDVSGG 247
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 1-259 2.21e-35

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 126.99  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGA--TVAACDLDRAAAceTVWLLGgqgsekvAPGGAHTAFQADVSEAG 78
Cdd:PRK07576    1 MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGAnvAVASRSQEKVDA--AVAQLQ-------QAGPEGLGVSADVRDYA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  79 AVRRLLEQVQACFSrPPSVVVSCAGltrDEFL---LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSI 155
Cdd:PRK07576   72 AVEAAFAQIADEFG-PIDVLVSGAA---GNFPapaAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG--ASIIQISAP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 156 VGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFI--TTPMTQKVPQKVL-DKVIGMIPMGHLGDPEDVA 232
Cdd:PRK07576  146 QAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIagTEGMARLAPSPELqAAVAQSVPLKRNGTKQDIA 225

                         250       260
                  ....*....|....*....|....*..
gi 1953284735 233 DAVTFLASEDSGYITGASVEVTGGLYM 259
Cdd:PRK07576  226 NAALFLASDMASYITGVVLPVDGGWSL 252
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 12-256 3.79e-35

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: 125.88  E-value: 3.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwLLGGQgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05323     3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAA--ELQAI-----NPKVKATFVQCDVTSWEQLAAAFKKAIEKF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRpPSVVVSCAGLT--RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSS--GCRGSIINISSIVGKVGNVGQTNY 167
Cdd:cd05323    76 GR-VDILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNkgGKGGVIVNIGSVAGLYPAPQFPVY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 168 AASKAGVIGLTQTAAREL-GRHGIRCNSVLPGFITTPMtqkVPQKVlDKVIGMIPMGHLGDPEDVADAVTFLASEDSGyi 246
Cdd:cd05323   155 SASKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPL---LPDLV-AKEAEMLPSAPTQSPEVVAKAIVYLIEDDEK-- 228

                         250
                  ....*....|
gi 1953284735 247 TGASVEVTGG 256
Cdd:cd05323   229 NGAIWIVDGG 238
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 12-256 1.56e-34

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: 124.43  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggQGSEKVAPGGAHT-AFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd08943     4 ALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIA---------EKVAEAAQGGPRAlGVQCDVTSEAQVQSAFEQAVLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd08943    75 FG-GLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTpmTQKVPQKVLDKVIGMIPmGHLGD-------------PEDVADAVTF 237
Cdd:cd08943   154 KAAEAHLARCLALEGGEDGIRVNTVNPDAVFR--GSKIWEGVWRAARAKAY-GLLEEeyrtrnllkrevlPEDVAEAVVA 230

                         250
                  ....*....|....*....
gi 1953284735 238 LASEDSGYITGASVEVTGG 256
Cdd:cd08943   231 MASEDFGKTTGAIVTVDGG 249
PRK07326 PRK07326
SDR family oxidoreductase;
12-238 2.05e-34

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 123.97  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsekvAPGGAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK07326    9 ALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELN-------NKGNVL-GLAADVRDEADVQRAVDAIVAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07326   81 GGL-DVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG--GYIINISSLAGTNFFAGGAAYNASK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQkvlDKVIGMIpmghlgDPEDVADAVTFL 238
Cdd:PRK07326  158 FGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPS---EKDAWKI------QPEDIAQLVLDL 215
PRK08628 PRK08628
SDR family oxidoreductase;
5-256 2.37e-34

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 124.30  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVWllggqgSEKVAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK08628    3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVI--FGRSAPDDEFA------EELRALQPRAEFVQVDLTDDAQCRDAV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPPSVVvSCAGlTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK08628   75 EQTVAKFGRIDGLV-NNAG-VNDGVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKAS--RGAIVNISSKTALTGQGGT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV------PQKVLDKVIGMIPMGH-LGDPEDVADAVTF 237
Cdd:PRK08628  151 SGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWiatfddPEAKLAAITAKIPLGHrMTTAEEIADTAVF 230

                         250
                  ....*....|....*....
gi 1953284735 238 LASEDSGYITGASVEVTGG 256
Cdd:PRK08628  231 LLSERSSHTTGQWLFVDGG 249
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 12-238 4.08e-34

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: 122.47  E-value: 4.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwlLGGQGSEkvapggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd08932     3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS--ASGGDVE---------AVPYDARDPEDARALVDALRDRF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd08932    72 G-RIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAG-SGRVVFLNSLSGKRVLAGNAGYSASK 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKvpqkvlDKVIGMIPMGHLGDPEDVADAVTFL 238
Cdd:cd08932   150 FALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQG------LTLVGAFPPEEMIQPKDIANLVRMV 210
PRK05855 PRK05855
SDR family oxidoreductase;
11-235 5.67e-34

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 128.95  E-value: 5.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapGGAHtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK05855  317 LVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAG------AVAH-AYRVDVSDADAMEAFAEWVRAE 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK05855  390 HG-VPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTGGHIVNVASAAAYAPSRSLPAYATS 468

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT------------QKVPQKVLDKVIGMIPMGhlgdPEDVADAV 235
Cdd:PRK05855  469 KAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVattrfagadaedEARRRGRADKLYQRRGYG----PEKVAKAI 541
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-235 7.23e-34

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 122.49  E-value: 7.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVA-----ACDLDRAAacetvwllggqgsEKVAPGGAHTAFQ-ADVSEAGAV 80
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGllartEENLKAVA-------------EEVEAYGVKVVIAtADVSDYEEV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:PRK07666   72 TAAIEQLKNELGSI-DILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQ-SGDIINISSTAGQKG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM------TQKVPQKVLdkvigmipmghlgDPEDVADA 234
Cdd:PRK07666  150 AAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMavdlglTDGNPDKVM-------------QPEDLAEF 216


                  .
gi 1953284735 235 V 235
Cdd:PRK07666  217 I 217
PRK06124 PRK06124
SDR family oxidoreductase;
1-257 7.65e-34

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 122.90  E-value: 7.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLggqgsekVAPGGAHTAFQADVSEAGAV 80
Cdd:PRK06124    3 ILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAAL-------RAAGGAAEALAFDIADEEAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:PRK06124   76 AAAFARIDAEHGRL-DILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQG-YGRIIAITSIAGQVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFL 238
Cdd:PRK06124  154 RAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAadPAVGPWLAQRTPLGRWGRPEEIAGAAVFL 233

                         250
                  ....*....|....*....
gi 1953284735 239 ASEDSGYITGASVEVTGGL 257
Cdd:PRK06124  234 ASPAASYVNGHVLAVDGGY 252
PRK07856 PRK07856
SDR family oxidoreductase;
4-256 8.30e-34

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 122.73  E-value: 8.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACdldraaacetvwllGGQGSEKVAPGGAHTAfQADVSEAGAVRRL 83
Cdd:PRK07856    1 NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVC--------------GRRAPETVDGRPAEFH-AADVRDPDQVAAL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVG 163
Cdd:PRK07856   66 VDAIVERHGRL-DVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGGSIVNIGSVSGRRPSPG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHgIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASE 241
Cdd:PRK07856  145 TAAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSELHygDAEGIAAVAATVPLGRLATPADIAWACLFLASD 223

                         250
                  ....*....|....*
gi 1953284735 242 DSGYITGASVEVTGG 256
Cdd:PRK07856  224 LASYVSGANLEVHGG 238
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 12-235 2.41e-33

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: 121.18  E-value: 2.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGgahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05374     3 VLITGCSSGIGLALALALAAQGYRVIATARNPDK-------LESLGELLNDNL---EVLELDVTDEESIKAAVKEVIERF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTrdEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05374    73 GRI-DVLVNNAGYG--LFgpLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQG-SGRIVNVSSVAGLVPTPFLGPYCA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ----------------KVLDKVIGMIPMGhlGDPEDVAD 233
Cdd:cd05374   149 SKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGsaledpeispyaperkEIKENAAGVGSNP--GDPEKVAD 226


                  ..
gi 1953284735 234 AV 235
Cdd:cd05374   227 VI 228
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 6-235 1.69e-32

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 119.66  E-value: 1.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtafqaDVSEAGAVRRLLE 85
Cdd:PRK07825    2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVVGGPL-----------DVTDPASFAAFLD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK07825   71 AVEADL-GPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRG-RGHVVNVASLAGKIPVPGMA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQkvldkvIGMIPMghlGDPEDVADAV 235
Cdd:PRK07825  149 TYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGG------AKGFKN---VEPEDVAAAI 209
PRK12746 PRK12746
SDR family oxidoreductase;
7-257 2.57e-32

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 118.98  E-value: 2.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12746    4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETI-------REIESNGGKAFLIEADLNSIDGVKKLVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACF-----SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQaaaQALVSSGCRGSIINISSIVGKVG 160
Cdd:PRK12746   77 QLKNELqirvgTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQ---QTLPLLRAEGRVINISSAEVRLG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFL 238
Cdd:PRK12746  154 FTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLldDPEIRNFATNSSVFGRIGQVEDIADAVAFL 233

                         250
                  ....*....|....*....
gi 1953284735 239 ASEDSGYITGASVEVTGGL 257
Cdd:PRK12746  234 ASSDSRWVTGQIIDVSGGF 252
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 3-256 2.66e-32

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 118.80  E-value: 2.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   3 SPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllgGQGSEKV-APGGAHTAFQADVSEAGAVR 81
Cdd:PRK06113    5 DNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAA--------NHVVDEIqQLGGQAFACRCDITSEQELS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  82 RLLEQVQACFSRPPSVVVSCAGLTRDEFLLRMseDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:PRK06113   77 ALADFALSKLGKVDILVNNAGGGGPKPFDMPM--ADFRRAYELNVFSFFHLSQLVAPEMEKNG-GGVILTITSMAAENKN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 VGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTP-----MTQKVPQKVLDKVigmiPMGHLGDPEDVADAVT 236
Cdd:PRK06113  154 INMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDalksvITPEIEQKMLQHT----PIRRLGQPQDIANAAL 229

                         250       260
                  ....*....|....*....|
gi 1953284735 237 FLASEDSGYITGASVEVTGG 256
Cdd:PRK06113  230 FLCSPAASWVSGQILTVSGG 249
PRK06947 PRK06947
SDR family oxidoreductase;
13-256 3.33e-32

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 118.37  E-value: 3.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGgqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06947    6 LITGASRGIGRATAVLAAARGWSVGINYArDAAAAEETADAVR-------AAGGRACVVAGDVANEADVIAMFDAVQSAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSS--GCRGSIINISSIVGKVGNVGQ-TNYA 168
Cdd:PRK06947   79 GRLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrgGRGGAIVNVSSIASRLGSPNEyVDYA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIG-MIPMGHLGDPEDVADAVTFLASEDSGYIT 247
Cdd:PRK06947  159 GSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLGaQTPLGRAGEADEVAETIVWLLSDAASYVT 238


                  ....*....
gi 1953284735 248 GASVEVTGG 256
Cdd:PRK06947  239 GALLDVGGG 247
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 12-256 1.16e-31

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: 116.90  E-value: 1.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVA-------AAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05365    75 GGITILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAG-GGAILNISSMSSENKNVRIAAYGSSK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTP-----MTQKVPQKVLDKVigmiPMGHLGDPEDVADAVTFLASEDSGYI 246
Cdd:cd05365   154 AAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDalasvLTPEIERAMLKHT----PLGRLGEPEDIANAALFLCSPASAWV 229

                         250
                  ....*....|
gi 1953284735 247 TGASVEVTGG 256
Cdd:cd05365   230 SGQVLTVSGG 239
PRK06128 PRK06128
SDR family oxidoreductase;
6-257 1.78e-31

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 117.65  E-value: 1.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL--DRAAACETVWLLGGQGSEKVA-PGgahtafqaDVSEAGAVRR 82
Cdd:PRK06128   52 RLQGRKALITGADSGIGRATAIAFAREGADIALNYLpeEEQDAAEVVQLIQAEGRKAVAlPG--------DLKDEAFCRQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGKVGNV 162
Cdd:PRK06128  124 LVERAVKELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG---ASIINTGSIQSYQPSP 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT-------QKVPQKVLDKvigmiPMGHLGDPEDVADAV 235
Cdd:PRK06128  201 TLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQpsggqppEKIPDFGSET-----PMKRPGQPVEMAPLY 275

                         250       260
                  ....*....|....*....|..
gi 1953284735 236 TFLASEDSGYITGASVEVTGGL 257
Cdd:PRK06128  276 VLLASQESSYVTGEVFGVTGGL 297
PRK09135 PRK09135
pteridine reductase; Provisional
 11-256 1.78e-31

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 116.57  E-value: 1.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVA------ACDLDRAAAcetvwllggqGSEKVAPGGAHtAFQADVSEAGAVRRLL 84
Cdd:PRK09135    8 VALITGGARRIGAAIARTLHAAGYRVAihyhrsAAEADALAA----------ELNALRPGSAA-ALQADLLDPDALPELV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPPSVVVSCAGLTRDEfLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvsSGCRGSIINISSIVGKVGNVGQ 164
Cdd:PRK09135   77 AACVAAFGRLDALVNNASSFYPTP-LGSITEAQWDDLFASNLKAPFFLSQAAAPQL--RKQRGAIVNITDIHAERPLKGY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHgIRCNSVLPGFITTP-MTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLAsEDS 243
Cdd:PRK09135  154 PVYCAAKAALEMLTRSLALELAPE-VRVNAVAPGAILWPeDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLL-ADA 231

                         250
                  ....*....|...
gi 1953284735 244 GYITGASVEVTGG 256
Cdd:PRK09135  232 SFITGQILAVDGG 244
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 12-204 3.17e-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: 115.43  E-value: 3.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATV--AACDLDR-AAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd08939     4 VLITGGSSGIGKALAKELVKEGANViiVARSESKlEEAVEEI------EAEANASGQKVSYISADLSDYEEVEQAFAQAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYA 168
Cdd:cd08939    78 EKGG-PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQR-PGHIVFVSSQAALVGIYGYSAYC 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1953284735 169 ASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM 204
Cdd:cd08939   156 PSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPG 191
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-256 4.28e-31

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 115.59  E-value: 4.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA-ACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLE 85
Cdd:PRK06077    4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEeMNETLKMVKENGGEGI-------GVLADVSTREGCETLAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRpPSVVVSCAGLTRdeFLLRMSEDD--WDRVIAVNLKGIFLVTQAAAQALVSSgcrGSIINISSIVGKVGNVG 163
Cdd:PRK06077   77 ATIDRYGV-ADILVNNAGLGL--FSPFLNVDDklIDKHISTDFKSVIYCSQELAKEMREG---GAIVNIASVAGIRPAYG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHgIRCNSVLPGFITTPMTQKVPqkvldKVIGMIP---------MGHLGDPEDVADA 234
Cdd:PRK06077  151 LSIYGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKLGESLF-----KVLGMSEkefaekftlMGKILDPEEVAEF 224

                         250       260
                  ....*....|....*....|..
gi 1953284735 235 VTFLASEDSgyITGASVEVTGG 256
Cdd:PRK06077  225 VAAILKIES--ITGQVFVLDSG 244
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 12-257 1.23e-30

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: 114.21  E-value: 1.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapggahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd09761     4 AIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNL----------FFVHGDVADETLVKFVVYAMLEKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd09761    74 GRI-DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK--GRIINIASTRAFQSEPDSEAYAASK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHgIRCNSVLPGFITTPMTQKVPQKVLDKV-IGMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:cd09761   151 GGLVALTHALAMSLGPD-IRVNCISPGWINTTEQQEFTAAPLTQEdHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGET 229


                  ....*..
gi 1953284735 251 VEVTGGL 257
Cdd:cd09761   230 FIVDGGM 236
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 12-256 1.49e-30

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: 114.12  E-value: 1.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDrAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQacf 91
Cdd:cd08942     9 VLVTGGSRGIGRMIAQGFLEAGARVIISARK-AEACADA-------AEELSAYGECIAIPADLSSEEGIEALVARVA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPS--VVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRG---SIINISSIVGKVGNVGQT- 165
Cdd:cd08942    78 ERSDRldVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAEnpaRVINIGSIAGIVVSGLENy 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDS 243
Cdd:cd08942   158 SYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLlnDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAG 237

                         250
                  ....*....|...
gi 1953284735 244 GYITGASVEVTGG 256
Cdd:cd08942   238 AYLTGAVIPVDGG 250
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 6-256 2.66e-30

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: 113.78  E-value: 2.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacETVWLLGGqgsEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:cd08937     1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-----ELVHEVLA---EILAAGDAAHVHTADLETYAGAQGVVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPpSVVVSCAGLT-RDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVgkVGNVGQ 164
Cdd:cd08937    73 AAVERFGRV-DVLINNVGGTiWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQ-QGVIVNVSSIA--TRGIYR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPmTQKVP--------------QKVLDKVIGMIPMGHLGDPED 230
Cdd:cd08937   149 IPYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP-PRKIPrnaapmseqekvwyQRIVDQTLDSSLMGRYGTIDE 227

                         250       260
                  ....*....|....*....|....*.
gi 1953284735 231 VADAVTFLASEDSGYITGASVEVTGG 256
Cdd:cd08937   228 QVRAILFLASDEASYITGTVLPVGGG 253
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-256 4.10e-30

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 113.76  E-value: 4.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   3 SPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQgsEKVApggahtAFQADVSEAGAVRR 82
Cdd:PLN02253   12 PSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGE--PNVC------FFHCDVTVEDDVSR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSrPPSVVVSCAGLTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:PLN02253   84 AVDFTVDKFG-TLDIMVNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLK-KGSIVSLCSVASAIG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT-QKVPQ--KVLDKVIGMIPM--------GHLGDPE 229
Cdd:PLN02253  162 GLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALAlAHLPEdeRTEDALAGFRAFagknanlkGVELTVD 241

                         250       260
                  ....*....|....*....|....*..
gi 1953284735 230 DVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PLN02253  242 DVANAVLFLASDEARYISGLNLMIDGG 268
PRK08267 PRK08267
SDR family oxidoreductase;
13-235 5.99e-30

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 112.72  E-value: 5.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAfQADVSEAGAVRRLLEQvqacFS 92
Cdd:PRK08267    5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGA--------GNAWTG-ALDVTDRAAWDAALAD----FA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPS----VVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQAL-VSSGCRgsIINISSIVGKVGNVGQTNY 167
Cdd:PRK08267   72 AATGgrldVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLkATPGAR--VINTSSASAIYGQPGLAVY 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 168 AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVI--GMIPMghlgDPEDVADAV 235
Cdd:PRK08267  150 SATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTkrLGVRL----TPEDVAEAV 215
PRK07577 PRK07577
SDR family oxidoreductase;
12-256 9.86e-30

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 111.36  E-value: 9.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETvwllggqgsekvaPGgahTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK07577    6 VLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDF-------------PG---ELFACDLADIEQTAATLAQINEIH 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 srPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVgKVGNVGQTNYAASK 171
Cdd:PRK07577   68 --PVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLRE-QGRIVNICSRA-IFGALDRTSYSAAK 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPM---TQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITG 248
Cdd:PRK07577  144 SALVGCTRTWALELAEYGITVNAVAPGPIETELfrqTRPVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITG 223


                  ....*...
gi 1953284735 249 ASVEVTGG 256
Cdd:PRK07577  224 QVLGVDGG 231
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 12-257 1.17e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 111.78  E-value: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHT-AFqaDVSEAGAVRRLLEQVQAC 90
Cdd:PRK07523   13 ALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLS------AHAlAF--DVTDHDAVRAAIDAFEAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK07523   85 IG-PIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARG-AGKIINIASVQSALARPGIAPYTAT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVpqkVLDKVIGM-----IPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:PRK07523  163 KGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAAL---VADPEFSAwlekrTPAGRWGKVEELVGACVFLASDASSF 239

                         250
                  ....*....|..
gi 1953284735 246 ITGASVEVTGGL 257
Cdd:PRK07523  240 VNGHVLYVDGGI 251
PRK07832 PRK07832
SDR family oxidoreductase;
12-235 1.22e-29

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 112.06  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSeKVApggAHTAFqaDVSEAGAVRRLLEQVQACF 91
Cdd:PRK07832    3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGG-TVP---EHRAL--DISDYDAVAAFAADIHAAH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07832   77 G-SMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-------PQKVLDKVIGMIPmGHLGDPEDVADAV 235
Cdd:PRK07832  156 FGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVeiagvdrEDPRVQKWVDRFR-GHAVTPEKAAEKI 225
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 6-256 4.22e-29

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 110.42  E-value: 4.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDldRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12823    5 RFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVD--RSELVHEV------AAELRAAGGEALALTADLETYAGAQAAMA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVgkVGNVGQT 165
Cdd:PRK12823   77 AAVEAFGRIDVLINNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQG-GGAIVNVSSIA--TRGINRV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPmTQKVP--------------QKVLDKVIGMIPMGHLGDPEDV 231
Cdd:PRK12823  154 PYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAP-PRRVPrnaapqseqekawyQQIVDQTLDSSLMKRYGTIDEQ 232

                         250       260
                  ....*....|....*....|....*
gi 1953284735 232 ADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK12823  233 VAAILFLASDEASYITGTVLPVGGG 257
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 13-256 1.10e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 109.89  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAC--DLDR-AAACETVWLLGGQGSEKVAPggahtafqADVSEAGAVRRLLEQVQA 89
Cdd:PRK05875   11 LVTGGGSGIGKGVAAGLVAAGAAVMIVgrNPDKlAAAAEEIEALKGAGAVRYEP--------ADVTDEDQVARAVDAATA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK05875   83 WHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGG-GGSFVGISSIAASNTHRWFGAYGV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ--KVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYIT 247
Cdd:PRK05875  162 TKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITEspELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWIT 241


                  ....*....
gi 1953284735 248 GASVEVTGG 256
Cdd:PRK05875  242 GQVINVDGG 250
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 7-256 1.58e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 109.01  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA-ACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEeAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQAcfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVGKVGNVGQT 165
Cdd:PRK12747   82 NRTG--STKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNS---RIINISSAATRISLPDFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDK--VIGMIPMGHLGDPEDVADAVTFLASEDS 243
Cdd:PRK12747  157 AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKqyATTISAFNRLGEVEDIADTAAFLASPDS 236

                         250
                  ....*....|...
gi 1953284735 244 GYITGASVEVTGG 256
Cdd:PRK12747  237 RWVTGQLIDVSGG 249
PRK07814 PRK07814
SDR family oxidoreductase;
6-257 1.73e-28

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 109.10  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATV-----AACDLDRAAacetvwllggqgsEKVAPGG--AHTAfQADVSEAG 78
Cdd:PRK07814    7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVliaarTESQLDEVA-------------EQIRAAGrrAHVV-AADLAHPE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  79 AVRRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGK 158
Cdd:PRK07814   73 ATAGLAGQAVEAFGRL-DIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGGGSVINISSTMGR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 159 VGNVGQTNYAASKAGVIGLTQTAARELGRHgIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVT 236
Cdd:PRK07814  152 LAGRGFAAYGTAKAALAHYTRLAALDLCPR-IRVNAIAPGSILTSALEVVAanDELRAPMEKATPLRRLGDPEDIAAAAV 230

                         250       260
                  ....*....|....*....|.
gi 1953284735 237 FLASEDSGYITGASVEVTGGL 257
Cdd:PRK07814  231 YLASPAGSYLTGKTLEVDGGL 251
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-256 3.37e-28

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 107.95  E-value: 3.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAG--SGIGRAVSVRLAKEGATV---AACDLDRaaacETVWllGGQGSEKV-------APGGAHTAFQA 72
Cdd:PRK12859    2 NQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIfftYWTAYDK----EMPW--GVDQDEQIqlqeellKNGVKVSSMEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  73 DVSEAGAVRRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQaLVSSGCRGSIINI 152
Cdd:PRK12859   76 DLTQNDAPKELLNKVTEQLGYP-HILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFAR-GFDKKSGGRIINM 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 153 SSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTP-MTQKVPQKVLDkvigMIPMGHLGDPEDV 231
Cdd:PRK12859  154 TSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTEEIKQGLLP----MFPFGRIGEPKDA 229

                         250       260
                  ....*....|....*....|....*
gi 1953284735 232 ADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK12859  230 ARLIKFLASEEAEWITGQIIHSEGG 254
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 1-256 5.45e-28

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: 107.63  E-value: 5.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKvapggahTAFQADVSEAGAV 80
Cdd:cd08936     2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSV-------TGTVCHVGKAEDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVG 160
Cdd:cd08936    75 ERLVATAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRG-GGSVVIVSSVAAFHP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV--PQKVLDKVIGMIPMGHLGDPEDVADAVTFL 238
Cdd:cd08936   154 FPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALwmDKAVEESMKETLRIRRLGQPEDCAGIVSFL 233

                         250
                  ....*....|....*...
gi 1953284735 239 ASEDSGYITGASVEVTGG 256
Cdd:cd08936   234 CSEDASYITGETVVVGGG 251
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
12-257 8.94e-28

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 106.73  E-value: 8.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDL-DRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK08063    7 ALVTGSSRGIGKAIALRLAEEGYDIAVNYArSRKAAEETAEEIEALGRKAL-------AVKANVGDVEKIKEMFAQIDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGCRGSIINISSIvGKVGNVgqTNYAA- 169
Cdd:PRK08063   80 FGR-LDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAA-KLMEKVGGGKIISLSSL-GSIRYL--ENYTTv 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 --SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:PRK08063  155 gvSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPnrEELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADM 234

                         250
                  ....*....|..
gi 1953284735 246 ITGASVEVTGGL 257
Cdd:PRK08063  235 IRGQTIIVDGGR 246
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 7-248 1.07e-27

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: 106.32  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAAACETVWLLG--GQGSEKV-APGGAHTAFQADVSEAGAVR 81
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVvvAAKTASEGDNGSAKSLPGtiEETAEEIeAAGGQALPIVVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  82 RLLEQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:cd05338    81 ALVEATVDQFGR-LDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAG-QGHILNISPPLSLRPA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 VGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPG-FITTP-MTQKVPQKVLDKVigmipmghlGDPEDVADAVTFLA 239
Cdd:cd05338   159 RGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIETPaATELSGGSDPARA---------RSPEILSDAVLAIL 229


                  ....*....
gi 1953284735 240 SEDSGYITG 248
Cdd:cd05338   230 SRPAAERTG 238
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 12-257 3.22e-27

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: 105.48  E-value: 3.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVA---PGGAHTaFQADVSEAGAVRRLLEQVQ 88
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDLCADDPAVGYPLATRAELDAVAaacPDQVLP-VIADVRDPAALAAAVALAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVS----SGCRgsIINISSIVGKVGNVGQ 164
Cdd:TIGR04504  83 ERWGRLDAAVAAAGVIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLArpdpRGGR--FVAVASAAATRGLPHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ----KVLDKVIGMIPMGHLGDPEDVADAVTFLAS 240
Cdd:TIGR04504 161 AAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAATARlyglTDVEEFAGHQLLGRLLEPEEVAAAVAWLCS 240

                         250
                  ....*....|....*..
gi 1953284735 241 EDSGYITGASVEVTGGL 257
Cdd:TIGR04504 241 PASSAVTGSVVHADGGF 257
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-256 1.07e-26

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: 104.15  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAA--ACETVWLLGGQGSEKVAPggahtafqADVSEAG 78
Cdd:cd08933     1 MASGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAgqALESELNRAGPGSCKFVP--------CDVTKEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  79 AVRRLLEQVQACFSRPpSVVVSCAGL-----TRDEfllrMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINIS 153
Cdd:cd08933    73 DIKTLISVTVERFGRI-DCLVNNAGWhpphqTTDE----TSAQEFRDLLNLNLISYFLASKYALPHLRKS--QGNIINLS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 154 SIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKViGMI-------PMGHLG 226
Cdd:cd08933   146 SLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTL-ATIkegelaqLLGRMG 224

                         250       260       270
                  ....*....|....*....|....*....|
gi 1953284735 227 DPEDVADAVTFLASEdSGYITGASVEVTGG 256
Cdd:cd08933   225 TEAESGLAALFLAAE-ATFCTGIDLLLSGG 253
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-256 1.31e-26

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 104.00  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGA--GSGIGRAVSVRLAKEGATVAA-------CDLDRAAACETVWLLGGqgsEKVAPGGAHTAFQADVS 75
Cdd:PRK12748    1 LPLMKKIALVTGAsrLNGIGAAVCRRLAAKGIDIFFtywspydKTMPWGMHDKEPVLLKE---EIESYGVRCEHMEIDLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  76 EAGAVRRLLEQVQACFSRPPSVVVSCAGLTRDEfLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvSSGCRGSIINISS- 154
Cdd:PRK12748   78 QPYAPNRVFYAVSERLGDPSILINNAAYSTHTR-LEELTAEQLDKHYAVNVRATMLLSSAFAKQY-DGKAGGRIINLTSg 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 155 -IVGKVgnVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFI-TTPMTQKVPQKVLDKvigmIPMGHLGDPEDVA 232
Cdd:PRK12748  156 qSLGPM--PDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTdTGWITEELKHHLVPK----FPQGRVGEPVDAA 229

                         250       260
                  ....*....|....*....|....
gi 1953284735 233 DAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK12748  230 RLIAFLVSEEAKWITGQVIHSEGG 253
PRK06949 PRK06949
SDR family oxidoreductase;
1-257 1.41e-26

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 103.69  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRaaacetvwlLGGQGSEKVAPGGAHTAFQADVSEAG 78
Cdd:PRK06949    1 MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVvlASRRVER---------LKELRAEIEAEGGAAHVVSLDVTDYQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  79 AVRRLLEQVQAcFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGC-------RGSIIN 151
Cdd:PRK06949   72 SIKAAVAHAET-EAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKgagntkpGGRIIN 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 152 ISSIVG-KV-GNVGQtnYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ-KVLDKVIGMIPMGHLGDP 228
Cdd:PRK06949  151 IASVAGlRVlPQIGL--YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWEtEQGQKLVSMLPRKRVGKP 228

                         250       260
                  ....*....|....*....|....*....
gi 1953284735 229 EDVADAVTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK06949  229 EDLDGLLLLLAADESQFINGAIISADDGF 257
PRK07454 PRK07454
SDR family oxidoreductase;
7-239 1.99e-26

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 103.12  E-value: 1.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVA--ACDLDRAAACetvwllggqgSEKVAPGGAHTAFQA-DVSEAGAVRRL 83
Cdd:PRK07454    4 NSMPRALITGASSGIGKATALAFAKAGWDLAlvARSQDALEAL----------AAELRSTGVKAAAYSiDLSNPEAIAPG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVG 163
Cdd:PRK07454   74 IAELLEQFG-CPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGG-GLIINVSSIAARNAFPQ 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284735 164 QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM--TQKVpQKVLDKViGMIPmghlgdPEDVADAVTFLA 239
Cdd:PRK07454  152 WGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLwdTETV-QADFDRS-AMLS------PEQVAQTILHLA 221
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 1-256 2.33e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 103.06  E-value: 2.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACdldraaacetvwllgGQGSEKVAPGGAHTAfQADVSEAGAV 80
Cdd:PRK06523    1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTT---------------ARSRPDDLPEGVEFV-AADLTTAEGC 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRPpSVVVSCAGLTRDEF--LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGK 158
Cdd:PRK06523   65 AAVARAVLERLGGV-DILVHVLGGSSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARG-SGVIIHVTSIQRR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 159 VGNVGQT-NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTP--------------MTQKVPQKVLDKVIGMIPMG 223
Cdd:PRK06523  143 LPLPESTtAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEaavalaerlaeaagTDYEGAKQIIMDSLGGIPLG 222

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1953284735 224 HLGDPEDVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK06523  223 RPAEPEEVAELIAFLASDRAASITGTEYVIDGG 255
PRK07985 PRK07985
SDR family oxidoreductase;
6-256 5.02e-26

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 103.15  E-value: 5.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDL--DRAAACETVWLLGGQGSEKV-APGgahtafqaDVSEAGAVRR 82
Cdd:PRK07985   46 RLKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLpvEEEDAQDVKKIIEECGRKAVlLPG--------DLSDEKFARS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGcrGSIINISSIVGKVGNV 162
Cdd:PRK07985  118 LVHEAHKALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAI-PLLPKG--ASIITTSSIQAYQPSP 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM--TQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLAS 240
Cdd:PRK07985  195 HLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALqiSGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLAS 274

                         250
                  ....*....|....*.
gi 1953284735 241 EDSGYITGASVEVTGG 256
Cdd:PRK07985  275 QESSYVTAEVHGVCGG 290
PRK09186 PRK09186
flagellin modification protein A; Provisional
 13-248 6.72e-26

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 101.99  E-value: 6.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLG-GQGSEKvapggaHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK09186    8 LITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGkEFKSKK------LSLVELDITDQESLEEFLSKSAEKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEF---LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG----KVGNVGQ 164
Cdd:PRK09186   82 GKI-DGAVNCAYPRNKDYgkkFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQG-GGNLVNISSIYGvvapKFEIYEG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TN------YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFIttpmTQKVPQKVLDKV------IGMIpmghlgDPEDVA 232
Cdd:PRK09186  160 TSmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGI----LDNQPEAFLNAYkkccngKGML------DPDDIC 229

                         250
                  ....*....|....*.
gi 1953284735 233 DAVTFLASEDSGYITG 248
Cdd:PRK09186  230 GTLVFLLSDQSKYITG 245
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 12-257 7.37e-26

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 101.96  E-value: 7.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDrAAACETvwlLGGQGSEKVApggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06200    9 ALITGGGSGIGRALVERFLAEGARVAVLERS-AEKLAS---LRQRFGDHVL------VVEGDVTSYADNQRAVDQTVDAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRpPSVVVSCAGLTrdEFLLRMSEDDW-------DRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK06200   79 GK-LDCFVGNAGIW--DYNTSLVDIPAetldtafDEIFNVNVKGYLLGAKAALPALKAS--GGSMIFTLSNSSFYPGGGG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHgIRCNSVLPGFITTPM-------TQKVPQK----VLDKVIGMIPMGHLGDPEDVAD 233
Cdd:PRK06200  154 PLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLrgpaslgQGETSISdspgLADMIAAITPLQFAPQPEDHTG 232

                         250       260
                  ....*....|....*....|....*
gi 1953284735 234 AVTFLAS-EDSGYITGASVEVTGGL 257
Cdd:PRK06200  233 PYVLLASrRNSRALTGVVINADGGL 257
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 6-257 2.28e-25

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: 100.50  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETvwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:cd05348     1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAV--LDRSAEKVA--------ELRADFGDAVVGVEGDVRSLADNERAVA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRpPSVVVSCAGLTrdEFLLRMSEDDWDR-------VIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGK 158
Cdd:cd05348    71 RCVERFGK-LDCFIGNAGIW--DYSTSLVDIPEEKldeafdeLFHINVKGYILGAKAALPALYAT--EGSVIFTVSNAGF 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 159 VGNVGQTNYAASKAGVIGLTQTAARELGRHgIRCNSVLPGFITTP--------MTQKVPQKVL--DKVIGMIPMGHLGDP 228
Cdd:cd05348   146 YPGGGGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDlrgpaslgQGETSISTPPldDMLKSILPLGFAPEP 224

                         250       260       270
                  ....*....|....*....|....*....|
gi 1953284735 229 EDVADAVTFLAS-EDSGYITGASVEVTGGL 257
Cdd:cd05348   225 EDYTGAYVFLASrGDNRPATGTVINYDGGM 254
PRK07062 PRK07062
SDR family oxidoreductase;
5-257 2.54e-25

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 100.50  E-value: 2.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAACETVwlLGGQgsekvAPGGAHTAFQADVSEAGAVRR 82
Cdd:PRK07062    4 IQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICgrDEERLASAEAR--LREK-----FPGARLLAARCDVLDEADVAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:PRK07062   77 FAAAVEARFG-GVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASA-AASIVCVNSLLALQPEP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGM------------IPMGHLGDPED 230
Cdd:PRK07062  155 HMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQSWeawtaalarkkgIPLGRLGRPDE 234

                         250       260
                  ....*....|....*....|....*..
gi 1953284735 231 VADAVTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK07062  235 AARALFFLASPLSSYTTGSHIDVSGGF 261
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 1-206 7.51e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 100.04  E-value: 7.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAV 80
Cdd:PRK05872    1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGG--------DDRVLTVVADVTDLAAM 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVG 160
Cdd:PRK05872   73 QAAAEEAVERFGG-IDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIER--RGYVLQVSSLAAFAA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284735 161 NVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQ 206
Cdd:PRK05872  150 APGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVR 195
PRK05650 PRK05650
SDR family oxidoreductase;
13-235 7.75e-25

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 99.34  E-value: 7.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapGGAHTAfQADVSEagaVRRLLEQVQACFS 92
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAG------GDGFYQ-RCDVRD---YSQLTALAQACEE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 R--PPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK05650   74 KwgGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQK-SGRIVNIASMAGLMQGPAMSSYNVA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFI----------TTPMTQKVPQKVLDKVigmiPMghlgDPEDVADAV 235
Cdd:PRK05650  153 KAGVVALSETLLVELADDEIGVHVVCPSFFqtnlldsfrgPNPAMKAQVGKLLEKS----PI----TAADIADYI 219
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 12-238 1.13e-24

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 97.96  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapgGAHTAfQADVSEAGAVRRLLEQVQACF 91
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELE---------GVLGL-AGDVRDEADVRRAVDAMEEAF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd08929    73 GGL-DALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRG-GGTIVNVGSLAGKNAFKGGAAYNASK 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPqkvldkvigmiPMGHLGDPEDVADAVTFL 238
Cdd:cd08929   151 FGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPE-----------GQAWKLAPEDVAQAVLFA 206
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 12-239 1.94e-24

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: 96.43  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGAtvaacdldraaacetvwllggqgsekvapggahtafqadvseagavrrllEQVQACF 91
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRGS--------------------------------------------------PKVLVVS 30

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAaQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd02266    31 RR--DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAA-RELMKAKRLGRFILISSVAGLFGAPGLGGYAASK 107

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLA 239
Cdd:cd02266   108 AALDGLAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNAL 175
PRK09134 PRK09134
SDR family oxidoreductase;
12-256 2.60e-24

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 97.69  E-value: 2.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAA-CDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK09134   12 ALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALA-------AEIRALGRRAVALQADLADEAEVRALVARASAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvSSGCRGSIINIssIVGKVGNVGQ--TNYA 168
Cdd:PRK09134   85 LG-PITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARAL-PADARGLVVNM--IDQRVWNLNPdfLSYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRHgIRCNSVLPGfITTPMTQKVPQKvLDKVIGMIPMGHLGDPEDVADAVTFLAseDSGYITG 248
Cdd:PRK09134  161 LSKAALWTATRTLAQALAPR-IRVNAIGPG-PTLPSGRQSPED-FARQHAATPLGRGSTPEEIAAAVRYLL--DAPSVTG 235


                  ....*...
gi 1953284735 249 ASVEVTGG 256
Cdd:PRK09134  236 QMIAVDGG 243
PRK12744 PRK12744
SDR family oxidoreductase;
7-256 2.82e-24

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 97.50  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAA----CDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRR 82
Cdd:PRK12744    6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynSAASKADAEETVAAVKAAGAKAVA-------FQADLTTAAAVEK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINI-SSIVGKVGN 161
Cdd:PRK12744   79 LFDDAKAAFGRP-DIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDNG---KIVTLvTSLLGAFTP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 vGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTqkVPQKVLDKV--------IGMIPMGHLGDPEDVAD 233
Cdd:PRK12744  155 -FYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFF--YPQEGAEAVayhktaaaLSPFSKTGLTDIEDIVP 231

                         250       260
                  ....*....|....*....|...
gi 1953284735 234 AVTFLASeDSGYITGASVEVTGG 256
Cdd:PRK12744  232 FIRFLVT-DGWWITGQTILINGG 253
PRK05717 PRK05717
SDR family oxidoreductase;
11-257 4.02e-24

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 97.27  E-value: 4.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAaacetvwllggQGSEKVAPGGAHTAFQA-DVSEAGAVRRLLEQVQA 89
Cdd:PRK05717   12 VALVTGAARGIGLGIAAWLIAEGWQVVLADLDRE-----------RGSKVAKALGENAWFIAmDVADEAQVAAGVAEVLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRPPSVVVSCA-GLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALvsSGCRGSIINISSIVGKVGNVGQTNYA 168
Cdd:PRK05717   81 QFGRLDALVCNAAiADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYL--RAHNGAIVNLASTRARQSEPDTEAYA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRHgIRCNSVLPGFITT--PMTQKV-PQKVLDKviGMIPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:PRK05717  159 ASKGGLLALTHALAISLGPE-IRVNAVSPGWIDArdPSQRRAePLSEADH--AQHPAGRVGTVEDVAAMVAWLLSRQAGF 235

                         250
                  ....*....|..
gi 1953284735 246 ITGASVEVTGGL 257
Cdd:PRK05717  236 VTGQEFVVDGGM 247
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 7-237 1.00e-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: 96.07  E-value: 1.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdldraaACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAI-------AARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVER 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPpSVVVSCAGLtrdeFLLRMSED----DWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:cd08934    74 TVEALGRL-DILVNNAGI----MLLGPVEDadttDWTRMIDTNLLGLMYTTHAALPHHLLRN-KGTIVNISSVAGRVAVR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV---PQKVLDK--VIGMIPMghlgDPEDVADAVTF 237
Cdd:cd08934   148 NSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHIthtITKEAYEerISTIRKL----QAEDIAAAVRY 223
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 13-257 2.90e-23

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: 94.87  E-value: 2.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwllggqgsekvapggahtaFQADVSEAGAVRRLLEQVQACFS 92
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTVIGIDLREAD------------------------VIADLSTPEGRAAAIADVLARCS 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPSVVVSCAGLTRDEFLlrmseddwDRVIAVNLKGIFLVTQAAAQALvSSGCRGSIINISSIVG--------------- 157
Cdd:cd05328    59 GVLDGLVNCAGVGGTTVA--------GLVLKVNYFGLRALMEALLPRL-RKGHGPAAVVVSSIAGagwaqdklelakala 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 158 ------------KVGNVGQTNYAASKAGVIGLTQTAARE-LGRHGIRCNSVLPGFITTPMTQKVPQKVL--DKVIGMI-P 221
Cdd:cd05328   130 agtearavalaeHAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRggESVDAFVtP 209

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1953284735 222 MGHLGDPEDVADAVTFLASEDSGYITGASVEVTGGL 257
Cdd:cd05328   210 MGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGL 245
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 12-240 3.30e-23

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: 94.65  E-value: 3.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDlDRAAACETVWL-LGGQGSEKVAPggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05346     3 VLITGASSGIGEATARRFAKAGAKLILTG-RRAERLQELADeLGAKFPVKVLP------LQLDVSDRESIEAALENLPEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRD-EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05346    76 FRDI-DILVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARN-QGHIINLGSIAGRYPYAGGNVYCA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQ---KVPQKVLDKVI-GMIPMghlgDPEDVADAVTFLAS 240
Cdd:cd05346   154 TKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLvrfHGDKEKADKVYeGVEPL----TPEDIAETILWVAS 224
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 12-208 4.73e-23

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: 93.93  E-value: 4.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRaaacetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQA 89
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAarRTDR---------LDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05350    72 ELG-GLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKG-RGHLVLISSVAALRGLPGAAAYSA 149

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV 208
Cdd:cd05350   150 SKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANM 188
PRK06181 PRK06181
SDR family oxidoreductase;
11-202 6.75e-23

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 93.89  E-value: 6.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVApggahtaFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK06181    3 VVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALV-------VPTDVSDAEACERLIEAAVAR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPpSVVVSCAGLTRDEFLLRMSEDDW-DRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK06181   76 FGGI-DILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKAS--RGQIVVVSSLAGLTGVPTRSGYAA 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITT 202
Cdd:PRK06181  153 SKHALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 6-240 1.00e-22

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: 93.35  E-value: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACdldrAAACETVWLLGGQGSEkvAPGGAHTAFQADVSEAgavrrllE 85
Cdd:cd05343     3 RWRGRVALVTGASVGIGAAVARALVQHGMKVVGC----ARRVDKIEALAAECQS--AGYPTLFPYQCDLSNE-------E 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPPS------VVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGC-RGSIINISSIVG- 157
Cdd:cd05343    70 QILSMFSAIRTqhqgvdVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVdDGHIININSMSGh 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 158 KVGNVGQTN-YAASKAGVIGLTQTAAREL--GRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDPEDVADA 234
Cdd:cd05343   150 RVPPVSVFHfYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANA 229


                  ....*.
gi 1953284735 235 VTFLAS 240
Cdd:cd05343   230 VLYVLS 235
PRK09072 PRK09072
SDR family oxidoreductase;
5-235 5.01e-22

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 91.54  E-value: 5.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVAPGGaHTAFQADVSEAGAVRRLL 84
Cdd:PRK09072    1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEK-------LEALAARLPYPGR-HRWVVADLTSEAGREAVL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQAcfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK09072   73 ARARE--MGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQP-SAMVVNVGSTFGSIGYPGY 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKvigmipmghLG----DPEDVADAV 235
Cdd:PRK09072  150 ASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEAVQALNRA---------LGnamdDPEDVAAAV 215
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 12-242 2.73e-21

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: 89.36  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAacdldrAAACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05373     2 AAVVGAGDGLGAAIARRFAAEGFSVA------LAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd05373    76 G-PLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARG-RGTIIFTGATASLRGRAGFAAFAGAK 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVL------PGFITTPMTQKVPQKVLDKVIgmipmghlgDPEDVADAVTFLASED 242
Cdd:cd05373   154 FALRALAQSMARELGPKGIHVAHVIidggidTDFIRERFPKRDERKEEDGIL---------DPDAIAEAYWQLHTQP 221
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 12-206 3.67e-21

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: 88.81  E-value: 3.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAacetvwllggqgSEKVAPGGAHT-AFQADVS-EAGAVRRLL 84
Cdd:cd05356     4 AVVTGATDGIGKAYAEELAKRGFNVILIsrtqeKLDAVA------------KEIEEKYGVETkTIAADFSaGDDIYERIE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQacfSRPPSVVVSCAGLTRD--EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:cd05356    72 KELE---GLDIGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRK-KGAIVNISSFAGLIPTP 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQ 206
Cdd:cd05356   148 LLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 12-205 1.08e-20

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: 87.29  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGA---TVAACDLDRaaacetvwllGGQGSEKVAPGGAHTAF-QADVSEAGAVRRLLEQV 87
Cdd:cd05324     3 ALVTGANRGIGFEIVRQLAKSGPgtvILTARDVER----------GQAAVEKLRAEGLSVRFhQLDVTDDASIEAAADFV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  88 QACFSRPpSVVVSCAGLTRDEFL-LRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVgnvgQTN 166
Cdd:cd05324    73 EEKYGGL-DILVNNAGIAFKGFDdSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPA-GRIVNVSSGLGSL----TSA 146

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT 205
Cdd:cd05324   147 YGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMG 185
PRK06194 PRK06194
hypothetical protein; Provisional
 12-246 1.19e-20

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 88.53  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK06194    9 AVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVL-------GVRTDVSDAAQVEALADAALERF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQA-----AAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK06194   82 G-AVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAftplmLAAAEKDPAYEGHIVNTASMAGLLAPPAMGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHG--IRCNSVLPGFITTPMTQ---------------KVPQKVLDKVIG-MIPMGHLGdP 228
Cdd:PRK06194  161 YNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQsernrpadlantappTRSQLIAQAMSQkAVGSGKVT-A 239

                         250
                  ....*....|....*...
gi 1953284735 229 EDVADAVTFLASEDSGYI 246
Cdd:PRK06194  240 EEVAQLVFDAIRAGRFYI 257
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 7-248 1.75e-20

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: 86.86  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVaacdldraaacetvwLLGGQGSEKVAPGGAHTA---------FQADVSEA 77
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATV---------------ILLGRNEEKLRQVADHINeeggrqpqwFILDLLTC 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  78 GA--VRRLLEQVQACFSRPPSVVVScAGLTRDEF-LLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISS 154
Cdd:cd05340    67 TSenCQQLAQRIAVNYPRLDGVLHN-AGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSD-AGSLVFTSS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 155 IVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-----PQKvldkvigmipmghLGDPE 229
Cdd:cd05340   145 SVGRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAfptedPQK-------------LKTPA 211

                         250
                  ....*....|....*....
gi 1953284735 230 DVADAVTFLASEDSGYITG 248
Cdd:cd05340   212 DIMPLYLWLMGDDSRRKTG 230
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 12-259 7.06e-20

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: 85.71  E-value: 7.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggQGSEKVAPGGAHTAFQADvseagavRRLLEQVQACF 91
Cdd:cd05361     4 ALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAER------QAFESENPGTKALSEQKP-------EELVDAVLQAG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVI-AVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:cd05361    71 GAIDVLVSNDYIPRPMNPIDGTSEADIRQAFeALSIFPFALLQAAIAQMKKAGG--GSIIFITSAVPKKPLAYNSLYGPA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM-----TQKVPQKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGY 245
Cdd:cd05361   149 RAAAVALAESLAKELSRDNILVYAIGPNFFNSPTyfptsDWENNPELRERVKRDVPLGRLGRPDEMGALVAFLASRRADP 228

                         250
                  ....*....|....
gi 1953284735 246 ITGASVEVTGGLYM 259
Cdd:cd05361   229 ITGQFFAFAGGYLP 242
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 12-253 1.30e-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: 83.79  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVaacdldraaacetvwllggqgsekVAPGGAHTAFQADVSEAGAVRRLLEQVQACf 91
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEV------------------------ITAGRSSGDYQVDITDEASIKALFEKVGHF- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 srppSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:cd11731    56 ----DAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND---GGSITLTSGILAQRPIPGGAAAATVN 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRhGIRCNSVLPGFITTPMtqkvpQKVLDKVIGMIPmghlGDPEDVADAVTFLAsedSGYITGASV 251
Cdd:cd11731   129 GALEGFVRAAAIELPR-GIRINAVSPGVVEESL-----EAYGDFFPGFEP----VPAEDVAKAYVRSV---EGAFTGQVL 195


                  ..
gi 1953284735 252 EV 253
Cdd:cd11731   196 HV 197
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 14-235 2.18e-19

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: 84.04  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  14 VTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACEtvwLLGGQGSEKVAPGgahtafQADVSEAGAVRRLLEQVQACFSR 93
Cdd:cd08931     5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAA---LAAELGAENVVAG------ALDVTDRAAWAAALADFAAATGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  94 PPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQAL-VSSGCRgsIINISSIVGKVGNVGQTNYAASKA 172
Cdd:cd08931    76 RLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLkATPGAR--VINTASSSAIYGQPDLAVYSATKF 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284735 173 GVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMghlgDPEDVADAV 235
Cdd:cd08931   154 AVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRVL----PVSDVAKVV 212
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 12-259 2.28e-19

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: 84.58  E-value: 2.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATV-AACdlDRAAACETVWllggqgSEKVAPGGAH--TAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd05327     4 VVITGANSGIGKETARELAKRGAHViIAC--RNEEKGEEAA------AEIKKETGNAkvEVIQLDLSSLASVRQFAEEFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFsRPPSVVVSCAGLTRDEFllRMSEDDWDRVIAVNLKGIFLVTQAAAQALV-SSGCRgsIINISSIVGKVGNVGQTN- 166
Cdd:cd05327    76 ARF-PRLDILINNAGIMAPPR--RLTKDGFELQFAVNYLGHFLLTNLLLPVLKaSAPSR--IVNVSSIAHRAGPIDFNDl 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 -------------YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ-KVLDKVIGmiPMGHLgDPEDVA 232
Cdd:cd05327   151 dlennkeyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSfFLLYKLLR--PFLKK-SPEQGA 227

                         250       260
                  ....*....|....*....|....*..
gi 1953284735 233 DAVTFLASEDsgyitgaSVEVTGGLYM 259
Cdd:cd05327   228 QTALYAATSP-------ELEGVSGKYF 247
PRK08264 PRK08264
SDR family oxidoreductase;
10-235 2.67e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 83.79  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  10 ALALVTGAGSGIGRAVSVRLAKEGAT---VAACDLDRAAAcetvwllggqGSEKVAPggahtaFQADVSEAGAVRRLLEQ 86
Cdd:PRK08264    7 KVVLVTGANRGIGRAFVEQLLARGAAkvyAAARDPESVTD----------LGPRVVP------LQLDVTDPASVAAAAEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 vqacfSRPPSVVVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08264   71 -----ASDVTILVNNAGiFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANG-GGAIVNVLSVLSWVNFPNLG 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPqkvLDKVigmipmghlgDPEDVADAV 235
Cdd:PRK08264  145 TYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLD---APKA----------SPADVARQI 201
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 14-241 3.03e-19

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: 83.59  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  14 VTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQACFSR 93
Cdd:cd05360     5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAI-------AVVADVADAAQVERAADTAVERFGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  94 pPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKAG 173
Cdd:cd05360    78 -IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRG-GGALINVGSLLGYRSAPLQAAYSASKHA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 174 VIGLTQTAARELGRHG--IRCNSVLPGFITTPMTQKVPQKvLDKVIGMIPMghLGDPEDVADAVTFLASE 241
Cdd:cd05360   156 VRGFTESLRAELAHDGapISVTLVQPTAMNTPFFGHARSY-MGKKPKPPPP--IYQPERVAEAIVRAAEH 222
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 12-257 3.71e-19

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: 84.21  E-value: 3.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllgGQGSEKVAPGGAHTAfQADVSEAGAV-RRLLEQVQAC 90
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTL----AAELNARRPNSAVTC-QADLSNSATLfSRCEAIIDAC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSR--PPSVVVSCAGLTRDEFLLRMSEDDWD-----------RVIAVNLKGIFLVTQAAAQALVSSG--CRG---SIINI 152
Cdd:TIGR02685  79 FRAfgRCDVLVNNASAFYPTPLLRGDAGEGVgdkkslevqvaELFGSNAIAPYFLIKAFAQRQAGTRaeQRStnlSIVNL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 153 SSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTqkVPQKVLDKVIGMIPMGHL-GDPEDV 231
Cdd:TIGR02685 159 CDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPDA--MPFEVQEDYRRKVPLGQReASAEQI 236

                         250       260
                  ....*....|....*....|....*.
gi 1953284735 232 ADAVTFLASEDSGYITGASVEVTGGL 257
Cdd:TIGR02685 237 ADVVIFLVSPKAKYITGTCIKVDGGL 262
PRK07775 PRK07775
SDR family oxidoreductase;
12-244 3.80e-19

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 84.04  E-value: 3.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVaACDLDRAAACETVwllggqgSEKV-APGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPV-ALGARRVEKCEEL-------VDKIrADGGEAVAFPLDVTDPDSVKSFVAQAEEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAAS 170
Cdd:PRK07775   85 LG-EIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERR-RGDLIFVGSDVALRQRPHMGAYGAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVI------GMIPMGHLGDPEDVADAVTFLASEDSG 244
Cdd:PRK07775  163 KAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSLPAEVIGPMLedwakwGQARHDYFLRASDLARAITFVAETPRG 242
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 7-256 1.29e-18

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 82.60  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATV-----AACDLDRAaacetvwllggqgSEKV---APGGAHTaFQADVSEAG 78
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVillsrNEENLKKA-------------REKIkseSNVDVSY-IVADLTKRE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  79 AVRRLLEQVQACFSrpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGK 158
Cdd:PRK08339   72 DLERTVKELKNIGE--PDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGF-GRIIYSTSVAIK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 159 --VGNVGQTNYAasKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ-----------KVLDKVIGMIPMGHL 225
Cdd:PRK08339  149 epIPNIALSNVV--RISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQdrakregksveEALQEYAKPIPLGRL 226

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953284735 226 GDPEDVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK08339  227 GEPEEIGYLVAFLASDLGSYINGAMIPVDGG 257
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 1-198 3.96e-18

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 83.43  E-value: 3.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   1 MASPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGsekvapGGAHTAFQADVSEAGAV 80
Cdd:COG3347   417 MPKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGY------GADAVDATDVDVTAEAA 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  81 RRLLEQVQACFSRPPSVVVSCAGL--TRDEFLLRMSedDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGK 158
Cdd:COG3347   491 VAAAFGFAGLDIGGSDIGVANAGIasSSPEEETRLS--FWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSKNAA 568

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284735 159 VGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPG 198
Cdd:COG3347   569 AAAYGAAAAATAKAAAQHLLRALAAEGGANGINANRVNPD 608
PRK07024 PRK07024
SDR family oxidoreductase;
11-233 3.98e-18

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 81.13  E-value: 3.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGqgsekvapGGAHTAFQADVSEAGAVRRlleQVQAC 90
Cdd:PRK07024    4 KVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPK--------AARVSVYAADVRDADALAA---AAADF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRP--PSVVVSCAGLTRDEfLLRMSED--DWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK07024   73 IAAHglPDVVIANAGISVGT-LTEEREDlaVFREVMDTNYFGMVATFQPFIAPMRAAR-RGTLVGIASVAGVRGLPGAGA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPqkvldkvigmIPMGHLGDPEDVAD 233
Cdd:PRK07024  151 YSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTAHNP----------YPMPFLMDADRFAA 207
PRK12742 PRK12742
SDR family oxidoreductase;
12-256 4.52e-18

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 80.57  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAacdldraaaceTVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQvqacf 91
Cdd:PRK12742    9 VLVLGGSRGIGAAIVRRFVTDGANVR-----------FTYAGSKDAAERLAQETGATAVQTDSADRDAVIDVVRK----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVG-KVGNVGQTNYAAS 170
Cdd:PRK12742   73 SGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEGG---RIIIIGSVNGdRMPVAGMAAYAAS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMT-QKVPQKvlDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGA 249
Cdd:PRK12742  150 KSALQGMARGLARDFGPRGITINVVQPGPIDTDANpANGPMK--DMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGA 227


                  ....*..
gi 1953284735 250 SVEVTGG 256
Cdd:PRK12742  228 MHTIDGA 234
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 12-210 4.94e-18

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: 80.42  E-value: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGAT--VAAC-DLDRAAACETvwlLGGQGSEKVAPggahtafQADVSE-----AGAVRRL 83
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNtvIATCrDPSAATELAA---LGASHSRLHIL-------ELDVTDeiaesAEAVAER 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQvqacfsRPPSVVVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGCRGSIINISSIVGKVGNV 162
Cdd:cd05325    71 LGD------AGLDVLINNAGiLHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFL-PLLLKGARAKIINISSRVGSIGDN 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953284735 163 ---GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ 210
Cdd:cd05325   144 tsgGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAK 194
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 12-239 5.32e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 81.89  E-value: 5.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK07109   11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEAL-------AVVADVADAEAVQAAADRAEEEL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07109   84 G-PIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRD-RGAIIQVGSALAYRSIPLQSAYCAAK 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHG--IRCNSVLPGFITTPMTQKVPQKvLDKVIGMIPMGHlgDPEDVADAVTFLA 239
Cdd:PRK07109  162 HAIRGFTDSLRCELLHDGspVSVTMVQPPAVNTPQFDWARSR-LPVEPQPVPPIY--QPEVVADAILYAA 228
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 11-252 1.10e-17

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: 79.64  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQ------ELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPPSVVVSCAGLT---RDEFLlrmSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNY 167
Cdd:cd05367    75 DGERDLLINNAGSLGpvsKIEFI---DLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKTVVNVSSGAAVNPFKGWGLY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 168 AASKAGVIGLTQTAARELgrHGIRCNSVLPGFITTPMTQKV-----PQKVLDKVIGMIPMGHLGDPEDVADAVTFLASED 242
Cdd:cd05367   152 CSSKAARDMFFRVLAAEE--PDVRVLSYAPGVVDTDMQREIretsaDPETRSRFRSLKEKGELLDPEQSAEKLANLLEKD 229

                         250
                  ....*....|
gi 1953284735 243 SgYITGASVE 252
Cdd:cd05367   230 K-FESGAHVD 238
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 13-250 1.35e-17

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 79.53  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVaacdldraaacetvwLLGGQGSEK--------VAPGGAHTA-FQADVSEAGA--VR 81
Cdd:PRK08945   16 LVTGAGDGIGREAALTYARHGATV---------------ILLGRTEEKleavydeiEAAGGPQPAiIPLDLLTATPqnYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  82 RLLEQVQACFSRPPSVVVScAGL--TRDEFLlRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKV 159
Cdd:PRK08945   81 QLADTIEEQFGRLDGVLHN-AGLlgELGPME-QQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPA-ASLVFTSSSVGRQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 160 GNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV-----PQKvldkvigmipmghLGDPEDVADA 234
Cdd:PRK08945  158 GRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRASAfpgedPQK-------------LKTPEDIMPL 224

                         250
                  ....*....|....*.
gi 1953284735 235 VTFLASEDSGYITGAS 250
Cdd:PRK08945  225 YLYLMGDDSRRKNGQS 240
PRK06914 PRK06914
SDR family oxidoreductase;
12-240 1.74e-17

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 79.68  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAAcetvwlLGGQGSEKVAPGGAHTaFQADVSEAGAVRRLLEQVQA 89
Cdd:PRK06914    6 AIVTGASSGFGLLTTLELAKKGYLVIATmrNPEKQEN------LLSQATQLNLQQNIKV-QQLDVTDQNSIHNFQLVLKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 cfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:PRK06914   79 --IGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQK-SGKIINISSISGRVGFPGLSPYVS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ-------------KVLDKVIGMIPMG--HLGDPEDVADA 234
Cdd:PRK06914  156 SKYALEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVGKQlaenqsettspykEYMKKIQKHINSGsdTFGNPIDVANL 235


                  ....*.
gi 1953284735 235 VTFLAS 240
Cdd:PRK06914  236 IVEIAE 241
PRK07041 PRK07041
SDR family oxidoreductase;
13-256 2.09e-17

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 78.54  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGA--TVAACDLDRAAAcetvwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLleqvqac 90
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGArvTIASRSRDRLAA----------AARALGGGAPVRTAALDITDEAAVDAF------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPPSV--VVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQAlvssgCRGSIINISSIVGKVGNVGQTNYA 168
Cdd:PRK07041   64 FAEAGPFdhVVITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAARIA-----PGGSLTFVSGFAAVRPSASGVLQG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 169 ASKAGVIGLTQTAARELGRhgIRCNSVLPGFITTPMTQKVP----QKVLDKVIGMIPMGHLGDPEDVADAVTFLASedSG 244
Cdd:PRK07041  139 AINAALEALARGLALELAP--VRVNTVSPGLVDTPLWSKLAgdarEAMFAAAAERLPARRVGQPEDVANAILFLAA--NG 214

                         250
                  ....*....|..
gi 1953284735 245 YITGASVEVTGG 256
Cdd:PRK07041  215 FTTGSTVLVDGG 226
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 12-202 2.09e-17

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 79.23  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHtAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05876    9 AVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFD------VH-GVMCDVRHREEVTHLADEAFRLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05876   82 GHV-DVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAK 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITT 202
Cdd:PRK05876  161 YGVVGLAETLAREVTADGIGVSVLCPMVVET 191
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 13-235 2.30e-17

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: 78.78  E-value: 2.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:cd05332     7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSP------HVVPLDMSDLEDAEQVVEEALKLFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:cd05332    81 GL-DILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERS-QGSIVVVSSIAGKIGVPFRTAYAASKH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284735 173 GVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGM-IPMGHLGDPEDVADAV 235
Cdd:cd05332   159 ALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMdDTTANGMSPEECALEI 222
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-256 2.71e-17

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 78.26  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEKVAPGgahtafqaDVSEAGAVRRLL 84
Cdd:PRK05786    1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYVVG--------DVSSTESARNVI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQACFSRPPSVVVSCAGLTRDEFllrmsED--DWDRVIAVNLKGIFLVTQAAAQALVssgcRGSIINISSIVGKVGNV 162
Cdd:PRK05786   73 EKAAKVLNAIDGLVVTVGGYVEDTV-----EEfsGLEEMLTNHIKIPLYAVNASLRFLK----EGSSIVLVSSMSGIYKA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 G--QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKvigmipmghLGD----PEDVADAVT 236
Cdd:PRK05786  144 SpdQLSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPERNWKKLRK---------LGDdmapPEDFAKVII 214

                         250       260
                  ....*....|....*....|
gi 1953284735 237 FLASEDSGYITGASVEVTGG 256
Cdd:PRK05786  215 WLLTDEADWVDGVVIPVDGG 234
PRK07201 PRK07201
SDR family oxidoreductase;
13-235 6.01e-17

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 80.00  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK07201  375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELV-------AEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHG 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RpPSVVVSCAG--------LTRDEFllrmseDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIvgkvgnvG- 163
Cdd:PRK07201  448 H-VDYLVNNAGrsirrsveNSTDRF------HDYERTMAVNYFGAVRLILGLLPHMRERR-FGHVVNVSSI-------Gv 512

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284735 164 QTN------YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTqkVPQKVLDKVIGMipmghlgDPEDVADAV 235
Cdd:PRK07201  513 QTNaprfsaYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMI--APTKRYNNVPTI-------SPEEAADMV 581
PRK08416 PRK08416
enoyl-ACP reductase;
130-256 6.64e-17

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 77.89  E-value: 6.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 130 FLV-TQAAAQALVSSGcRGSIINISSivgkVGN-VGQTNYAA---SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM 204
Cdd:PRK08416  128 FVVgAQEAAKRMEKVG-GGSIISLSS----TGNlVYIENYAGhgtSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDA 202

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953284735 205 TQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK08416  203 LKAFTnyEEVKAKTEELSPLNRMGQPEDLAGACLFLCSEKASWLTGQTIVVDGG 256
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 12-219 7.31e-17

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: 76.96  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggahtafQADVSEAGAVRRLLEQVQACF 91
Cdd:cd05370     8 VLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIHTI-----------VLDVGDAESVEALAEALLSEY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSE--DDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05370    77 PNL-DILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQP-EATIVNVSSGLAFVPMAANPVYCA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGM 219
Cdd:cd05370   155 TKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKM 204
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 13-235 8.01e-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: 77.12  E-value: 8.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAAcetvwllggqgsekvAPGGAHTaFQADVSEAGAVRRLLEQV 87
Cdd:COG3967     9 LITGGTSGIGLALAKRLHARGNTVIITgrreeKLEEAAA---------------ANPGLHT-IVLDVADPASIAALAEQV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  88 QACFsrpPS--VVVSCAGLTRDEFLLRmSEDDWD---RVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNV 162
Cdd:COG3967    73 TAEF---PDlnVLINNAGIMRAEDLLD-EAEDLAdaeREITTNLLGPIRLTAAFLPHLKAQP-EAAIVNVSSGLAFVPLA 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVldkviGMIPmghlgdPEDVADAV 235
Cdd:COG3967   148 VTPTYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDP-----RAMP------LDEFADEV 209
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 13-169 3.03e-16

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: 77.41  E-value: 3.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAK-EGATVAAcdLDRAAACETVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAcF 91
Cdd:cd08953   209 LVTGGAGGIGRALARALARrYGARLVL--LGRSPLPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRE-R 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVssgcrGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd08953   286 YGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPL-----DFFVLFSSVSAFFGGAGQADYAA 358
PRK08219 PRK08219
SDR family oxidoreductase;
10-237 5.11e-16

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 74.58  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  10 ALALVTGAGSGIGRAVSVRLAkEGATVaacdldraaacetvwLLGGQGSEKVAP-----GGAHTaFQADVSEAGAVRRLL 84
Cdd:PRK08219    4 PTALITGASRGIGAAIARELA-PTHTL---------------LLGGRPAERLDElaaelPGATP-FPVDLTDPEAIAAAV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVqacfsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQ 164
Cdd:PRK08219   67 EQL-----GRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAA--HGHVVFINSGAGLRANPGW 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQtAARELGRHGIRCNSVLPGFITTPMTQKV---------PQKVLdkvigmipmghlgDPEDVADAV 235
Cdd:PRK08219  140 GSYAASKFALRALAD-ALREEEPGNVRVTSVHPGRTDTDMQRGLvaqeggeydPERYL-------------RPETVAKAV 205


                  ..
gi 1953284735 236 TF 237
Cdd:PRK08219  206 RF 207
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 13-210 9.75e-16

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: 74.62  E-value: 9.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdldraaACETVWLLGGQGSEKVAPGGAHTaFQADVSEAGAVRRLLEQVQAcfs 92
Cdd:cd09805     4 LITGCDSGFGNLLAKKLDSLGFTVLA-------GCLTKNGPGAKELRRVCSDRLRT-LQLDVTKPEQIKRAAQWVKE--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 rppSV-------VVSCAG---LTRDEFLLRMseDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNV 162
Cdd:cd09805    73 ---HVgekglwgLVNNAGilgFGGDEELLPM--DDYRKCMEVNLFGTVEVTKAFLPLLRRA--KGRVVNVSSMGGRVPFP 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ 210
Cdd:cd09805   146 AGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSEL 193
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 12-235 1.26e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 74.17  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAACETVWLLggqgsekvapggahtafQADVSEAGAVRRLLEQVQA 89
Cdd:PRK06179    7 ALVTGASSGIGRATAEKLARAGYRVFGTsrNPARAAPIPGVELL-----------------ELDVTDDASVQAAVDEVIA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRpPSVVVSCAGLT----RDEFllrmSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK06179   70 RAGR-IDVLVNNAGVGlagaAEES----SIAQAQALFDTNVFGILRMTRAVLPHMRAQG-SGRIINISSVLGFLPAPYMA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ------------KVLDKVIGMIpMGHLGDPEDVAD 233
Cdd:PRK06179  144 LYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEpdsplaeydrerAVVSKAVAKA-VKKADAPEVVAD 222


                  ..
gi 1953284735 234 AV 235
Cdd:PRK06179  223 TV 224
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 5-257 1.46e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 73.92  E-value: 1.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDR-AAACETVWLLGGQGSekvapggahTAFQADVSEAGAVR 81
Cdd:PRK06125    3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLhlVARDADAlEALAADLRAAHGVDV---------AVHALDLSSPEARE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  82 RLLEQVQacfsrPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINIssivgkVGN 161
Cdd:PRK06125   74 QLAAEAG-----DIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARG-SGVIVNV------IGA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 VGQT---NY---AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTP-----MTQKVPQKVLD-----KVIGMIPMGHL 225
Cdd:PRK06125  142 AGENpdaDYicgSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDrmltlLKGRARAELGDesrwqELLAGLPLGRP 221

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1953284735 226 GDPEDVADAVTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK06125  222 ATPEEVADLVAFLASPRSGYTSGTVVTVDGGI 253
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 7-241 1.87e-15

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: 73.63  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQ------LPGTAEEIEARGGKCIPVRCDHSDDDEVEALFER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPPSVVVSCA-------GLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIvGKV 159
Cdd:cd09763    75 VAREQQGRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAG-KGLIVIISST-GGL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 160 GNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQK----VLDKVIGMIPMGHlgDPEDVADAV 235
Cdd:cd09763   153 EYLFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDdegsWHAKERDAFLNGE--TTEYSGRCV 230


                  ....*.
gi 1953284735 236 TFLASE 241
Cdd:cd09763   231 VALAAD 236
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 13-169 2.42e-15

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: 71.82  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGAT----VAACDLDRAAACETVWLLGGQGSEKVAPggahtafQADVSEAGAVRRLLEQVQ 88
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhlvlLSRSAAPRPDAQALIAELEARGVEVVVV-------ACDVSDPDAVAALLAEIK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 AcfsRPPSV--VVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVssgcrGSIINISSIVGKVGNVGQTN 166
Cdd:pfam08659  77 A---EGPPIrgVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPL-----DFFVLFSSIAGLLGSPGQAN 148


                  ...
gi 1953284735 167 YAA 169
Cdd:pfam08659 149 YAA 151
PRK08862 PRK08862
SDR family oxidoreductase;
7-197 6.72e-15

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 71.68  E-value: 6.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLgGQGSEKVAPggahtaFQADVSEAGAVRRLLEQ 86
Cdd:PRK08862    3 IKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQC-SALTDNVYS------FQLKDFSQESIRHLFDA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACFSRPPSVVVSC----------AGLTRDEFLLRMSEddwdrvIAVNLkgiFLVTQAAAQALVSSGCRGSIINissiV 156
Cdd:PRK08862   76 IEQQFNRAPDVLVNNwtssplpslfDEQPSESFIQQLSS------LASTL---FTYGQVAAERMRKRNKKGVIVN----V 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953284735 157 GKVGNVGQ-TNYAASKAGVIGLTQTAARELGRHGIRCNSVLP 197
Cdd:PRK08862  143 ISHDDHQDlTGVESSNALVSGFTHSWAKELTPFNIRVGGVVP 184
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 13-235 4.21e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 70.07  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGgqgsEKVAPggahtaFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK08263    7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYG----DRLLP------LALDVTDRAAVFAAVETAVEHFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK08263   77 RL-DIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQR-SGHIIQISSIGGISAFPMSGIYHASKW 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284735 173 GVIGLTQTAARELGRHGIRCNSVLPG-----FITTPMTQKVP----QKVLDKVIGMIPMGHL-GDPEDVADAV 235
Cdd:PRK08263  155 ALEGMSEALAQEVAEFGIKVTLVEPGgystdWAGTSAKRATPldayDTLREELAEQWSERSVdGDPEAAAEAL 227
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 12-235 5.91e-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: 68.97  E-value: 5.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGAT---VAACDLDRAAAcetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEqvq 88
Cdd:cd05354     6 VLVTGANRGIGKAFVESLLAHGAKkvyAAVRDPGSAAH------LVAKYGDKVVPLRLDVTDPESIKAAAAQAKDVD--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 acfsrppsVVVSCAGLTRDEFLLRMSEDDWDRVIA-VNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNY 167
Cdd:cd05354    77 --------VVINNAGVLKPATLLEEGALEALKQEMdVNVFGLLRLAQAFAPVLKANG-GGAIVNLNSVASLKNFPAMGTY 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953284735 168 AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPqkvldkvigmipmGHLGDPEDVADAV 235
Cdd:cd05354   148 SASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAG-------------GPKESPETVAEAV 202
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-169 6.29e-14

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: 67.89  E-value: 6.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   13 LVTGAGSGIGRAVSVRLAKEGAT----VAACDLDRAAACETVWLLGGQGsekvapgGAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlvlLSRSGPDAPGAAALLAELEAAG-------ARVTVVACDVADRDALAAVLAAIP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   89 ACFsRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcrgsIINISSIVGKVGNVGQTNYA 168
Cdd:smart00822  77 AVE-GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF-----FVLFSSIAGVLGSPGQANYA 150


                   .
gi 1953284735  169 A 169
Cdd:smart00822 151 A 151
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
49-257 6.53e-14

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 69.26  E-value: 6.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  49 TVWLLGGQGSEKV-----APGGAHTAF-QADVSEAGAVRRLLEQVQAcfsrPPSVVVSCAGLTrdefllrmSEDDWDRVI 122
Cdd:PRK12428    1 TARLLRFLGARVIgvdrrEPGMTLDGFiQADLGDPASIDAAVAALPG----RIDALFNIAGVP--------GTAPVELVA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 123 AVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVGK------------VGNVG---------------QTNYAASKAGVI 175
Cdd:PRK12428   69 RVNFLGLRHLTEALLPRMAPGG---AIVNVASLAGAewpqrlelhkalAATASfdegaawlaahpvalATGYQLSKEALI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 176 GLTQTAARE-LGRHGIRCNSVLPGFITTPM----TQKVPQKVLDKVigMIPMGHLGDPEDVADAVTFLASEDSGYITGAS 250
Cdd:PRK12428  146 LWTMRQAQPwFGARGIRVNCVAPGPVFTPIlgdfRSMLGQERVDSD--AKRMGRPATADEQAAVLVFLCSDAARWINGVN 223


                  ....*..
gi 1953284735 251 VEVTGGL 257
Cdd:PRK12428  224 LPVDGGL 230
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 12-235 1.30e-13

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 67.55  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwlLGGQGSEKVApggahTAFQADVSEAGAVRRLLEQVQacf 91
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGA-------LAGLAAEVGA-----LARPADVAAELEVWALAQELG--- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 srPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAqALVSSGCRGsiINISSIVGKVGNVGQTNYAASK 171
Cdd:cd11730    66 --PLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHAL-ALLAAGARL--VFLGAYPELVMLPGLSAYAAAK 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953284735 172 AGVIGLTQTAARELgrHGIRCNSVLPGFITTPMTQKVpqkvldkviGMIPMGHLgDPEDVADAV 235
Cdd:cd11730   141 AALEAYVEVARKEV--RGLRLTLVRPPAVDTGLWAPP---------GRLPKGAL-SPEDVAAAI 192
PRK07102 PRK07102
SDR family oxidoreductase;
13-235 2.51e-13

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 67.64  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAAACEtvwllggqgSEKVAPGGAHTAFQA-DVSEAGAVRRLLEQVQA 89
Cdd:PRK07102    5 LIIGATSDIARACARRYAAAGARLylAARDVERLERLA---------DDLRARGAVAVSTHElDILDTASHAAFLDSLPA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CfsrpPSVVVSCAGLTRDEfllRMSEDDWD---RVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNvgQTN 166
Cdd:PRK07102   76 L----PDIVLIAVGTLGDQ---AACEADPAlalREFRTNFEGPIALLTLLANRFEARG-SGTIVGISSVAGDRGR--ASN 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953284735 167 Y--AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKvldkviGMIpmghLGDPEDVADAV 235
Cdd:PRK07102  146 YvyGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTAGLKLP------GPL----TAQPEEVAKDI 206
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 13-256 1.88e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 65.43  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGsGIGRAVSVRLAKeGATVAACDLDRAAACETVWLLGGQGSEKvapggahTAFQADVSEAGAVRRLLEQVQACfs 92
Cdd:PRK06940    6 VVIGAG-GIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREAGFDV-------STQEVDVSSRESVKALAATAQTL-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPSVVVSCAGLTRdefllrmSEDDWDRVIAVNLKGIFLVTQAAAQaLVSSGcrGSIINISSIVG--------------- 157
Cdd:PRK06940   75 GPVTGLVHTAGVSP-------SQASPEAILKVDLYGTALVLEEFGK-VIAPG--GAGVVIASQSGhrlpaltaeqerala 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 158 -------------KVGNVGQTNYA--ASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQK---VPQ-KVLDKVIG 218
Cdd:PRK06940  145 ttpteellslpflQPDAIEDSLHAyqIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDelnGPRgDGYRNMFA 224

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1953284735 219 MIPMGHLGDPEDVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK06940  225 KSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 13-255 7.38e-12

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: 63.11  E-value: 7.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAacetvwllggQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAcfs 92
Cdd:cd05334     5 LVYGGRGALGSAVVQAFKSRGWWVASIDLAENE----------EADASIIVLDSDSFTEQAKQVVASVARLSGKVDA--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 rppsvVVSCAG------LTRDEFLlrmseDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrgSIINISSIVGKVGNVGQTN 166
Cdd:cd05334    72 -----LICVAGgwaggsAKSKSFV-----KNWDLMWKQNLWTSFIASHLATKHLLSGG---LLVLTGAKAALEPTPGMIG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAARELG--RHGIRCNSVLPGFITTPMTQK-VPQKVLDKVIgmipmghlgDPEDVADAVTFLASEDS 243
Cdd:cd05334   139 YGAAKAAVHQLTQSLAAENSglPAGSTANAILPVTLDTPANRKaMPDADFSSWT---------PLEFIAELILFWASGAA 209

                         250
                  ....*....|..
gi 1953284735 244 GYITGASVEVTG 255
Cdd:cd05334   210 RPKSGSLIPVVT 221
PRK06101 PRK06101
SDR family oxidoreductase;
13-207 7.46e-12

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 63.35  E-value: 7.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllgGQGSEKVAPggahtaFQADVSEAGAVRRLLEQVQACfs 92
Cdd:PRK06101    5 LITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDEL-----HTQSANIFT------LAFDVTDHPGTKAALSQLPFI-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 rpPSVVVSCAGLTrdEFLlrmseDD-------WDRVIAVNLKGIFLVTQAAaQALVSSGCRgsIINISSIVGKVGNVGQT 165
Cdd:PRK06101   72 --PELWIFNAGDC--EYM-----DDgkvdatlMARVFNVNVLGVANCIEGI-QPHLSCGHR--VVIVGSIASELALPRAE 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQK 207
Cdd:PRK06101  140 AYGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDK 181
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 12-256 1.62e-11

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 62.35  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAG--SGIGRAVSVRLAKEGATVAACDLDRAAAcETVwllggqgsEKVAPG-GAHTAFQADVSEAGAVRRLLEQVQ 88
Cdd:COG0623     8 GLITGVAndRSIAWGIAKALHEEGAELAFTYQGEALK-KRV--------EPLAEElGSALVLPCDVTDDEQIDALFDEIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRV-IAVNLKGIFLVTQA-AAQALVSSGcrGSIINISSivgkvgnvgqtn 166
Cdd:COG0623    79 EKWGKLDFLVHSIAFAPKEELGGRFLDTSREGFlLAMDISAYSLVALAkAAEPLMNEG--GSIVTLTY------------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKA----GVIGLTQTA--------ARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVA 232
Cdd:COG0623   145 LGAERVvpnyNVMGVAKAAleasvrylAADLGPKGIRVNAISAGPIKTLAASGIPgfDKLLDYAEERAPLGRNVTIEEVG 224

                         250       260
                  ....*....|....*....|....
gi 1953284735 233 DAVTFLASEDSGYITGASVEVTGG 256
Cdd:COG0623   225 NAAAFLLSDLASGITGEIIYVDGG 248
PRK08340 PRK08340
SDR family oxidoreductase;
13-257 1.63e-11

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 62.51  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAC-----DLDRAAacetvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQV 87
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKKGARVVISsrneeNLEKAL-------------KELKEYGEVYAVKADLSDKDDLKNLVKEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  88 QACFSRPPSVVVScAGLTRDE--FLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQT 165
Cdd:PRK08340   71 WELLGGIDALVWN-AGNVRCEpcMLHEAGYSDWLEAALLHLVAPGYLTTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDK------------VIGMIPMGHLGDPEDVAD 233
Cdd:PRK08340  150 LADVTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTPGARENLARIAEErgvsfeetwereVLERTPLKRTGRWEELGS 229

                         250       260
                  ....*....|....*....|....
gi 1953284735 234 AVTFLASEDSGYITGASVEVTGGL 257
Cdd:PRK08340  230 LIAFLLSENAEYMLGSTIVFDGAM 253
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
11-242 1.75e-11

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 62.39  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVWLLGGQGSEkvapggaHTAFQADVSEAGAVRRLLEQV--Q 88
Cdd:PRK06924    3 YVIITGTSQGLGEAIANQLLEKGTHVIS--ISRTENKELTKLAEQYNSN-------LTFHSLDLQDVHELETNFNEIlsS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSRPPSV-VVSCAG-LTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK06924   74 IQEDNVSSIhLINNAGmVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRVINISSGAAKNPYFGWSA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 YAASKAGVIGLTQTAA--RELGRHGIRCNSVLPGFITTPMtQKVPQKV-------LDKVIGMIPMGHLGDPEDVADAV-T 236
Cdd:PRK06924  154 YCSSKAGLDMFTQTVAteQEEEEYPVKIVAFSPGVMDTNM-QAQIRSSskedftnLDRFITLKEEGKLLSPEYVAKALrN 232


                  ....*.
gi 1953284735 237 FLASED 242
Cdd:PRK06924  233 LLETED 238
PRK06482 PRK06482
SDR family oxidoreductase;
13-243 2.73e-11

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 62.06  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdldraaaceTVWLLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK06482    6 FITGASSGFGRGMTERLLARGDRVAA----------TVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK06482   76 RI-DVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQG-GGRIVQVSSEGGQIAYPGFSLYHATKW 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 173 GVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHL------------GDPEDVADAVTFLAS 240
Cdd:PRK06482  154 GIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDAYDDTPVGDLrraladgsfaipGDPQKMVQAMIASAD 233


                  ...
gi 1953284735 241 EDS 243
Cdd:PRK06482  234 QTP 236
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 13-200 1.05e-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: 60.86  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGA---TVAACDLDRAAACETVWLLGGQGSEKVAPggahtafQADVSEAGAVRRLLEQVQA 89
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGArhlVLLSRRGPAPRAAARAALLRAGGARVSVV-------RCDVTDPAALAALLAELAA 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 cfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQalvSSGCRgsIINISSIVGKVGNVGQTNYAA 169
Cdd:cd05274   227 --GGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPD---LPLDF--FVLFSSVAALLGGAGQAAYAA 299

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1953284735 170 SKAGVIGLtqtaARELGRHGIRCNSVLPGFI 200
Cdd:cd05274   300 ANAFLDAL----AAQRRRRGLPATSVQWGAW 326
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 13-256 1.34e-10

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 59.56  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATV--------AACDLDRAAacetvwllggqgsekvapgGAhTAFQADVSEAGAVRRLL 84
Cdd:PRK06483    6 LITGAGQRIGLALAWHLLAQGQPVivsyrthyPAIDGLRQA-------------------GA-QCIQADFSTNAGIMAFI 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  85 EQVQacfSRPPSV--VVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCRGS-IINISSIVGKVGN 161
Cdd:PRK06483   66 DELK---QHTDGLraIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHAASdIIHITDYVVEKGS 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 162 VGQTNYAASKAGVIGLTQTAARELGRHgIRCNSVLPGFIttpMTQ-----KVPQKVLDKVIgmipMGHLGDPEDVADAVT 236
Cdd:PRK06483  143 DKHIAYAASKAALDNMTLSFAAKLAPE-VKVNSIAPALI---LFNegddaAYRQKALAKSL----LKIEPGEEEIIDLVD 214

                         250       260
                  ....*....|....*....|
gi 1953284735 237 FLAseDSGYITGASVEVTGG 256
Cdd:PRK06483  215 YLL--TSCYVTGRSLPVDGG 232
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
13-239 2.07e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.61  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAcfs 92
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGA------------ANLAALPGVEFVRGDLRDPEALAAALAGVDA--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 rppsvVVSCAGLTRDefllrmSEDDWDRVIAVNLKGiflvTQAAAQALVSSGCRgSIINISSI--VGKVGNV-------- 162
Cdd:COG0451    68 -----VVHLAAPAGV------GEEDPDETLEVNVEG----TLNLLEAARAAGVK-RFVYASSSsvYGDGEGPidedtplr 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 163 GQTNYAASKAGVIGLTQTAARelgRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLGDP---------EDVAD 233
Cdd:COG0451   132 PVSPYGASKLAAELLARAYAR---RYGLPVTILRPGNVYGPGDRGVLPRLIRRALAGEPVPVFGDGdqrrdfihvDDVAR 208


                  ....*.
gi 1953284735 234 AVTFLA 239
Cdd:COG0451   209 AIVLAL 214
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 13-240 2.61e-10

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 59.00  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDlDRAAACETVwllggqgseKVAPGGAHTAFQADVSEAGAVRRLLEQVQACFs 92
Cdd:PRK10538    4 LVTGATAGFGECITRRFIQQGHKVIATG-RRQERLQEL---------KDELGDNLYIAQLDVRNRAAIEEMLASLPAEW- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPSVVVSCAGLTRD-EFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK10538   73 RNIDVLVNNAGLALGlEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERN-HGHIINIGSTAGSWPYAGGNVYGATK 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMGHLG-DPEDVADAVTFLAS 240
Cdd:PRK10538  152 AFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVAlTPEDVSEAVWWVAT 221
PRK05693 PRK05693
SDR family oxidoreductase;
12-211 3.44e-10

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 59.03  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACdldrAAACETVWLLGGQGsekvapggaHTAFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05693    4 VLITGCSSGIGRALADAFKAAGYEVWAT----ARKAEDVEALAAAG---------FTAVQLDVNDGAALARLAEELEAEH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSgcRGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK05693   71 GGL-DVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRS--RGLVVNIGSVSGVLVTPFAGAYCASK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQK 211
Cdd:PRK05693  148 AAVHALSDALRLELAPFGVQVMEVQPGAIASQFASNASRE 187
PRK05866 PRK05866
SDR family oxidoreductase;
3-204 5.65e-10

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 58.60  E-value: 5.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   3 SPLRLRSALALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAAcetvwLLGGQGSEKVAPGGAHTAFQADVSEAGAVRR 82
Cdd:PRK05866   34 QPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVA--VARRED-----LLDAVADRITRAGGDAMAVPCDLSDLDAVDA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  83 LLEQVQACFSrPPSVVVSCAGLTRDEFLLRmSEDDW---DRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKV 159
Cdd:PRK05866  107 LVADVEKRIG-GVDILINNAGRSIRRPLAE-SLDRWhdvERTMVLNYYAPLRLIRGLAPGMLERG-DGHIINVATWGVLS 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953284735 160 GNVGQ-TNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM 204
Cdd:PRK05866  184 EASPLfSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 13-198 1.28e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 57.23  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggQGSEKVAPGGAHtAFQADVSEAGAVRRLLEQVQACFS 92
Cdd:PRK06180    8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAAR---------ADFEALHPDRAL-ARLLDVTDFDAIDAVVADAEATFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 rPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAASKA 172
Cdd:PRK06180   78 -PIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARR-RGHIVNITSMGGLITMPGIGYYCGSKF 155

                         170       180
                  ....*....|....*....|....*.
gi 1953284735 173 GVIGLTQTAARELGRHGIRCNSVLPG 198
Cdd:PRK06180  156 ALEGISESLAKEVAPFGIHVTAVEPG 181
PRK06182 PRK06182
short chain dehydrogenase; Validated
 8-203 1.38e-09

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 57.28  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   8 RSALALVTGAGSGIGRAVSVRLAKEGATV--AACDLDRAaacetvwllggqgsEKVAPGGAHtAFQADVSEAGAVRRLLE 85
Cdd:PRK06182    2 QKKVALVTGASSGIGKATARRLAAQGYTVygAARRVDKM--------------EDLASLGVH-PLSLDVTDEASIKAAVD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRpPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQT 165
Cdd:PRK06182   67 TIIAEEGR-IDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQR-SGRIINISSMGGKIYTPLGA 144

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953284735 166 NYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTP 203
Cdd:PRK06182  145 WYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
PRK09291 PRK09291
SDR family oxidoreductase;
13-221 2.76e-09

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 56.16  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdldraaacetvwllGGQGSEKVapggahTAFQADVSEAGAVRRLLE------- 85
Cdd:PRK09291    6 LITGAGSGFGREVALRLARKGHNVIA---------------GVQIAPQV------TALRAEAARRGLALRVEKldltdai 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQACFSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVG--KVGNVG 163
Cdd:PRK09291   65 DRAQAAEWDVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARG-KGKVVFTSSMAGliTGPFTG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 164 QtnYAASKAGVIGLTQTAARELGRHGIRCNSVLPGF----------------------------ITTPMTQKVPQKVLDK 215
Cdd:PRK09291  144 A--YCASKHALEAIAEAMHAELKPFGIQVATVNPGPyltgfndtmaetpkrwydparnftdpedLAFPLEQFDPQEMIDA 221


                  ....*.
gi 1953284735 216 VIGMIP 221
Cdd:PRK09291  222 MVEVIP 227
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 13-208 4.90e-09

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: 55.54  E-value: 4.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGAT---VAACDLDRAAACETVWLLGGqgsekvAPGGAHTAFQADVSEAGAVRRLLEQVQa 89
Cdd:cd09806     4 LITGCSSGIGLHLAVRLASDPSKrfkVYATMRDLKKKGRLWEAAGA------LAGGTLETLQLDVCDSKSVAAAVERVT- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 cfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNYAA 169
Cdd:cd09806    77 --ERHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRG-SGRILVTSSVGGLQGLPFNDVYCA 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKV 208
Cdd:cd09806   154 SKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKV 192
PRK08251 PRK08251
SDR family oxidoreductase;
13-210 8.98e-09

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 54.56  E-value: 8.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAACETVwLLGGQGSEKVApggahtAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK08251    6 LITGASSGLGAGMAREFAAKGRDLALCarRTDRLEELKAE-LLARYPGIKVA------VAALDVNDHDQVFEVFAEFRDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPPSVVVScAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVG-QTNYAA 169
Cdd:PRK08251   79 LGGLDRVIVN-AGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQG-SGHLVLISSVSAVRGLPGvKAAYAA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ 210
Cdd:PRK08251  157 SKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAKS 197
PRK08017 PRK08017
SDR family oxidoreductase;
13-215 1.53e-08

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 53.94  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATV-AACDldRAAACETVWLLGGQGSEkvapggahtafqADVSEAGAVRRLLEQVQACF 91
Cdd:PRK08017    6 LITGCSSGIGLEAALELKRRGYRVlAACR--KPDDVARMNSLGFTGIL------------LDLDDPESVERAADEVIALT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGCrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK08017   72 DNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGE-GRIVMTSSVMGLISTPGRGAYAASK 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953284735 172 AGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDK 215
Cdd:PRK08017  151 YALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNVNQTQSDK 194
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 12-257 1.57e-08

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 53.74  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGS--GIGRAVSVRLAKEGATVAacdldraaacetvwlLGGQG---SEKVAP-----GGAHTAFQADVSEAGAVR 81
Cdd:cd05372     4 ILITGIANdrSIAWGIAKALHEAGAELA---------------FTYQPealRKRVEKlaerlGESALVLPCDVSNDEEIK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  82 RLLEQVQACFSRPPSVVVSCAGLTRDEF---LLRMSEDDWDrvIAVNLKGIFLVTQA-AAQALVSSGcrGSIINISSIVG 157
Cdd:cd05372    69 ELFAEVKKDWGKLDGLVHSIAFAPKVQLkgpFLDTSRKGFL--KALDISAYSLVSLAkAALPIMNPG--GSIVTLSYLGS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 158 KVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAV 235
Cdd:cd05372   145 ERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITgfDKMLEYSEQRAPLGRNVTAEEVGNTA 224

                         250       260
                  ....*....|....*....|..
gi 1953284735 236 TFLASEDSGYITGASVEVTGGL 257
Cdd:cd05372   225 AFLLSDLSSGITGEIIYVDGGY 246
PRK06139 PRK06139
SDR family oxidoreductase;
6-239 2.65e-08

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 53.57  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   6 RLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLE 85
Cdd:PRK06139    4 PLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVA-------EECRALGAEVLVVPTDVTDADQVKALAT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  86 QVQAcFSRPPSVVVSCAGL----TRDEFLLRMSEddwdRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGN 161
Cdd:PRK06139   77 QAAS-FGGRIDVWVNNVGVgavgRFEETPIEAHE----QVIQTNLIGYMRDAHAALPIFKKQG-HGIFINMISLGGFAAQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284735 162 VGQTNYAASKAGVIGLTQTAARELGRH-GIRCNSVLPGFITTPMTQKVPQKVLDKVIGMIPMghlGDPEDVADAVTFLA 239
Cdd:PRK06139  151 PYAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTPGFRHGANYTGRRLTPPPPV---YDPRRVAKAVVRLA 226
PRK08278 PRK08278
SDR family oxidoreductase;
12-248 4.81e-08

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 52.60  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAC--------DLD----RAAAcetvwllggqgsEKVAPGGAHTAFQADVSEAGA 79
Cdd:PRK08278    9 LFITGASRGIGLAIALRAARDGANIVIAaktaephpKLPgtihTAAE------------EIEAAGGQALPLVGDVRDEDQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  80 VRRLLEQVQACFSRPpSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVgkv 159
Cdd:PRK08278   77 VAAAVAKAVERFGGI-DICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSE-NPHILTLSPPL--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 160 gNV------GQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLP-GFITTPMTQKVPQkvldkviGMIPMGHLGDPEDVA 232
Cdd:PRK08278  152 -NLdpkwfaPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrTTIATAAVRNLLG-------GDEAMRRSRTPEIMA 223

                         250
                  ....*....|....*.
gi 1953284735 233 DAVTFLASEDSGYITG 248
Cdd:PRK08278  224 DAAYEILSRPAREFTG 239
PRK08703 PRK08703
SDR family oxidoreductase;
13-203 6.19e-08

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 51.86  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAA-ACETVWllggqgSEKVAPGGAH-TAFQADVSEAG--AVRRLLEQVQ 88
Cdd:PRK08703   10 LVTGASQGLGEQVAKAYAAAGATVIL--VARHQkKLEKVY------DAIVEAGHPEpFAIRFDLMSAEekEFEQFAATIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSRPPSVVVSCAGLTRDEFLLRMSE-DDWDRVIAVNLKGIFLVTQAAAQALVSSGcRGSIINISSIVGKVGNVGQTNY 167
Cdd:PRK08703   82 EATQGKLDGIVHCAGYFYALSPLDFQTvAEWVNQYRINTVAPMGLTRALFPLLKQSP-DASVIFVGESHGETPKAYWGGF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1953284735 168 AASKAGVIGLTQTAARELGRHG-IRCNSVLPGFITTP 203
Cdd:PRK08703  161 GASKAALNYLCKVAADEWERFGnLRANVLVPGPINSP 197
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 13-202 1.82e-07

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: 50.93  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATV-AAC-DLDRA--AACEtvwLLGGQGSEKVapggahTAFQADVSEAGAVRRLLEQVQ 88
Cdd:cd09807     5 IITGANTGIGKETARELARRGARViMACrDMAKCeeAAAE---IRRDTLNHEV------IVRHLDLASLKSIRAFAAEFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 ACFSRpPSVVVSCAGLTRDEFLLrmSEDDWDRVIAVNLKGIFLVTQAAAQAL-VSSGCRgsIINISSIVGKVGNVG---- 163
Cdd:cd09807    76 AEEDR-LDVLINNAGVMRCPYSK--TEDGFEMQFGVNHLGHFLLTNLLLDLLkKSAPSR--IVNVSSLAHKAGKINfddl 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953284735 164 --------QTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITT 202
Cdd:cd09807   151 nseksyntGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 13-204 4.76e-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: 49.41  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVA--ACDLDRAAAcetvwllggqgSEKVAPGGAHtAFQADVSEAGAVRRLLEQVQAc 90
Cdd:cd08951    11 FITGSSDGLGLAAARTLLHQGHEVVlhARSQKRAAD-----------AKAACPGAAG-VLIGDLSSLAETRKLADQVNA- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPPSVVVScAGLTRDEFLLRMSEDDwDRVIAVNLKGIF----LVTQAAAQALVSSGC-RGSIINISSIV-GKVGNVGQ 164
Cdd:cd08951    78 IGRFDAVIHN-AGILSGPNRKTPDTGI-PAMVAVNVLAPYvltaLIRRPKRLIYLSSGMhRGGNASLDDIDwFNRGENDS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953284735 165 TNYAASKAGVIGLTQTAARELGRhgIRCNSVLPGFITTPM 204
Cdd:cd08951   156 PAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKM 193
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 12-241 7.81e-07

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: 49.21  E-value: 7.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAAceTVWLLGGQGSEKVapggahtafQADVSEAGAVRRLLEQVQAcf 91
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRA--LVRSGS--DAVLLDGLPVEVV---------EGDLTDAASLAAAMKGCDR-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 srppsvVVSCAGLTrdefllRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcrgSIINISSI-VGKVGNVGQTN---- 166
Cdd:cd05228    66 ------VFHLAAFT------SLWAKDRKELYRTNVEGTRNVLDAALEAGVR-----RVVHTSSIaALGGPPDGRIDettp 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 ---------YAASKAgvigLTQTAARELGRHGIRCNSVLPGFI-------TTPMTQKVPQKVLDKVIGMIPMG-HLGDPE 229
Cdd:cd05228   129 wnerpfpndYYRSKL----LAELEVLEAAAEGLDVVIVNPSAVfgpgdegPTSTGLDVLDYLNGKLPAYPPGGtSFVDVR 204

                         250
                  ....*....|..
gi 1953284735 230 DVADAVTfLASE 241
Cdd:cd05228   205 DVAEGHI-AAME 215
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 13-204 1.04e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 47.89  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEgatvaacdldraaacetvwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLLEQVqacfs 92
Cdd:PRK07578    4 LVIGASGTIGRAVVAELSKR-------------------------HEVITAGRSSGDVQVDITDPASIRALFEKV----- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  93 RPPSVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKG-IFLVTqaAAQALVSSGcrGSIINISSIVGKVGNVGQTNYAASK 171
Cdd:PRK07578   54 GKVDAVVSAAGKVHFAPLAEMTDEDFNVGLQSKLMGqVNLVL--IGQHYLNDG--GSFTLTSGILSDEPIPGGASAATVN 129

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1953284735 172 AGVIGLTQTAARELGRhGIRCNSVLPGFITTPM 204
Cdd:PRK07578  130 GALEGFVKAAALELPR-GIRINVVSPTVLTESL 161
PRK06196 PRK06196
oxidoreductase; Provisional
 7-210 1.60e-06

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 48.14  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwLLGGQGSEKVApggahtafqADVSEAGAVRRLLEQ 86
Cdd:PRK06196   24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREA--LAGIDGVEVVM---------LDLADLESVRAFAER 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  87 VQACfSRPPSVVVSCAG-----LTRDefllrmsEDDWDRVIAVNLKGIF---------LVTQAAAQ--ALVSSGCRGSII 150
Cdd:PRK06196   93 FLDS-GRRIDILINNAGvmacpETRV-------GDGWEAQFATNHLGHFalvnllwpaLAAGAGARvvALSSAGHRRSPI 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953284735 151 NISSIVGKVGNVGQTNYAASKAG----VIGLTQtaareLGR-HGIRCNSVLPGFITTPMTQKVPQ 210
Cdd:PRK06196  165 RWDDPHFTRGYDKWLAYGQSKTAnalfAVHLDK-----LGKdQGVRAFSVHPGGILTPLQRHLPR 224
PRK06720 PRK06720
hypothetical protein; Provisional
 5-125 2.47e-06

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 46.50  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   5 LRLRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqgSEKVAPGGAHTAFQADVSEAGAVRRLL 84
Cdd:PRK06720   12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATV-------EEITNLGGEALFVSYDMEKQGDWQRVI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953284735  85 EQVQACFSRpPSVVVSCAGLTR-DEFLLRMSEDDwDRVIAVN 125
Cdd:PRK06720   85 SITLNAFSR-IDMLFQNAGLYKiDSIFSRQQEND-SNVLCIN 124
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
171-257 2.67e-06

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 47.24  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVPQ--KVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITG 248
Cdd:PRK07533  166 KAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDfdALLEDAAERAPLRRLVDIDDVGAVAAFLASDAARRLTG 245


                  ....*....
gi 1953284735 249 ASVEVTGGL 257
Cdd:PRK07533  246 NTLYIDGGY 254
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 13-154 5.28e-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: 46.47  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAAcetvwllggqgsekvapggahtaFQADVSEAGAVRRLLEQVQacfs 92
Cdd:cd05254     3 LITGATGMLGRALVRLLKERGYEVIGTGRSRASL-----------------------FKLDLTDPDAVEEAIRDYK---- 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284735  93 rpPSVVVSCAGLTR-DEfllrmSEDDWDRVIAVNLKGIFLVTQAAAQAlvssGCRgsIINISS 154
Cdd:cd05254    56 --PDVIINCAAYTRvDK-----CESDPELAYRVNVLAPENLARAAKEV----GAR--LIHIST 105
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 13-177 1.23e-05

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: 45.74  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATvaacdldraaaceTVWLLGGQG---------SEKVAPGGAHTAFQADVSEAGAVRRL 83
Cdd:cd08955   153 LITGGLGGLGLLVAEWLVERGAR-------------HLVLTGRRApsaaarqaiAALEEAGAEVVVLAADVSDRDALAAA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  84 LEQVQAcfSRPP-SVVVSCAGLTRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSsgcrgSIINISSIVGKVGNV 162
Cdd:cd08955   220 LAQIRA--SLPPlRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLD-----FFVLFSSVASLLGSP 292

                         170
                  ....*....|....*
gi 1953284735 163 GQTNYAASKAGVIGL 177
Cdd:cd08955   293 GQANYAAANAFLDAL 307
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 12-172 1.73e-05

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: 45.62  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGAtvaacdldraaacETVWLLGGQGSEkvAPG-----------GAHTAFQA-DVSEAGA 79
Cdd:cd08952   233 VLVTGGTGALGAHVARWLARRGA-------------EHLVLTSRRGPD--APGaaelvaeltalGARVTVAAcDVADRDA 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  80 VRRLLEQVQAcfSRPPSVVVSCAGLTRDEFLLRMSEDDWDRVI------AVNLKGifLVTQAAAQALVSsgcrgsiinIS 153
Cdd:cd08952   298 LAALLAALPA--GHPLTAVVHAAGVLDDGPLDDLTPERLAEVLrakvagARHLDE--LTRDRDLDAFVL---------FS 364

                         170
                  ....*....|....*....
gi 1953284735 154 SIVGKVGNVGQTNYAASKA 172
Cdd:cd08952   365 SIAGVWGSGGQGAYAAANA 383
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 12-239 2.48e-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: 44.21  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAAcdLDRAAACETVWLLGGQgsekvapggahTAFQADVSEAGAVRRLLEQVQacf 91
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIG--LDRLTSASNTARLADL-----------RFVEGDLTDRDALEKLLADVR--- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 srpPSVVVSCAGLTrdefLLRMSEDDWDRVIAVNLKGiflvTQAAAQALVSSGCRgSIINISS--IVGKVGNVGQTN--- 166
Cdd:pfam01370  65 ---PDAVIHLAAVG----GVGASIEDPEDFIEANVLG----TLNLLEAARKAGVK-RFLFASSseVYGDGAEIPQEEttl 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 167 ---------YAASKAGVIGLTQTAARELGRHGI--R-CNSVLPGFITTPMTQKVPQKVLDKVIGM-IPMGHLGDP----- 228
Cdd:pfam01370 133 tgplapnspYAAAKLAGEWLVLAYAAAYGLRAVilRlFNVYGPGDNEGFVSRVIPALIRRILEGKpILLWGDGTQrrdfl 212

                         250
                  ....*....|...
gi 1953284735 229 --EDVADAVTFLA 239
Cdd:pfam01370 213 yvDDVARAILLAL 225
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
13-139 6.82e-05

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 43.20  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDraaacetvwllggqgsekvapggahtafQADVSEAGAVRRLLEQVQacfs 92
Cdd:COG1091     3 LVTGANGQLGRALVRLLAERGYEVVALDRS----------------------------ELDITDPEAVAALLEEVR---- 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284735  93 rpPSVVVSCAGLTR-DEfllrmSEDDWDRVIAVNLKGIFLVTQAAAQA 139
Cdd:COG1091    51 --PDVVINAAAYTAvDK-----AESEPELAYAVNATGPANLAEACAEL 91
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
105-256 7.50e-05

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 42.79  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 105 TRDEFLLrmseddwdrviAVNLKGIFLVTQA-AAQALVSSGcrGSIINISSIVGKVG----NVGQTNYAASKAGVIGLtq 179
Cdd:PRK08594  111 SRDGFLL-----------AQNISAYSLTAVArEAKKLMTEG--GSIVTLTYLGGERVvqnyNVMGVAKASLEASVKYL-- 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284735 180 taARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK08594  176 --ANDLGKDGIRVNAISAGPIRTLSAKGVGgfNSILKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSG 252
PRK07806 PRK07806
SDR family oxidoreductase;
7-103 7.80e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 42.78  E-value: 7.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   7 LRSALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVwllggqGSEKVAPGGAHTAFQADVSEAGAVRRLLEQ 86
Cdd:PRK07806    4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKV------VAEIEAAGGRASAVGADLTDEESVAALMDT 77

                          90
                  ....*....|....*..
gi 1953284735  87 VQACFSRPPSVVVSCAG 103
Cdd:PRK07806   78 AREEFGGLDALVLNASG 94
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 4-204 1.16e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 42.68  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   4 PLRLRSALALVTGAGSGIGRAVSVRLAKEGATV---------AACDLDRAAACEtvwllggQGSEKV-APGGAHTAFQAD 73
Cdd:PRK08303    3 MKPLRGKVALVAGATRGAGRGIAVELGAAGATVyvtgrstraRRSEYDRPETIE-------ETAELVtAAGGRGIAVQVD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  74 VSEAGAVRRLLEQVQACFSRPPSVVVSCAGltrDEFLLRMSEDDWDRVIAVNLK----GIF--LVTQAAAQALVSSGCRG 147
Cdd:PRK08303   76 HLVPEQVRALVERIDREQGRLDILVNDIWG---GEKLFEWGKPVWEHSLDKGLRmlrlAIDthLITSHFALPLLIRRPGG 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953284735 148 SIINISSivgKVGNVGQTNYAAS------KAGVIGLTQTAARELGRHGIRCNSVLPGFITTPM 204
Cdd:PRK08303  153 LVVEITD---GTAEYNATHYRLSvfydlaKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEM 212
PRK07023 PRK07023
SDR family oxidoreductase;
11-244 1.90e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 41.54  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqgsekvAPGGAHTAFQADVSEAGAVRRLLEQ-VQA 89
Cdd:PRK07023    3 RAIVTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSLAA------------AAGERLAEVELDLSDAAAAAAWLAGdLLA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  90 CFSRPPSVVV------------SCAGLTRDEFLlrmseddwdRVIAVNLKGIFLVTQAAAQAlVSSGCRGSIINISSIVG 157
Cdd:PRK07023   71 AFVDGASRVLlinnagtvepigPLATLDAAAIA---------RAVGLNVAAPLMLTAALAQA-ASDAAERRILHISSGAA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 158 KVGNVGQTNYAASKAGVIGLTQTAARElGRHGIRCNSVLPGFITTPM--------TQKVPQkvLDKVIGMIPMGHLGDPE 229
Cdd:PRK07023  141 RNAYAGWSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGMqatiratdEERFPM--RERFRELKASGALSTPE 217

                         250
                  ....*....|....*.
gi 1953284735 230 DVA-DAVTFLASEDSG 244
Cdd:PRK07023  218 DAArRLIAYLLSDDFG 233
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 12-198 2.07e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 41.81  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  12 ALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLLGGQGSEkvapggAHTAFQA-DVSEAGAVRRLLEQVQAC 90
Cdd:cd09809     4 IIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHK------ARVEAMTlDLASLRSVQRFAEAFKAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSrPPSVVVSCAGLTRDEFllRMSEDDWDRVIAVNLKGIFLVTQaAAQALVSSGCRGSIINISS-------IVGKVGNVG 163
Cdd:cd09809    78 NS-PLHVLVCNAAVFALPW--TLTEDGLETTFQVNHLGHFYLVQ-LLEDVLRRSAPARVIVVSSeshrftdLPDSCGNLD 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953284735 164 -------QTNYAA------SKAGVIGLTQTAARELGRHGIRCNSVLPG 198
Cdd:cd09809   154 fsllsppKKKYWSmlaynrAKLCNILFSNELHRRLSPRGITSNSLHPG 201
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 13-255 2.26e-04

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: 41.37  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAAC--DLDRAAAcetvwllggqgsekVAPGGAHTAfQADVSEAGAVRRLLEQVQAc 90
Cdd:COG0702     3 LVTGATGFIGRRVVRALLARGHPVRALvrDPEKAAA--------------LAAAGVEVV-QGDLDDPESLAAALAGVDA- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 fsrppsvVVSCAGltrdeflLRMSEDDWDRVIAvnlkgiflvTQAAAQALVSSGCRgSIINISSIVgkVGNVGQTNYAAS 170
Cdd:COG0702    67 -------VFLLVP-------SGPGGDFAVDVEG---------ARNLADAAKAAGVK-RIVYLSALG--ADRDSPSPYLRA 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 171 KAGVigltqtaARELGRHGIRCNSVLPGFITTPMTQKVPQKVLDKVIgMIPMGHLG----DPEDVADAVTFLASEDSGYi 246
Cdd:COG0702   121 KAAV-------EEALRASGLPYTILRPGWFMGNLLGFFERLRERGVL-PLPAGDGRvqpiAVRDVAEAAAAALTDPGHA- 191


                  ....*....
gi 1953284735 247 tGASVEVTG 255
Cdd:COG0702   192 -GRTYELGG 199
PRK07984 PRK07984
enoyl-ACP reductase FabI;
13-257 2.34e-04

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 41.43  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGS--GIGRAVSVRLAKEGATVAACDLDRAaacetvwlLGGQGSEKVAPGGAHTAFQADVSEAGAVRRLLEQVQAC 90
Cdd:PRK07984   10 LVTGVASklSIAYGIAQAMHREGAELAFTYQNDK--------LKGRVEEFAAQLGSDIVLPCDVAEDASIDAMFAELGKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRPPSVVVSCAGLTRDEFllrmsedDWDRVIAVNLKGIFLVTQAAAQALVS--SGCRgSIINISSIVGKVGNVGQT--- 165
Cdd:PRK07984   82 WPKFDGFVHSIGFAPGDQL-------DGDYVNAVTREGFKIAHDISSYSFVAmaKACR-SMLNPGSALLTLSYLGAErai 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 166 -NY---AASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMGHLGDPEDVADAVTFLA 239
Cdd:PRK07984  154 pNYnvmGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKdfRKMLAHCEAVTPIRRTVTIEDVGNSAAFLC 233

                         250
                  ....*....|....*...
gi 1953284735 240 SEDSGYITGASVEVTGGL 257
Cdd:PRK07984  234 SDLSAGISGEVVHVDGGF 251
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 13-239 5.53e-04

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: 40.27  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETvwllggqGSEKVAPGGAHTAFQ--ADVSEAGAVRRLLEQVQAC 90
Cdd:cd09808     5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEA-------RKEIETESGNQNIFLhiVDMSDPKQVWEFVEEFKEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  91 FSRpPSVVVSCAGLTRDEflLRMSEDDWDRVIAVNLKGIFLVTQAAAQAL----------VSSGcrGSII---NISSIVG 157
Cdd:cd09808    78 GKK-LHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLekeedprvitVSSG--GMLVqklNTNNLQS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 158 KVGNV-GQTNYAASKAGVIGLTQTAARelGRHGIRCNSVLPGFITTP-MTQKVP---QKVLDKvigmipmghLGDPEDVA 232
Cdd:cd09808   153 ERTAFdGTMVYAQNKRQQVIMTEQWAK--KHPEIHFSVMHPGWADTPaVRNSMPdfhARFKDR---------LRSEEQGA 221


                  ....*..
gi 1953284735 233 DAVTFLA 239
Cdd:cd09808   222 DTVVWLA 228
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
135-256 1.77e-03

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 38.80  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 135 AAAQALVSSGCRGSIINISSIvGKVGNVGQTNYAA-SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QK 211
Cdd:PRK08690  128 AKAARPMMRGRNSAIVALSYL-GAVRAIPNYNVMGmAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIAdfGK 206

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1953284735 212 VLDKVIGMIPMGHLGDPEDVADAVTFLASEDSGYITGASVEVTGG 256
Cdd:PRK08690  207 LLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGG 251
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 11-93 2.52e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 38.47  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  11 LALVTGAGSGIGRAVSVRLAKEGATV--AACDLDR-AAACETVwllggqgsEKVAPGGAHTAFQADVSEAGAVRRLLEQV 87
Cdd:PRK06197   18 VAVVTGANTGLGYETAAALAAKGAHVvlAVRNLDKgKAAAARI--------TAATPGADVTLQELDLTSLASVRAAADAL 89


                  ....*.
gi 1953284735  88 QACFSR 93
Cdd:PRK06197   90 RAAYPR 95
PRK06953 PRK06953
SDR family oxidoreductase;
9-219 4.00e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 37.74  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735   9 SALALVTGAGSGIGRAVSVRLAKEGATVAACDLDRAAACETVWLlggqgsekvapgGAHtAFQADVSEAGAVRRLLEQVQ 88
Cdd:PRK06953    1 MKTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQAL------------GAE-ALALDVADPASVAGLAWKLD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  89 AcfsRPPSVVVSCAGL--TRDEFLLRMSEDDWDRVIAVNLKGIFLVTQAAAQALVSSGcrGSIINISSIVGKVGNVGQTN 166
Cdd:PRK06953   68 G---EALDAAVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAG--GVLAVLSSRMGSIGDATGTT 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953284735 167 ---YAASKAGVIGLTQTAARElGRHGIrCNSVLPGFITTPM-TQKVPQKVLDKVIGM 219
Cdd:PRK06953  143 gwlYRASKAALNDALRAASLQ-ARHAT-CIALHPGWVRTDMgGAQAALDPAQSVAGM 197
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
170-259 4.26e-03

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 37.61  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735 170 SKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQKVP--QKVLDKVIGMIPMG-HLGDPEDVADAVTFLASEDSGYI 246
Cdd:PRK07889  161 AKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAIPgfELLEEGWDERAPLGwDVKDPTPVARAVVALLSDWFPAT 240

                          90
                  ....*....|...
gi 1953284735 247 TGASVEVTGGLYM 259
Cdd:PRK07889  241 TGEIVHVDGGAHA 253
PRK05599 PRK05599
SDR family oxidoreductase;
13-235 6.91e-03

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 37.17  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  13 LVTGAGSGIGRAVSVRLAkegatvaaCDLDRAAACETVWLLGGQGSEKVAPGGAHT-AFQADVSEAGAVRRLLEQVQACF 91
Cdd:PRK05599    4 LILGGTSDIAGEIATLLC--------HGEDVVLAARRPEAAQGLASDLRQRGATSVhVLSFDAQDLDTHRELVKQTQELA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953284735  92 SRPPSVVVScAGLTRDEfllrmSEDDWDRVIAVNLKGIFLVTQAA-----AQALVSSGCRGSIINISSIVGKVGNVGQTN 166
Cdd:PRK05599   76 GEISLAVVA-FGILGDQ-----ERAETDEAHAVEIATVDYTAQVSmltvlADELRAQTAPAAIVAFSSIAGWRARRANYV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953284735 167 YAASKAGVIGLTQTAARELGRHGIRCNSVLPGFITTPMTQkvpqkvldkviGMIPMGHLGDPEDVADAV 235
Cdd:PRK05599  150 YGSTKAGLDAFCQGLADSLHGSHVRLIIARPGFVIGSMTT-----------GMKPAPMSVYPRDVAAAV 207
 
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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