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Conserved domains on  [gi|1447699393|ref|NP_309312|]
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3-oxoacyl-[acyl-carrier protein] reductase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

SDR family NAD(P)-dependent oxidoreductase( domain architecture ID 11437015)

SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to Bacillus subtilis NADPH-dependent reductase BacG, which is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0070403|GO:0016491
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
7-252 2.93e-90

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: 266.65  E-value: 2.93e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAE-ALEAAAAELRAaGGRALAVAADVTDEAAVEALVAAAVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:COG1028    81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA--VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:COG1028   161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAeeVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQV 240

                  ....*....
gi 1447699393 244 IVIDGGLVM 252
Cdd:COG1028   241 LAVDGGLTA 249
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
7-252 2.93e-90

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: 266.65  E-value: 2.93e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAE-ALEAAAAELRAaGGRALAVAADVTDEAAVEALVAAAVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:COG1028    81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA--VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:COG1028   161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAeeVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQV 240

                  ....*....
gi 1447699393 244 IVIDGGLVM 252
Cdd:COG1028   241 LAVDGGLTA 249
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
8-252 9.26e-90

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 265.49  E-value: 9.26e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKV-VIYDSNEEAAEALAAELRAaGGEARVLVFDVSDEAAVRALIEAAVEAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK05653   81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK05653  161 VIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPV 240

                  ....*.
gi 1447699393 247 DGGLVM 252
Cdd:PRK05653  241 NGGMYM 246
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
12-251 1.04e-87

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: 260.17  E-value: 1.04e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:cd05333    81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGLV 251
Cdd:cd05333   161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
14-251 2.08e-77

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: 234.03  E-value: 2.08e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQAGKIDVL 92
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKAlGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTR 172
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 173 TLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGLV 251
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
18-250 3.19e-65

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: 202.66  E-value: 3.19e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  18 GASGD--IGLGICEKYLEQNCDVYALYKSNDV--QLTALKASHPAgdklHIVQCDLACPQSVSALCEQIERQAGKIDVLV 93
Cdd:pfam13561   1 GAANEsgIGWAIARALAEEGAEVVLTDLNEALakRVEELAEELGA----AVLPCDVTDEEQVEALVAAAVEKFGRLDILV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIV--KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:pfam13561  77 NNAGFApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMK--EGGSIVNLSSIGAERVVPNYNAYGAAKAALEALT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:pfam13561 155 RYLAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGG 234

                  .
gi 1447699393 250 L 250
Cdd:pfam13561 235 Y 235
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
12-162 3.25e-15

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 71.36  E-value: 3.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   12 KTVLVTGASGDIGLGICEkYLEQNCDVYaLY------KSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:smart00822   1 GTYLITGGLGGLGRALAR-WLAERGARR-LVllsrsgPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSifrltkdALMLLRAAENP---AIINVASIAALIPSVGQANYSA 162
Cdd:smart00822  79 EGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAG-------AWNLHELTADLpldFFVLFSSIAGVLGSPGQANYAA 151
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
7-252 2.93e-90

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: 266.65  E-value: 2.93e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAE-ALEAAAAELRAaGGRALAVAADVTDEAAVEALVAAAVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:COG1028    81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA--VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:COG1028   161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAeeVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQV 240

                  ....*....
gi 1447699393 244 IVIDGGLVM 252
Cdd:COG1028   241 LAVDGGLTA 249
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
8-252 9.26e-90

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 265.49  E-value: 9.26e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKV-VIYDSNEEAAEALAAELRAaGGEARVLVFDVSDEAAVRALIEAAVEAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK05653   81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK05653  161 VIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPV 240

                  ....*.
gi 1447699393 247 DGGLVM 252
Cdd:PRK05653  241 NGGMYM 246
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
12-251 1.04e-87

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: 260.17  E-value: 1.04e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:cd05333    81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGLV 251
Cdd:cd05333   161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
8-253 3.75e-85

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 253.96  E-value: 3.75e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK05557    2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGAlGGKALAVQGDVSDAESVERAVDEAKAEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK05557   82 GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK05557  162 VIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHV 241

                  ....*..
gi 1447699393 247 DGGLVMR 253
Cdd:PRK05557  242 NGGMVMG 248
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
14-251 2.08e-77

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: 234.03  E-value: 2.08e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQAGKIDVL 92
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKAlGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTR 172
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 173 TLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGLV 251
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
14-247 1.64e-76

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: 231.40  E-value: 1.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVLV 93
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEE-ALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTRT 173
Cdd:cd05233    80 NNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699393 174 LAAEMAPWGVRVNAVAPGMIESKMVKKVSR-AVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVID 247
Cdd:cd05233   160 LALELAPYGIRVNAVAPGLVDTPMLAKLGPeEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-252 2.50e-73

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 223.98  E-value: 2.50e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK12825    3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEAlGRRAQAVQADVTDKAALEAAVAAAVERF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK12825   83 GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK12825  163 LVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEV 242

                  ....*.
gi 1447699393 247 DGGLVM 252
Cdd:PRK12825  243 TGGVDV 248
PRK12826 PRK12826
SDR family oxidoreductase;
8-252 9.34e-72

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 219.79  E-value: 9.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK12826    3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALI-PSVGQANYSASKGA 166
Cdd:PRK12826   83 RLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAASKAG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIV 245
Cdd:PRK12826  163 LVGFTRALALELAARNITVNSVHPGGVDTPMAGNLgDAQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLP 242

                  ....*..
gi 1447699393 246 IDGGLVM 252
Cdd:PRK12826  243 VDGGATL 249
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-249 5.32e-69

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 212.78  E-value: 5.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK05565    2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEiKEEGGDAIAVKADVSSEEDVENLVEQIVEKF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK05565   82 GKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK05565  162 VNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITV 241

                  ...
gi 1447699393 247 DGG 249
Cdd:PRK05565  242 DGG 244
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
12-253 4.66e-68

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 210.39  E-value: 4.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSN-DVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGnDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:PRK12824   83 ILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGL 250
Cdd:PRK12824  163 TKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISINGGL 242

                  ...
gi 1447699393 251 VMR 253
Cdd:PRK12824  243 YMH 245
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
12-252 1.05e-66

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: 206.90  E-value: 1.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTA-LKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNEERAEAwLQEQGALGFDFRVVEGDVSSFESCKAAVAKVEAELGPVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:TIGR01829  81 VLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGL 250
Cdd:TIGR01829 161 TKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSINGGL 240

                  ..
gi 1447699393 251 VM 252
Cdd:TIGR01829 241 YM 242
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
18-250 3.19e-65

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: 202.66  E-value: 3.19e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  18 GASGD--IGLGICEKYLEQNCDVYALYKSNDV--QLTALKASHPAgdklHIVQCDLACPQSVSALCEQIERQAGKIDVLV 93
Cdd:pfam13561   1 GAANEsgIGWAIARALAEEGAEVVLTDLNEALakRVEELAEELGA----AVLPCDVTDEEQVEALVAAAVEKFGRLDILV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIV--KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:pfam13561  77 NNAGFApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMK--EGGSIVNLSSIGAERVVPNYNAYGAAKAALEALT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:pfam13561 155 RYLAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGG 234

                  .
gi 1447699393 250 L 250
Cdd:pfam13561 235 Y 235
FabG-like PRK07231
SDR family oxidoreductase;
7-250 1.09e-61

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 194.28  E-value: 1.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVQLTALKASHP---AGDKLHIVQCDLACPQSVSALCEQIE 83
Cdd:PRK07231    1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVV----TDRNEEAAERVAAeilAGGRAIAVAADVSDEADVEAAVAAAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  84 RQAGKIDVLVNNAGI--VKDSLfASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYS 161
Cdd:PRK07231   77 ERFGSVDILVNNAGTthRNGPL-LDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK---KVSRAVVRA-VTSTIPLRRLGKCEEVANTIVFLSSSASS 237
Cdd:PRK07231  156 ASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEafmGEPTPENRAkFLATIPLGRLGTPEDIANAALFLASDEAS 235
                         250
                  ....*....|...
gi 1447699393 238 YIVGQTIVIDGGL 250
Cdd:PRK07231  236 WITGVTLVVDGGR 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
9-229 1.10e-61

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 194.32  E-value: 1.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAE-RLEALAAELRAaGARVEVVALDVTDPDAVAALAEAVLARFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:COG0300    82 PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTiplrrlgkcEEVANTIV 229
Cdd:COG0300   162 EGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLSP---------EEVARAIL 214
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
11-251 2.20e-60

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: 190.95  E-value: 2.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:cd05344    81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIES--------KMVKKVSRAV---VRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYI 239
Cdd:cd05344   161 VKTLSRELAPDGVTVNSVLPGYIDTervrrlleARAEKEGISVeeaEKEVASQIPLGRVGKPEELAALIAFLASEKASYI 240
                         250
                  ....*....|..
gi 1447699393 240 VGQTIVIDGGLV 251
Cdd:cd05344   241 TGQAILVDGGLT 252
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
8-252 3.88e-60

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 190.13  E-value: 3.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICeKYLEQNCDVYALYKSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK12936    3 DLSGRKALVTGASGGIGEEIA-RLLHAQGAIVGLHGTRVEKLEALAAE--LGERVKIFPANLSDRDEVKALGQKAEADLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK12936   80 GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVID 247
Cdd:PRK12936  160 IGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVN 239

                  ....*
gi 1447699393 248 GGLVM 252
Cdd:PRK12936  240 GGMAM 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
12-205 5.85e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 187.82  E-value: 5.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAV 205
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
9-250 9.05e-59

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: 186.82  E-value: 9.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSN-DVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKeDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL-MLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05358    81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIkRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASKGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-----SRAVvraVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:cd05358   161 VKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAwddpeQRAD---LLSLIPMGRIGEPEEIAAAAAWLASDEASYVTG 237

                  ....*....
gi 1447699393 242 QTIVIDGGL 250
Cdd:cd05358   238 TTLFVDGGM 246
PRK12829 PRK12829
short chain dehydrogenase; Provisional
7-250 2.12e-57

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 183.72  E-value: 2.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPaGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK12829    7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEA-ALAATAARLP-GAKVTATVADVADPAQVERVFDTAVERF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVK-DSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAE-NPAIINVASIAALIPSVGQANYSASK 164
Cdd:PRK12829   85 GGLDVLVNNAGIAGpTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALSSVAGRLGYPGRTPYAASK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVT-----------STIPLRRLGKCEEVANTIVFLSS 233
Cdd:PRK12829  165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGigldemeqeylEKISLGRMVEPEDIAATALFLAS 244
                         250
                  ....*....|....*..
gi 1447699393 234 SASSYIVGQTIVIDGGL 250
Cdd:PRK12829  245 PAARYITGQAISVDGNV 261
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
8-249 6.32e-57

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: 181.79  E-value: 6.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05347     2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd05347    82 KIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIV 245
Cdd:cd05347   162 AGLTKALATEWARHGIQVNAIAPGYFATEMTEAVvaDPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIF 241

                  ....
gi 1447699393 246 IDGG 249
Cdd:cd05347   242 VDGG 245
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
12-231 3.74e-56

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: 179.61  E-value: 3.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHpaGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:COG4221     6 KVALITGASSGIGAATARALAAAGARVVLAARRAE-RLEALAAEL--GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:COG4221    83 LVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLS 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFL 231
Cdd:COG4221   163 ESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFA 222
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
9-250 7.90e-56

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: 179.18  E-value: 7.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA-G 87
Cdd:cd05329     4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd05329    84 KLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIV 245
Cdd:cd05329   164 NQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQIIA 243

                  ....*
gi 1447699393 246 IDGGL 250
Cdd:cd05329   244 VDGGL 248
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
8-250 5.31e-54

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 174.75  E-value: 5.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALY--KSNDVQlTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK08213    9 DLSGKTALVTGGSRGLGLQIAEALGEAGARV-VLSarKAEELE-EAAAHLEALGIDALWIAADVADEADIERLAEETLER 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL---MLLRaaENPAIINVASIAAL----IPSVGQA 158
Cdd:PRK08213   87 FGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAkrsMIPR--GYGRIINVASVAGLggnpPEVMDTI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 159 NYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK08213  165 AYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASKH 244
                         250
                  ....*....|..
gi 1447699393 239 IVGQTIVIDGGL 250
Cdd:PRK08213  245 ITGQILAVDGGV 256
PRK09242 PRK09242
SDR family oxidoreductase;
9-250 6.29e-54

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 174.55  E-value: 6.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDV---QLTALKASHPAGdKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK09242    7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADAlaqARDELAEEFPER-EVHGLAADVSDDEDRRAILDWVEDH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK09242   86 WDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:PRK09242  166 ALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlsDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQC 245

                  ....*..
gi 1447699393 244 IVIDGGL 250
Cdd:PRK09242  246 IAVDGGF 252
PRK12939 PRK12939
short chain dehydrogenase; Provisional
7-253 9.04e-53

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 171.31  E-value: 9.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK12939    3 SNLAGKRALVTGAARGLGAAFAEALAEAGATV-AFNDGLAAEARELAAAlEAAGGRAHAIAADLADPASVQRFFDAAAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK12939   82 LGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:PRK12939  162 AVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVpADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLL 241

                  ....*....
gi 1447699393 245 VIDGGLVMR 253
Cdd:PRK12939  242 PVNGGFVMN 250
PRK06484 PRK06484
short chain dehydrogenase; Validated
12-249 1.98e-52

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 177.73  E-value: 1.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKyLEQNCDVYALYKSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK06484    6 RVVLVTGAAGGIGRAACQR-FARAGDQVVVADRNVERARERADS--LGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASM--SYEDFTQVIETNMFSIFRLTKDALMLLRAA-ENPAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:PRK06484   83 LVNNAGVTDPTMTATLdtTLEEFARLQAINLTGAYLVAREALRLMIEQgHGAAIVNVASGAGLVALPKRTAYSASKAAVI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAV---VRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIV 245
Cdd:PRK06484  163 SLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGkldPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTLV 242

                  ....
gi 1447699393 246 IDGG 249
Cdd:PRK06484  243 VDGG 246
PRK12827 PRK12827
short chain dehydrogenase; Provisional
9-251 1.09e-51

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 168.74  E-value: 1.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALY---KSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpMRGRAEADAVAAGIEAaGGKALGLAFDVRDFAATRAALDAGVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALM-LLRAAENPAIINVASIAALIPSVGQANYSAS 163
Cdd:PRK12827   84 EFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPpMIRARRGGRIVNIASVAGVRGNRGQVNYAAS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVsrAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:PRK12827  164 KAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNA--APTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASYVTGQV 241

                  ....*...
gi 1447699393 244 IVIDGGLV 251
Cdd:PRK12827  242 IPVDGGFC 249
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
14-250 1.67e-51

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: 167.91  E-value: 1.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALY-KSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVL 92
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYrKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTR 172
Cdd:cd05359    81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 173 TLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGL 250
Cdd:cd05359   161 YLAVELGPRGIRVNAVSPGVIDTDALAHFpnREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDGGL 240
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
9-249 1.93e-51

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: 167.76  E-value: 1.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDV-QLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVlEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPA-IINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05369    81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGsILNISATYAYTGSPFQVHSAAAKAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESK--MVKKVSRAV-VRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:cd05369   161 VDALTRSLAVEWGPYGIRVNAIAPGPIPTTegMERLAPSGKsEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTT 240

                  ....*.
gi 1447699393 244 IVIDGG 249
Cdd:cd05369   241 LVVDGG 246
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
12-253 3.65e-51

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: 167.55  E-value: 3.65e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDV-YALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:cd05366     3 KVAIITGAAQGIGRAIAERLAADGFNIvLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSFD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL-MLLRAAENPAIINVASIAALIPSVGQANYSASKGAILG 169
Cdd:cd05366    83 VMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAArQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVRG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 170 FTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRA-----------VTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:cd05366   163 LTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIagkpegegfaeFSSSIPLGRLSEPEDVAGLVSFLASEDSDY 242
                         250
                  ....*....|....*
gi 1447699393 239 IVGQTIVIDGGLVMR 253
Cdd:cd05366   243 ITGQTILVDGGMVYR 257
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
9-252 1.71e-50

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 165.56  E-value: 1.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTAL-KASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK12935    4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLvNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK12935   84 KVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSAsSYIVGQTIVID 247
Cdd:PRK12935  164 LGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDG-AYITGQQLNIN 242

                  ....*
gi 1447699393 248 GGLVM 252
Cdd:PRK12935  243 GGLYM 247
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
9-249 6.73e-50

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: 164.12  E-value: 6.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTA-----LKASHPAgDKLHIVQCDLACPQSVSALCEQIE 83
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARL-ALTGRDAERLEEtrqscLQAGVSE-KKILLVVADLTEEEGQDRIISTTL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  84 RQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENpAIINVASIAALIPSVGQANYSAS 163
Cdd:cd05364    79 AKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKG-EIVNVSSVAGGRSFPGVLYYCIS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESK------MVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASS 237
Cdd:cd05364   158 KAALDQFTRCTALELAPKGVRVNSVSPGVIVTGfhrrmgMPEEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASS 237
                         250
                  ....*....|..
gi 1447699393 238 YIVGQTIVIDGG 249
Cdd:cd05364   238 FITGQLLPVDGG 249
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
6-250 5.47e-49

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 162.20  E-value: 5.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   6 YNDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQ-LTALKASHPAGDKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK08936    2 YSDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEaNDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL-MLLRAAENPAIINVASIAALIPSVGQANYSAS 163
Cdd:PRK08936   82 EFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIkYFVEHDIKGNIINMSSVHEQIPWPLFVHYAAS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM-VKKVSRAVVRA-VTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK08936  162 KGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPInAEKFADPKQRAdVESMIPMGYIGKPEEIAAVAAWLASSEASYVTG 241

                  ....*....
gi 1447699393 242 QTIVIDGGL 250
Cdd:PRK08936  242 ITLFADGGM 250
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
7-249 1.29e-48

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 160.82  E-value: 1.29e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDvqltaLKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK08220    4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGF----D-----QAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK08220   75 GPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV------SRAVVRAVTST----IPLRRLGKCEEVANTIVFLSSSAS 236
Cdd:PRK08220  155 LTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLwvdedgEQQVIAGFPEQfklgIPLGKIARPQEIANAVLFLASDLA 234
                         250
                  ....*....|...
gi 1447699393 237 SYIVGQTIVIDGG 249
Cdd:PRK08220  235 SHITLQDIVVDGG 247
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
8-249 1.63e-48

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: 160.57  E-value: 1.63e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKA-SHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:cd05352     5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEElAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQ--ANYSASK 164
Cdd:cd05352    85 GKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNRPQpqAAYNASK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:cd05352   165 AAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDL 244

                  ....*
gi 1447699393 245 VIDGG 249
Cdd:cd05352   245 IIDGG 249
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
12-252 3.15e-48

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: 159.55  E-value: 3.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAE--AGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNA--GIVKDSL----FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:cd05349    79 IVNNAliDFPFDPDqrktFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMI-ESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:cd05349   159 ALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNL 238

                  ....*...
gi 1447699393 245 VIDGGLVM 252
Cdd:cd05349   239 VVDGGLVM 246
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
10-249 3.72e-48

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: 159.42  E-value: 3.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYAL---YKSNDvQLTALKASHPaGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLILAdinAPALE-QLKEELTNLY-KNRVIALELDITSKESIKELIESYLEKF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGI---VKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALI-PS-------- 154
Cdd:cd08930    79 GRIDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIaPDfriyentq 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 155 -VGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMvkkvSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSS 233
Cdd:cd08930   159 mYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQ----PSEFLEKYTKKCPLKRMLNPEDLRGAIIFLLS 234
                         250
                  ....*....|....*.
gi 1447699393 234 SASSYIVGQTIVIDGG 249
Cdd:cd08930   235 DASSYVTGQNLVIDGG 250
PRK06398 PRK06398
aldose dehydrogenase; Validated
6-253 3.78e-48

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 159.61  E-value: 3.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   6 YNDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksndvqltalKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK06398    1 DLGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINF-----------DIKEPSYNDVDYFKVDVSNKEQVIKGIDYVISK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK06398   70 YGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKH 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPwGVRVNAVAPGMIESKMVKKVSRAVV----RAVTSTI-------PLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK06398  150 AVLGLTRSIAVDYAP-TIRCVAVCPGSIRTPLLEWAAELEVgkdpEHVERKIrewgemhPMKRVGKPEEVAYVVAFLASD 228
                         250
                  ....*....|....*....
gi 1447699393 235 ASSYIVGQTIVIDGGLVMR 253
Cdd:PRK06398  229 LASFITGECVTVDGGLRAL 247
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
8-249 9.61e-48

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 159.02  E-value: 9.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksndvqltALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK06171    6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNA---------DIHGGDGQHENYQFVPTDVSSAEEVNHTVAEIIEKFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFAS---------MSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQA 158
Cdd:PRK06171   77 RIDGLVNNAGINIPRLLVDekdpagkyeLNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 159 NYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESK------------MVKKVSRAVVRA---VTSTIPLRRLGKCEE 223
Cdd:PRK06171  157 CYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEATglrtpeyeealaYTRGITVEQLRAgytKTSTIPLGRSGKLSE 236
                         250       260
                  ....*....|....*....|....*.
gi 1447699393 224 VANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK06171  237 VADLVCYLLSDRASYITGVTTNIAGG 262
PRK07856 PRK07856
SDR family oxidoreductase;
8-249 1.27e-47

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 158.17  E-value: 1.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvqltalkaSHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07856    3 DLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAP--------ETVDGRPAEFHAADVRDPDQVAALVDAIVERHG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRA-AENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK07856   75 RLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSGRRPSPGTAAYGAAKAG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPwGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:PRK07856  155 LLNLTRSLAVEWAP-KVRVNAVVVGLVRTEQSELHygDAEGIAAVAATVPLGRLATPADIAWACLFLASDLASYVSGANL 233

                  ....*
gi 1447699393 245 VIDGG 249
Cdd:PRK07856  234 EVHGG 238
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
9-252 5.43e-47

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 156.33  E-value: 5.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTA-LKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK12938    1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKwLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAENpaIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK12938   81 EIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIdgMVERGWGR--IINISSVNGQKGQFGQTNYSTAKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIV 245
Cdd:PRK12938  159 GIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFS 238

                  ....*..
gi 1447699393 246 IDGGLVM 252
Cdd:PRK12938  239 LNGGLHM 245
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
8-249 1.23e-46

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: 155.72  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDkLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd08942     3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGE-CIAIPADLSSEEGIEALVARVAERSD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRA---AENPA-IINVASIAALIPSVGQA-NYSA 162
Cdd:cd08942    82 RLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAaatAENPArVINIGSIAGIVVSGLENySYGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR--AVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIV 240
Cdd:cd08942   162 SKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNdpAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAYLT 241

                  ....*....
gi 1447699393 241 GQTIVIDGG 249
Cdd:cd08942   242 GAVIPVDGG 250
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
7-249 1.90e-46

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: 155.23  E-value: 1.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYAlykSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:cd05341     1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVL---SDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05341    78 GRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAP--WGVRVNAVAPGMIESKMVKKVSRAVV-RAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:cd05341   158 VRGLTKSAALECATqgYGIRVNSVHPGYIYTPMTDELLIAQGeMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSE 237

                  ....*.
gi 1447699393 244 IVIDGG 249
Cdd:cd05341   238 LVVDGG 243
PRK07062 PRK07062
SDR family oxidoreductase;
8-250 4.49e-46

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 154.81  E-value: 4.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTA----LKASHPaGDKLHIVQCDLACPQSVSALCEQIE 83
Cdd:PRK07062    5 QLEGRVAVVTGGSSGIGLATVELLLEAGASV-AICGRDEERLASaearLREKFP-GARLLAARCDVLDEADVAAFAAAVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  84 RQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSAS 163
Cdd:PRK07062   83 ARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKvsRAVVRAVTST--------------IPLRRLGKCEEVANTIV 229
Cdd:PRK07062  163 RAGLLNLVKSLATELAPKGVRVNSILLGLVESGQWRR--RYEARADPGQsweawtaalarkkgIPLGRLGRPDEAARALF 240
                         250       260
                  ....*....|....*....|.
gi 1447699393 230 FLSSSASSYIVGQTIVIDGGL 250
Cdd:PRK07062  241 FLASPLSSYTTGSHIDVSGGF 261
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
14-249 4.73e-46

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: 153.78  E-value: 4.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKAShpaGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVLV 93
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIAL----DLPFVLLLEY---GDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTRT 173
Cdd:cd05331    74 NCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 174 LAAEMAPWGVRVNAVAPGMIESKMVKKV----SRA--VVRAVTST----IPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:cd05331   154 LGLELAPYGVRCNVVSPGSTDTAMQRTLwhdeDGAaqVIAGVPEQfrlgIPLGKIAQPADIANAVLFLASDQAGHITMHD 233

                  ....*.
gi 1447699393 244 IVIDGG 249
Cdd:cd05331   234 LVVDGG 239
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-252 5.00e-46

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 153.96  E-value: 5.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQL-TALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK08217    2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKL-ALIDLNQEKLeEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLF---------ASMSYEDFTQVIETNMFSIFRLTKD-ALMLLRAAENPAIINVASIAAlIPSVG 156
Cdd:PRK08217   81 GQLNGLINNAGILRDGLLvkakdgkvtSKMSLEQFQSVIDVNLTGVFLCGREaAAKMIESGSKGVIINISSIAR-AGNMG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 157 QANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLssSAS 236
Cdd:PRK08217  160 QTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTVRFI--IEN 237
                         250
                  ....*....|....*.
gi 1447699393 237 SYIVGQTIVIDGGLVM 252
Cdd:PRK08217  238 DYVTGRVLEIDGGLRL 253
PRK06841 PRK06841
short chain dehydrogenase; Provisional
8-249 2.17e-45

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 152.51  E-value: 2.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAShpaGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK06841   12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLL---GGNAKGLVCDVSDSQSVEAAVAAVISAFG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK06841   89 RIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK06841  169 VGMTKVLALEWGPYGITVNAISPTVVLTELGKKAwAGEKGERAKKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLVI 248

                  ...
gi 1447699393 247 DGG 249
Cdd:PRK06841  249 DGG 251
PRK06484 PRK06484
short chain dehydrogenase; Validated
12-251 2.26e-45

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 158.86  E-value: 2.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNcDVYALYKSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK06484  270 RVVAITGGARGIGRAVADRFAAAG-DRLLIIDRDAEGAKKLAEA--LGDEHLSVQADITDEAAVESAFAQIQARWGRLDV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSL-FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAEnpAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:PRK06484  347 LVNNAGIAEVFKpSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGG--VIVNLGSIASLLALPPRNAYCASKAAVTML 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIESKMV---KKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVID 247
Cdd:PRK06484  425 SRSLACEWAPAGIRVNTVAPGYIETPAVlalKASGRADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVD 504

                  ....
gi 1447699393 248 GGLV 251
Cdd:PRK06484  505 GGWT 508
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
9-252 4.18e-45

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 151.96  E-value: 4.18e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQL-TALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK12429    2 LKGKVALVTGAASGIGLEIALALAKEGAKV-VIADLNDEAAaAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK12429   81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKK------------VSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSA 235
Cdd:PRK12429  161 IGLTKVVALEGATHGVTVNAICPGYVDTPLVRKqipdlakergisEEEVLEDVLLPLVPQKRFTTVEEIADYALFLASFA 240
                         250
                  ....*....|....*..
gi 1447699393 236 SSYIVGQTIVIDGGLVM 252
Cdd:PRK12429  241 AKGVTGQAWVVDGGWTA 257
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-249 5.36e-45

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 151.47  E-value: 5.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAShpagdKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK06463    5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREK-----GVFTIKCDVGNRDQVKKSKEVVEKEFGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAAL-IPSVGQANYSASKGAI 167
Cdd:PRK06463   80 VDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAITKAGI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKM---------VKKVsRAVVRAVTStipLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK06463  160 IILTRRLAFELGKYGIRVNAVAPGWVETDMtlsgksqeeAEKL-RELFRNKTV---LKTTGKPEDIANIVLFLASDDARY 235
                         250
                  ....*....|.
gi 1447699393 239 IVGQTIVIDGG 249
Cdd:PRK06463  236 ITGQVIVADGG 246
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
9-251 5.75e-45

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: 151.27  E-value: 5.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd05362    81 GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR--DGGRIINISSSLTAAYTPNYGAYAGSKAAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMV--KKVSRAVVRAVTSTiPLRRLGKCEEVANTIVFLSSSASSYIVGQTIV 245
Cdd:cd05362   159 EAFTRVLAKELGGRGITVNAVAPGPVDTDMFyaGKTEEAVEGYAKMS-PLGRLGEPEDIAPVVAFLASPDGRWVNGQVIR 237

                  ....*.
gi 1447699393 246 IDGGLV 251
Cdd:cd05362   238 ANGGYV 243
PRK05867 PRK05867
SDR family oxidoreductase;
8-249 1.01e-44

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 150.96  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDV-YALYKSNDVQLTALKASHPAGDKLHIvQCDLACPQSVSALCEQIERQA 86
Cdd:PRK05867    6 DLHGKRALITGASTGIGKRVALAYVEAGAQVaIAARHLDALEKLADEIGTSGGKVVPV-CCDVSQHQQVTSMLDQVTAEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFrLTKDALM--LLRAAENPAIINVASIAALIPSVGQ--ANYSA 162
Cdd:PRK05867   85 GGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVF-LTAQAAAkaMVKQGQGGVIINTASMSGHIINVPQqvSHYCA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRaVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQ 242
Cdd:PRK05867  164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTE-YQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMTGS 242

                  ....*..
gi 1447699393 243 TIVIDGG 249
Cdd:PRK05867  243 DIVIDGG 249
PRK07577 PRK07577
SDR family oxidoreductase;
9-249 1.41e-44

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 149.88  E-value: 1.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksndvqltalkASHPAGD-KLHIVQCDLACPQSVSALCEQIeRQAG 87
Cdd:PRK07577    1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGI------------ARSAIDDfPGELFACDLADIEQTAATLAQI-NEIH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALiPSVGQANYSASKGAI 167
Cdd:PRK07577   68 PVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIF-GALDRTSYSAAKSAL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA---VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:PRK07577  147 VGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPVgseEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVL 226

                  ....*
gi 1447699393 245 VIDGG 249
Cdd:PRK07577  227 GVDGG 231
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-249 3.24e-44

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 148.96  E-value: 3.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTalkashpagDKLHIVQCDLACPqsvsalCEQIERQAG 87
Cdd:PRK06550    2 EFMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLS---------GNFHFLQLDLSDD------LEPLFDWVP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKD-SLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK06550   67 SVDILCNTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIES----------KMVKKVSRAVvravtstiPLRRLGKCEEVANTIVFLSSSAS 236
Cdd:PRK06550  147 LAGFTKQLALDYAKDGIQVFGIAPGAVKTpmtaadfepgGLADWVARET--------PIKRWAEPEEVAELTLFLASGKA 218
                         250
                  ....*....|...
gi 1447699393 237 SYIVGQTIVIDGG 249
Cdd:PRK06550  219 DYMQGTIVPIDGG 231
PRK12828 PRK12828
short chain dehydrogenase; Provisional
7-252 3.54e-44

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 148.79  E-value: 3.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKASHP--AGDKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK12828    3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALI----GRGAAPLSQTLPgvPADALRIGGIDLVDPQAARRAVDEVNR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASK 164
Cdd:PRK12828   79 QFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKkvsravvravtSTIPLRRLG---KCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK12828  159 AGVARLTEALAAELLDRGITVNAVLPSIIDTPPNR-----------ADMPDADFSrwvTPEQIAAVIAFLLSDEAQAITG 227
                         250
                  ....*....|.
gi 1447699393 242 QTIVIDGGLVM 252
Cdd:PRK12828  228 ASIPVDGGVAL 238
PRK06138 PRK06138
SDR family oxidoreductase;
8-250 8.26e-44

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 148.38  E-value: 8.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAShPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK06138    2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAI-AAGGRAFARQGDVGSAEAVEALVDFVAARWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK06138   81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV------SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK06138  161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIfarhadPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240

                  ....*....
gi 1447699393 242 QTIVIDGGL 250
Cdd:PRK06138  241 TTLVVDGGW 249
PRK08628 PRK08628
SDR family oxidoreductase;
8-251 9.65e-44

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 148.57  E-value: 9.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCdVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK08628    4 NLKDKVVIVTGGASGIGAAISLRLAEEGA-IPVIFGRSAPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGiVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENpAIINVASIAALipsVGQAN---YSASK 164
Cdd:PRK08628   83 RIDGLVNNAG-VNDGVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKASRG-AIVNISSKTAL---TGQGGtsgYAAAK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV------SRAVVRAVTSTIPL-RRLGKCEEVANTIVFLSSSASS 237
Cdd:PRK08628  158 GAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWiatfddPEAKLAAITAKIPLgHRMTTAEEIADTAVFLLSERSS 237
                         250
                  ....*....|....
gi 1447699393 238 YIVGQTIVIDGGLV 251
Cdd:PRK08628  238 HTTGQWLFVDGGYV 251
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
9-249 1.43e-43

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 148.02  E-value: 1.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPaGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK08226    4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGR-GHRCTAVVADVRDPASVAAAIKRAKEKEGR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAA-LIPSVGQANYSASKGAI 167
Cdd:PRK08226   83 IDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKAAI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR--------AVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYI 239
Cdd:PRK08226  163 VGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARqsnpedpeSVLTEMAKAIPLRRLADPLEVGELAAFLASDESSYL 242
                         250
                  ....*....|
gi 1447699393 240 VGQTIVIDGG 249
Cdd:PRK08226  243 TGTQNVIDGG 252
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-253 1.63e-43

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 147.96  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   1 MNMYKYN----DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTAlKASHPAGDKLHIVQCDLACPQSVS 76
Cdd:PRK06935    1 MELDKFSmdffSLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDETR-RLIEKEGRKVTFVQVDLTKPESAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  77 ALCEQIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAA-----L 151
Cdd:PRK06935   80 KVVKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSfqggkF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 152 IPSvgqanYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVR--AVTSTIPLRRLGKCEEVANTIV 229
Cdd:PRK06935  160 VPA-----YTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRndEILKRIPAGRWGEPDDLMGAAV 234
                         250       260
                  ....*....|....*....|....
gi 1447699393 230 FLSSSASSYIVGQTIVIDGGLVMR 253
Cdd:PRK06935  235 FLASRASDYVNGHILAVDGGWLVR 258
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
9-251 2.85e-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: 2.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKS---NDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:cd05355    24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPeeeDDAEETK-KLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAG--IVKDSLfASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSAS 163
Cdd:cd05355   103 FGKLDILVNNAAyqHPQESI-EDITTEQLEKTFRTNIFSMFYLTKAALPHLK--KGSSIINTTSVTAYKGSPHLLDYAAT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPG-----MIESKMVKKvsraVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:cd05355   180 KGAIVAFTRGLSLQLAEKGIRVNAVAPGpiwtpLIPSSFPEE----KVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSY 255
                         250
                  ....*....|...
gi 1447699393 239 IVGQTIVIDGGLV 251
Cdd:cd05355   256 VTGQVLHVNGGEI 268
PRK12743 PRK12743
SDR family oxidoreductase;
12-250 3.12e-43

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 147.10  E-value: 3.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSN--DVQLTALKASHpAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDeeGAKETAEEVRS-HGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL-MLLRAAENPAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:PRK12743   82 DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAArHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPGMIESKM-------VKKVSRAvvravtsTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK12743  162 GLTKAMALELVEHGILVNAVAPGAIATPMngmddsdVKPDSRP-------GIPLGRPGDTHEIASLVAWLCSEGASYTTG 234

                  ....*....
gi 1447699393 242 QTIVIDGGL 250
Cdd:PRK12743  235 QSLIVDGGF 243
PRK07035 PRK07035
SDR family oxidoreductase;
8-251 2.15e-42

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 144.77  E-value: 2.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDV-YALYKSNDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK07035    5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHViVSSRKLDGCQAVA-DAIVAAGGKAEALACHIGEMEQIDALFAHIRERH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGivKDSLFASMSYED---FTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSAS 163
Cdd:PRK07035   84 GRLDILVNNAA--ANPYFGHILDTDlgaFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSIT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR--AVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK07035  162 KAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKndAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTG 241
                         250
                  ....*....|
gi 1447699393 242 QTIVIDGGLV 251
Cdd:PRK07035  242 ECLNVDGGYL 251
PRK08589 PRK08589
SDR family oxidoreductase;
9-252 2.18e-42

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 145.31  E-value: 2.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHpAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK08589    4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIKS-NGGKAKAYHVDISDEQQVKDFASEIKEQFGR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDS-LFASMSYEDFTQVIETNMFSIFRLTKdALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK08589   83 VDVLFNNAGVDNAAgRIHEYPVDVFDKIMAVDMRGTFLMTK-MLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAAKGAV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--------RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYI 239
Cdd:PRK08589  162 INFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTgtsedeagKTFRENQKWMTPLGRLGKPEEVAKLVVFLASDDSSFI 241
                         250
                  ....*....|...
gi 1447699393 240 VGQTIVIDGGlVM 252
Cdd:PRK08589  242 TGETIRIDGG-VM 253
PRK06701 PRK06701
short chain dehydrogenase; Provisional
4-249 2.28e-42

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 145.95  E-value: 2.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   4 YKYND-LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKS--NDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCE 80
Cdd:PRK06701   38 YKGSGkLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDehEDANETK-QRVEKEGVKCLLIPGDVSDEAFCKDAVE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  81 QIERQAGKIDVLVNNAG--IVKDSlFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQA 158
Cdd:PRK06701  117 ETVRELGRLDILVNNAAfqYPQQS-LEDITAEQLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYEGNETLI 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 159 NYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMI------ESKMVKKVSRavvraVTSTIPLRRLGKCEEVANTIVFLS 232
Cdd:PRK06701  194 DYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIwtplipSDFDEEKVSQ-----FGSNTPMQRPGQPEELAPAYVFLA 268
                         250
                  ....*....|....*..
gi 1447699393 233 SSASSYIVGQTIVIDGG 249
Cdd:PRK06701  269 SPDSSYITGQMLHVNGG 285
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
12-201 9.37e-42

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: 142.75  E-value: 9.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqLTALKASHPAGdkLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDK-LESLGELLNDN--LEVLELDVTDEESIKAAVKEVIERFGRIDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVkdslfASMSYEDFT-----QVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05374    78 LVNNAGYG-----LFGPLEETSieevrELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAA 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV 201
Cdd:cd05374   153 LEALSESLRLELAPFGIKVTIIEPGPVRTGFADNA 187
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
12-249 2.74e-41

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: 141.45  E-value: 2.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKASHpAGDKLHIVQCDLACPQSVSALCEQIERqagkIDV 91
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREGANVIAT----DINEEKLKELE-RGPGITTRVLDVTDKEQVAALAKEEGR----IDV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSV-GQANYSASKGAILGF 170
Cdd:cd05368    74 LFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVpNRFVYSTTKAAVIGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA------VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:cd05368   154 TKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAqpdpeeALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAV 233

                  ....*
gi 1447699393 245 VIDGG 249
Cdd:cd05368   234 VIDGG 238
PRK06124 PRK06124
SDR family oxidoreductase;
1-253 3.41e-41

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 141.77  E-value: 3.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   1 MNMYKYNDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCE 80
Cdd:PRK06124    1 MSILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  81 QIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANY 160
Cdd:PRK06124   81 RIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESK----MVKkvSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSAS 236
Cdd:PRK06124  161 PAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATEtnaaMAA--DPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAA 238
                         250
                  ....*....|....*..
gi 1447699393 237 SYIVGQTIVIDGGLVMR 253
Cdd:PRK06124  239 SYVNGHVLAVDGGYSVH 255
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
14-251 4.06e-41

3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well conserved family of proteins closely related to the FabG family, TIGR01830, and possibly equal in function. In all completed genomes with a member of this family, a FabG in TIGR01830 is also found. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 141.20  E-value: 4.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSN----DVQLTALKAShpaGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:TIGR01831   1 VLVTGASRGIGRAIANQLAADGFNIGVHYHSDaagaQETLNAIVAN---GGNGRLLSFDVADRVACREVLEADIAQHGAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALM-LLRAAENPAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:TIGR01831  78 YGVVLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMpMIGARQGGRIITLASVSGVMGNRGQVNYSAAKAGLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVtSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDG 248
Cdd:TIGR01831 158 GATKALAIELAKRKITVNCIAPGLIDTGMIAMEESALKEAL-SMVPMKRMGQPEEVAGLASFLMSDIAGYVTRQVISVNG 236

                  ...
gi 1447699393 249 GLV 251
Cdd:TIGR01831 237 GML 239
PRK06172 PRK06172
SDR family oxidoreductase;
8-251 4.81e-41

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 141.43  E-value: 4.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK06172    4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGI-VKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK06172   84 RLDYAFNNAGIeIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRA---VTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:PRK06172  164 VIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRKaefAAAMHPVGRIGKVEEVASAVLYLCSDGASFTTGHA 243

                  ....*...
gi 1447699393 244 IVIDGGLV 251
Cdd:PRK06172  244 LMVDGGAT 251
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
10-252 6.19e-41

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: 140.89  E-value: 6.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQGAKVVIL----DLPNSPGETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGI---VKDSLFASM---SYEDFTQVIETNMFSIFRLTKdaLMLLRAAENPA--------IINVASIAALIPSV 155
Cdd:cd05371    77 DIVVNCAGIavaAKTYNKKGQqphSLELFQRVINVNLIGTFNVIR--LAAGAMGKNEPdqggergvIINTASVAAFEGQI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 156 GQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIP-LRRLGKCEEVANTIVFLSSs 234
Cdd:cd05371   155 GQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPfPSRLGDPAEYAHLVQHIIE- 233
                         250
                  ....*....|....*...
gi 1447699393 235 aSSYIVGQTIVIDGGLVM 252
Cdd:cd05371   234 -NPYLNGEVIRLDGAIRM 250
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-252 8.40e-41

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 140.61  E-value: 8.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK08642    2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADE--LGDRAIALQADVTDREQVQAMFATATEHFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 K-IDVLVNNA-------GIVKDSlFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQAN 159
Cdd:PRK08642   80 KpITTVVNNAladfsfdGDARKK-ADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK08642  159 YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAAtPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPWARA 238
                         250
                  ....*....|....
gi 1447699393 239 IVGQTIVIDGGLVM 252
Cdd:PRK08642  239 VTGQNLVVDGGLVM 252
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
12-253 1.10e-40

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: 1.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVY--ALYKSNDVQ-LTALKASHPAGDKLHIvQCDLACPQSVSALCEQIERQAGK 88
Cdd:cd08940     3 KVALVTGSTSGIGLGIARALAAAGANIVlnGFGDAAEIEaVRAGLAAKHGVKVLYH-GADLSKPAAIEDMVAYAQRQFGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:cd08940    82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPGMIESKMVKK------------VSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSAS 236
Cdd:cd08940   162 GLTKVVALETAGTGVTCNAICPGWVLTPLVEKqisalaqkngvpQEQAARELLLEKQPSKQFVTPEQLGDTAVFLASDAA 241
                         250
                  ....*....|....*..
gi 1447699393 237 SYIVGQTIVIDGGLVMR 253
Cdd:cd08940   242 SQITGTAVSVDGGWTAQ 258
PRK07831 PRK07831
SDR family oxidoreductase;
9-244 1.60e-40

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 140.17  E-value: 1.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGD-IGLGICEKYLEQNCDVYAlyksNDVQLTALKASHPA------GDKLHIVQCDLACPQSVSALCEQ 81
Cdd:PRK07831   15 LAGKVVLVTAAAGTgIGSATARRALEEGARVVI----SDIHERRLGETADElaaelgLGRVEAVVCDVTSEAQVDALIDA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  82 IERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENP-AIINVASIAALIPSVGQANY 160
Cdd:PRK07831   91 AVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGgVIVNNASVLGWRAQHGQAHY 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA-VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYI 239
Cdd:PRK07831  171 AAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVTSAeLLDELAAREAFGRAAEPWEVANVIAFLASDYSSYL 250

                  ....*
gi 1447699393 240 VGQTI 244
Cdd:PRK07831  251 TGEVV 255
PRK06500 PRK06500
SDR family oxidoreductase;
9-249 5.13e-40

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 138.55  E-value: 5.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK06500    4 LQGKTALITGGTSGIGLETARQFLAEGARV-AITGRDPASLEAARAE--LGESALVIRADAGDVAAQKALAQALAEAFGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLraaENPA-IINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK06500   81 LDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL---ANPAsIVLNGSINAHIGMPNSSVYAASKAAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV------SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK06500  158 LSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLglpeatLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVG 237

                  ....*...
gi 1447699393 242 QTIVIDGG 249
Cdd:PRK06500  238 SEIIVDGG 245
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
14-249 5.47e-40

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: 138.09  E-value: 5.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVY-ALYKSNDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVL 92
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVViADLKSEGAEAVA-AAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLFA-SMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:cd05365    81 VNNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:cd05365   161 RNLAFDLGPKGIRVNAVAPGAVKTDALASVlTPEIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
PRK12937 PRK12937
short chain dehydrogenase; Provisional
9-251 5.96e-40

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 138.34  E-value: 5.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK12937    3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEiEAAGGRAIAVQADVADAAAVTRLFDAAETAFG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK12937   83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLG--QGGRIINLSTSVIALPLPGYGPYAASKAAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKM-VKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK12937  161 EGLVHVLANELRGRGITVNAVAPGPVATELfFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLRV 240

                  ....*
gi 1447699393 247 DGGLV 251
Cdd:PRK12937  241 NGGFA 245
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
12-251 6.14e-40

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 138.71  E-value: 6.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYAL-YKSNDVQLTALKASHPAGDKLhIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:PRK08643    3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVdYNEETAQAAADKLSKDGGKAI-AVKADVSDRDQVFAAVRQVVDTFGDLN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRA-AENPAIINVASIAALIPSVGQANYSASKGAILG 169
Cdd:PRK08643   82 VVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKlGHGGKIINATSQAGVVGNPELAVYSSTKFAVRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 170 FTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAV-----------TSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK08643  162 LTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGENAgkpdewgmeqfAKDITLGRLSEPEDVANCVSFLAGPDSDY 241
                         250
                  ....*....|...
gi 1447699393 239 IVGQTIVIDGGLV 251
Cdd:PRK08643  242 ITGQTIIVDGGMV 254
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
9-251 9.60e-40

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 138.06  E-value: 9.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK06113    9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFaSMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:PRK06113   89 VDILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAAS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVID 247
Cdd:PRK06113  168 HLVRNMAFDLGEKNIRVNGIAPGAILTDALKSViTPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVS 247

                  ....
gi 1447699393 248 GGLV 251
Cdd:PRK06113  248 GGGV 251
PRK06523 PRK06523
short chain dehydrogenase; Provisional
7-251 3.59e-39

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 136.57  E-value: 3.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYAlyksndvqlTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK06523    5 LELAGKRALVTGGTKGIGAATVARLLEAGARVVT---------TARSRPDDLPEGVEFVAADLTTAEGCAAVARAVLERL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSL--FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQ-ANYSAS 163
Cdd:PRK06523   76 GGVDILVHVLGGSSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPEStTAYAAA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESK----MVKKVSRA----------VVRAVTSTIPLRRLGKCEEVANTIV 229
Cdd:PRK06523  156 KAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEaavaLAERLAEAagtdyegakqIIMDSLGGIPLGRPAEPEEVAELIA 235
                         250       260
                  ....*....|....*....|..
gi 1447699393 230 FLSSSASSYIVGQTIVIDGGLV 251
Cdd:PRK06523  236 FLASDRAASITGTEYVIDGGTV 257
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-244 4.34e-39

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 140.74  E-value: 4.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQltalkashPAGDKLHIV---------QCDLACPQSVSALCEQI 82
Cdd:PRK08261  211 KVALVTGAARGIGAAIAEVLARDGAHVVCL----DVP--------AAGEALAAVanrvggtalALDITAPDAPARIAEHL 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTkDALM---LLRaaENPAIINVASIAALIPSVGQAN 159
Cdd:PRK08261  279 AERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRIT-EALLaagALG--DGGRIVGVSSISGIAGNRGQTN 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMvkkvsravvravTSTIPL------RRL------GKCEEVANT 227
Cdd:PRK08261  356 YAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM------------TAAIPFatreagRRMnslqqgGLPVDVAET 423
                         250
                  ....*....|....*..
gi 1447699393 228 IVFLSSSASSYIVGQTI 244
Cdd:PRK08261  424 IAWLASPASGGVTGNVV 440
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
12-231 5.25e-39

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: 135.18  E-value: 5.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKsndvQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLR----NPEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:cd08932    77 LVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRavvravTSTIPLRRLGKCEEVANTIVFL 231
Cdd:cd08932   157 HALRQEGWDHGVRVSAVCPGFVDTPMAQGLTL------VGAFPPEEMIQPKDIANLVRMV 210
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
9-249 8.14e-39

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: 135.21  E-value: 8.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLT-ALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05345     3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIA----DINADgAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIV-KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05345    79 RLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV----SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQ 242
Cdd:cd05345   159 VVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFmgedTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGV 238

                  ....*..
gi 1447699393 243 TIVIDGG 249
Cdd:cd05345   239 ALEVDGG 245
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
12-250 1.06e-38

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: 135.36  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd08945     4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALML--LRAAENPAIINVASIAALIPSVGQANYSASKGAILG 169
Cdd:cd08945    84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 170 FTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-----------SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:cd08945   164 FTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAAA 243
                         250
                  ....*....|..
gi 1447699393 239 IVGQTIVIDGGL 250
Cdd:cd08945   244 VTAQALNVCGGL 255
PRK06947 PRK06947
SDR family oxidoreductase;
12-249 1.65e-38

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 134.55  E-value: 1.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSND--VQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAaaAEETA-DAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSL-FASMSYEDFTQVIETNMFSIFRLTKDALMLL---RAAENPAIINVASIAALIPSVGQ-ANYSASK 164
Cdd:PRK06947   82 DALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLstdRGGRGGAIVNVSSIASRLGSPNEyVDYAGSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK---KVSRAVVRAVTStiPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK06947  162 GAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHAsggQPGRAARLGAQT--PLGRAGEADEVAETIVWLLSDAASYVTG 239

                  ....*...
gi 1447699393 242 QTIVIDGG 249
Cdd:PRK06947  240 ALLDVGGG 247
PRK07063 PRK07063
SDR family oxidoreductase;
7-250 3.86e-38

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 134.02  E-value: 3.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVQLTALK------ASHPAGDKLHIVQCDLACPQSVSALCE 80
Cdd:PRK07063    3 NRLAGKVALVTGAAQGIGAAIARAFAREGAAVAL----ADLDAALAEraaaaiARDVAGARVLAVPADVTDAASVAAAVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  81 QIERQAGKIDVLVNNAGIvkdSLFA---SMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAEnpAIINVASIAA--LIP 153
Cdd:PRK07063   79 AAEEAFGPLDVLVNNAGI---NVFAdplAMTDEDWRRCFAVDLDGAWNGCRAVLpgMVERGRG--SIVNIASTHAfkIIP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 154 svGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV------SRAVVRAVTSTIPLRRLGKCEEVANT 227
Cdd:PRK07063  154 --GCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWwnaqpdPAAARAETLALQPMKRIGRPEEVAMT 231
                         250       260
                  ....*....|....*....|...
gi 1447699393 228 IVFLSSSASSYIVGQTIVIDGGL 250
Cdd:PRK07063  232 AVFLASDEAPFINATCITIDGGR 254
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-253 1.65e-37

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 131.95  E-value: 1.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   1 MNMYkynDLNEKTVLVTGASGDIGLGICEKYLEQNCDV----YALYKSNDVQLTALkashpaGDKLHIVQCDLACPQSVS 76
Cdd:PRK12481    1 MQLF---DLNGKVAIITGCNTGLGQGMAIGLAKAGADIvgvgVAEAPETQAQVEAL------GRKFHFITADLIQQKDID 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  77 ALCEQIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKD-ALMLLRAAENPAIINVASIAALIPSV 155
Cdd:PRK12481   72 SIVSQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAvAKQFVKQGNGGKIINIASMLSFQGGI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 156 GQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVR--AVTSTIPLRRLGKCEEVANTIVFLSS 233
Cdd:PRK12481  152 RVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARneAILERIPASRWGTPDDLAGPAIFLSS 231
                         250       260
                  ....*....|....*....|
gi 1447699393 234 SASSYIVGQTIVIDGGLVMR 253
Cdd:PRK12481  232 SASDYVTGYTLAVDGGWLAR 251
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
9-250 2.05e-37

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: 131.81  E-value: 2.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQ--LTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVIA----DIDddAGQAVAAELGDPDISFVHCDVTVEADVRAAVDTAVARF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSY--EDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASK 164
Cdd:cd05326    78 GRLDIMFNNAGVLGAPCYSILETslEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMV--------KKVSRAVVRAVTstiPLRRLGKCEEVANTIVFLSSSAS 236
Cdd:cd05326   158 HAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLtagfgvedEAIEEAVRGAAN---LKGTALRPEDIAAAVLYLASDDS 234
                         250
                  ....*....|....
gi 1447699393 237 SYIVGQTIVIDGGL 250
Cdd:cd05326   235 RYVSGQNLVVDGGL 248
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
12-249 2.82e-37

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: 131.46  E-value: 2.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVQLTALKA--SHPAGDKLHIvQCDLACPQSVSALCEQIERQAGKI 89
Cdd:cd08944     4 KVAIVTGAGAGIGAACAARLAREGARVVV----ADIDGGAAQAvvAQIAGGALAL-RVDVTDEQQVAALFERAVEEFGGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVK-DSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:cd08944    79 DLLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPGMIESKMVK-------KVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:cd08944   159 NLTRTLAAELRHAGIRCNALAPGLIDTPLLLaklagfeGALGPGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFITG 238

                  ....*...
gi 1447699393 242 QTIVIDGG 249
Cdd:cd08944   239 QVLCVDGG 246
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
8-249 3.05e-37

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: 131.81  E-value: 3.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd08935     2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAG--------------IVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIP 153
Cdd:cd08935    82 TVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 154 SVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV---------SRAvvRAVTSTIPLRRLGKCEEV 224
Cdd:cd08935   162 LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLlinpdgsytDRS--NKILGRTPMGRFGKPEEL 239
                         250       260
                  ....*....|....*....|....*.
gi 1447699393 225 ANTIVFLSS-SASSYIVGQTIVIDGG 249
Cdd:cd08935   240 LGALLFLASeKASSFVTGVVIPVDGG 265
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
12-198 1.15e-36

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 129.68  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDV---QLTALKASHPAGD-KLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd08939     2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKleeAVEEIEAEANASGqKVSYISADLSDYEEVEQAFAQAVEKGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd08939    82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFAL 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMV 198
Cdd:cd08939   162 RGLAESLRQELKPYNIRVSVVYPPDTDTPGF 192
PRK09072 PRK09072
SDR family oxidoreductase;
8-219 1.25e-36

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 130.06  E-value: 1.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKsNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALcEQIERQAG 87
Cdd:PRK09072    2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGR-NAEKLEALAARLPYPGRHRWVVADLTSEAGREAV-LARAREMG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK09072   80 GINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFAL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKM------------------VKKVSRAVVRAVTSTIPLRRLG 219
Cdd:PRK09072  160 RGFSEALRRELADTGVRVLYLAPRATRTAMnseavqalnralgnamddPEDVAAAVLQAIEKERAERWLG 229
PRK09135 PRK09135
pteridine reductase; Provisional
12-249 1.31e-36

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 129.66  E-value: 1.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKA--SHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK09135    7 KVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAelNALRPGSAAALQADLLDPDALPELVAACVAAFGRL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENpAIINVASIAALIPSVGQANYSASKGAILG 169
Cdd:PRK09135   87 DALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRG-AIVNITDIHAERPLKGYPVYCAAKAALEM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 170 FTRTLAAEMAPwGVRVNAVAPGMI---ESKmvKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSAsSYIVGQTIVI 246
Cdd:PRK09135  166 LTRSLALELAP-EVRVNAVAPGAIlwpEDG--NSFDEEARQAILARTPLKRIGTPEDIAEAVRFLLADA-SFITGQILAV 241

                  ...
gi 1447699393 247 DGG 249
Cdd:PRK09135  242 DGG 244
PRK07774 PRK07774
SDR family oxidoreductase;
8-253 1.62e-36

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 129.48  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVY-ALYKSNDVQLTALKASHPAGDKLHiVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK07774    3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVvADINAEGAERVAKQIVADGGTAIA-VQVDVSDPDSAKAMADATVSAF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGI---VKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSvgqANYSAS 163
Cdd:PRK07774   82 GGIDYLVNNAAIyggMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYS---NFYGLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA-VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQ 242
Cdd:PRK07774  159 KVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKeFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQ 238
                         250
                  ....*....|.
gi 1447699393 243 TIVIDGGLVMR 253
Cdd:PRK07774  239 IFNVDGGQIIR 249
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
9-252 2.43e-36

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 129.38  E-value: 2.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDV-YALYKSNDVQLTALKASHPAgdklHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVvIADIKPARARLAALEIGPAA----IAVSLDVTRQDSIDRIVAAAVERFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMF-SIFRLTKDALMLLRAAENPAIINVASIA-----ALIpsvgqANYS 161
Cdd:PRK07067   80 GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKgLFFLMQAVARHMVEQGRGGKIINMASQAgrrgeALV-----SHYC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR-----------AVVRAVTSTIPLRRLGKCEEVANTIVF 230
Cdd:PRK07067  155 ATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVDAlfaryenrppgEKKRLVGEAVPLGRMGVPDDLTGMALF 234
                         250       260
                  ....*....|....*....|..
gi 1447699393 231 LSSSASSYIVGQTIVIDGGLVM 252
Cdd:PRK07067  235 LASADADYIVAQTYNVDGGNWM 256
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
12-249 3.26e-36

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: 128.16  E-value: 3.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDElNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:cd05357    81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 171 TRTLAAEMAPwGVRVNAVAPGMIESKMvkKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSsaSSYIVGQTIVIDGG 249
Cdd:cd05357   161 TRSAALELAP-NIRVNGIAPGLILLPE--DMDAEYRENALRKVPLKRRPSAEEIADAVIFLLD--SNYITGQIIKVDGG 234
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
13-202 4.33e-36

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: 128.13  E-value: 4.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKA-SHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKV-VILDINEKGAEETANnVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:cd05339    80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1447699393 172 RTLAAEMAPW---GVRVNAVAPGMIESKMVKKVS 202
Cdd:cd05339   160 ESLRLELKAYgkpGIKTTLVCPYFINTGMFQGVK 193
PRK07814 PRK07814
SDR family oxidoreductase;
9-252 6.26e-36

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 128.36  E-value: 6.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTES-QLDEVAEQiRAAGRRAHVVAADLAHPEATAGLAGQAVEAFG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL-MLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK07814   87 RLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVpLMLEHSGGGSVINISSTMGRLAGRGFAAYGTAKAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPwGVRVNAVAPGMIESKMVKKVSR--AVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:PRK07814  167 LAHYTRLAALDLCP-RIRVNAIAPGSILTSALEVVAAndELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTL 245

                  ....*...
gi 1447699393 245 VIDGGLVM 252
Cdd:PRK07814  246 EVDGGLTF 253
PRK08265 PRK08265
short chain dehydrogenase; Provisional
8-249 1.43e-35

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 127.43  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHpaGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK08265    3 GLAGKVAIVTGGATLIGAAVARALVAAGARV-AIVDIDADNGAAVAASL--GERARFIATDITDDAAIERAVATVVARFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASmSYEDFTQVIETNMFSifrltkdALMLLRAAEN------PAIINVASIAALIPSVGQANYS 161
Cdd:PRK08265   80 RVDILVNLACTYLDDGLAS-SRADWLAALDVNLVS-------AAMLAQAAHPhlarggGAIVNFTSISAKFAQTGRWLYP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS---RAVVRAVTSTI-PLRRLGKCEEVANTIVFLSSSASS 237
Cdd:PRK08265  152 ASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSggdRAKADRVAAPFhLLGRVGDPEEVAQVVAFLCSDAAS 231
                         250
                  ....*....|..
gi 1447699393 238 YIVGQTIVIDGG 249
Cdd:PRK08265  232 FVTGADYAVDGG 243
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
8-190 2.53e-35

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: 126.04  E-value: 2.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqLTALKASHPAgdkLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:COG3967     2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEK-LEEAAAANPG---LHTIVLDVADPASIAALAEQVTAEFP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFAS--MSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:COG3967    78 DLNVLINNAGIMRAEDLLDeaEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKA 157
                         170       180
                  ....*....|....*....|....*
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAP 190
Cdd:COG3967   158 ALHSYTQSLRHQLKDTSVKVIELAP 182
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
11-249 2.99e-35

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: 126.48  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHPAGD---KLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05330     3 DKVVLITGGGSGLGLATAVRLAKEGAKL-SLVDLNEEGLEAAKAALLEIApdaEVLLIKADVSDEAQVEAYVDATVEQFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIV-KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05330    82 RIDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMV----KKVS----RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:cd05330   162 VVGLTRNSAVEYGQYGIRINAIAPGAILTPMVegslKQLGpenpEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAGY 241
                         250
                  ....*....|.
gi 1447699393 239 IVGQTIVIDGG 249
Cdd:cd05330   242 VNAAVVPIDGG 252
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
11-253 3.16e-35

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: 126.42  E-value: 3.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKA-SHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:cd05337     1 RPVAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAeVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIV----KDSLfaSMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENP------AIINVASIAALIPSVGQAN 159
Cdd:cd05337    81 DCLVNNAGIAvrprGDLL--DLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRfdgphrSIIFVTSINAYLVSPNRGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTS-TIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:cd05337   159 YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAgLVPIRRWGQPEDIAKAVRTLASGLLPY 238
                         250
                  ....*....|....*
gi 1447699393 239 IVGQTIVIDGGLVMR 253
Cdd:cd05337   239 STGQPINIDGGLSMR 253
PRK09730 PRK09730
SDR family oxidoreductase;
12-249 3.35e-35

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 126.12  E-value: 3.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNdvqltaLKASHP-------AGDKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQN------LHAAQEvvnlitqAGGKAFVLQADISDENQVVAMFTAIDQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIV-KDSLFASMSYEDFTQVIETNMFSIFRLTKDAL--MLLR-AAENPAIINVASIAALIPSVGQ-AN 159
Cdd:PRK09730   76 HDEPLAALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCREAVkrMALKhGGSGGAIVNVSSAASRLGAPGEyVD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM------VKKVSRavvraVTSTIPLRRLGKCEEVANTIVFLSS 233
Cdd:PRK09730  156 YAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMhasggePGRVDR-----VKSNIPMQRGGQPEEVAQAIVWLLS 230
                         250
                  ....*....|....*.
gi 1447699393 234 SASSYIVGQTIVIDGG 249
Cdd:PRK09730  231 DKASYVTGSFIDLAGG 246
PRK07060 PRK07060
short chain dehydrogenase; Provisional
8-253 3.77e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 125.60  E-value: 3.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALykSNDVQLTALKASHPAGdklHIVQCDLACPQSVSAlceqIERQAG 87
Cdd:PRK07060    6 DFSGKSVLVTGASSGIGRACAVALAQRGARVVAA--ARNAAALDRLAGETGC---EPLRLDVGDDAAIRA----ALAAAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKD-ALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK07060   77 AFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHvARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRA-VTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:PRK07060  157 LDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAwSDPQKSGpMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSL 236

                  ....*....
gi 1447699393 245 VIDGGLVMR 253
Cdd:PRK07060  237 PVDGGYTAR 245
PRK07069 PRK07069
short chain dehydrogenase; Validated
15-250 7.55e-35

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 125.21  E-value: 7.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  15 LVTGASGDIGLGICEKYLEQNCDVYaLYKSNDVQ-LTALKASHPAGdklHIVQCDLACPQSVS------ALCEQIERQAG 87
Cdd:PRK07069    3 FITGAAGGLGRAIARRMAEQGAKVF-LTDINDAAgLDAFAAEINAA---HGEGVAFAAVQDVTdeaqwqALLAQAADAMG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK07069   79 GLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAP--WGVRVNAVAPGMIESKMVKKVS-----RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIV 240
Cdd:PRK07069  159 ASLTKSIALDCARrgLDVRCNSIHPTFIRTGIVDPIFqrlgeEEATRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVT 238
                         250
                  ....*....|
gi 1447699393 241 GQTIVIDGGL 250
Cdd:PRK07069  239 GAELVIDGGI 248
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
8-250 2.42e-34

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 124.02  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07097    7 SLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK07097   87 VIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRA--------VTSTIPLRRLGKCEEVANTIVFLSSSASSYI 239
Cdd:PRK07097  167 KMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGsrhpfdqfIIAKTPAARWGDPEDLAGPAVFLASDASNFV 246
                         250
                  ....*....|.
gi 1447699393 240 VGQTIVIDGGL 250
Cdd:PRK07097  247 NGHILYVDGGI 257
PRK07890 PRK07890
short chain dehydrogenase; Provisional
9-253 4.09e-34

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 123.53  E-value: 4.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07890    3 LKGKVVVVSGVGPGLGRTLAVRAARAGADV-VLAARTAERLDEVAAEiDDLGRRALAVPTDITDEDQCANLVALALERFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAgiVKDSLFASMSYEDFTQ---VIETNMFSIFRLTKDALMLLrAAENPAIINVASIAALIPSVGQANYSASK 164
Cdd:PRK07890   82 RVDALVNNA--FRVPSMKPLADADFAHwraVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK-----------KVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSS 233
Cdd:PRK07890  159 GALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfrhqagkygVTVEQIYAETAANSDLKRLPTDDEVASAVLFLAS 238
                         250       260
                  ....*....|....*....|
gi 1447699393 234 SASSYIVGQTIVIDGGLVMR 253
Cdd:PRK07890  239 DLARAITGQTLDVNCGEYHH 258
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-252 5.75e-34

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 123.15  E-value: 5.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLT-ALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK12745    1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAaTQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGI---VKDSLFAsMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAENPA----IINVASIAALIPSVGQAN 159
Cdd:PRK12745   81 IDCLVNNAGVgvkVRGDLLD-LTPESFDRVLAINLRGPFFLTQAVAkrMLAQPEPEELphrsIVFVSSVNAIMVSPNRGE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS-RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK12745  160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTaKYDALIAKGLVPMPRWGEPEDVARAVAALASGDLPY 239
                         250
                  ....*....|....
gi 1447699393 239 IVGQTIVIDGGLVM 252
Cdd:PRK12745  240 STGQAIHVDGGLSI 253
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
12-197 6.98e-34

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: 121.96  E-value: 6.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNcdvyalykSNDVQLTA------LKASH---PAGDKLHIVQCDLACPQSVSALCEQI 82
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSG--------PGTVILTArdvergQAAVEklrAEGLSVRFHQLDVTDDASIEAAADFV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIV-KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIpsvgQANYS 161
Cdd:cd05324    73 EEKYGGLDILVNNAGIAfKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSL----TSAYG 148
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:cd05324   149 VSKAALNALTRILAKELKETGIKVNACCPGWVKTDM 184
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-253 8.69e-34

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 122.29  E-value: 8.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksNDVQLT-ALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK08993    7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGI---NIVEPTeTIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKD-ALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK08993   84 GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAaAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVR--AVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:PRK08993  164 GVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRsaEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYT 243
                         250
                  ....*....|
gi 1447699393 244 IVIDGGLVMR 253
Cdd:PRK08993  244 IAVDGGWLAR 253
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
12-251 9.82e-34

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 128.42  E-value: 9.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTAL-KASHPAGDKLHI--VQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK08324  423 KVALVTGAAGGIGKATAKRLAAEGACVVLA----DLDEEAAeAAAAELGGPDRAlgVACDVTDEAAVQAAFEEAALAFGG 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENP-AIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK08324  499 VDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgSIVFIASKNAVNPGPNFGAYGAAKAAE 578
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAP-------GMIESKMVKKvsRAVVRAVTSTIP---------LRRLGKCEEVANTIVFL 231
Cdd:PRK08324  579 LHLVRQLALELGPDGIRVNGVNPdavvrgsGIWTGEWIEA--RAAAYGLSEEELeefyrarnlLKREVTPEDVAEAVVFL 656
                         250       260
                  ....*....|....*....|
gi 1447699393 232 SSSASSYIVGQTIVIDGGLV 251
Cdd:PRK08324  657 ASGLLSKTTGAIITVDGGNA 676
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
14-203 1.22e-33

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: 121.63  E-value: 1.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNC-DVYALYKSNDV--QLTALKASHPagdKLHIVQCDLACPQSVSAlcEQIER--QAGK 88
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNnTVIATCRDPSAatELAALGASHS---RLHILELDVTDEIAESA--EAVAErlGDAG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIV-KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIIN----VASIAAlIPSVGQANYSAS 163
Cdd:cd05325    76 LDVLINNAGILhSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINissrVGSIGD-NTSGGWYSYRAS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR 203
Cdd:cd05325   155 KAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAK 194
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
9-249 1.26e-33

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: 122.25  E-value: 1.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQlTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:cd08937     2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVH-EVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAG-IVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAalIPSVGQANYSASKGAI 167
Cdd:cd08937    81 VDVLINNVGgTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIA--TRGIYRIPYSAAKGGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKmVKKVSRA--------------VVRAVTSTIPLRRLGKCEEVANTIVFLSS 233
Cdd:cd08937   159 NALTASLAFEHARDGIRVNAVAPGGTEAP-PRKIPRNaapmseqekvwyqrIVDQTLDSSLMGRYGTIDEQVRAILFLAS 237
                         250
                  ....*....|....*.
gi 1447699393 234 SASSYIVGQTIVIDGG 249
Cdd:cd08937   238 DEASYITGTVLPVGGG 253
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
11-253 1.93e-33

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 121.68  E-value: 1.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGLGICEKYLEQNCDV-YALYKSNDVQLTALKASHPAG-DKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK12384    2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVaVADINSEKAANVAQEINAEYGeGMAYGFGADATSEQSVLALSRGVDEIFGR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDA--LMLLRAAENpAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK12384   82 VDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFsrLMIRDGIQG-RIIQINSKSGKVGSKHNSGYSAAKFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPG-MIESKM--------VKK--VSRAVVRAV-TSTIPLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK12384  161 GVGLTQSLALDLAEYGITVHSLMLGnLLKSPMfqsllpqyAKKlgIKPDEVEQYyIDKVPLKRGCDYQDVLNMLLFYASP 240
                         250
                  ....*....|....*....
gi 1447699393 235 ASSYIVGQTIVIDGGLVMR 253
Cdd:PRK12384  241 KASYCTGQSINVTGGQVMF 259
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
12-253 2.74e-33

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: 120.76  E-value: 2.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVyaLYKSNDVQLTALKAShPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd09761     2 KVAIVTGGGHGIGKQICLDFLEAGDKV--VFADIDEERGADFAE-AEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAaENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:cd09761    79 LVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIK-NKGRIINIASTRAFQSEPDSEAYAASKGGLVALT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 172 RTLAAEMAPWgVRVNAVAPGMIESKMVKKVSRAVVRAVT-STIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGL 250
Cdd:cd09761   158 HALAMSLGPD-IRVNCISPGWINTTEQQEFTAAPLTQEDhAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDGGM 236

                  ...
gi 1447699393 251 VMR 253
Cdd:cd09761   237 TKK 239
PRK06057 PRK06057
short chain dehydrogenase; Provisional
9-250 3.14e-33

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 120.99  E-value: 3.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVQLTALKAshpAGDKLH--IVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK06057    5 LAGRVAVITGGGSGIGLATARRLAAEGATVVV----GDIDPEAGKA---AADEVGglFVPTDVTDEDAVNALFDTAAETY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIV--KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPS-VGQANYSAS 163
Cdd:PRK06057   78 GSVDIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSaTSQISYTAS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-----SRAVVRAVtsTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK06057  158 KGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELfakdpERAARRLV--HVPMGRFAEPEEIAAAVAFLASDDASF 235
                         250
                  ....*....|..
gi 1447699393 239 IVGQTIVIDGGL 250
Cdd:PRK06057  236 ITASTFLVDGGI 247
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
7-253 3.44e-33

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 121.16  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK13394    3 SNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL-MLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK13394   83 GSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALkHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKK------------VSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSS 233
Cdd:PRK13394  163 GLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqipeqakelgisEEEVVKKVMLGKTVDGVFTTVEDVAQTVLFLSS 242
                         250       260
                  ....*....|....*....|
gi 1447699393 234 SASSYIVGQTIVIDGGLVMR 253
Cdd:PRK13394  243 FPSAALTGQSFVVSHGWFMQ 262
PRK07576 PRK07576
short chain dehydrogenase; Provisional
8-249 3.89e-33

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 120.83  E-value: 3.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSND-VQLTA--LKASHPAGDKlhiVQCDLACPQSVSALCEQIER 84
Cdd:PRK07576    6 DFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEkVDAAVaqLQQAGPEGLG---VSADVRDYAAVEAAFAQIAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAeNPAIINVASIAALIPSVGQANYSASK 164
Cdd:PRK07576   83 EFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRP-GASIIQISAPQAFVPMPMQAHVCAAK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESK--MVKKVSRAVVR-AVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK07576  162 AGVDMLTRTLALEWGPEGIRVNSIVPGPIAGTegMARLAPSPELQaAVAQSVPLKRNGTKQDIANAALFLASDMASYITG 241

                  ....*...
gi 1447699393 242 QTIVIDGG 249
Cdd:PRK07576  242 VVLPVDGG 249
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
8-249 7.15e-33

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 120.78  E-value: 7.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK08277    7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAG---------------IVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALI 152
Cdd:PRK08277   87 PCDILINGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 153 PSVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV---------SRAvvRAVTSTIPLRRLGKCEE 223
Cdd:PRK08277  167 PLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALlfnedgsltERA--NKILAHTPMGRFGKPEE 244
                         250       260
                  ....*....|....*....|....*..
gi 1447699393 224 VANTIVFL-SSSASSYIVGQTIVIDGG 249
Cdd:PRK08277  245 LLGTLLWLaDEKASSFVTGVVLPVDGG 271
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
8-249 2.03e-32

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: 118.73  E-value: 2.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPAgdkLHIVQCDLACPQSVsalcEQIERQAG 87
Cdd:cd05351     4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQA-DLDSLVRECPG---IEPVCVDLSDWDAT----EEALGSVG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENP-AIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05351    76 PVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPgSIVNVSSQASQRALTNHTVYCSTKAA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR--AVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTI 244
Cdd:cd05351   156 LDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSdpEKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTL 235

                  ....*
gi 1447699393 245 VIDGG 249
Cdd:cd05351   236 PVDGG 240
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
12-249 3.28e-32

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 118.17  E-value: 3.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQ-LTALKASHPAGdKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGaAAELQAINPKV-KATFVQCDVTSWEQLAAAFKKAIEKFGRVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIV--KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAA---ENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:cd05323    80 ILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLYPAPQFPVYSASKH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEM-APWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIplrrLGKCEEVANTIVFLSSSASSYivGQTI 244
Cdd:cd05323   160 GVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAP----TQSPEVVAKAIVYLIEDDEKN--GAIW 233

                  ....*
gi 1447699393 245 VIDGG 249
Cdd:cd05323   234 IVDGG 238
PRK07074 PRK07074
SDR family oxidoreductase;
12-250 5.19e-32

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 117.95  E-value: 5.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKA--SHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK07074    3 RTALVTGAAGGIGQALARRFLAAGDRVLAL----DIDAAALAAfaDALGDARFVPVACDLTDAASLAAALANAAAERGPV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVkdslfASMSYEDFTQVI-----ETNMFSIFRLTKDALMLLRAAENPAIINVASIAALiPSVGQANYSASK 164
Cdd:PRK07074   79 DVLVANAGAA-----RAASLHDTTPASwradnALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGM-AALGHPAYSAAK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA---VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVG 241
Cdd:PRK07074  153 AGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAAnpqVFEELKKWYPLQDFATPDDVANAVLFLASPAARAITG 232

                  ....*....
gi 1447699393 242 QTIVIDGGL 250
Cdd:PRK07074  233 VCLPVDGGL 241
PRK06128 PRK06128
SDR family oxidoreductase;
9-250 5.41e-32

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 118.81  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALY----KSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK06128   53 LQGRKALITGADSGIGRATAIAFAREGADIALNYlpeeEQDAAEVVQLIQA--EGRKAVALPGDLKDEAFCRQLVERAVK 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAG---IVKDslFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAenPAIINVASIAALIPSVGQANYS 161
Cdd:PRK06128  131 ELGGLDILVNIAGkqtAVKD--IADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG--ASIINTGSIQSYQPSPTLLDYA 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKK--VSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYI 239
Cdd:PRK06128  207 STKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSggQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQESSYV 286
                         250
                  ....*....|.
gi 1447699393 240 VGQTIVIDGGL 250
Cdd:PRK06128  287 TGEVFGVTGGL 297
PRK06125 PRK06125
short chain dehydrogenase; Provisional
8-250 1.65e-31

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 116.68  E-value: 1.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALK----ASHPAGDKLHIVqcDLACPQSVsalcEQIE 83
Cdd:PRK06125    4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHL-HLVARDADALEALAadlrAAHGVDVAVHAL--DLSSPEAR----EQLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  84 RQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPsvgQANY--- 160
Cdd:PRK06125   77 AEAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENP---DADYicg 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRavVRAVT------------STIPLRRLGKCEEVANTI 228
Cdd:PRK06125  154 SAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLK--GRARAelgdesrwqellAGLPLGRPATPEEVADLV 231
                         250       260
                  ....*....|....*....|..
gi 1447699393 229 VFLSSSASSYIVGQTIVIDGGL 250
Cdd:PRK06125  232 AFLASPRSGYTSGTVVTVDGGI 253
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
12-249 1.76e-31

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: 116.34  E-value: 1.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKASHPA---GDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAEGAAVVVA----DIDPEIAEKVAEAaqgGPRALGVQCDVTSEAQVQSAFEQAVLEFGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAE-NPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd08943    78 LDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNAAAYSAAKAAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAP-----GMIESKMVKKVSRAVVRA------VTSTIpLRRLGKCEEVANTIVFLSSSAS 236
Cdd:cd08943   158 AHLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWRAARAKAYGlleeeyRTRNL-LKREVLPEDVAEAVVAMASEDF 236
                         250
                  ....*....|...
gi 1447699393 237 SYIVGQTIVIDGG 249
Cdd:cd08943   237 GKTTGAIVTVDGG 249
PRK06123 PRK06123
SDR family oxidoreductase;
12-249 4.39e-31

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 115.26  E-value: 4.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:PRK06123    3 KVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAiRRQGGEALAVAADVADEADVLRLFEAVDRELGRLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSL-FASMSYEDFTQVIETNMFSIFRLTKDAL--MLLR-AAENPAIINVASIAALIPSVGQ-ANYSASKG 165
Cdd:PRK06123   83 ALVNNAGILEAQMrLEQMDAARLTRIFATNVVGSFLCAREAVkrMSTRhGGRGGAIVNVSSMAARLGSPGEyIDYAASKG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKM------VKKVSRavvraVTSTIPLRRLGKCEEVANTIVFLSSSASSYI 239
Cdd:PRK06123  163 AIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIhasggePGRVDR-----VKAGIPMGRGGTAEEVARAILWLLSDEASYT 237
                         250
                  ....*....|
gi 1447699393 240 VGQTIVIDGG 249
Cdd:PRK06123  238 TGTFIDVSGG 247
PRK06179 PRK06179
short chain dehydrogenase; Provisional
10-229 4.63e-31

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 115.77  E-value: 4.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYAlyKSNDVQltalKASHPAGDKLhiVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK06179    3 NSKVALVTGASSGIGRATAEKLARAGYRVFG--TSRNPA----RAAPIPGVEL--LELDVTDDASVQAAVDEVIARAGRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIvkdSLFASM---SYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK06179   75 DVLVNNAGV---GLAGAAeesSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKM----------------VKKVSRAVVRAVTSTIPLRrlgkcEEVANTIV 229
Cdd:PRK06179  152 VEGYSESLDHEVRQFGIRVSLVEPAYTKTNFdanapepdsplaeydrERAVVSKAVAKAVKKADAP-----EVVADTVV 225
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
11-250 1.47e-30

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 114.05  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGLGICEKYLEQNCDVYALY-KSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK08063    4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNYaRSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNA--GIVKDSLFASMSYEDFTqvIETNMFSIFRLTKDALMLLRAAENPAIINVASIAAL--IPsvgqaNYSA--- 162
Cdd:PRK08063   84 DVFVNNAasGVLRPAMELEESHWDWT--MNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIryLE-----NYTTvgv 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA--VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIV 240
Cdd:PRK08063  157 SKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNReeLLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIR 236
                         250
                  ....*....|
gi 1447699393 241 GQTIVIDGGL 250
Cdd:PRK08063  237 GQTIIVDGGR 246
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
87-249 1.77e-30

(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: 113.57  E-value: 1.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05353    87 GRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAAKLG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPgMIESKMVKKVSRAvvravtstiPLRRLGKCEEVANTIVFLsSSASSYIVGQTIVI 246
Cdd:cd05353   167 LLGLSNTLAIEGAKYNITCNTIAP-AAGSRMTETVMPE---------DLFDALKPEYVAPLVLYL-CHESCEVTGGLFEV 235

                  ...
gi 1447699393 247 DGG 249
Cdd:cd05353   236 GAG 238
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
12-249 2.50e-30

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: 113.78  E-value: 2.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVyaLYKSNDVQL-----TALKASHPAGDKLhiVQCDLACPQSVSALCEQIERQA 86
Cdd:cd08933    10 KVVIVTGGSRGIGRGIVRAFVENGAKV--VFCARGEAAgqaleSELNRAGPGSCKF--VPCDVTKEEDIKTLISVTVERF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGI-VKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENpaiiNVASIAALIPSVGQAN---YSA 162
Cdd:cd08933    86 GRIDCLVNNAGWhPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQG----NIINLSSLVGSIGQKQaapYVA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS------RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSAs 236
Cdd:cd08933   162 TKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAaqtpdtLATIKEGELAQLLGRMGTEAESGLAALFLAAEA- 240
                         250
                  ....*....|...
gi 1447699393 237 SYIVGQTIVIDGG 249
Cdd:cd08933   241 TFCTGIDLLLSGG 253
PRK08267 PRK08267
SDR family oxidoreductase;
12-228 2.60e-30

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 113.49  E-value: 2.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHPAGDkLHIVQCDLACPQSVSALCEQI-ERQAGKID 90
Cdd:PRK08267    2 KSIFITGAASGIGRATALLFAAEGWRV-GAYDINEAGLAALAAELGAGN-AWTGALDVTDRAAWDAALADFaAATGGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:PRK08267   80 VLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGkcEEVANTI 228
Cdd:PRK08267  160 TEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTKRLGVRLTP--EDVAEAV 215
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
9-253 3.98e-30

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 113.13  E-value: 3.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHpaGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK06200    4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAE-KLASLRQRF--GDHVLVVEGDVTSYADNQRAVDQTVDAFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSL-FASMSYED----FTQVIETNMFSIFRLTKDALMLLRAAeNPAIINVASIAALIPSVGQANYSAS 163
Cdd:PRK06200   81 LDCFVGNAGIWDYNTsLVDIPAETldtaFDEIFNVNVKGYLLGAKAALPALKAS-GGSMIFTLSNSSFYPGGGGPLYTAS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPwGVRVNAVAPGMIESKM---------VKKVSRAVVRA--VTSTIPLRRLGKCEEVANTIVFLS 232
Cdd:PRK06200  160 KHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLrgpaslgqgETSISDSPGLAdmIAAITPLQFAPQPEDHTGPYVLLA 238
                         250       260
                  ....*....|....*....|..
gi 1447699393 233 SSA-SSYIVGQTIVIDGGLVMR 253
Cdd:PRK06200  239 SRRnSRALTGVVINADGGLGIR 260
PRK06114 PRK06114
SDR family oxidoreductase;
8-251 3.98e-30

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 112.95  E-value: 3.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYAL-YKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK06114    5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFdLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVG--QANYSASK 164
Cdd:PRK06114   85 GALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllQAHYNASK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA-VVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:PRK06114  165 AGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVhQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVD 244

                  ....*...
gi 1447699393 244 IVIDGGLV 251
Cdd:PRK06114  245 LLVDGGFV 252
PRK07791 PRK07791
short chain dehydrogenase; Provisional
87-251 6.91e-30

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 112.84  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAE------NPAIINVASIAALIPSVGQANY 160
Cdd:PRK07791   91 GGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAESkagravDARIINTSSGAGLQGSVGQGNY 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAP----GMIESKMVKKVSRAVVRAVTSTIPlrrlgkcEEVANTIVFLSSSAS 236
Cdd:PRK07791  171 SAAKAGIAALTLVAAAELGRYGVTVNAIAPaartRMTETVFAEMMAKPEEGEFDAMAP-------ENVSPLVVWLGSAES 243
                         170
                  ....*....|....*
gi 1447699393 237 SYIVGQTIVIDGGLV 251
Cdd:PRK07791  244 RDVTGKVFEVEGGKI 258
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-251 8.15e-30

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 112.19  E-value: 8.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGAS--GDIGLGICEKYLEQNCDVYALYKSN-DVQLT-ALKASHPA---------GDKLHIVQCDLACPQ 73
Cdd:PRK12859    2 NQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTYWTAyDKEMPwGVDQDEQIqlqeellknGVKVSSMELDLTQND 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  74 SVSALCEQIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIP 153
Cdd:PRK12859   82 APKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 154 SVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESK-MVKKVSRAVVravtSTIPLRRLGKCEEVANTIVFLS 232
Cdd:PRK12859  162 MVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTEEIKQGLL----PMFPFGRIGEPKDAARLIKFLA 237
                         250
                  ....*....|....*....
gi 1447699393 233 SSASSYIVGQTIVIDGGLV 251
Cdd:PRK12859  238 SEEAEWITGQIIHSEGGFK 256
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
12-209 8.71e-30

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: 111.34  E-value: 8.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNC-DVYALYKSNDvQLTALKASHpaGDKLHIVQCDLACPQSVSALCEQierqAGKID 90
Cdd:cd05354     4 KTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPG-SAAHLVAKY--GDKVVPLRLDVTDPESIKAAAAQ----AKDVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVK-DSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILG 169
Cdd:cd05354    77 VVINNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1447699393 170 FTRTLAAEMAPWGVRVNAVAPGMIESKMVKK----------VSRAVVRAV 209
Cdd:cd05354   157 LTQGLRAELAAQGTLVLSVHPGPIDTRMAAGaggpkespetVAEAVLKAL 206
PRK08264 PRK08264
SDR family oxidoreductase;
8-199 1.85e-29

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 110.75  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCD-VYAlyksndvqlTA--LKASHPAGDKLHIVQCDLACPQSVSALCEQier 84
Cdd:PRK08264    3 DIKGKVVLVTGANRGIGRAFVEQLLARGAAkVYA---------AArdPESVTDLGPRVVPLQLDVTDPASVAAAAEA--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 qAGKIDVLVNNAGIVK-DSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSAS 163
Cdd:PRK08264   71 -ASDVTILVNNAGIFRtGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSAS 149
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK 199
Cdd:PRK08264  150 KAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA 185
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
9-250 2.60e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 110.61  E-value: 2.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVqlTALKASHPA------GDKLHIVQCDLACPQSVSALCEQI 82
Cdd:PRK08085    7 LAGKNILITGSAQGIGFLLATGLAEYGAEIII----NDI--TAERAELAVaklrqeGIKAHAAPFNVTHKQEVEAAIEHI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSA 162
Cdd:PRK08085   81 EKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIV 240
Cdd:PRK08085  161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALveDEAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVN 240
                         250
                  ....*....|
gi 1447699393 241 GQTIVIDGGL 250
Cdd:PRK08085  241 GHLLFVDGGM 250
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
3-253 2.68e-29

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


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 110.71  E-value: 2.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   3 MYKYNDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQI 82
Cdd:cd08936     2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIvkDSLFASM---SYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQAN 159
Cdd:cd08936    82 VNLHGGVDILVSNAAV--NPFFGNIldsTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASS 237
Cdd:cd08936   160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALwmDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDAS 239
                         250
                  ....*....|....*.
gi 1447699393 238 YIVGQTIVIDGGLVMR 253
Cdd:cd08936   240 YITGETVVVGGGTPSR 255
PRK06949 PRK06949
SDR family oxidoreductase;
8-251 3.44e-29

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 110.62  E-value: 3.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK06949    6 NLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVE-RLKELRAEiEAEGGAAHVVSLDVTDYQSIKAAVAHAETEA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAENPA------IINVASIAAL--IPSVG 156
Cdd:PRK06949   85 GTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAkrMIARAKGAGNtkpggrIINIASVAGLrvLPQIG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 157 QanYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSA 235
Cdd:PRK06949  165 L--YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHwETEQGQKLVSMLPRKRVGKPEDLDGLLLLLAADE 242
                         250
                  ....*....|....*.
gi 1447699393 236 SSYIVGQTIVIDGGLV 251
Cdd:PRK06949  243 SQFINGAIISADDGFG 258
PRK07985 PRK07985
SDR family oxidoreductase;
9-249 3.57e-29

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 111.24  E-value: 3.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALY---KSNDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK07985   47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYlpvEEEDAQDVK-KIIEECGRKAVLLPGDLSDEKFARSLVHEAHKA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAG---IVKDslFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAEnpAIINVASIAALIPSVGQANYSA 162
Cdd:PRK07985  126 LGGLDIMALVAGkqvAIPD--IADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGA--SIITTSSIQAYQPSPHLLDYAA 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIES--KMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIV 240
Cdd:PRK07985  202 TKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTalQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYVT 281

                  ....*....
gi 1447699393 241 GQTIVIDGG 249
Cdd:PRK07985  282 AEVHGVCGG 290
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
12-233 3.69e-29

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: 110.06  E-value: 3.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPA--GDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAE-RLQELADELGAkfPVKVLPLQLDVSDRESIEAALENLPEEFRDI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVK--DSLfASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd05346    80 DILVNNAGLALglDPA-QEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESK--MV-----KKVSRAVVRAVTSTIPlrrlgkcEEVANTIVFLSS 233
Cdd:cd05346   159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEfsLVrfhgdKEKADKVYEGVEPLTP-------EDIAETILWVAS 224
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
8-250 6.17e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 109.86  E-value: 6.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHP-AGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK07523    7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEV-ILNGRDPAKLAAAAESLKgQGLSAHALAFDVTDHDAVRAAIDAFEAEI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAENpaIINVASIAALIPSVGQANYSASK 164
Cdd:PRK07523   86 GPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVArhMIARGAGK--IINIASVQSALARPGIAPYTATK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMvkkvSRAVVRA------VTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK07523  164 GAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPL----NAALVADpefsawLEKRTPAGRWGKVEELVGACVFLASDASSF 239
                         250
                  ....*....|..
gi 1447699393 239 IVGQTIVIDGGL 250
Cdd:PRK07523  240 VNGHVLYVDGGI 251
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-249 8.27e-29

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 109.43  E-value: 8.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVY--ALYKSNDVQLTaLKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK06077    3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnAKKRAEEMNET-LKMVKENGGEGIGVLADVSTREGCETLAKATIDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK06077   82 YGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMR--EGGAIVNIASVAGIRPAYGLSIYGAMKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPwGVRVNAVAPGMIESKM---VKKVSRAVVRAVTSTIPLrrLGKC---EEVANTIVFLSSSASsyI 239
Cdd:PRK06077  160 AVINLTKYLALELAP-KIRVNAIAPGFVKTKLgesLFKVLGMSEKEFAEKFTL--MGKIldpEEVAEFVAAILKIES--I 234
                         250
                  ....*....|
gi 1447699393 240 VGQTIVIDGG 249
Cdd:PRK06077  235 TGQVFVLDSG 244
PRK07454 PRK07454
SDR family oxidoreductase;
12-191 9.71e-29

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 108.89  E-value: 9.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:PRK07454    7 PRALITGASSGIGKATALAFAKAGWDLALVARSQD-ALEALAAElRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:PRK07454   86 VLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165
                         170       180
                  ....*....|....*....|.
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPG 191
Cdd:PRK07454  166 TKCLAEEERSHGIRVCTITLG 186
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-249 1.01e-28

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 109.39  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGAS--GDIGLGICEKYLEQNCDVYALY-------------KSNDVQLTALKASHpaGDKLHIVQCDLACPQ 73
Cdd:PRK12748    3 LMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYwspydktmpwgmhDKEPVLLKEEIESY--GVRCEHMEIDLSQPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  74 SVSALCEQIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKdalMLLRAAENPA---IINVASIAA 150
Cdd:PRK12748   81 APNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSS---AFAKQYDGKAggrIINLTSGQS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 151 LIPSVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESK-MVKKVSRAVVRAvtstIPLRRLGKCEEVANTIV 229
Cdd:PRK12748  158 LGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGwITEELKHHLVPK----FPQGRVGEPVDAARLIA 233
                         250       260
                  ....*....|....*....|
gi 1447699393 230 FLSSSASSYIVGQTIVIDGG 249
Cdd:PRK12748  234 FLVSEEAKWITGQVIHSEGG 253
PRK09186 PRK09186
flagellin modification protein A; Provisional
9-249 1.10e-28

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 109.31  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVQLTALKA------SHPAGDKLHIVQCDLACPQSVSALCEQI 82
Cdd:PRK09186    2 LKGKTILITGAGGLIGSALVKAILEAGGIVIA----ADIDKEALNElleslgKEFKSKKLSLVELDITDQESLEEFLSKS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIVKDS---LFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALI------- 152
Cdd:PRK09186   78 AEKYGKIDGAVNCAYPRNKDygkKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVapkfeiy 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 153 ---PSVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAvVRAVTSTIPLRrlgKCEEVANTIV 229
Cdd:PRK09186  158 egtSMTSPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFLNA-YKKCCNGKGML---DPDDICGTLV 233
                         250       260
                  ....*....|....*....|
gi 1447699393 230 FLSSSASSYIVGQTIVIDGG 249
Cdd:PRK09186  234 FLLSDQSKYITGQNIIVDDG 253
PRK05650 PRK05650
SDR family oxidoreductase;
14-191 1.44e-28

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 108.97  E-value: 1.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTA-LKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVL 92
Cdd:PRK05650    3 VMITGAASGLGRAIALRWAREGWRL-ALADVNEEGGEEtLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTR 172
Cdd:PRK05650   82 VNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSE 161
                         170
                  ....*....|....*....
gi 1447699393 173 TLAAEMAPWGVRVNAVAPG 191
Cdd:PRK05650  162 TLLVELADDEIGVHVVCPS 180
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
12-252 1.84e-28

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: 108.71  E-value: 1.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYAL-YKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:cd05322     3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVAdINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKD-ALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILG 169
Cdd:cd05322    83 LLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREfSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 170 FTRTLAAEMAPWGVRVNAVAPG------MIES---KMVKKVS---RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASS 237
Cdd:cd05322   163 LTQSLALDLAEHGITVNSLMLGnllkspMFQSllpQYAKKLGikeSEVEQYYIDKVPLKRGCDYQDVLNMLLFYASPKAS 242
                         250
                  ....*....|....*
gi 1447699393 238 YIVGQTIVIDGGLVM 252
Cdd:cd05322   243 YCTGQSINITGGQVM 257
PRK07326 PRK07326
SDR family oxidoreductase;
9-191 1.85e-28

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 108.17  E-value: 1.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK07326    4 LKGKVALITGGSKGIGFAIAEALLAEGYKV-AITARDQKELEEAAAELNNKGNVLGLAADVRDEADVQRAVDAIVAAFGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENpAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:PRK07326   83 LDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGG-YIINISSLAGTNFFAGGAAYNASKFGLV 161
                         170       180
                  ....*....|....*....|...
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPG 191
Cdd:PRK07326  162 GFSEAAMLDLRQYGIKVSTIMPG 184
PRK06198 PRK06198
short chain dehydrogenase; Provisional
7-247 2.83e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 108.17  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK06198    2 GRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEAlGAKAVFVQADLSDVEDCRRVVAAADEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENP-AIINVASIAALipsVGQ---ANYS 161
Cdd:PRK06198   82 FGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEgTIVNIGSMSAH---GGQpflAAYC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRA-------VTSTIPLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK06198  159 ASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIQREFHGApddwlekAAATQPFGRLLDPDEVARAVAFLLSD 238
                         250
                  ....*....|...
gi 1447699393 235 ASSYIVGQTIVID 247
Cdd:PRK06198  239 ESGLMTGSVIDFD 251
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
9-229 2.96e-28

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: 108.06  E-value: 2.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKAS--HPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARL-VLSARREERLEEVKSEclELGAPSPHVVPLDMSDLEDAEQVVEEALKLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05332    80 GGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAV-TSTIPLRRLGKCEEVANTIV 229
Cdd:cd05332   160 LQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSaKMDDTTANGMSPEECALEIL 223
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
8-197 3.04e-28

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: 107.39  E-value: 3.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqLTALKASHPAgdkLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05370     2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREER-LAEAKKELPN---IHTIVLDVGDAESVEALAEALLSEYP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFA--SMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:cd05370    78 NLDILINNAGIQRPIDLRdpASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKA 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:cd05370   158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTEL 189
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
12-252 5.42e-28

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: 107.70  E-value: 5.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTA---LKASHPaGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAaaeIKKETG-NAKVEVIQLDLSSLASVRQFAEEFLARFPR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVkdSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQAN--------- 159
Cdd:cd05327    81 LDILINNAGIM--APPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDFNDldlennkey 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 -----YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-SRAVVRAVtstipLRRLGK--CEEVANTIVFL 231
Cdd:cd05327   159 spykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNgSFFLLYKL-----LRPFLKksPEQGAQTALYA 233
                         250       260
                  ....*....|....*....|.
gi 1447699393 232 SSSASSYIVGQTIVIDGGLVM 252
Cdd:cd05327   234 ATSPELEGVSGKYFSDCKIKM 254
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
8-253 1.17e-27

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: 106.28  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHpaGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05348     1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAE-KVAELRADF--GDAVVGVEGDVRSLADNERAVARCVERFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSL-FASMSYED----FTQVIETNMFSIFRLTKDALMLLRAAENPAIINVaSIAALIPSVGQANYSA 162
Cdd:cd05348    78 KLDCFIGNAGIWDYSTsLVDIPEEKldeaFDELFHINVKGYILGAKAALPALYATEGSVIFTV-SNAGFYPGGGGPLYTA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWgVRVNAVAPGMIESKM----------VKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLS 232
Cdd:cd05348   157 SKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLrgpaslgqgeTSISTPPLDDMLKSILPLGFAPEPEDYTGAYVFLA 235
                         250       260
                  ....*....|....*....|..
gi 1447699393 233 SSASS-YIVGQTIVIDGGLVMR 253
Cdd:cd05348   236 SRGDNrPATGTVINYDGGMGVR 257
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
12-249 1.22e-27

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 106.57  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK12823    9 KVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVA-AELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNN-AGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAAliPSVGQANYSASKGAILGF 170
Cdd:PRK12823   88 LINNvGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIAT--RGINRVPYSAAKGGVNAL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIE-------------SKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASS 237
Cdd:PRK12823  166 TASLAFEYAEHGIRVNAVAPGGTEapprrvprnaapqSEQEKAWYQQIVDQTLDSSLMKRYGTIDEQVAAILFLASDEAS 245
                         250
                  ....*....|..
gi 1447699393 238 YIVGQTIVIDGG 249
Cdd:PRK12823  246 YITGTVLPVGGG 257
PRK08219 PRK08219
SDR family oxidoreductase;
12-201 2.65e-27

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 104.63  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNcDVYALYKSNDvQLTALKASHPAgdkLHIVQCDLACPQSVSALCEQIERqagkIDV 91
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAPTH-TLLLGGRPAE-RLDELAAELPG---ATPFPVDLTDPEAIAAAVEQLGR----LDV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAI-INvaSIAALIPSVGQANYSASKGAILGF 170
Cdd:PRK08219   75 LVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVfIN--SGAGLRANPGWGSYAASKFALRAL 152
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699393 171 TRTLAAEMAPwGVRVNAVAPGMIESKMVKKV 201
Cdd:PRK08219  153 ADALREEEPG-NVRVTSVHPGRTDTDMQRGL 182
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
65-251 7.39e-27

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: 104.11  E-value: 7.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  65 VQCDLACPQSVSALCEQI-ERQAGKIDVLVNNAGiVKDSLFASMsyedftqVIETNMFSIFRLTKDALMLLRAAENPAII 143
Cdd:cd05328    36 VIADLSTPEGRAAAIADVlARCSGVLDGLVNCAG-VGGTTVAGL-------VLKVNYFGLRALMEALLPRLRKGHGPAAV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 144 NVASIAAL---------------------------IPSVGQANYSASKGAILGFTRTLAAE-MAPWGVRVNAVAPGMIES 195
Cdd:cd05328   108 VVSSIAGAgwaqdklelakalaagtearavalaehAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVET 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 196 KMVKKvSRAVVRAVTST----IPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGLV 251
Cdd:cd05328   188 PILQA-FLQDPRGGESVdafvTPMGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGLD 246
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
12-204 8.01e-27

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: 103.69  E-value: 8.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGiCEKYLEQNCDVYALYKSNDVQLTALKASHPAGDkLHIVQCDLACPQS-VSALCEQIERQAGKID 90
Cdd:cd08931     1 KAIFITGAASGIGRE-TALLFARNGWFVGLYDIDEDGLAALAAELGAEN-VVAGALDVTDRAAwAAALADFAAATGGRLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:cd08931    79 ALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGL 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1447699393 171 TRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA 204
Cdd:cd08931   159 TEALDVEWARHGIRVADVWPWFVDTPILTKGETG 192
PRK06181 PRK06181
SDR family oxidoreductase;
12-199 1.02e-26

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 103.90  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALK---ASHpaGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK06181    2 KVVIITGASEGIGRALAVRLARAGAQL-VLAARNETRLASLAqelADH--GGEALVVPTDVSDAEACERLIEAAVARFGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMS-YEDFTQVIETNMFSIFRLTKDALMLLRAAENpAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK06181   79 IDILVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASRG-QIVVVSSLAGLTGVPTRSGYAASKHAL 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK 199
Cdd:PRK06181  158 HGFFDSLRIELADDGVAVTVVCPGFVATDIRK 189
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
9-193 1.07e-26

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: 103.63  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVY--------ALYKSND-----VQLTAlKASHPAGDKLHIVQCDLACPQSV 75
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVvaaktaseGDNGSAKslpgtIEETA-EEIEAAGGQALPIVVDVRDEDQV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  76 SALCEQIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSV 155
Cdd:cd05338    80 RALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1447699393 156 GQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMI 193
Cdd:cd05338   160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTA 197
PRK05717 PRK05717
SDR family oxidoreductase;
10-250 1.96e-26

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 103.05  E-value: 1.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVyaLYKSNDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK05717    9 NGRVALVTGAARGIGLGIAAWLIAEGWQV--VLADLDRERGS-KVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIV--KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAaENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK05717   86 DALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRA-HNGAIVNLASTRARQSEPDTEAYAASKGGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 168 LGFTRTLAAEMAPwGVRVNAVAPGMIESK-MVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVI 246
Cdd:PRK05717  165 LALTHALAISLGP-EIRVNAVSPGWIDARdPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVV 243

                  ....
gi 1447699393 247 DGGL 250
Cdd:PRK05717  244 DGGM 247
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
13-201 2.81e-26

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: 102.36  E-value: 2.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLE--QNCDVYALYKSNDvQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKrgSPSVVVLLARSEE-PLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKD-SLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENP-AIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:cd05367    80 LLINNAGSLGPvSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKkTVVNVSSGAAVNPFKGWGLYCSSKAARD 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1447699393 169 GFTRTLAAEMApwGVRVNAVAPGMIESKMVKKV 201
Cdd:cd05367   160 MFFRVLAAEEP--DVRVLSYAPGVVDTDMQREI 190
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-251 3.81e-26

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 103.71  E-value: 3.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGdiGLGICEkyleqncdVYALYKS------NDVQlTALKAS------HPAGDKLHIVQCDLACPQS 74
Cdd:PRK07792    8 TDLSGKVAVVTGAAA--GLGRAE--------ALGLARLgatvvvNDVA-SALDASdvldeiRAAGAKAVAVAGDISQRAT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  75 VSALCEQIErQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPA-------IINVAS 147
Cdd:PRK07792   77 ADELVATAV-GLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKAAggpvygrIVNTSS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 148 IAALIPSVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPgMIESKMVKKVSRAVVRAVTSTI-PLrrlgKCEEVAN 226
Cdd:PRK07792  156 EAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICP-RARTAMTADVFGDAPDVEAGGIdPL----SPEHVVP 230
                         250       260
                  ....*....|....*....|....*
gi 1447699393 227 TIVFLSSSASSYIVGQTIVIDGGLV 251
Cdd:PRK07792  231 LVQFLASPAAAEVNGQVFIVYGPMV 255
PRK07478 PRK07478
short chain dehydrogenase; Provisional
7-249 4.16e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 102.32  E-value: 4.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:PRK07478    2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQA-ELDQLVAEiRAEGGEAVALAGDVRDEAYAKALVALAVER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 AGKIDVLVNNAGIVKDSL-FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASI---AALIPsvGQANYS 161
Cdd:PRK07478   81 FGGLDIAFNNAGTLGEMGpVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFvghTAGFP--GMAAYA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV-----SRAVVRAVTstiPLRRLGKCEEVANTIVFLSSSAS 236
Cdd:PRK07478  159 ASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMgdtpeALAFVAGLH---ALKRMAQPEEIAQAALFLASDAA 235
                         250
                  ....*....|...
gi 1447699393 237 SYIVGQTIVIDGG 249
Cdd:PRK07478  236 SFVTGTALLVDGG 248
PRK07825 PRK07825
short chain dehydrogenase; Provisional
8-229 5.16e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 102.33  E-value: 5.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALyksNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07825    2 DLRGKVVAITGGARGIGLATARALAALGARV-AI---GDLDEALAKETAAELGLVVGGPLDVTDPASFAAFLDAVEADLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAENpaIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK07825   78 PIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAprMVPRGRGH--VVNVASLAGKIPVPGMATYCASKH 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVkkvsravvrAVTSTIPLRRLGKCEEVANTIV 229
Cdd:PRK07825  156 AVVGFTDAARLELRGTGVHVSVVLPSFVNTELI---------AGTGGAKGFKNVEPEDVAAAIV 210
PRK07677 PRK07677
short chain dehydrogenase; Provisional
12-249 5.94e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 101.68  E-value: 5.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK07677    2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAG---IVKDSlfaSMSYEDFTQVIETNMFSIFRLTkdalmllRAAEN--------PAIINVASIAALIPSVGQANY 160
Cdd:PRK07677   82 LINNAAgnfICPAE---DLSVNGWNSVIDIVLNGTFYCS-------QAVGKywiekgikGNIINMVATYAWDAGPGVIHS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 161 SASKGAILGFTRTLAAEmapWG----VRVNAVAPGMIE-----SKMVKkvSRAVVRAVTSTIPLRRLGKCEEVANTIVFL 231
Cdd:PRK07677  152 AAAKAGVLAMTRTLAVE---WGrkygIRVNAIAPGPIErtggaDKLWE--SEEAAKRTIQSVPLGRLGTPEEIAGLAYFL 226
                         250
                  ....*....|....*...
gi 1447699393 232 SSSASSYIVGQTIVIDGG 249
Cdd:PRK07677  227 LSDEAAYINGTCITMDGG 244
PRK05693 PRK05693
SDR family oxidoreductase;
12-217 1.92e-25

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 101.02  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYA-LYKSNDVQltALKAshpAGdkLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:PRK05693    2 PVVLITGCSSGIGRALADAFKAAGYEVWAtARKAEDVE--ALAA---AG--FTAVQLDVNDGAALARLAEELEAEHGGLD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGivkdslFASMS------YEDFTQVIETNMFSIFRLTKDALMLLRAAENpAIINVASIAALIPSVGQANYSASK 164
Cdd:PRK05693   75 VLINNAG------YGAMGplldggVEAMRRQFETNVFAVVGVTRALFPLLRRSRG-LVVNIGSVSGVLVTPFAGAYCASK 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR---AVVRAVTSTIPLRR 217
Cdd:PRK05693  148 AAVHALSDALRLELAPFGVQVMEVQPGAIASQFASNASReaeQLLAEQSPWWPLRE 203
PRK09134 PRK09134
SDR family oxidoreductase;
12-249 4.00e-25

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 99.62  E-value: 4.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:PRK09134   10 RAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRDEAEALAAEiRALGRRAVALQADLADEAEVRALVARASAALGPIT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:PRK09134   90 LLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNMIDQRVWNLNPDFLSYTLSKAALWTA 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 171 TRTLAAEMAPwGVRVNAVAPGmIESKMVKKVSRAVVRAVTSTiPLRRLGKCEEVANTIVFLSSSASsyIVGQTIVIDGG 249
Cdd:PRK09134  170 TRTLAQALAP-RIRVNAIGPG-PTLPSGRQSPEDFARQHAAT-PLGRGSTPEEIAAAVRYLLDAPS--VTGQMIAVDGG 243
PRK06914 PRK06914
SDR family oxidoreductase;
10-191 5.41e-25

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 99.71  E-value: 5.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYALYK--SNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEqIERQAG 87
Cdd:PRK06914    2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRnpEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIHNFQL-VLKEIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK06914   81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160
                         170       180
                  ....*....|....*....|....
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPG 191
Cdd:PRK06914  161 EGFSESLRLELKPFGIDVALIEPG 184
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-201 5.71e-25

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 98.99  E-value: 5.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKS-NDVQLTAlKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK07666    4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTeENLKAVA-EEVEAYGVKVVIATADVSDYEEVTAAIEQLKNEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAENpaIINVASIAALIPSVGQANYSASK 164
Cdd:PRK07666   83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLpsMIERQSGD--IINISSTAGQKGAAVTSAYSASK 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV 201
Cdd:PRK07666  161 FGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDL 197
PRK06180 PRK06180
short chain dehydrogenase; Provisional
10-191 6.31e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 99.60  E-value: 6.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKsNDVQLTALKASHPagDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK06180    3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVR-SEAARADFEALHP--DRALARLLDVTDFDAIDAVVADAEATFGPI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILG 169
Cdd:PRK06180   80 DVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEG 159
                         170       180
                  ....*....|....*....|..
gi 1447699393 170 FTRTLAAEMAPWGVRVNAVAPG 191
Cdd:PRK06180  160 ISESLAKEVAPFGIHVTAVEPG 181
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
7-249 7.07e-25

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: 98.94  E-value: 7.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGD--IGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLhIVQCDLACPQSVSALCEQIER 84
Cdd:COG0623     1 GLLKGKRGLITGVANDrsIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEELGSAL-VLPCDVTDDEQIDALFDEIKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLV------NNAGIVKDslFASMSYEDFTQVIETNMFSIFRLTKDALMLLraAENPAIINVASIAA--LIPsvg 156
Cdd:COG0623    80 KWGKLDFLVhsiafaPKEELGGR--FLDTSREGFLLAMDISAYSLVALAKAAEPLM--NEGGSIVTLTYLGAerVVP--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 157 qaNY---SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCEEVANTIVFL 231
Cdd:COG0623   153 --NYnvmGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLAASGIPgfDKLLDYAEERAPLGRNVTIEEVGNAAAFL 230
                         250
                  ....*....|....*...
gi 1447699393 232 SSSASSYIVGQTIVIDGG 249
Cdd:COG0623   231 LSDLASGITGEIIYVDGG 248
PRK12746 PRK12746
SDR family oxidoreductase;
8-252 7.30e-25

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 98.95  E-value: 7.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQL-TALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ- 85
Cdd:PRK12746    3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAAdETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNEl 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  86 -----AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENpaIINVASIAALIPSVGQANY 160
Cdd:PRK12746   83 qirvgTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGR--VINISSAEVRLGFTGSIAY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK12746  161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLldDPEIRNFATNSSVFGRIGQVEDIADAVAFLASSDSRW 240
                         250
                  ....*....|....
gi 1447699393 239 IVGQTIVIDGGLVM 252
Cdd:PRK12746  241 VTGQIIDVSGGFCL 254
PRK07041 PRK07041
SDR family oxidoreductase;
15-249 1.01e-24

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 98.19  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  15 LVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPAGDKLHIVQCDLACPQSVSALCeqieRQAGKIDVLVN 94
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRD-RLAAAARALGGGAPVRTAALDITDEAAVDAFF----AEAGPFDHVVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  95 NAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAlmllRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTRTL 174
Cdd:PRK07041   76 TAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGL 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 175 AAEMAPwgVRVNAVAPGMIE----SKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLssSASSYIVGQTIVIDGG 249
Cdd:PRK07041  152 ALELAP--VRVNTVSPGLVDtplwSKLAGDAREAMFAAAAERLPARRVGQPEDVANAILFL--AANGFTTGSTVLVDGG 226
PRK06182 PRK06182
short chain dehydrogenase; Validated
12-195 2.50e-24

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 98.11  E-value: 2.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAshpAGdkLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVD-KMEDLAS---LG--VHPLSLDVTDEASIKAAVDTIIAEEGRIDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGivkdslFASM-SYEDFT-----QVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK06182   78 LVNNAG------YGSYgAIEDVPidearRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKF 151
                         170       180       190
                  ....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIES 195
Cdd:PRK06182  152 ALEGFSDALRLEVAPFGIDVVVIEPGGIKT 181
PRK12747 PRK12747
short chain dehydrogenase; Provisional
9-249 3.22e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 97.45  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALY--KSNDVQLTALKASHPAGDKLHIvQCDLACPQSV----SALCEQI 82
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYgnRKEEAEETVYEIQSNGGSAFSI-GANLESLHGVealySSLDNEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAG--KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANY 160
Cdd:PRK12747   81 QNRTGstKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLR--DNSRIINISSAATRISLPDFIAY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM-VKKVSRAVVRAVTSTI-PLRRLGKCEEVANTIVFLSSSASSY 238
Cdd:PRK12747  159 SMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMnAELLSDPMMKQYATTIsAFNRLGEVEDIADTAAFLASPDSRW 238
                         250
                  ....*....|.
gi 1447699393 239 IVGQTIVIDGG 249
Cdd:PRK12747  239 VTGQLIDVSGG 249
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
9-249 3.34e-24

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: 97.30  E-value: 3.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKA-SHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIA----DINLEAARAtAAEIGPAACAISLDVTDQASIDRCVAALVDRWG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMF-SIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd05363    77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSgTLFMMQAVARAMIAQGRGGKIINMASQAGRRGEALVGVYCATKAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVV-----------RAVTSTIPLRRLGKCEEVANTIVFLSSSA 235
Cdd:cd05363   157 VISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFAryenrprgekkRLVGEAVPFGRMGRAEDLTGMAIFLASTD 236
                         250
                  ....*....|....
gi 1447699393 236 SSYIVGQTIVIDGG 249
Cdd:cd05363   237 ADYIVAQTYNVDGG 250
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
11-250 1.83e-23

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: 94.96  E-value: 1.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGD--IGLGICEKYLEQNCDVyALYKSNDVQLTALKA-SHPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd05372     1 GKRILITGIANDrsIAWGIAKALHEAGAEL-AFTYQPEALRKRVEKlAERLGESALVLPCDVSNDEEIKELFAEVKKDWG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLV------NNAGIVKDslFASMSYEDFTQVIETNMFSIFRLTKDALMLLraAENPAIINVASIAA--LIPSVGqaN 159
Cdd:cd05372    80 KLDGLVhsiafaPKVQLKGP--FLDTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYLGSerVVPGYN--V 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASS 237
Cdd:cd05372   154 MGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITgfDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDLSS 233
                         250
                  ....*....|...
gi 1447699393 238 YIVGQTIVIDGGL 250
Cdd:cd05372   234 GITGEIIYVDGGY 246
PLN02253 PLN02253
xanthoxin dehydrogenase
12-249 7.35e-23

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 94.12  E-value: 7.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTA---LKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PLN02253   19 KVALVTGGATGIGESIVRLFHKHGAKVCIV----DLQDDLgqnVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKFGT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIV--KDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PLN02253   95 LDIMVNNAGLTgpPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCE-----------EVANTIVFLSSSA 235
Cdd:PLN02253  175 VLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDALAGFRAFAGKNanlkgveltvdDVANAVLFLASDE 254
                         250
                  ....*....|....
gi 1447699393 236 SSYIVGQTIVIDGG 249
Cdd:PLN02253  255 ARYISGLNLMIDGG 268
PRK08416 PRK08416
enoyl-ACP reductase;
7-253 1.40e-22

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 92.91  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSND--VQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK08416    4 NEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVeeANKIAEDLEQKYGIKAKAYPLNILEPETYKELFKKIDE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASmsYEDFTQVIETNMFSIFRLTKDALML--LRAAE------NPAIINVASIAALIPSVG 156
Cdd:PRK08416   84 DFDRVDFFISNAIISGRAVVGG--YTKFMRLKPKGLNNIYTATVNAFVVgaQEAAKrmekvgGGSIISLSSTGNLVYIEN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 157 QANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR-AVVRAVTSTI-PLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK08416  162 YAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNyEEVKAKTEELsPLNRMGQPEDLAGACLFLCSE 241
                         250
                  ....*....|....*....
gi 1447699393 235 ASSYIVGQTIVIDGGLVMR 253
Cdd:PRK08416  242 KASWLTGQTIVVDGGTTFK 260
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
14-201 1.45e-22

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: 92.39  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPAGDK-LHIVQCDLACPQSVSALCEQIERQAGKIDVL 92
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTD-RLDELKAELLNPNPsVEVEILDVTDEERNQLVIAELEAELGGLDLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTR 172
Cdd:cd05350    80 IINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAE 159
                         170       180
                  ....*....|....*....|....*....
gi 1447699393 173 TLAAEMAPWGVRVNAVAPGMIESKMVKKV 201
Cdd:cd05350   160 SLRYDVKKRGIRVTVINPGFIDTPLTANM 188
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
15-252 2.11e-22

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: 92.68  E-value: 2.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  15 LVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPA--GDKLHIVQCDLACPQSVSALCEQI----ERQAGK 88
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNArrPNSAVTCQADLSNSATLFSRCEAIidacFRAFGR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKDSLFASMSYEDF--------TQVIE---TNMFSIFRLTKdALMLLRAAENPA-------IINVASIAA 150
Cdd:TIGR02685  85 CDVLVNNASAFYPTPLLRGDAGEGvgdkksleVQVAElfgSNAIAPYFLIK-AFAQRQAGTRAEqrstnlsIVNLCDAMT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 151 LIPSVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGM--IESKMVKKVSRAVVRAVtstiPL-RRLGKCEEVANT 227
Cdd:TIGR02685 164 DQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLslLPDAMPFEVQEDYRRKV----PLgQREASAEQIADV 239
                         250       260
                  ....*....|....*....|....*
gi 1447699393 228 IVFLSSSASSYIVGQTIVIDGGLVM 252
Cdd:TIGR02685 240 VIFLVSPKAKYITGTCIKVDGGLSL 264
PRK07109 PRK07109
short chain dehydrogenase; Provisional
9-209 2.37e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 93.83  E-value: 2.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07109    6 IGRQVVVITGASAGVGRATARAFARRGAKV-VLLARGEEGLEALAAEiRAAGGEALAVVADVADAEAVQAAADRAEEELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK07109   85 PIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAI 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699393 168 LGFTRTLAAEM--APWGVRVNAVAPGMIE--------SKMVKK------------VSRAVVRAV 209
Cdd:PRK07109  165 RGFTDSLRCELlhDGSPVSVTMVQPPAVNtpqfdwarSRLPVEpqpvppiyqpevVADAILYAA 228
PRK08263 PRK08263
short chain dehydrogenase; Provisional
10-191 3.86e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 92.02  E-value: 3.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKsNDVQLTALKASHpaGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:PRK08263    2 MEKVWFITGASRGFGRAWTEAALERGDRVVATAR-DTATLADLAEKY--GDRLLPLALDVTDRAAVFAAVETAVEHFGRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALI--PSVGQanYSASKGAI 167
Cdd:PRK08263   79 DIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISafPMSGI--YHASKWAL 156
                         170       180
                  ....*....|....*....|....
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPG 191
Cdd:PRK08263  157 EGMSEALAQEVAEFGIKVTLVEPG 180
PRK05855 PRK05855
SDR family oxidoreductase;
12-229 4.96e-22

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 94.66  E-value: 4.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVQLTALKAS----HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK05855  316 KLVVVTGAGSGIGRETALAFAREGAEVVA----SDIDEAAAERTaeliRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHG 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIF---RLTkdALMLLRAAENPAIINVASIAALIPSVGQANYSASK 164
Cdd:PRK05855  392 VPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIhgcRLF--GRQMVERGTGGHIVNVASAAAYAPSRSLPAYATSK 469
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK----------KVSRAVVRAvTSTIPLRRLGKcEEVANTIV 229
Cdd:PRK05855  470 AAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVAttrfagadaeDEARRRGRA-DKLYQRRGYGP-EKVAKAIV 542
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
12-216 5.43e-22

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: 90.64  E-value: 5.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRV-GICARDEARLAAAAAQ--ELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFT 171
Cdd:cd08929    78 LVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLS 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699393 172 RTLAAEMAPWGVRVNAVAPGMI----------ESKMVK--KVSRAVV-------RAVTSTIPLR 216
Cdd:cd08929   158 EAAMLDLREANIRVVNVMPGSVdtgfagspegQAWKLApeDVAQAVLfalempaRALVSRIELR 221
PRK05866 PRK05866
SDR family oxidoreductase;
8-199 9.73e-22

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 91.34  E-value: 9.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK05866   37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDL-LDAVADRiTRAGGDAMAVPCDLSDLDAVDALVADVEKRI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAG-----IVKDSLfasMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQ-ANY 160
Cdd:PRK05866  116 GGVDILINNAGrsirrPLAESL---DRWHDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLfSVY 192
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK 199
Cdd:PRK05866  193 NASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIA 231
PRK05993 PRK05993
SDR family oxidoreductase;
11-196 1.24e-21

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 90.86  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGlGICEKYLEQNC-DVYA-LYKSNDVQltALKAshpagDKLHIVQCDLACPQSVSALCEQ-IERQAG 87
Cdd:PRK05993    4 KRSILITGCSSGIG-AYCARALQSDGwRVFAtCRKEEDVA--ALEA-----EGLEAFQLDYAEPESIAALVAQvLELSGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNN-----AGIVKDslfasMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSA 162
Cdd:PRK05993   76 RLDALFNNgaygqPGAVED-----LPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNA 150
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESK 196
Cdd:PRK05993  151 SKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETR 184
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
12-191 5.72e-21

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: 88.87  E-value: 5.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYA--LYKSNDvQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAGKI 89
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAgcLTKNGP-GAKELRRV--CSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DV--LVNNAGIVKDS-LFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENpAIINVASIAALIPSVGQANYSASKGA 166
Cdd:cd09805    78 GLwgLVNNAGILGFGgDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKG-RVVNVSSMGGRVPFPAGGAYCASKAA 156
                         170       180
                  ....*....|....*....|....*
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPG 191
Cdd:cd09805   157 VEAFSDSLRRELQPWGVKVSIIEPG 181
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
9-197 6.72e-21

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 88.01  E-value: 6.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIG----------------LGICEKYLEQncdVYAlyksndvQLTALKASHPAgdklhIVQCDL--A 70
Cdd:PRK08945   10 LKDRIILVTGAGDGIGreaaltyarhgatvilLGRTEEKLEA---VYD-------EIEAAGGPQPA-----IIPLDLltA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  71 CPQSVSALCEQIERQAGKIDVLVNNAGIVKD-SLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASia 149
Cdd:PRK08945   75 TPQNYQQLADTIEEQFGRLDGVLHNAGLLGElGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSS-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1447699393 150 alipSVG---QAN---YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:PRK08945  153 ----SVGrqgRANwgaYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
72-252 9.39e-21

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: 87.63  E-value: 9.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  72 PQsVSALCEQIERQA--------GKIDVLVNNagivkdSLFASM-------SYEDFTQVIETNMFSIFRLTKDALMLLRA 136
Cdd:cd05361    49 PG-TKALSEQKPEELvdavlqagGAIDVLVSN------DYIPRPmnpidgtSEADIRQAFEALSIFPFALLQAAIAQMKK 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 137 AENPAIINVASIAALIPSVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK-----KVSRAVVRAVTS 211
Cdd:cd05361   122 AGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTYFptsdwENNPELRERVKR 201
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1447699393 212 TIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGLVM 252
Cdd:cd05361   202 DVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAGGYLP 242
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
12-245 1.51e-20

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: 87.18  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPAGDKLHIV--QCDLACPQSVSALCEQIERQAGKI 89
Cdd:cd05343     7 RVALVTGASVGIGAAVARALVQHGMKVVGCARRVD-KIEALAAECQSAGYPTLFpyQCDLSNEEQILSMFSAIRTQHQGV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDAL--MLLRAAENPAIINVASIAA-LIPSVGQAN-YSASKG 165
Cdd:cd05343    86 DVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYqsMKERNVDDGHIININSMSGhRVPPVSVFHfYAATKH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 166 AILGFTRTLAAEM--APWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:cd05343   166 AVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYVLSTPPHVQIHDI 245

                  ..
gi 1447699393 244 IV 245
Cdd:cd05343   246 LL 247
PRK05872 PRK05872
short chain dehydrogenase; Provisional
3-229 1.81e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 88.10  E-value: 1.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   3 MYKYNDLNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQI 82
Cdd:PRK05872    1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKL-ALVDLEEAELAALAAELGGDDRVLTVVADVTDLAAMQAAAEEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALmllraaenPAIIN-------VASIAALIPSV 155
Cdd:PRK05872   80 VERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATL--------PALIErrgyvlqVSSLAAFAAAP 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699393 156 GQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR--AVVRAVTSTIP--LRRLGKCEEVANTIV 229
Cdd:PRK05872  152 GMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADAdlPAFRELRARLPwpLRRTTSVEKCAAAFV 229
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
14-211 3.43e-20

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: 85.90  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVL 92
Cdd:cd05360     3 VVITGASSGIGRATALAFAERGAKVVLAARSAEA-LHELAREvRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTR 172
Cdd:cd05360    82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699393 173 TLAAEMAPWG--VRVNAVAPGMIE--------SKMVKK------------VSRAVVRAVTS 211
Cdd:cd05360   162 SLRAELAHDGapISVTLVQPTAMNtpffgharSYMGKKpkppppiyqperVAEAIVRAAEH 222
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
14-199 3.92e-20

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: 86.12  E-value: 3.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKA--SHPAGDKLHIVQCDLACP----QSVSALCEQIErqag 87
Cdd:cd05356     4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQE-KLDAVAKeiEEKYGVETKTIAADFSAGddiyERIEKELEGLD---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 kIDVLVNNAGIVKD--SLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:cd05356    79 -IGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK 199
Cdd:cd05356   158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
9-230 4.11e-20

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: 86.05  E-value: 4.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAV-AIAARRVDRLEALADElEAEGGKALVLELDVTDEQQVDAAVERTVEALG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd08934    80 RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR-----AVVRAVTSTIPLrrlgKCEEVANTIVF 230
Cdd:cd08934   160 NAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHtitkeAYEERISTIRKL----QAEDIAAAVRY 223
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
65-251 6.65e-20

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 85.44  E-value: 6.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  65 VQCDLACPQSVSALCEQIErqaGKIDVLVNNAGI--VKDSLFasmsyedftqVIETNMFSIFRLTKDalMLLRAAENPAI 142
Cdd:PRK12428   28 IQADLGDPASIDAAVAALP---GRIDALFNIAGVpgTAPVEL----------VARVNFLGLRHLTEA--LLPRMAPGGAI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 143 INVASIAAL--------------IPSV--GQA-----------NYSASKGAILGFTRTLAAemaPW----GVRVNAVAPG 191
Cdd:PRK12428   93 VNVASLAGAewpqrlelhkalaaTASFdeGAAwlaahpvalatGYQLSKEALILWTMRQAQ---PWfgarGIRVNCVAPG 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699393 192 MIESKMVKKVsRAVV---RAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGLV 251
Cdd:PRK12428  170 PVFTPILGDF-RSMLgqeRVDSDAKRMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGGLA 231
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
64-249 1.18e-19

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 85.15  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  64 IVQCDLACPQSVSALCEQIERQAGKIDVLV------NNAGIVKDslFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaa 137
Cdd:PRK07370   63 FLPCDVQDDAQIEETFETIKQKWGKLDILVhclafaGKEELIGD--FSATSREGFARALEISAYSLAPLCKAAKPLMS-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 138 ENPAIINVASIAAL--IPsvgqaNYS---ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKmvkkVSRAV------V 206
Cdd:PRK07370  139 EGGSIVTLTYLGGVraIP-----NYNvmgVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTL----ASSAVggildmI 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1447699393 207 RAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK07370  210 HHVEEKAPLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAG 252
PRK05875 PRK05875
short chain dehydrogenase; Provisional
9-253 1.58e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 85.24  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTA----LKASHPAGdKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAV-MIVGRNPDKLAAaaeeIEALKGAG-AVRYEPADVTDEDQVARAVDAATA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGivkdslfASMSYEDFTQV--------IETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVG 156
Cdd:PRK05875   83 WHGRLHGVVHCAG-------GSETIGPITQIdsdawrrtVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRW 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 157 QANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKV--SRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK05875  156 FGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPIteSPELSADYRACTPLPRVGEVEDVANLAMFLLSD 235
                         250
                  ....*....|....*....
gi 1447699393 235 ASSYIVGQTIVIDGGLVMR 253
Cdd:PRK05875  236 AASWITGQVINVDGGHMLR 254
PRK06482 PRK06482
SDR family oxidoreductase;
12-191 1.88e-19

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 84.78  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqLTALKASHpaGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK06482    3 KTWFITGASSGFGRGMTERLLARGDRVAATVRRPDA-LDDLKARY--GDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIvkdSLFAS---MSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:PRK06482   80 VVSNAGY---GLFGAaeeLSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIE 156
                         170       180
                  ....*....|....*....|...
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPG 191
Cdd:PRK06482  157 GFVEAVAQEVAPFGIEFTIVEPG 179
PRK05876 PRK05876
short chain dehydrogenase; Provisional
12-203 8.51e-19

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 83.08  E-value: 8.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYAlyksNDVQLTALKAS----HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK05876    7 RGAVITGGASGIGLATGTEFARRGARVVL----GDVDKPGLRQAvnhlRAEGFDVHGVMCDVRHREEVTHLADEAFRLLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMF-SIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK05876   83 HVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWgSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYG 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR 203
Cdd:PRK05876  163 VVGLAETLAREVTADGIGVSVLCPMVVETNLVANSER 199
PRK07201 PRK07201
SDR family oxidoreductase;
9-183 1.14e-18

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 85.00  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAS-HPAGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK07201  369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGE-ALDELVAEiRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHG 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAG-IVKDSLFASMS-YEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKG 165
Cdd:PRK07201  448 HVDYLVNNAGrSIRRSVENSTDrFHDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYVASKA 527
                         170
                  ....*....|....*...
gi 1447699393 166 AILGFTRTLAAEMAPWGV 183
Cdd:PRK07201  528 ALDAFSDVAASETLSDGI 545
PRK12744 PRK12744
SDR family oxidoreductase;
5-253 1.55e-18

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 82.09  E-value: 1.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   5 KYNDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYAL-YKSN------DVQLTALKAshpAGDKLHIVQCDLACPQSVSA 77
Cdd:PRK12744    2 ADHSLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIhYNSAaskadaEETVAAVKA---AGAKAVAFQADLTTAAAVEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  78 LCEQIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLraAENPAIINVAS--IAALIPsv 155
Cdd:PRK12744   79 LFDDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTLVTslLGAFTP-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 156 GQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMV------KKVSRAVVRAVTSTIPLRRLGKCEEVANTIV 229
Cdd:PRK12744  155 FYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFypqegaEAVAYHKTAAALSPFSKTGLTDIEDIVPFIR 234
                         250       260
                  ....*....|....*....|....
gi 1447699393 230 FLSSSAsSYIVGQTIVIDGGLVMR 253
Cdd:PRK12744  235 FLVTDG-WWITGQTILINGGYTTK 257
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
88-236 1.63e-18

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: 80.25  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd02266    31 RRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAAL 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSAS 236
Cdd:cd02266   111 DGLAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDRPK 179
PRK12742 PRK12742
SDR family oxidoreductase;
7-249 1.76e-18

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 81.34  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAgdklHIVQCDLAcpqSVSALCEQIeRQA 86
Cdd:PRK12742    2 GAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQETGA----TAVQTDSA---DRDAVIDVV-RKS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIV--KDSLfaSMSYEDFTQVIETNMFSIFRLTKDALMllRAAENPAIINVASIAA-LIPSVGQANYSAS 163
Cdd:PRK12742   74 GALDILVVNAGIAvfGDAL--ELDADDIDRLFKINIHAPYHASVEAAR--QMPEGGRIIIIGSVNGdRMPVAGMAAYAAS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 164 KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMvKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQT 243
Cdd:PRK12742  150 KSALQGMARGLARDFGPRGITINVVQPGPIDTDA-NPANGPMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAM 228

                  ....*.
gi 1447699393 244 IVIDGG 249
Cdd:PRK12742  229 HTIDGA 234
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
12-197 2.90e-18

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 81.27  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALkaSHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKL--AEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 ----LVNNAGIV----------KDSLFASMSYEDFTQVIETNMFsiFRLTKDALMLLRaaenpaIINVASIAALIPSVGQ 157
Cdd:PRK06924   80 ssihLINNAGMVapikpiekaeSEELITNVHLNLLAPMILTSTF--MKHTKDWKVDKR------VINISSGAAKNPYFGW 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1447699393 158 ANYSASKGAILGFTRTLAAEMA--PWGVRVNAVAPGMIESKM 197
Cdd:PRK06924  152 SAYCSSKAGLDMFTQTVATEQEeeEYPVKIVAFSPGVMDTNM 193
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
12-205 3.81e-18

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: 80.97  E-value: 3.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYL---EQNCDVYALYKSNDVQLTALKASHP-AGDKLHIVQCDLACPQSVSALCEQIerQAG 87
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLAsdpSKRFKVYATMRDLKKKGRLWEAAGAlAGGTLETLQLDVCDSKSVAAAVERV--TER 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:cd09806    79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFAL 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAV 205
Cdd:cd09806   159 EGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSP 196
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
14-247 4.30e-18

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: 79.55  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVyalyksndvqltaLKASHPAGDklhiVQCDLACPQSVSALCEQIerqaGKIDVLV 93
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEV-------------ITAGRSSGD----YQVDITDEASIKALFEKV----GHFDAIV 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSASKGAILGFTRT 173
Cdd:cd11731    60 STAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLN--DGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRA 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699393 174 LAAEMaPWGVRVNAVAPGMIESKMVKKVSRavvraVTSTIPlrrlGKCEEVANTIVFlssSASSYIVGQTIVID 247
Cdd:cd11731   138 AAIEL-PRGIRINAVSPGVVEESLEAYGDF-----FPGFEP----VPAEDVAKAYVR---SVEGAFTGQVLHVD 198
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
12-249 9.94e-18

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 79.21  E-value: 9.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAshpAGDKLHivQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PRK06483    3 APILITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQ---AGAQCI--QADFSTNAGIMAFIDELKQHTDGLRA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAgivkdSLFASMSYEDFTQVIETNMFSIFRLTKDALM-----LLRAAENPA--IINVASIAALIPSVGQANYSASK 164
Cdd:PRK06483   78 IIHNA-----SDWLAEKPGAPLADVLARMMQIHVNAPYLLNlaledLLRGHGHAAsdIIHITDYVVEKGSDKHIAYAASK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPwGVRVNAVAPGMIeskMVKKVSRAVVRAVTstipLRR--LGK---CEEVANTIVFLssSASSYI 239
Cdd:PRK06483  153 AALDNMTLSFAAKLAP-EVKVNSIAPALI---LFNEGDDAAYRQKA----LAKslLKIepgEEEIIDLVDYL--LTSCYV 222
                         250
                  ....*....|
gi 1447699393 240 VGQTIVIDGG 249
Cdd:PRK06483  223 TGRSLPVDGG 232
PRK08339 PRK08339
short chain dehydrogenase; Provisional
8-249 1.14e-17

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 79.90  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGD-KLHIVQCDLACPQSVSALCEQIeRQA 86
Cdd:PRK08339    5 DLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNvDVSYIVADLTKREDLERTVKEL-KNI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK08339   84 GEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRIS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRAVTST-----------IPLRRLGKCEEVANTIVFLSSSA 235
Cdd:PRK08339  164 MAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKREGKSveealqeyakpIPLGRLGEPEEIGYLVAFLASDL 243
                         250
                  ....*....|....
gi 1447699393 236 SSYIVGQTIVIDGG 249
Cdd:PRK08339  244 GSYINGAMIPVDGG 257
PRK07024 PRK07024
SDR family oxidoreductase;
14-197 1.52e-16

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 76.51  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVLV 93
Cdd:PRK07024    5 VFITGASSGIGQALAREYARQGATLGLVARRTDA-LQAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVKDSLFASmsYED---FTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAAL--IPsvGQANYSASKGAIL 168
Cdd:PRK07024   84 ANAGISVGTLTEE--REDlavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVrgLP--GAGAYSASKAAAI 159
                         170       180
                  ....*....|....*....|....*....
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:PRK07024  160 KYLESLRVELRPAGVRVVTIAPGYIRTPM 188
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
9-243 1.66e-16

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: 76.08  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDV------QLTALKASHPAGDKLHIVQCdlaCPQSVSALCEQI 82
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKlrqvadHINEEGGRQPQWFILDLLTC---TSENCQQLAQRI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIVKDSL-FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYS 161
Cdd:cd05340    79 AVNYPRLDGVLHNAGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 162 ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMvkkvsRAvvravtSTIPL---RRLGKCEEVANTIVFLSSSASSY 238
Cdd:cd05340   159 VSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAM-----RA------SAFPTedpQKLKTPADIMPLYLWLMGDDSRR 227

                  ....*
gi 1447699393 239 IVGQT 243
Cdd:cd05340   228 KTGMT 232
PRK08017 PRK08017
SDR family oxidoreductase;
11-204 2.18e-16

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 76.28  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGLgICEKYLEQN--CDVYALYKSNDVQ-LTALKashpagdkLHIVQCDLACPQSVS-ALCEQIERQA 86
Cdd:PRK08017    2 QKSVLITGCSSGIGL-EAALELKRRgyRVLAACRKPDDVArMNSLG--------FTGILLDLDDPESVErAADEVIALTD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGA 166
Cdd:PRK08017   73 NRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYA 152
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA 204
Cdd:PRK08017  153 LEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNVNQT 190
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
12-202 2.36e-16

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: 76.35  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKsnDVqltaLKASHPAGD--------KLHIVQCDLACPQSVSALCEQIE 83
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVIMACR--DM----AKCEEAAAEirrdtlnhEVIVRHLDLASLKSIRAFAAEFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  84 RQAGKIDVLVNNAGIVKdslFASMSYED-FTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVG------ 156
Cdd:cd09807    76 AEEDRLDVLINNAGVMR---CPYSKTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINfddlns 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1447699393 157 ------QANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS 202
Cdd:cd09807   153 eksyntGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTG 204
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
12-248 4.96e-16

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: 74.67  E-value: 4.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVyalyKSNDVqltalkASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:cd05334     2 RVVLVYGGRGALGSAVVQAFKSRGWWV----ASIDL------AENEEADASIIVLDSDSFTEQAKQVVASVARLSGKVDA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAG-IVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:cd05334    72 LICVAGgWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLL--SGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 171 TRTLAAE--MAPWGVRVNAVAPGMIESKMVKKvsrAVVRA-VTSTIPLrrlgkcEEVANTIVFLSSSASSYIVGQTIVID 247
Cdd:cd05334   150 TQSLAAEnsGLPAGSTANAILPVTLDTPANRK---AMPDAdFSSWTPL------EFIAELILFWASGAARPKSGSLIPVV 220

                  .
gi 1447699393 248 G 248
Cdd:cd05334   221 T 221
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
9-200 1.10e-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: 74.41  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPA-GDKLHIVQCDLACPQSVSALCEQIER-QA 86
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEEIEArGGKCIPVRCDHSDDDEVEALFERVAReQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSyEDFTQVIETNMFSIFRL--------TKDALMLLRAAENPAIINVASIAALIPSVGQA 158
Cdd:cd09763    81 GRLDILVNNAYAAVQLILVGVA-KPFWEEPPTIWDDINNVglrahyacSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1447699393 159 nYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKK 200
Cdd:cd09763   160 -YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLE 200
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
14-193 1.26e-15

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 74.02  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAShpAGDKLHIVQCDLACPQSVSALCEQIERQAGKIDVLV 93
Cdd:PRK10538    3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQE-RLQELKDE--LGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVKDSLFA-SMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGFTR 172
Cdd:PRK10538   80 NNAGLALGLEPAhKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSL 159
                         170       180
                  ....*....|....*....|.
gi 1447699393 173 TLAAEMAPWGVRVNAVAPGMI 193
Cdd:PRK10538  160 NLRTDLHGTAVRVTDIEPGLV 180
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
13-185 1.97e-15

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: 73.19  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKAS--HPAGDKLHIVQCDLACPQSVSALCEQIERQAGKID 90
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREA-KLEALLVDiiRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  91 VLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAILGF 170
Cdd:cd05373    80 VLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRAL 159
                         170
                  ....*....|....*
gi 1447699393 171 TRTLAAEMAPWGVRV 185
Cdd:cd05373   160 AQSMARELGPKGIHV 174
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
12-162 3.25e-15

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 71.36  E-value: 3.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   12 KTVLVTGASGDIGLGICEkYLEQNCDVYaLY------KSNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQ 85
Cdd:smart00822   1 GTYLITGGLGGLGRALAR-WLAERGARR-LVllsrsgPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   86 AGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSifrltkdALMLLRAAENP---AIINVASIAALIPSVGQANYSA 162
Cdd:smart00822  79 EGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAG-------AWNLHELTADLpldFFVLFSSIAGVLGSPGQANYAA 151
PRK07578 PRK07578
short chain dehydrogenase; Provisional
12-209 6.09e-15

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 71.00  E-value: 6.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEkyleqncdvyALYKSNDVqltaLKASHPAGDklhiVQCDLACPQSVSALCEQIerqaGKIDV 91
Cdd:PRK07578    1 MKILVIGASGTIGRAVVA----------ELSKRHEV----ITAGRSSGD----VQVDITDPASIRALFEKV----GKVDA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIVKDSLFASMSYEDFtqvietnMFSIfrltKDALM----LLRA-----AENPAIINVASIAALIPSVGQANYSA 162
Cdd:PRK07578   59 VVSAAGKVHFAPLAEMTDEDF-------NVGL----QSKLMgqvnLVLIgqhylNDGGSFTLTSGILSDEPIPGGASAAT 127
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699393 163 SKGAILGFTRTLAAEMaPWGVRVNAVAPGMIESKMVK--------------KVSRAVVRAV 209
Cdd:PRK07578  128 VNGALEGFVKAAALEL-PRGIRINVVSPTVLTESLEKygpffpgfepvpaaRVALAYVRSV 187
PRK07832 PRK07832
SDR family oxidoreductase;
12-206 2.51e-14

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 70.46  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYaLYKSNDVQL-------TALKASHPAGDKLHIVQCDlacpqSVSALCEQIER 84
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAELF-LTDRDADGLaqtvadaRALGGTVPEHRALDISDYD-----AVAAFAADIHA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIvkdSLFAS---MSYEDFTQVIETN-MFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANY 160
Cdd:PRK07832   75 AHGSMDVVMNIAGI---SAWGTvdrLTHEQWRRMVDVNlMGPIHVIETFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAY 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1447699393 161 SASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVV 206
Cdd:PRK07832  152 SASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAGV 197
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
9-249 3.26e-14

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 70.38  E-value: 3.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTG--ASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLhIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK08690    4 LQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVVDKLEERVRKMAAELDSEL-VFRCDVASDDEINQVFADLGKHW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIV-KDSL----FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAaENPAIINVASIAAL--IPsvgqaN 159
Cdd:PRK08690   83 DGLDGLVHSIGFApKEALsgdfLDSISREAFNTAHEISAYSLPALAKAARPMMRG-RNSAIVALSYLGAVraIP-----N 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSA---SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK08690  157 YNVmgmAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIAdfGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSD 236
                         250
                  ....*....|....*
gi 1447699393 235 ASSYIVGQTIVIDGG 249
Cdd:PRK08690  237 LSSGITGEITYVDGG 251
PRK09291 PRK09291
SDR family oxidoreductase;
12-191 3.90e-14

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 70.03  E-value: 3.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNdVQLTALKA-SHPAGDKLHIVQCDLACPqsvsalceqIER-QAGK- 88
Cdd:PRK09291    3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIA-PQVTALRAeAARRGLALRVEKLDLTDA---------IDRaQAAEw 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 -IDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK09291   73 dVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHAL 152
                         170       180
                  ....*....|....*....|....
gi 1447699393 168 LGFTRTLAAEMAPWGVRVNAVAPG 191
Cdd:PRK09291  153 EAIAEAMHAELKPFGIQVATVNPG 176
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
67-250 1.01e-13

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 68.81  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  67 CDLACPQSVSALCEQIERQAGKIDVLVNN-AGIVKDSLFASM---SYEDFTQVIETNMFSIFRLTKDALMLLRaaENPAI 142
Cdd:PRK07533   67 LDVREPGQLEAVFARIAEEWGRLDFLLHSiAFAPKEDLHGRVvdcSREGFALAMDVSCHSFIRMARLAEPLMT--NGGSL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 143 INVASIAA--LIPsvgqaNYS---ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKK-------VSRAVVRAvt 210
Cdd:PRK07533  145 LTMSYYGAekVVE-----NYNlmgPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGiddfdalLEDAAERA-- 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1447699393 211 stiPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGGL 250
Cdd:PRK07533  218 ---PLRRLVDIDDVGAVAAFLASDAARRLTGNTLYIDGGY 254
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-249 1.16e-13

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 68.25  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNEN-KLKRMKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLNA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGivkdsLFASMSYEDFT---QVIETNMFSIFRLTKDALMLLRaaENPAIINVASIAAL-IPSVGQANYSASK 164
Cdd:PRK05786   82 IDGLVVTVG-----GYVEDTVEEFSgleEMLTNHIKIPLYAVNASLRFLK--EGSSIVLVSSMSGIyKASPDQLSYAVAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVvravtstipLRRLGKC----EEVANTIVFLSSSASSYIV 240
Cdd:PRK05786  155 AGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPERNWKK---------LRKLGDDmappEDFAKVIIWLLTDEADWVD 225

                  ....*....
gi 1447699393 241 GQTIVIDGG 249
Cdd:PRK05786  226 GVVIPVDGG 234
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
59-249 1.70e-13

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 68.22  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  59 GDKLHIVQCDLACPQSVSALCEQIERQAGKIDVLVNN-AGIVKDSL---FASMSYEDFTQVIETNMFSIFRLTKDALMLL 134
Cdd:PRK08594   58 GQESLLLPCDVTSDEEITACFETIKEEVGVIHGVAHCiAFANKEDLrgeFLETSRDGFLLAQNISAYSLTAVAREAKKLM 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 135 ---------------RAAENPAIINVASiAALIPSVgqanysaskgailgftRTLAAEMAPWGVRVNAVAPGMIESKMVK 199
Cdd:PRK08594  138 teggsivtltylggeRVVQNYNVMGVAK-ASLEASV----------------KYLANDLGKDGIRVNAISAGPIRTLSAK 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1447699393 200 KVS--RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK08594  201 GVGgfNSILKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSG 252
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
8-194 3.54e-13

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: 68.18  E-value: 3.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYK---SNDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIeR 84
Cdd:cd05274   147 GGLDGTYLITGGLGGLGLLVARWLAARGARHLVLLSrrgPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAEL-A 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIET------NMFSIFRLTKDALMLLraaenpaiinVASIAALIPSVGQA 158
Cdd:cd05274   226 AGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAkvagalNLHELTPDLPLDFFVL----------FSSVAALLGGAGQA 295
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1447699393 159 NYSASKGAILGftrtLAAEMAPWGVRVNAVAPGMIE 194
Cdd:cd05274   296 AYAAANAFLDA----LAAQRRRRGLPATSVQWGAWA 327
PRK05854 PRK05854
SDR family oxidoreductase;
8-191 5.69e-13

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 67.40  E-value: 5.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKS---NDVQLTALKASHPAGdKLHIVQCDLACPQSVSALCEQIER 84
Cdd:PRK05854   11 DLSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNrakGEAAVAAIRTAVPDA-KLSLRALDLSSLASVAALGEQLRA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASMSyEDFTQVIETNMFSIFRLTKDALMLLRAAeNPAIINVASIAALIPSV--------- 155
Cdd:PRK05854   90 EGRPIHLLINNAGVMTPPERQTTA-DGFELQFGTNHLGHFALTAHLLPLLRAG-RARVTSQSSIAARRGAInwddlnwer 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1447699393 156 ---GQANYSASKGAILGFTRTLA--AEMAPWGVRVNAVAPG 191
Cdd:PRK05854  168 syaGMRAYSQSKIAVGLFALELDrrSRAAGWGITSNLAHPG 208
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
74-250 5.90e-13

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 67.15  E-value: 5.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  74 SVSALCEQIERQAGKIDVLVN---NAGIVKDSLFASmSYEDFTQVIETNMFSIFRLTKDALMLLRA-AENPAIINVASIA 149
Cdd:PRK06300  105 TISEVAEQVKKDFGHIDILVHslaNSPEISKPLLET-SRKGYLAALSTSSYSFVSLLSHFGPIMNPgGSTISLTYLASMR 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 150 AlIPSVGqANYSASKGAILGFTRTLAAEMA-PWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCEEVAN 226
Cdd:PRK06300  184 A-VPGYG-GGMSSAKAALESDTKVLAWEAGrRWGIRVNTISAGPLASRAGKAIGfiERMVDYYQDWAPLPEPMEAEQVGA 261
                         170       180
                  ....*....|....*....|....
gi 1447699393 227 TIVFLSSSASSYIVGQTIVIDGGL 250
Cdd:PRK06300  262 AAAFLVSPLASAITGETLYVDHGA 285
PRK08177 PRK08177
SDR family oxidoreductase;
12-197 7.89e-13

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 65.82  E-value: 7.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKsNDVQLTALKASHPAgdklHIVQCDLACPQSVSALCEQIERQAgkIDV 91
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQVTATVR-GPQQDTALQALPGV----HIEKLDMNDPASLDQLLQRLQGQR--FDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIV--KDSLFASMSYEDFTQVIETNMFSIFRLTKdALMLLRAAENPAIINVASIAALI---PSVGQANYSASKGA 166
Cdd:PRK08177   75 LFVNAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLAR-RLLGQVRPGQGVLAFMSSQLGSVelpDGGEMPLYKASKAA 153
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699393 167 ILGFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:PRK08177  154 LNSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK06139 PRK06139
SDR family oxidoreductase;
9-234 9.53e-13

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 66.67  E-value: 9.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCD-VYALYKSNDVQLTALKASHPAGDKLhIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK06139    5 LHGAVVVITGASSGIGQATAEAFARRGARlVLAARDEEALQAVAEECRALGAEVL-VVPTDVTDADQVKALATQAASFGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQANYSASKGAI 167
Cdd:PRK06139   84 RIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGL 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699393 168 LGFTRTLAAEMAPW-GVRVNAVAPGMIESKMVKKVSRAVVRAVTSTIPL---RRlgkceeVANTIVFLSSS 234
Cdd:PRK06139  164 RGFSEALRGELADHpDIHVCDVYPAFMDTPGFRHGANYTGRRLTPPPPVydpRR------VAKAVVRLADR 228
PRK07023 PRK07023
SDR family oxidoreductase;
15-197 9.97e-13

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 65.80  E-value: 9.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  15 LVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALkashpAGDKLHIVQCDLACPQSV-----SALCEQIERQAGKI 89
Cdd:PRK07023    5 IVTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSLAAA-----AGERLAEVELDLSDAAAAaawlaGDLLAAFVDGASRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 dVLVNNAGIVK-----DSLFASMsyedFTQVIETNMFSIFRLTKdalMLLRAAENPA---IINVASIAALIPSVGQANYS 161
Cdd:PRK07023   80 -LLINNAGTVEpigplATLDAAA----IARAVGLNVAAPLMLTA---ALAQAASDAAerrILHISSGAARNAYAGWSVYC 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1447699393 162 ASKGAILGFTRTLAAEmAPWGVRVNAVAPGMIESKM 197
Cdd:PRK07023  152 ATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGM 186
PRK06194 PRK06194
hypothetical protein; Provisional
7-187 1.29e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 65.81  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKY--LEQNCdVYAlyksnDVQLTALKAS----HPAGDKLHIVQCDLACPQSVSALCE 80
Cdd:PRK06194    2 KDFAGKVAVITGAASGFGLAFARIGaaLGMKL-VLA-----DVQQDALDRAvaelRAQGAEVLGVRTDVSDAAQVEALAD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  81 QIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTK--DALMLLRAAENPA----IINVASIAALIPS 154
Cdd:PRK06194   76 AALERFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRafTPLMLAAAEKDPAyeghIVNTASMAGLLAP 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1447699393 155 VGQANYSASKGAILGFTRTLAAEMAPWGVRVNA 187
Cdd:PRK06194  156 PAMGIYNVSKHAVVSLTETLYQDLSLVTDQVGA 188
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
13-162 1.48e-12

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: 66.62  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQ-NCDVYALYKS-----NDVQLTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:cd08953   207 VYLVTGGAGGIGRALARALARRyGARLVLLGRSplppeEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERY 286
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLtkdaLMLLRAAENPAIINVASIAALIPSVGQANYSA 162
Cdd:cd08953   287 GAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNL----AQALADEPLDFFVLFSSVSAFFGGAGQADYAA 358
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
9-249 1.96e-12

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 65.13  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASG--DIGLGICEKYLEQNCDVYALYKsNDVQLTALKASHPAGDKLhiVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK06079    5 LSGKKIVVMGVANkrSIAWGCAQAIKDQGATVIYTYQ-NDRMKKSLQKLVDEEDLL--VECDVASDESIERAFATIKERV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDvlvnnaGIVKDSLFASMsyEDFTQVIETNMFSIFRLTKD--ALMLLRAAE--NPAIINVASIAAL--------IPs 154
Cdd:PRK06079   82 GKID------GIVHAIAYAKK--EELGGNVTDTSRDGYALAQDisAYSLIAVAKyaRPLLNPGASIVTLtyfgseraIP- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 155 vgqaNYSA---SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK---------KVSRA-VVRAVTSTIplrrlgkc 221
Cdd:PRK06079  153 ----NYNVmgiAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTgikghkdllKESDSrTVDGVGVTI-------- 220
                         250       260
                  ....*....|....*....|....*...
gi 1447699393 222 EEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK06079  221 EEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK08340 PRK08340
SDR family oxidoreductase;
14-250 3.16e-12

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 64.44  E-value: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGdKLHIVQCDLACPQSVSALCEQIERQAGKIDVLV 93
Cdd:PRK08340    3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDALV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVK--DSLFASMSYEDFTQVIETNMFSIFRLTkdALMLLRAAENP---AIINVASIAALIPSVGQANYSASKGAIL 168
Cdd:PRK08340   82 WNAGNVRcePCMLHEAGYSDWLEAALLHLVAPGYLT--TLLIQAWLEKKmkgVLVYLSSVSVKEPMPPLVLADVTRAGLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 169 GFTRTLAAEMAPWGVRVNAV------APGMIESkmVKKV--SRAVV------RAVTSTIPLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK08340  160 QLAKGVSRTYGGKGIRAYTVllgsfdTPGAREN--LARIaeERGVSfeetweREVLERTPLKRTGRWEELGSLIAFLLSE 237
                         250
                  ....*....|....*.
gi 1447699393 235 ASSYIVGQTIVIDGGL 250
Cdd:PRK08340  238 NAEYMLGSTIVFDGAM 253
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
64-249 4.79e-12

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 64.38  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  64 IVQCDLACPQSVSALCEQIERQAGKIDVLVNNAGIV-KDSL---FASMSYEDFTQVIETNMFSIFRLTKDALMLLRaaEN 139
Cdd:PRK08415   59 VYELDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFApKEALegsFLETSKEAFNIAMEISVYSLIELTRALLPLLN--DG 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 140 PAIINVASIAAL--IPsvgqaNYS---ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTST 212
Cdd:PRK08415  137 ASVLTLSYLGGVkyVP-----HYNvmgVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKTLAASGIGdfRMILKWNEIN 211
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1447699393 213 IPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK08415  212 APLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAG 248
PRK07984 PRK07984
enoyl-ACP reductase FabI;
9-250 5.51e-12

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 63.77  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGD--IGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPAGDKLhIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK07984    4 LSGKRILVTGVASKlsIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDI-VLPCDVAEDASIDAMFAELGKVW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  87 GKIDVLVNNAGIVK-DSL----FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAaeNPAIINVASIAA--LIPsvgqaN 159
Cdd:PRK07984   83 PKFDGFVHSIGFAPgDQLdgdyVNAVTREGFKIAHDISSYSFVAMAKACRSMLNP--GSALLTLSYLGAerAIP-----N 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 YSA---SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCEEVANTIVFLSSS 234
Cdd:PRK07984  156 YNVmglAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKdfRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSD 235
                         250
                  ....*....|....*.
gi 1447699393 235 ASSYIVGQTIVIDGGL 250
Cdd:PRK07984  236 LSAGISGEVVHVDGGF 251
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
9-190 2.19e-11

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 62.08  E-value: 2.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQ-------LTALKASHPAGDKLHIVQCDLACPQSVSALCEQ 81
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHpklpgtiYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  82 IERQAGKIDVLVNNAGIVK--DSLFASMSYEDFTQVIETNmfSIFRLTKDALMLLRAAENPAIINVASIAALIPS--VGQ 157
Cdd:cd09762    81 AVEKFGGIDILVNNASAISltGTLDTPMKRYDLMMGVNTR--GTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKwfKNH 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1447699393 158 ANYSASKGAILGFTRTLAAEMAPWGVRVNAVAP 190
Cdd:cd09762   159 TAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
13-162 2.99e-11

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: 60.65  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICeKYLEQNCDVYALYKS------NDVQ--LTALKAShpaGDKLHIVQCDLACPQSVSALCEQIER 84
Cdd:pfam08659   2 TYLITGGLGGLGRELA-RWLAERGARHLVLLSrsaaprPDAQalIAELEAR---GVEVVVVACDVSDPDAVAALLAEIKA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699393  85 QAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKdalmLLRAAENPAIINVASIAALIPSVGQANYSA 162
Cdd:pfam08659  78 EGPPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHE----ATPDEPLDFFVLFSSIAGLLGSPGQANYAA 151
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
12-197 4.15e-11

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 61.63  E-value: 4.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALY---------KSNDVqLTALKASHP-AGDKLHIVQCDLACPQSVSALCEQ 81
Cdd:cd08941     2 KVVLVTGANSGLGLAICERLLAEDDENPELTlilacrnlqRAEAA-CRALLASHPdARVVFDYVLVDLSNMVSVFAAAKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  82 IERQAGKIDVLVNNAGI---------------VKDSLFA--SMSY----------------EDFTQVIETNMFSIFRLTK 128
Cdd:cd08941    81 LKKRYPRLDYLYLNAGImpnpgidwigaikevLTNPLFAvtNPTYkiqaegllsqgdkateDGLGEVFQTNVFGHYYLIR 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393 129 DALMLLRAAENPA-IINVASIAALIPSV---------GQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:cd08941   161 ELEPLLCRSDGGSqIIWTSSLNASPKYFslediqhlkGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNL 239
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
9-249 8.75e-11

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 60.53  E-value: 8.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGD--IGLGICEKYLEQNCDVYALYksndvQLTAL-KASHPAGDKLH---IVQCDLACPQSVSALCEQI 82
Cdd:PRK06505    5 MQGKRGLIMGVANDhsIAWGIAKQLAAQGAELAFTY-----QGEALgKRVKPLAESLGsdfVLPCDVEDIASVDAVFEAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQAGKIDVLVNNAGIVKDS----LFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPsvgqa 158
Cdd:PRK06505   80 EKKWGKLDFVVHAIGFSDKNelkgRYADTTRENFSRTMVISCFSFTEIAKRAAKLMPDGGSMLTLTYGGSTRVMP----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 159 NYSA---SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAvvRAVTS----TIPLRRLGKCEEVANTIVFL 231
Cdd:PRK06505  155 NYNVmgvAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGIGDA--RAIFSyqqrNSPLRRTVTIDEVGGSALYL 232
                         250
                  ....*....|....*...
gi 1447699393 232 SSSASSYIVGQTIVIDGG 249
Cdd:PRK06505  233 LSDLSSGVTGEIHFVDSG 250
PRK07775 PRK07775
SDR family oxidoreductase;
68-197 9.61e-11

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 60.54  E-value: 9.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  68 DLACPQSVSALCEQIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVAS 147
Cdd:PRK07775   67 DVTDPDSVKSFVAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGS 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1447699393 148 IAALIPSVGQANYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:PRK07775  147 DVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
64-249 9.84e-11

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 60.22  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  64 IVQCDLACPQSVSALCEQIERQAGKIDVLVNNAGIVKDSLFA-----SMSYEDFTQVIETNMFSIFRLTKDALMLLraAE 138
Cdd:PRK06997   60 VFPCDVASDEQIDALFASLGQHWDGLDGLVHSIGFAPREAIAgdfldGLSRENFRIAHDISAYSFPALAKAALPML--SD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 139 NPAIINVASIAA--LIPsvgqaNYSA---SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIES---KMVKKVSRaVVRAVT 210
Cdd:PRK06997  138 DASLLTLSYLGAerVVP-----NYNTmglAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaaSGIKDFGK-ILDFVE 211
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1447699393 211 STIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK06997  212 SNAPLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSG 250
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
13-193 1.21e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 60.38  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQltalkASHPAGDKLHIVQCDLACPQSVSALCEqierqagKIDVL 92
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGA-----ANLAALPGVEFVRGDLRDPEALAAALA-------GVDAV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNAGIvkdslfASMSYEDFTQVIETNMfsifRLTKDALMLLRAAENPAIINVASIAAL----------IPSVGQANYSA 162
Cdd:COG0451    69 VHLAAP------AGVGEEDPDETLEVNV----EGTLNLLEAARAAGVKRFVYASSSSVYgdgegpidedTPLRPVSPYGA 138
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699393 163 SKGAILGFTRTLAAEmapWGVRVNAVAPGMI 193
Cdd:COG0451   139 SKLAAELLARAYARR---YGLPVTILRPGNV 166
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
74-250 1.38e-10

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 60.17  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  74 SVSALCEQIERQAGKIDVLV----NNAGIVKDSLfaSMSYEDFTQVIETNMFSIFRLTKDALMLLraaeNP--AIINVAS 147
Cdd:PLN02730  106 TVQEVAESVKADFGSIDILVhslaNGPEVTKPLL--ETSRKGYLAAISASSYSFVSLLQHFGPIM----NPggASISLTY 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 148 IAA--LIPSVGqANYSASKGAILGFTRTLAAEMA-PWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPLRRLGKCE 222
Cdd:PLN02730  180 IASerIIPGYG-GGMSSAKAALESDTRVLAFEAGrKYKIRVNTISAGPLGSRAAKAIGfiDDMIEYSYANAPLQKELTAD 258
                         170       180
                  ....*....|....*....|....*...
gi 1447699393 223 EVANTIVFLSSSASSYIVGQTIVIDGGL 250
Cdd:PLN02730  259 EVGNAAAFLASPLASAITGATIYVDNGL 286
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
15-203 3.74e-10

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 58.77  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  15 LVTGASGDIGLGICEKYLEQNCD---VYALYKSNDVQLTALKASHPA---GDKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKCLKSpgsVLVLSARNDEALRQLKAEIGAersGLRVVRVSLDLGAEAGLEQLLKALRELPRP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 ID----VLVNNAGIVKDSLFASMSYEDFTQV---IETNMFSIFRLTKDALMLLRAAE--NPAIINVASIAALIPSVGQAN 159
Cdd:TIGR01500  84 KGlqrlLLINNAGTLGDVSKGFVDLSDSTQVqnyWALNLTSMLCLTSSVLKAFKDSPglNRTVVNISSLCAIQPFKGWAL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1447699393 160 YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSR 203
Cdd:TIGR01500 164 YCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVRE 207
PRK08251 PRK08251
SDR family oxidoreductase;
12-204 4.12e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 58.41  E-value: 4.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVyALYKSNDVQLTALK----ASHPaGDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK08251    3 QKILITGASSGLGAGMAREFAAKGRDL-ALCARRTDRLEELKaellARYP-GIKVAVAALDVNDHDQVFEVFAEFRDELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAAL--IPSVgQANYSASKG 165
Cdd:PRK08251   81 GLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVrgLPGV-KAAYAASKA 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1447699393 166 AILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA 204
Cdd:PRK08251  160 GVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAKST 198
PRK08278 PRK08278
SDR family oxidoreductase;
8-190 4.41e-10

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 58.38  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQ-------LTALKASHPAGDKLHIVQCDLACPQSVSALCE 80
Cdd:PRK08278    3 SLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHpklpgtiHTAAEEIEAAGGQALPLVGDVRDEDQVAAAVA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  81 QIERQAGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSV--GQA 158
Cdd:PRK08278   83 KAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPKWfaPHT 162
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1447699393 159 NYSASKGAILGFTRTLAAEMAPWGVRVNAVAP 190
Cdd:PRK08278  163 AYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
64-249 5.96e-10

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 58.10  E-value: 5.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  64 IVQCDLACPQSVSALCEQIERQAGKIDVLVNNAGIV-KDSL---FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAEN 139
Cdd:PRK06603   62 VSELDVTNPKSISNLFDDIKEKWGSFDFLLHGMAFAdKNELkgrYVDTSLENFHNSLHISCYSLLELSRSAEALMHDGGS 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 140 PAIINVASIAALIPsvgqaNYSA---SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIP 214
Cdd:PRK06603  142 IVTLTYYGAEKVIP-----NYNVmgvAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGdfSTMLKSHAATAP 216
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1447699393 215 LRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK06603  217 LKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCG 251
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
67-249 4.62e-09

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 55.53  E-value: 4.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  67 CDLACPQSVSALCEQIERQAGKIDVLVNNAGIV-KDSL---FASMSYEDFTQVIETNMFSIFRLTKDALMLLraAENPAI 142
Cdd:PRK08159   67 CDVTDEASIDAVFETLEKKWGKLDFVVHAIGFSdKDELtgrYVDTSRDNFTMTMDISVYSFTAVAQRAEKLM--TDGGSI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 143 INVASIAA--LIPsvgqaNYSA---SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTSTIPL 215
Cdd:PRK08159  145 LTLTYYGAekVMP-----HYNVmgvAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGdfRYILKWNEYNAPL 219
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1447699393 216 RRLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK08159  220 RRTVTIEEVGDSALYLLSDLSRGVTGEVHHVDSG 253
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
10-197 4.85e-09

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: 55.19  E-value: 4.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNCDVYaLYKSNDVQLTALKASHPAGdkLHIVQCDLACPQSVSALCEQIErQAGKI 89
Cdd:cd08951     6 PMKRIFITGSSDGLGLAAARTLLHQGHEVV-LHARSQKRAADAKAACPGA--AGVLIGDLSSLAETRKLADQVN-AIGRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSlFASMSYEDFTQVIETNMFSIFRLTkdALM-----LLRAAENPAIINVASIAALI----PSVGQANY 160
Cdd:cd08951    82 DAVIHNAGILSGP-NRKTPDTGIPAMVAVNVLAPYVLT--ALIrrpkrLIYLSSGMHRGGNASLDDIDwfnrGENDSPAY 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1447699393 161 SASKGAILgftrTLAAEMAPW--GVRVNAVAPGMIESKM 197
Cdd:cd08951   159 SDSKLHVL----TLAAAVARRwkDVSSNAVHPGWVPTKM 193
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
14-229 2.31e-08

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: 52.91  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKyLEQNCDVYALYKSNDVQLTALKASHPAgdklHIVQCDLACPQSVSALCEQierqAGKIDVLV 93
Cdd:cd11730     1 ALILGATGGIGRALARA-LAGRGWRLLLSGRDAGALAGLAAEVGA----LARPADVAAELEVWALAQE----LGPLDLLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQanYSASKGAILGFTRT 173
Cdd:cd11730    72 YAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPELVMLPGLSA--YAAAKAALEAYVEV 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699393 174 LAAEMApwGVRVNAVAPGMIESKMVKKVSRAVVRAVTStiplrrlgkcEEVANTIV 229
Cdd:cd11730   150 ARKEVR--GLRLTLVRPPAVDTGLWAPPGRLPKGALSP----------EDVAAAIL 193
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
11-162 9.00e-08

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: 52.29  E-value: 9.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  11 EKTVLVTGASGDIGLGICEKYLEQNCDVYALYK----SNDVQlTALKASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:cd08955   149 DATYLITGGLGGLGLLVAEWLVERGARHLVLTGrrapSAAAR-QAIAALEEAGAEVVVLAADVSDRDALAAALAQIRASL 227
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393  87 GKIDVLVNNAGIVKDSLFASMSYEDFTQVIE---TNMFSIFRLTKDALMLLraaenpaIINVASIAALIPSVGQANYSA 162
Cdd:cd08955   228 PPLRGVIHAAGVLDDGVLANQDWERFRKVLApkvQGAWNLHQLTQDLPLDF-------FVLFSSVASLLGSPGQANYAA 299
PRK09009 PRK09009
SDR family oxidoreductase;
12-199 1.21e-07

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 51.22  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCD--VYALYKSNDVQLTAlkashpagDKLHIVQCDLACPQSVSALCEQIErqagKI 89
Cdd:PRK09009    1 MNILIVGGSGGIGKAMVKQLLERYPDatVHATYRHHKPDFQH--------DNVQWHALDVTDEAEIKQLSEQFT----QL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIV-------KDSLfASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIinvASIAALIPSV------G 156
Cdd:PRK09009   69 DWLINCVGMLhtqdkgpEKSL-QALDADFFLQNITLNTLPSLLLAKHFTPKLKQSESAKF---AVISAKVGSIsdnrlgG 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1447699393 157 QANYSASKGAILGFTRTLAAEmapW-----GVRVNAVAPGMIESKMVK 199
Cdd:PRK09009  145 WYSYRASKAALNMFLKTLSIE---WqrslkHGVVLALHPGTTDTALSK 189
PRK08862 PRK08862
SDR family oxidoreductase;
8-190 1.41e-07

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 50.88  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALyksnDVQLTALKASHPA----GDKLHIVQCDLACPQSVSALCEQIE 83
Cdd:PRK08862    2 DIKSSIILITSAGSVLGRTISCHFARLGATLILC----DQDQSALKDTYEQcsalTDNVYSFQLKDFSQESIRHLFDAIE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  84 RQAGK-IDVLVNN-AGIVKDSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPA-IINVASIAALIPSVGQANy 160
Cdd:PRK08862   78 QQFNRaPDVLVNNwTSSPLPSLFDEQPSESFIQQLSSLASTLFTYGQVAAERMRKRNKKGvIVNVISHDDHQDLTGVES- 156
                         170       180       190
                  ....*....|....*....|....*....|
gi 1447699393 161 saSKGAILGFTRTLAAEMAPWGVRVNAVAP 190
Cdd:PRK08862  157 --SNALVSGFTHSWAKELTPFNIRVGGVVP 184
PRK08703 PRK08703
SDR family oxidoreductase;
9-195 1.43e-07

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 51.09  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   9 LNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKS----NDVQLTALKASHPagdKLHIVQCDL--ACPQSVSALCEQI 82
Cdd:PRK08703    4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHqkklEKVYDAIVEAGHP---EPFAIRFDLmsAEEKEFEQFAATI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  83 ERQ-AGKIDVLVNNAGivkdsLFASMSYEDFTQVIE-TNMFSI-----FRLTKDALMLLRAAENPAIINVASIAALIPSV 155
Cdd:PRK08703   81 AEAtQGKLDGIVHCAG-----YFYALSPLDFQTVAEwVNQYRIntvapMGLTRALFPLLKQSPDASVIFVGESHGETPKA 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1447699393 156 GQANYSASKGAILGFTRTLAAEMAPWG-VRVNAVAPGMIES 195
Cdd:PRK08703  156 YWGGFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINS 196
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
14-211 2.29e-07

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs 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: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 49.32  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSndvqltALKASHPAGDKLHIVQCDLACPQSVSALCEQierqagkIDVLV 93
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHEVTLLVRN------TKRLSKEDQEPVAVVEGDLRDLDSLSDAVQG-------VDVVI 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGivkdslfASMSYEDFTQVIETNMFSIfrltkdaLMLLRAAENPAIINVASIAALIPSVGQANYSASkGAILGFTRT 173
Cdd:cd05226    68 HLAG-------APRDTRDFCEVDVEGTRNV-------LEAAKEAGVKHFIFISSLGAYGDLHEETEPSPS-SPYLAVKAK 132
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1447699393 174 LAAEMAPWGVRVNAVAPGMIeskmVKKVSRAVVRAVTS 211
Cdd:cd05226   133 TEAVLREASLPYTIVRPGVI----YGDLARAIANAVVT 166
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
62-169 2.88e-07

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: 50.29  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  62 LHIVqcDLACPQSVSALCEQIERQAGKIDVLVNNAGIVKDSlfASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPA 141
Cdd:cd09808    56 LHIV--DMSDPKQVWEFVEEFKEEGKKLHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPR 131
                          90       100
                  ....*....|....*....|....*...
gi 1447699393 142 IINVASIAALIPSVGQANYSASKGAILG 169
Cdd:cd09808   132 VITVSSGGMLVQKLNTNNLQSERTAFDG 159
PRK08303 PRK08303
short chain dehydrogenase; Provisional
7-197 3.96e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 50.00  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   7 NDLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQL-----------TALKAShPAGDKLHIVQCDLACPQSV 75
Cdd:PRK08303    4 KPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTRARRseydrpetieeTAELVT-AAGGRGIAVQVDHLVPEQV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  76 SALCEQIERQAGKIDVLVNN--AGivkDSLFasmsyEDFTQVIETNmfsifrLTKDALMLLRAAENPAIINVASIAALIP 153
Cdd:PRK08303   83 RALVERIDREQGRLDILVNDiwGG---EKLF-----EWGKPVWEHS------LDKGLRMLRLAIDTHLITSHFALPLLIR 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699393 154 SVG--------------QANYSAS------KGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKM 197
Cdd:PRK08303  149 RPGglvveitdgtaeynATHYRLSvfydlaKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEM 212
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
12-174 4.77e-07

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 49.82  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGiCEKYLEQNCDVYALYKSNDVqLTALKASHPAG---DKLHIVQCDLACPQSVSALCEQIERQAGK 88
Cdd:cd09810     2 GTVVITGASSGLGLA-AAKALARRGEWHVVMACRDF-LKAEQAAQEVGmpkDSYSVLHCDLASLDSVRQFVDNFRRTGRP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGI----VKDSLFASMSYEdftQVIETNMFSIFRLTKDALMLLRAAEN--PAIINVASIAALIPSV-GQANYS 161
Cdd:cd09810    80 LDALVCNAAVylptAKEPRFTADGFE---LTVGVNHLGHFLLTNLLLEDLQRSENasPRIVIVGSITHNPNTLaGNVPPR 156
                         170
                  ....*....|...
gi 1447699393 162 ASKGAILGFTRTL 174
Cdd:cd09810   157 ATLGDLEGLAGGL 169
PRK06197 PRK06197
short chain dehydrogenase; Provisional
12-215 6.08e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 49.25  E-value: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYA----LYKSNDVqLTALKASHPAGDkLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK06197   17 RVAVVTGANTGLGYETAAALAAKGAHVVLavrnLDKGKAA-AARITAATPGAD-VTLQELDLTSLASVRAAADALRAAYP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVKDSlfASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVGQ---------- 157
Cdd:PRK06197   95 RIDLLINNAGVMYTP--KQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHRIRAAIHfddlqwerry 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699393 158 ---ANYSASKGAILGFTRTLAAEMAPWGVRVNAVA--PGMIESKMVKKVSRAVVRAVTSTIPL 215
Cdd:PRK06197  173 nrvAAYGQSKLANLLFTYELQRRLAAAGATTIAVAahPGVSNTELARNLPRALRPVATVLAPL 235
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
14-192 7.21e-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: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvqltalKASHPAGDKLHIVQCDLACPQSVSALCEQierqagkIDVLV 93
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSGS------DAVLLDGLPVEVVEGDLTDAASLAAAMKG-------CDRVF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGIVkdslfaSMSYEDFTQVIETNMfsifrltKDALMLLRAAENPAI---INVASIAALIPSVGQA---NYSASKGAI 167
Cdd:cd05228    68 HLAAFT------SLWAKDRKELYRTNV-------EGTRNVLDAALEAGVrrvVHTSSIAALGGPPDGRideTTPWNERPF 134
                         170       180
                  ....*....|....*....|....*...
gi 1447699393 168 LGF---TRTLAAEMApwgvrVNAVAPGM 192
Cdd:cd05228   135 PNDyyrSKLLAELEV-----LEAAAEGL 157
PRK07806 PRK07806
SDR family oxidoreductase;
8-96 1.04e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 48.56  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTAL-KASHPAGDKLHIVQCDLACPQSVSALCEQIERQA 86
Cdd:PRK07806    3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVvAEIEAAGGRASAVGADLTDEESVAALMDTAREEF 82
                          90
                  ....*....|
gi 1447699393  87 GKIDVLVNNA 96
Cdd:PRK07806   83 GGLDALVLNA 92
PRK06940 PRK06940
short chain dehydrogenase; Provisional
176-251 1.22e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 48.48  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 176 AEMAPWG---VRVNAVAPGMIESKM----VKKVSRAVVRAVTSTIPLRRLGKCEEVANTIVFLSSSASSYIVGQTIVIDG 248
Cdd:PRK06940  182 AEAVKWGergARINSISPGIISTPLaqdeLNGPRGDGYRNMFAKSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDG 261

                  ...
gi 1447699393 249 GLV 251
Cdd:PRK06940  262 GAT 264
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
13-122 4.18e-06

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. 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: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 46.91  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKASHPaGDKLHIVQCDLACPQSVSALCEqierqagKIDVL 92
Cdd:cd05257     1 NVLVTGADGFIGSHLTERLLREGHEVRALDIYNSFNSWGLLDNAV-HDRFHFISGDVRDASEVEYLVK-------KCDVV 72
                          90       100       110
                  ....*....|....*....|....*....|
gi 1447699393  93 VNNAGIVKDSLfasmSYEDFTQVIETNMFS 122
Cdd:cd05257    73 FHLAALIAIPY----SYTAPLSYVETNVFG 98
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
10-204 6.20e-06

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 46.24  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  10 NEKTVLVTGASGDIGLGICEKYLEQNcdvyalykSNDVQLTALKaSHPAGDKLhIVQCDLACPQSVS------------- 76
Cdd:PRK07904    7 NPQTILLLGGTSEIGLAICERYLKNA--------PARVVLAALP-DDPRRDAA-VAQMKAAGASSVEvidfdaldtdshp 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  77 ALCEQIERQaGKIDVLVNNAGIVKDSLFASMSYEDFTQVIETNM---FSIFRLTKDALmllRAAENPAIINVASIAAliP 153
Cdd:PRK07904   77 KVIDAAFAG-GDVDVAIVAFGLLGDAEELWQNQRKAVQIAEINYtaaVSVGVLLGEKM---RAQGFGQIIAMSSVAG--E 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1447699393 154 SVGQAN--YSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRA 204
Cdd:PRK07904  151 RVRRSNfvYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSAHAKEA 203
PRK06953 PRK06953
SDR family oxidoreductase;
12-119 1.18e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 45.06  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKSnDVQLTALKAshpAGDKLHIVqcDLACPQSVSALCEQIERQagKIDV 91
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIATARD-AAALAALQA---LGAEALAL--DVADPASVAGLAWKLDGE--ALDA 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1447699393  92 LVNNAGIV--KDSLFASMSYEDFTQVIETN 119
Cdd:PRK06953   74 AVYVAGVYgpRTEGVEPITREDFDAVMHTN 103
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
12-197 1.38e-05

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: 45.28  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVY----ALYKSNDVQLTALKASHPAgdKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:cd09809     2 KVIIITGANSGIGFETARSFALHGAHVIlacrNMSRASAAVSRILEEWHKA--RVEAMTLDLASLRSVQRFAEAFKAKNS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGIVkdSLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVAS----IAALIPSVGQAN---- 159
Cdd:cd09809    80 PLHVLVCNAAVF--ALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSeshrFTDLPDSCGNLDfsll 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1447699393 160 ------------YSASKGAILGFTRTLAAEMAPWGVRVNAVAPG-MIESKM 197
Cdd:cd09809   158 sppkkkywsmlaYNRAKLCNILFSNELHRRLSPRGITSNSLHPGnMMYSSI 208
PRK06101 PRK06101
SDR family oxidoreductase;
13-200 1.68e-05

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 44.86  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVqltaLKASHPAGDKLHIVQCDLACPQSVSALCEQIERQAgkiDVL 92
Cdd:PRK06101    3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSV----LDELHTQSANIFTLAFDVTDHPGTKAALSQLPFIP---ELW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  93 VNNA--------GIVKDSLFAsmsyedftQVIETNMFSIFRLTKDALMLLRAAENPAIinVASIAALIPSVGQANYSASK 164
Cdd:PRK06101   76 IFNAgdceymddGKVDATLMA--------RVFNVNVLGVANCIEGIQPHLSCGHRVVI--VGSIASELALPRAEAYGASK 145
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKK 200
Cdd:PRK06101  146 AAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDK 181
PRK06196 PRK06196
oxidoreductase; Provisional
8-208 2.08e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 44.67  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393   8 DLNEKTVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALKAShpagDKLHIVQCDLACPQSVSALCEQIERQAG 87
Cdd:PRK06196   23 DLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI----DGVEVVMLDLADLESVRAFAERFLDSGR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  88 KIDVLVNNAGI-------VKDSLFASMSyedftqvieTNMFSIFRLTKDALMLLRAAENPAIINVASIAALIPSVG---- 156
Cdd:PRK06196   99 RIDILINNAGVmacpetrVGDGWEAQFA---------TNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRSPIRwddp 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699393 157 ---------QAnYSASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVSRAVVRA 208
Cdd:PRK06196  170 hftrgydkwLA-YGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQRHLPREEQVA 229
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
14-150 2.12e-05

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. 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: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 44.67  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvQLTALKASHPAG---DKLHIVQCDLACPQ-SVSAlcEQIERQAGKI 89
Cdd:cd05263     1 VFVTGGTGFLGRHLVKRLLENGFKVLVLVRSES-LGEAHERIEEAGleaDRVRVLEGDLTQPNlGLSA--AASRELAGKV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699393  90 DVLVNNAgivkdslfASMSYEDFTQVI-ETNMFSifrlTKDALMLLRAAENPAIINVASIAA 150
Cdd:cd05263    78 DHVIHCA--------ASYDFQAPNEDAwRTNIDG----TEHVLELAARLDIQRFHYVSTAYV 127
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
14-208 3.80e-05

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 43.83  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNDVQLTALkashpaGDKLHIVQCDLACPQSVSALCEQIerqagKIDVLV 93
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTAR------LADLRFVEGDLTDRDALEKLLADV-----RPDAVI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  94 NNAGI--VKDSLfasmsyEDFTQVIETNmfsiFRLTKDALMLLRAAENPAIINVASIA-----ALIPSVGQAN------- 159
Cdd:pfam01370  70 HLAAVggVGASI------EDPEDFIEAN----VLGTLNLLEAARKAGVKRFLFASSSEvygdgAEIPQEETTLtgplapn 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699393 160 --YSASKgaiLGFTRTLAAEMAPWGVRV------NAVAPGMIESKMVKKVSRAVVRA 208
Cdd:pfam01370 140 spYAAAK---LAGEWLVLAYAAAYGLRAvilrlfNVYGPGDNEGFVSRVIPALIRRI 193
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
13-98 6.16e-05

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 42.61  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvqltalKASHPAGDKLHIVQCDLACPQSVSALCEqierqagKIDVL 92
Cdd:cd05243     1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPS------QAEKLEAAGAEVVVGDLTDAESLAAALE-------GIDAV 67

                  ....*.
gi 1447699393  93 VNNAGI 98
Cdd:cd05243    68 ISAAGS 73
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
13-105 7.06e-05

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: 42.53  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVYALYKSNDvqltalKASHPAGDKLHIVQCDLACPQSVSALCEqierqaGkIDVL 92
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPE------KAAALAAAGVEVVQGDLDDPESLAAALA------G-VDAV 67
                          90
                  ....*....|...
gi 1447699393  93 VNNAGIVKDSLFA 105
Cdd:COG0702    68 FLLVPSGPGGDFA 80
PRK07102 PRK07102
SDR family oxidoreductase;
12-209 8.87e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 42.60  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYaLYKSNDVQLTALKASHPA--GDKLHIVQCDLACPQSVSALCEQIErqaGKI 89
Cdd:PRK07102    2 KKILIIGATSDIARACARRYAAAGARLY-LAARDVERLERLADDLRArgAVAVSTHELDILDTASHAAFLDSLP---ALP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  90 DVLVNNAGIVKDSLFASMSYEDFTQVIETNMFSIfrltkdALMLLRAAENPAIINVASIAAlIPSVG-----QANY--SA 162
Cdd:PRK07102   78 DIVLIAVGTLGDQAACEADPALALREFRTNFEGP------IALLTLLANRFEARGSGTIVG-ISSVAgdrgrASNYvyGS 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 163 SKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMV-------------KKVSRAVVRAV 209
Cdd:PRK07102  151 AKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTaglklpgpltaqpEEVAKDIFRAI 210
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
13-69 2.71e-04

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. 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. 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: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 41.49  E-value: 2.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCDVYALYKS--NDVQLTALKASHPAGDKLHIVQCDL 69
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLKAGYKVRGTVRSlsKSAKLKALLKAAGYNDRLEFVIVDD 59
PLN02780 PLN02780
ketoreductase/ oxidoreductase
89-199 3.09e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 41.39  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  89 IDVLVNNAGIVKD--SLFASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAENPAIINVASIAA-LIPSVG-QANYSASK 164
Cdd:PLN02780  133 VGVLINNVGVSYPyaRFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAiVIPSDPlYAVYAATK 212
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1447699393 165 GAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVK 199
Cdd:PLN02780  213 AYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMAS 247
PRK05884 PRK05884
SDR family oxidoreductase;
141-249 9.24e-04

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 39.41  E-value: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 141 AIINVAsiaALIPSVGQANySASKGAILGFTRTLAAEMAPWGVRVNAVAPGmieskmvkKVSRAVVRAVTSTIPlrrlGK 220
Cdd:PRK05884  125 SIISVV---PENPPAGSAE-AAIKAALSNWTAGQAAVFGTRGITINAVACG--------RSVQPGYDGLSRTPP----PV 188
                          90       100
                  ....*....|....*....|....*....
gi 1447699393 221 CEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK05884  189 AAEIARLALFLTTPAARHITGQTLHVSHG 217
PLN00015 PLN00015
protochlorophyllide reductase
15-150 9.83e-04

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 39.69  E-value: 9.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  15 LVTGASGDIGLGiCEKYLEQNCDVYALYKSNDVqLTALKASHPAG---DKLHIVQCDLACPQSVSALCEQIERQAGKIDV 91
Cdd:PLN00015    1 IITGASSGLGLA-TAKALAETGKWHVVMACRDF-LKAERAAKSAGmpkDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699393  92 LVNNAGI----VKDSLFASmsyEDFTQVIETNMFSIFRLTKDALMLLRAAENPA--IINVASIAA 150
Cdd:PLN00015   79 LVCNAAVylptAKEPTFTA---DGFELSVGTNHLGHFLLSRLLLDDLKKSDYPSkrLIIVGSITG 140
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
13-162 1.59e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 39.17  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGlGICEKYLEQNCDVY----------------ALYKsndvQLTALKAShpagdkLHIVQCDLACPQSVS 76
Cdd:cd08956   195 TVLITGGTGTLG-ALLARHLVTEHGVRhlllvsrrgpdapgaaELVA----ELAALGAE------VTVAACDVADRAALA 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  77 ALCEQIERQAGKIDVlVNNAGIVKDSLFASMSYEDFTQVietnmfsiFRLTKDALMLL----RAAENPAIINVASIAALI 152
Cdd:cd08956   264 ALLAAVPADHPLTAV-VHAAGVLDDGVLTSLTPERLDAV--------LRPKVDAAWHLheltRDLDLAAFVLFSSAAGVL 334
                         170
                  ....*....|
gi 1447699393 153 PSVGQANYSA 162
Cdd:cd08956   335 GSPGQANYAA 344
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
13-253 1.60e-03

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 39.32  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  13 TVLVTGASGDIGLGICEKYLEQNCD--VYALYKSNDVQ---------LTALKASHPAG--DKLHIVQCDLACPQSVSAlC 79
Cdd:TIGR01746   1 TVLLTGATGFLGAYLLEELLRRSTRakVICLVRADSEEhamerlreaLRSYRLWHENLamERIEVVAGDLSKPRLGLS-D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  80 EQIERQAGKIDVLVNNAGIVkDSLFasmSYEDFTqviETNMfsifRLTKDALMLLRAAENPAIINVASIAALIPSVGQAN 159
Cdd:TIGR01746  80 AEWERLAENVDTIVHNGALV-NHVY---PYSELR---GANV----LGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 160 Y-------SASKGAILGFTRT------LAAEMAPWGVRVNAVAPGMI---ESKMVKKVSRAVVRAVTSTIPLRRLGKCEE 223
Cdd:TIGR01746 149 VteddatvTPYPGLAGGYTQSkwvaelLVREASDRGLPVTIVRPGRIlgdSYTGAWNSSDILWRMVKGCLALGAYPQSPE 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1447699393 224 ----------VANTIVFLSSSASSYIVGQTIVIDGGLVMR 253
Cdd:TIGR01746 229 ltedltpvdfVARAIVALSSRPAASAGGIVFHVVNPNPVP 268
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
14-100 1.92e-03

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


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 38.57  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSndvqltalkashpagdklhivQCDLACPQSVSALCEQIerqagKIDVLV 93
Cdd:COG1091     2 ILVTGANGQLGRALVRLLAERGYEVVALDRS---------------------ELDITDPEAVAALLEEV-----RPDVVI 55

                  ....*..
gi 1447699393  94 NNAGIVK 100
Cdd:COG1091    56 NAAAYTA 62
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
64-249 1.93e-03

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 38.77  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  64 IVQCDLACPQSVSALCEQIERQAGKIDVLVNNAGIVKDSL----FASMSYEDFTQVIETNMFSIFRLTKDALMLLRAAen 139
Cdd:PRK07889   61 VLELDVTNEEHLASLADRVREHVDGLDGVVHSIGFAPQSAlggnFLDAPWEDVATALHVSAYSLKSLAKALLPLMNEG-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393 140 paiinvASIAALI--PSVGQANYS---ASKGAILGFTRTLAAEMAPWGVRVNAVAPGMIESKMVKKVS--RAVVRAVTST 212
Cdd:PRK07889  139 ------GSIVGLDfdATVAWPAYDwmgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAIPgfELLEEGWDER 212
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1447699393 213 IPLR-RLGKCEEVANTIVFLSSSASSYIVGQTIVIDGG 249
Cdd:PRK07889  213 APLGwDVKDPTPVARAVVALLSDWFPATTGEIVHVDGG 250
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
12-98 2.96e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 38.00  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  12 KTVLVTGASGDIGLGICEKYLEQNCDVYALYKsNDVQLTALKASHPAGDkLHIVQCDLACPQSvsalceqIERQAGKIDV 91
Cdd:cd05271     1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYR-CEAYARRLLVMGDLGQ-VLFVEFDLRDDES-------IRKALEGSDV 71

                  ....*..
gi 1447699393  92 LVNNAGI 98
Cdd:cd05271    72 VINLVGR 78
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
14-100 3.28e-03

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: 37.99  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699393  14 VLVTGASGDIGLGICEKYLEQNCDVYALYKSNdvqltalkashpagdkLHIVQCDLACPQSVSALCEQIerqagKIDVLV 93
Cdd:cd05254     2 ILITGATGMLGRALVRLLKERGYEVIGTGRSR----------------ASLFKLDLTDPDAVEEAIRDY-----KPDVII 60

                  ....*..
gi 1447699393  94 NNAGIVK 100
Cdd:cd05254    61 NCAAYTR 67
 
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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