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Conserved domains on  [gi|1482408268|gb|AYC36488|]
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Dihydroanticapsin 7-dehydrogenase [Streptomyces griseorubiginosus]

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
PubMed:  7742302|19011748|12604210|19011750
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 ...
 1-241 3.75e-84

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: 251.24  E-value: 3.75e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:COG1028     1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEaaaaelraagGRALAVAADVTDEAAVEALVAAAVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:COG1028    81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgadDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:COG1028   161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALL----GAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236

                         250
                  ....*....|.
gi 1482408268 231 TGTALAVDGGM 241
Cdd:COG1028   237 TGQVLAVDGGL 247
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-241 3.75e-84

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: 251.24  E-value: 3.75e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:COG1028     1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEaaaaelraagGRALAVAADVTDEAAVEALVAAAVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:COG1028    81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgadDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:COG1028   161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALL----GAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236

                         250
                  ....*....|.
gi 1482408268 231 TGTALAVDGGM 241
Cdd:COG1028   237 TGQVLAVDGGL 247
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 9-238 2.29e-69

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: 213.30  E-value: 2.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH---------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAelaaiealgGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1482408268 160 AADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAEraalnARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVD 238
Cdd:cd05233   161 ALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELA-----AAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4-241 1.21e-66

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 206.55  E-value: 1.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK05653    3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEalaaelraagGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK05653   83 LDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK05653  163 GFTKALALELASRGITVNAVAPGFIDTDMTEGL------PEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQ 236


                  ....*...
gi 1482408268 234 ALAVDGGM 241
Cdd:PRK05653  237 VIPVNGGM 244
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 16-241 1.93e-63

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: 198.04  E-value: 1.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  16 SGIGRAVAERLAERGANVAVLDLDPSGVH--------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGIG--A 85
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKrveelaeeLGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFApkL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  86 VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVR 165
Cdd:pfam13561  86 KGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGG--SIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482408268 166 EGIRVNCVNPGTVDTPwvsrLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGGM 241
Cdd:pfam13561 164 RGIRVNAISPGPIKTL----AASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 9-241 7.44e-52

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: 168.54  E-value: 7.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLD-------------LDPSGVHGplTGIRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYrsseegaeevveeLKALGVKA--LGVVLDVSDREDVKAVVEEIEEELGTID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:TIGR01830  79 ILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:TIGR01830 159 TKSLAKELASRNITVNAVAPGFIDTDMTDKL------SEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVI 232


                  ....*.
gi 1482408268 236 AVDGGM 241
Cdd:TIGR01830 233 HVDGGM 238
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 10-147 6.15e-09

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: 54.03  E-value: 6.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   10 VVTGGASGIGRAVAERLAERGA-NVAVL---DLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGLD 75
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLsrsGPDAPGAAALLAELEAagarvtvvacDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268   76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPH-LRRsahasVVNVCSIAATAGLPQRALYSA 147
Cdd:smart00822  84 GVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLpLDF-----FVLFSSIAGVLGSPGQANYAA 151
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-241 3.75e-84

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: 251.24  E-value: 3.75e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:COG1028     1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEaaaaelraagGRALAVAADVTDEAAVEALVAAAVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:COG1028    81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgadDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:COG1028   161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALL----GAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236

                         250
                  ....*....|.
gi 1482408268 231 TGTALAVDGGM 241
Cdd:COG1028   237 TGQVLAVDGGL 247
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 9-238 2.29e-69

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: 213.30  E-value: 2.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH---------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAelaaiealgGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1482408268 160 AADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAEraalnARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVD 238
Cdd:cd05233   161 ALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELA-----AAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
4-241 1.21e-66

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 206.55  E-value: 1.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK05653    3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEalaaelraagGEARVLVFDVSDEAAVRALIEAAVEAFGA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK05653   83 LDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK05653  163 GFTKALALELASRGITVNAVAPGFIDTDMTEGL------PEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQ 236


                  ....*...
gi 1482408268 234 ALAVDGGM 241
Cdd:PRK05653  237 VIPVNGGM 244
PRK06138 PRK06138
SDR family oxidoreductase;
9-240 2.35e-66

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 206.16  E-value: 2.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH---------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PRK06138    8 AIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAErvaaaiaagGRAFARQGDVGSAEAVEALVDFVAARWGRLDVLVN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:PRK06138   88 NAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASLTRAM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 160 AADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDG 239
Cdd:PRK06138  168 ALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATGTTLVVDG 247


                  .
gi 1482408268 240 G 240
Cdd:PRK06138  248 G 248
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 16-241 1.93e-63

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: 198.04  E-value: 1.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  16 SGIGRAVAERLAERGANVAVLDLDPSGVH--------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGIG--A 85
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKrveelaeeLGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFApkL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  86 VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVR 165
Cdd:pfam13561  86 KGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGG--SIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482408268 166 EGIRVNCVNPGTVDTPwvsrLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGGM 241
Cdd:pfam13561 164 RGIRVNAISPGPIKTL----AASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-241 9.08e-63

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 197.01  E-value: 9.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAV-LDLDPSGV----------HGPLTGIRADVSDDVGVRAAVAAAAE 69
Cdd:PRK12825    1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVVVhYRSDEEAAeelveavealGRRAQAVQADVTDKAALEAAVAAAVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  70 RLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATK 149
Cdd:PRK12825   81 RFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRlldgadDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK12825  161 AGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEA------TIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDY 234

                         250
                  ....*....|..
gi 1482408268 230 VTGTALAVDGGM 241
Cdd:PRK12825  235 ITGQVIEVTGGV 246
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-244 1.36e-61

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 194.51  E-value: 1.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGP--------LTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK12829    6 LKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATaarlpgakVTATVADVADPAQVERVFDTAVERFG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH-ASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:PRK12829   86 GLDVLVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHgGVIIALSSVAGRLGYPGRTPYAASKW 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRlLDGADDPEAERAALNARQ------PLGRLVTADEVAAAVLYLAG 224
Cdd:PRK12829  166 AVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRR-VIEARAQQLGIGLDEMEQeylekiSLGRMVEPEDIAATALFLAS 244

                         250       260
                  ....*....|....*....|
gi 1482408268 225 PSAGSVTGTALAVDGGMQGL 244
Cdd:PRK12829  245 PAARYITGQAISVDGNVEYL 264
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-241 1.51e-61

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 193.52  E-value: 1.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV-LDLDPSGVHGPLTGIR----------ADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK05565    8 AIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKeeggdaiavkADVSSEEDVENLVEQIVEKFGKIDIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK05565   88 VNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVNAFTK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAV 237
Cdd:PRK05565  168 ALAKELAPSGIRVNAVAPGAIDTEMWSSF------SEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITV 241


                  ....
gi 1482408268 238 DGGM 241
Cdd:PRK05565  242 DGGW 245
PRK12826 PRK12826
SDR family oxidoreductase;
1-242 1.91e-61

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 193.59  E-value: 1.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV----------HGPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK12826    1 TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAaataelveaaGGKARARQVDVRDRAALKAAVAAGVED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAA-TAGLPQRALYSATK 149
Cdd:PRK12826   81 FGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGpRVGYPGLAHYAASK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDgaddpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK12826  161 AGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGD-----AQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARY 235

                         250
                  ....*....|...
gi 1482408268 230 VTGTALAVDGGMQ 242
Cdd:PRK12826  236 ITGQTLPVDGGAT 248
FabG-like PRK07231
SDR family oxidoreductase;
4-241 1.41e-60

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 191.20  E-value: 1.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV---------HGPLTGIRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK07231    3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAervaaeilaGGRAIAVAADVSDEADVEAAVAAALERFGSV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIG-AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK07231   83 DILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdGADDPEAeRAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK07231  163 TLTKALAAELGPDKIRVNAVAPVVVETGLLEAFM-GEPTPEN-RAKFLATIPLGRLGTPEDIANAALFLASDEASWITGV 240


                  ....*...
gi 1482408268 234 ALAVDGGM 241
Cdd:PRK07231  241 TLVVDGGR 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 9-223 2.90e-60

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: 190.01  E-value: 2.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV-------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:COG4221     8 ALITGASSGIGAATARALAAAGARVVLAARRAERLealaaelGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:COG4221    88 GVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1482408268 162 DHVREGIRVNCVNPGTVDTPWVSRLLDGadDPEAERAALNARQPLgrlvTADEVAAAVLYLA 223
Cdd:COG4221   168 ELRPTGIRVTVIEPGAVDTEFLDSVFDG--DAEAAAAVYEGLEPL----TPEDVAEAVLFAL 223
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 2-241 1.73e-59

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 188.48  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   2 TEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS-----------GVHGPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK05557    1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEagaealvaeigALGGKALAVQGDVSDAESVERAVDEAKAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:PRK05557   81 FGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:PRK05557  161 GVIGFTKSLARELASRGITVNAVAPGFIETDMTDAL------PEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYI 234

                         250
                  ....*....|.
gi 1482408268 231 TGTALAVDGGM 241
Cdd:PRK05557  235 TGQTLHVNGGM 245
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-241 8.68e-59

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: 186.52  E-value: 8.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS-----GVHGPLTGIRADVSDDVGVraavAAAAERLGGLDILVN 79
Cdd:cd05368     1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEklkelERGPGITTRVLDVTDKEQV----AALAKEEGRIDVLFN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAAT-AGLPQRALYSATKGAVLSLTLA 158
Cdd:cd05368    77 CAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSiKGVPNRFVYSTTKAAVIGLTKS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVD 238
Cdd:cd05368   157 VAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVID 236


                  ...
gi 1482408268 239 GGM 241
Cdd:cd05368   237 GGW 239
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-223 2.20e-56

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 180.45  E-value: 2.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEalaaelraagARVEVVALDVTDPDAVAALAEAVLARFGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:COG0300    83 IDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPeaeraalnarqplgrLVTADEVAAAVLYLA 223
Cdd:COG0300   163 GFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRP---------------LLSPEEVARAILRAL 217
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 9-241 2.40e-56

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: 180.05  E-value: 2.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLT----------GIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05333     3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEeikalggnaaALEADVSDREAVEALVEKVEAEFGPVDILV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:cd05333    83 NNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVD 238
Cdd:cd05333   163 LAKELASRGITVNAVAPGFIDTDMTDAL------PEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVN 236


                  ...
gi 1482408268 239 GGM 241
Cdd:cd05333   237 GGM 239
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 9-181 1.59e-53

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 171.26  E-value: 1.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEavakelgalgGKALFIQGDVTDRAQVKALVEQAVERLGRLDILV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:pfam00106  83 NNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRS 162

                         170       180
                  ....*....|....*....|...
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTP 181
Cdd:pfam00106 163 LALELAPHGIRVNAVAPGGVDTD 185
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 6-240 9.08e-53

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 172.53  E-value: 9.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS-------------GVHGPLtgIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK06701   46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHedanetkqrvekeGVKCLL--IPGDVSDEAFCKDAVEETVRELG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGA-VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAATAGLPQRALYSATKGA 151
Cdd:PRK06701  124 RLDILVNNAAFQYpQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGS--AIINTGSITGYEGNETLIDYSATKGA 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 152 VLSLTLAMAADHVREGIRVNCVNPGTVDTPwvsrlLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:PRK06701  202 IHAFTRSLAQSLVQKGIRVNAVAPGPIWTP-----LIPSDFDEEKVSQFGSNTPMQRPGQPEELAPAYVFLASPDSSYIT 276


                  ....*....
gi 1482408268 232 GTALAVDGG 240
Cdd:PRK06701  277 GQMLHVNGG 285
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-241 9.19e-53

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: 171.39  E-value: 9.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAV-------LDLDPSGVHGP---LTGIRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:cd05347     4 KGKVALVTGASRGIGFGIASGLAEAGANIVInsrneekAEEAQQLIEKEgveATAFTCDVSDEEAIKAAVEAIEEDFGKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd05347    84 DILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldGADDPEAERaaLNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:cd05347   164 LTKALATEWARHGIQVNAIAPGYFATEMTEAV--VADPEFNDD--ILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQI 239


                  ....*..
gi 1482408268 235 LAVDGGM 241
Cdd:cd05347   240 IFVDGGW 246
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 9-241 7.44e-52

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: 168.54  E-value: 7.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLD-------------LDPSGVHGplTGIRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYrsseegaeevveeLKALGVKA--LGVVLDVSDREDVKAVVEEIEEELGTID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:TIGR01830  79 ILVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:TIGR01830 159 TKSLAKELASRNITVNAVAPGFIDTDMTDKL------SEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVI 232


                  ....*.
gi 1482408268 236 AVDGGM 241
Cdd:TIGR01830 233 HVDGGM 238
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-240 1.22e-51

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 168.68  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK06841   13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEvaaqllgGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:PRK06841   93 LVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGMT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGaddPEAERAalNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALA 236
Cdd:PRK06841  173 KVLALEWGPYGITVNAISPTVVLTELGKKAWAG---EKGERA--KKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLV 247


                  ....
gi 1482408268 237 VDGG 240
Cdd:PRK06841  248 IDGG 251
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 9-240 6.28e-51

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: 166.41  E-value: 6.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:cd05345     8 AIVTGAGSGFGEGIARRFAQEGARVVIADINADGAErvaadigEAAIAIQADVTKRADVEAMVEAALSKFGRLDILVNNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGT-VEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMA 160
Cdd:cd05345    88 GITHRNKpMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTATKAMA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 161 ADHVREGIRVNCVNPGTVDTPWVSRLLdGADDPEAeRAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:cd05345   168 VELAPRNIRVNCLCPVAGETPLLSMFM-GEDTPEN-RAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVALEVDGG 245
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 6-241 6.33e-51

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: 166.68  E-value: 6.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAV-------LDLDPSGVHGPLTG---IRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAIcarnrenLERAASELRAGGAGvlaVVADLTDPEDIDRLVEKAGDAFGRVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:cd05344    81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTP-WVSRLLDGAD----DPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:cd05344   161 VKTLSRELAPDGVTVNSVLPGYIDTErVRRLLEARAEkegiSVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKASYI 240

                         250
                  ....*....|.
gi 1482408268 231 TGTALAVDGGM 241
Cdd:cd05344   241 TGQAILVDGGL 251
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-241 1.25e-50

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: 166.02  E-value: 1.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAV-LDLDPSG----------VHGPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:cd05358     2 KGKVALVTGASSGIGKAIAIRLATAGANVVVnYRSKEDAaeevveeikaVGGKAIAVQADVSKEEDVVALFQSAIKEFGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRS-AHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:cd05358    82 LDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSkIKGKIINMSSVHEKIPWPGHVNYAASKGGV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrllDGADDPEAERAALNaRQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:cd05358   162 KMMTKTLAQEYAPKGIRVNAIAPGAINTPINA---EAWDDPEQRADLLS-LIPMGRIGEPEEIAAAAAWLASDEASYVTG 237


                  ....*....
gi 1482408268 233 TALAVDGGM 241
Cdd:cd05358   238 TTLFVDGGM 246
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 9-242 1.30e-50

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: 166.01  E-value: 1.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLD-------------PSGVHGplTGIRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:cd05366     5 AIITGAAQGIGRAIAERLAADGFNIVLADLNleeaakstiqeisEAGYNA--VAVGADVTDKDDVEALIDQAVEKFGSFD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHAS-VVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd05366    83 VMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGkIINASSIAGVQGFPNLGAYSASKFAVRG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDG----ADDPEAERAALNARQ-PLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:cd05366   163 LTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEvgeiAGKPEGEGFAEFSSSiPLGRLSEPEDVAGLVSFLASEDSDY 242

                         250
                  ....*....|...
gi 1482408268 230 VTGTALAVDGGMQ 242
Cdd:cd05366   243 ITGQTILVDGGMV 255
PRK07069 PRK07069
short chain dehydrogenase; Validated
 8-241 1.41e-50

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 165.65  E-value: 1.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV-----------HGPLTGIRA--DVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK07069    1 RAFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGldafaaeinaaHGEGVAFAAvqDVTDEAQWQALLAQAADAMGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK07069   81 SVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNC--VNPGTVDTPWVSRLLDGADDPEAERAAlnARQ-PLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:PRK07069  161 LTKSIALDCARRGLDVRCnsIHPTFIRTGIVDPIFQRLGEEEATRKL--ARGvPLGRLGEPDDVAHAVLYLASDESRFVT 238

                         250
                  ....*....|
gi 1482408268 232 GTALAVDGGM 241
Cdd:PRK07069  239 GAELVIDGGI 248
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
9-242 3.82e-50

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 164.90  E-value: 3.82e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK08643    5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQaaadklskdgGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNVVV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH-ASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK08643   85 NNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVGNPELAVYSSTKFAVRGLTQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTP-WVS---RLLDGADDPEAERAALNARQ-PLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK08643  165 TAARDLASEGITVNAYAPGIVKTPmMFDiahQVGENAGKPDEWGMEQFAKDiTLGRLSEPEDVANCVSFLAGPDSDYITG 244

                         250
                  ....*....|
gi 1482408268 233 TALAVDGGMQ 242
Cdd:PRK08643  245 QTIIVDGGMV 254
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-241 4.36e-50

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 164.37  E-value: 4.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK12939    2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARelaaaleaagGRAHAIAADLADPASVQRFFDAAAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:PRK12939   82 LGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVsrlldgADDPEAERAALNARQ-PLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK12939  162 AVIGMTRSLARELGGRGITVNAIAPGLTATEAT------AYVPADERHAYYLKGrALERLQVPDDVAGAVLFLLSDAARF 235

                         250
                  ....*....|..
gi 1482408268 230 VTGTALAVDGGM 241
Cdd:PRK12939  236 VTGQLLPVNGGF 247
PRK09242 PRK09242
SDR family oxidoreductase;
6-241 4.75e-50

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 164.54  E-value: 4.75e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANV------------AVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK09242    9 GQTALITGASKGIGLAIAREFLGLGADVlivardadalaqARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHWDG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK09242   89 LHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAALL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEAERAALNaRQPLGRLVTADEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK09242  169 QMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPL---SDPDYYEQVIE-RTPMRRVGEPEEVAAAVAFLCMPAASYITGQ 244


                  ....*...
gi 1482408268 234 ALAVDGGM 241
Cdd:PRK09242  245 CIAVDGGF 252
PRK07062 PRK07062
SDR family oxidoreductase;
3-240 1.06e-49

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 164.06  E-value: 1.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDP---SGVHGPLTG---------IRADVSDDVGVRAAVAAAAER 70
Cdd:PRK07062    5 QLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEerlASAEARLREkfpgarllaARCDVLDEADVAAFAAAVEAR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:PRK07062   85 FGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARQ------PLGRLVTADEVAAAVLYLAG 224
Cdd:PRK07062  165 GLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQSWEAWTAALarkkgiPLGRLGRPDEAARALFFLAS 244

                         250
                  ....*....|....*.
gi 1482408268 225 PSAGSVTGTALAVDGG 240
Cdd:PRK07062  245 PLSSYTTGSHIDVSGG 260
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 9-223 6.11e-49

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: 161.24  E-value: 6.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGP-------LTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:cd05374     3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLgellndnLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:cd05374    83 GYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLRL 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 162 DHVREGIRVNCVNPGTVDTPWVSRLLDGAD--------DPEAERAALNARQPLGRLVTADEVAAAVLYLA 223
Cdd:cd05374   163 ELAPFGIKVTIIEPGPVRTGFADNAAGSALedpeispyAPERKEIKENAAGVGSNPGDPEKVADVIVKAL 232
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 9-240 8.30e-49

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 161.21  E-value: 8.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK12429    7 ALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAaaaealqkagGKAIGVAMDVTDEEAINAGIDYAVETFGGVDILV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:PRK12429   87 NNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGLTKV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTPWVSRLLD------GADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK12429  167 VALEGATHGVTVNAICPGYVDTPLVRKQIPdlakerGISEEEVLEDVLLPLVPQKRFTTVEEIADYALFLASFAAKGVTG 246


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:PRK12429  247 QAWVVDGG 254
PRK06398 PRK06398
aldose dehydrogenase; Validated
 1-244 1.76e-48

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 160.77  E-value: 1.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGVhgPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PRK06398    1 DLGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIkEPSYN--DVDYFKVDVSNKEQVIKGIDYVISKYGRIDILVN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:PRK06398   79 NAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 160 AADHVrEGIRVNCVNPGTVDTP---WVSRLLDGADDPEAERAALN--ARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:PRK06398  159 AVDYA-PTIRCVAVCPGSIRTPlleWAAELEVGKDPEHVERKIREwgEMHPMKRVGKPEEVAYVVAFLASDLASFITGEC 237

                         250
                  ....*....|
gi 1482408268 235 LAVDGGMQGL 244
Cdd:PRK06398  238 VTVDGGLRAL 247
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-240 2.11e-48

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 160.05  E-value: 2.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHG-PLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:PRK08220    5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDyPFATFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:PRK08220   85 GILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 162 DHVREGIRVNCVNPGTVDTPwVSRLLDGADDPEAERAALNARQ-----PLGRLVTADEVAAAVLYLAGPSAGSVTGTALA 236
Cdd:PRK08220  165 ELAPYGVRCNVVSPGSTDTD-MQRTLWVDEDGEQQVIAGFPEQfklgiPLGKIARPQEIANAVLFLASDLASHITLQDIV 243


                  ....
gi 1482408268 237 VDGG 240
Cdd:PRK08220  244 VDGG 247
PRK06172 PRK06172
SDR family oxidoreductase;
1-240 3.79e-48

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 159.53  E-value: 3.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAER 70
Cdd:PRK06172    2 SMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREaggealfvacDVTRDAEVKALVEQTIAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATK 149
Cdd:PRK06172   82 YGRLDYAFNNAGIeIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGadDPEAeRAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK06172  162 HAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEA--DPRK-AEFAAAMHPVGRIGKVEEVASAVLYLCSDGASF 238

                         250
                  ....*....|.
gi 1482408268 230 VTGTALAVDGG 240
Cdd:PRK06172  239 TTGHALMVDGG 249
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 9-249 6.00e-48

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 159.13  E-value: 6.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSG---VHGPLTG--IRADVSDDVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:PRK06057   10 AVITGGGSGIGLATARRLAAEGATVVVGDIDPEAgkaAADEVGGlfVPTDVTDEDAVNALFDTAAETYGSVDIAFNNAGI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAV--GTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRAL-YSATKGAVLSLTLAMA 160
Cdd:PRK06057   90 SPPedDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIsYTASKGGVLAMSRELG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 161 ADHVREGIRVNCVNPGTVDTPWVSRLLdgADDPeaERAALN-ARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDG 239
Cdd:PRK06057  170 VQFARQGIRVNALCPGPVNTPLLQELF--AKDP--ERAARRlVHVPMGRFAEPEEIAAAVAFLASDDASFITASTFLVDG 245

                         250
                  ....*....|
gi 1482408268 240 GMQGLRLRPV 249
Cdd:PRK06057  246 GISGAYVTPL 255
PRK06500 PRK06500
SDR family oxidoreductase;
1-241 8.35e-48

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 158.58  E-value: 8.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV--------HGPLTgIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK06500    1 MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLeaaraelgESALV-IRADAGDVAAQKALAQALAEAFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK06500   80 RLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPA--SIVLNGSINAHIGMPNSSVYAASKAAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK06500  158 LSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVG 237


                  ....*....
gi 1482408268 233 TALAVDGGM 241
Cdd:PRK06500  238 SEIIVDGGM 246
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-240 9.49e-48

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 157.82  E-value: 9.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDP-SGVHGPLTGIRADVSDDVGvraavaAAAERLGGLDILVNNA 81
Cdd:PRK06550    2 EFMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDkPDLSGNFHFLQLDLSDDLE------PLFDWVPSVDILCNTA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMA 160
Cdd:PRK06550   76 GIlDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 161 ADHVREGIRVNCVNPGTVDTPwvsrlLDGADDPEAERAALNARQ-PLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDG 239
Cdd:PRK06550  156 LDYAKDGIQVFGIAPGAVKTP-----MTAADFEPGGLADWVAREtPIKRWAEPEEVAELTLFLASGKADYMQGTIVPIDG 230


                  .
gi 1482408268 240 G 240
Cdd:PRK06550  231 G 231
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 9-240 1.68e-47

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: 157.54  E-value: 1.68e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA-------DVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:cd05341     8 AIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDaarffhlDVTDEDGWTAVVDTAREAFGRLDVLVNNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:cd05341    88 GILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKSAAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 162 D--HVREGIRVNCVNPGTVDTPWVSRLLDGADDPeaeraALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDG 239
Cdd:cd05341   168 EcaTQGYGIRVNSVHPGYIYTPMTDELLIAQGEM-----GNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSELVVDG 242


                  .
gi 1482408268 240 G 240
Cdd:cd05341   243 G 243
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-240 1.97e-47

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 166.56  E-value: 1.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS---------GVHGPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK08324  419 PLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEaaeaaaaelGGPDRALGVACDVTDEAAVQAAFEEAALAFGG 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH-ASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK08324  499 VDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNPGPNFGAYGAAKAAE 578

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPwvSRLLDGA-------------DDPEAERAALNArqpLGRLVTADEVAAAV 219
Cdd:PRK08324  579 LHLVRQLALELGPDGIRVNGVNPDAVVRG--SGIWTGEwiearaaayglseEELEEFYRARNL---LKREVTPEDVAEAV 653

                         250       260
                  ....*....|....*....|.
gi 1482408268 220 LYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK08324  654 VFLASGLLSKTTGAIITVDGG 674
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 6-241 4.95e-47

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: 156.84  E-value: 4.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPL----------TGIRADVSDDVGVRAAVAAAAERLGG-L 74
Cdd:cd05329     6 GKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLtewrekgfkvEGSVCDVSSRSERQELMDTVASHFGGkL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd05329    86 NILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQ 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEaERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:cd05329   166 LTRSLACEWAKDNIRVNAVAPWVIATPLVEPVI---QQKE-NLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQI 241


                  ....*..
gi 1482408268 235 LAVDGGM 241
Cdd:cd05329   242 IAVDGGL 248
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 9-240 9.77e-47

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: 156.07  E-value: 9.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPS-----------GVHGPLTG-IRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:cd08940     5 ALVTGSTSGIGLGIARALAAAGANIVLNGFGDAaeieavraglaAKHGVKVLyHGADLSKPAAIEDMVAYAQRQFGGVDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:cd08940    85 LVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVVGLT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTPWVSRLLD------GADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:cd08940   165 KVVALETAGTGVTCNAICPGWVLTPLVEKQISalaqknGVPQEQAARELLLEKQPSKQFVTPEQLGDTAVFLASDAASQI 244

                         250
                  ....*....|
gi 1482408268 231 TGTALAVDGG 240
Cdd:cd08940   245 TGTAVSVDGG 254
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-240 1.56e-46

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 154.95  E-value: 1.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGI--------RADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK12828    2 EHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVpadalrigGIDLVDPQAARRAVDEVNRQFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK12828   82 RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPwvsrlLDGADDPEAEraalnarqpLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK12828  162 ARLTEALAAELLDRGITVNAVLPSIIDTP-----PNRADMPDAD---------FSRWVTPEQIAAVIAFLLSDEAQAITG 227


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:PRK12828  228 ASIPVDGG 235
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 9-240 2.15e-46

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: 155.18  E-value: 2.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGV---------HGPLT-GIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd05352    11 AIVTGGSRGIGLAIARALAEAGADVAIIYNsAPRAEekaeelakkYGVKTkAYKCDVSSQESVEKTFKQIQKDFGKIDIL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAAT-AGLPQ-RALYSATKGAVLSL 155
Cdd:cd05352    91 IANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTiVNRPQpQAAYNASKAAVIHL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPwvsrlLDGADDPEAeRAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:cd05352   171 AKSLAVEWAKYFIRVNSISPGYIDTD-----LTDFVDKEL-RKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDL 244


                  ....*
gi 1482408268 236 AVDGG 240
Cdd:cd05352   245 IIDGG 249
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-240 2.15e-46

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: 155.53  E-value: 2.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLD--------------PSGVHGPLtgIRADVSDDVGVRAAVAAAAER 70
Cdd:cd05355    25 KGKKALITGGDSGIGRAVAIAFAREGADVAINYLPeeeddaeetkklieEEGRKCLL--IPGDLGDESFCRDLVKEVVKE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIG-AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAATAGLPQRALYSATK 149
Cdd:cd05355   103 FGKLDILVNNAAYQhPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKGS--SIINTTSVTAYKGSPHLLDYAATK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrlldgADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:cd05355   181 GAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIP-----SSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSY 255

                         250
                  ....*....|.
gi 1482408268 230 VTGTALAVDGG 240
Cdd:cd05355   256 VTGQVLHVNGG 266
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
9-240 1.50e-45

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 152.61  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV-----------LDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK12824    5 ALVTGAKRGIGSAIARELLNDGYRVIAtyfsgndcakdWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK12824   85 VNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGFTK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAalnarqPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAV 237
Cdd:PRK12824  165 ALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQI------PMKRLGTPEEIAAAVAFLVSEAAGFITGETISI 238


                  ...
gi 1482408268 238 DGG 240
Cdd:PRK12824  239 NGG 241
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 4-240 1.89e-45

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: 152.57  E-value: 1.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS------------GVHG-PLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAErleetrqsclqaGVSEkKILLVVADLTEEEGQDRIISTTLAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:cd05364    81 FGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT-KGEIVNVSSVAGGRSFPGVLYYCISKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldGADDPEAER--AALNARQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:cd05364   160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRM--GMPEEQYIKflSRAKETHPLGRPGTVDEVAEAIAFLASDASS 237

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:cd05364   238 FITGQLLPVDGG 249
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 1-240 1.16e-44

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 150.93  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK08265    1 MIGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAavaaslgERARFIATDITDDAAIERAVATVVARFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNA------GIGAvgtvedhTDEQWHHVLDVNVVGMVRVTRAALPHLRRsAHASVVNVCSIAATAGLPQRALYSA 147
Cdd:PRK08265   81 VDILVNLActylddGLAS-------SRADWLAALDVNLVSAAMLAQAAHPHLAR-GGGAIVNFTSISAKFAQTGRWLYPA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGaDDPEAERAALNArQPLGRLVTADEVAAAVLYLAGPSA 227
Cdd:PRK08265  153 SKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGG-DRAKADRVAAPF-HLLGRVGDPEEVAQVVAFLCSDAA 230

                         250
                  ....*....|...
gi 1482408268 228 GSVTGTALAVDGG 240
Cdd:PRK08265  231 SFVTGADYAVDGG 243
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 9-240 1.16e-44

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: 150.14  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTG----------IRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05323     3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQainpkvkatfVQCDVTSWEQLAAAFKKAIEKFGRVDILI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIG--AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH---ASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:cd05323    83 NNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQFPVYSASKHGVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMA-ADHVREGIRVNCVNPGTVDTPWVsrlldgaddpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGsvTG 232
Cdd:cd05323   163 GFTRSLAdLLEYKTGVRVNAICPGFTNTPLL----------PDLVAKEAEMLPSAPTQSPEVVAKAIVYLIEDDEK--NG 230


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:cd05323   231 AIWIVDGG 238
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 9-240 1.39e-44

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: 150.12  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV----------------LDLDPSGVhgpltGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:cd05362     6 ALVTGASRGIGRAIAKRLARDGASVVVnyasskaaaeevvaeiEAAGGKAI-----AVQADVSDPSQVARLFDAAEKAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHasVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:cd05362    81 GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGR--IINISSSLTAAYTPNYGAYAGSKAAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPwvsrLLDGADDPEAErAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:cd05362   159 EAFTRVLAKELGGRGITVNAVAPGPVDTD----MFYAGKTEEAV-EGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNG 233


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:cd05362   234 QVIRANGG 241
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 9-240 4.64e-44

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: 148.77  E-value: 4.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPS---GVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGIGA 85
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVlllEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAGVLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  86 VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVR 165
Cdd:cd05331    81 PGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 166 EGIRVNCVNPGTVDTPWVSRLLDGaDDPEAERAALNARQ-----PLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:cd05331   161 YGVRCNVVSPGSTDTAMQRTLWHD-EDGAAQVIAGVPEQfrlgiPLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGG 239
PRK08589 PRK08589
SDR family oxidoreductase;
9-240 4.87e-44

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 149.54  E-value: 4.87e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDpSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK08589    9 AVITGASTGIGQASAIALAQEGAYVLAVDIA-EAVSetvdkiksngGKAKAYHVDISDEQQVKDFASEIKEQFGRVDVLF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPhLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK08589   88 NNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLP-LMMEQGGSIINTSSFSGQAADLYRSGYNAAKGAVINFTK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAE--RAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:PRK08589  167 SIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKtfRENQKWMTPLGRLGKPEEVAKLVVFLASDDSSFITGETI 246


                  ....*
gi 1482408268 236 AVDGG 240
Cdd:PRK08589  247 RIDGG 251
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-241 9.48e-44

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 147.94  E-value: 9.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANV-----AVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAaaerLGGLD 75
Cdd:PRK07060    4 AFDFSGKSVLVTGASSGIGRACAVALAQRGARVvaaarNAAALDRLAGETGCEPLRLDVGDDAAIRAALAA----AGAFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHA-SVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK07060   80 GLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGgSIVNVSSQAALVGLPDHLAYCASKAALDA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEAERAALnARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:PRK07060  160 ITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAW---SDPQKSGPML-AAIPLGRFAEVDDVAAPILFLLSDAASMVSGVS 235


                  ....*..
gi 1482408268 235 LAVDGGM 241
Cdd:PRK07060  236 LPVDGGY 242
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 2-241 2.37e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 147.36  E-value: 2.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   2 TEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLD-PSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNN 80
Cdd:PRK06523    5 LELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSrPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDILVHV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AG--IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRAL-YSATKGAVLSLTL 157
Cdd:PRK06523   85 LGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPESTTaYAAAKAALSTYSK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTPWVSRLLD------GADDPEAERAALNARQ--PLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK06523  165 SLSKEVAPKGVRVNTVSPGWIETEAAVALAErlaeaaGTDYEGAKQIIMDSLGgiPLGRPAEPEEVAELIAFLASDRAAS 244

                         250
                  ....*....|..
gi 1482408268 230 VTGTALAVDGGM 241
Cdd:PRK06523  245 ITGTEYVIDGGT 256
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-240 3.32e-43

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 147.10  E-value: 3.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHG-------PLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK07067    1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLaaleigpAAIAVSLDVTRQDSIDRIVAAAVERFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHL-RRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK07067   81 IDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMvEQGRGGKIINMASQAGRRGEALVSHYCATKAAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTP-WvsrllDGAD---------DPEAERAALNARQPLGRLVTADEVAAAVLYL 222
Cdd:PRK07067  161 ISYTQSAALALIRHGINVNAIAPGVVDTPmW-----DQVDalfaryenrPPGEKKRLVGEAVPLGRMGVPDDLTGMALFL 235

                         250
                  ....*....|....*...
gi 1482408268 223 AGPSAGSVTGTALAVDGG 240
Cdd:PRK07067  236 ASADADYIVAQTYNVDGG 253
PRK08267 PRK08267
SDR family oxidoreductase;
11-220 4.95e-43

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 146.62  E-value: 4.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLDPSGV------HGPLTGIRA--DVSDDVGVRAAVAAAAERLGG-LDILVNNA 81
Cdd:PRK08267    6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLaalaaeLGAGNAWTGalDVTDRAAWDAALADFAAATGGrLDVLFNNA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:PRK08267   86 GILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEALDL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1482408268 162 DHVREGIRVNCVNPGTVDTPwvsrLLDGadDPEAERAAlnARQPLGRLVTADEVAAAVL 220
Cdd:PRK08267  166 EWRRHGIRVADVMPLFVDTA----MLDG--TSNEVDAG--STKRLGVRLTPEDVAEAVW 216
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 5-248 5.78e-43

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: 146.28  E-value: 5.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGI------RADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGdncrfvPVDVTSEKDVKAALALAKAKFGRLDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIG-AVGTV-----EDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHAS------VVNVCSIAATAGLPQRALYS 146
Cdd:cd05371    81 NCAGIAvAAKTYnkkgqQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQggergvIINTASVAAFEGQIGQAAYS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 147 ATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQP-LGRLVTADEVAAAVLYLAGP 225
Cdd:cd05371   161 ASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGL------PEKVRDFLAKQVPfPSRLGDPAEYAHLVQHIIEN 234

                         250       260
                  ....*....|....*....|...
gi 1482408268 226 SAgsVTGTALAVDGgmqGLRLRP 248
Cdd:cd05371   235 PY--LNGEVIRLDG---AIRMPP 252
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 1-232 6.66e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 146.30  E-value: 6.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVL-------------DLDPSGVhgPLTGIRADVSDDVGVRAAVAAA 67
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVIcgrnaekgeaqaaELEALGA--KAVFVQADLSDVEDCRRVVAAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  68 AERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLR-RSAHASVVNVCSIAATAGLPQRALYS 146
Cdd:PRK06198   79 DEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRrRKAEGTIVNIGSMSAHGGQPFLAAYC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 147 ATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPW---VSRLLDGADDPEAERAAlnARQPLGRLVTADEVAAAVLYLA 223
Cdd:PRK06198  159 ASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEGedrIQREFHGAPDDWLEKAA--ATQPFGRLLDPDEVARAVAFLL 236


                  ....*....
gi 1482408268 224 GPSAGSVTG 232
Cdd:PRK06198  237 SDESGLMTG 245
PRK07063 PRK07063
SDR family oxidoreductase;
6-240 7.75e-43

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 145.96  E-value: 7.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLDLD------------PSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK07063    7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDaalaeraaaaiaRDVAGARVLAVPADVTDAASVAAAVAAAEEAFGP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK07063   87 LDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKHGLL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK07063  167 GLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLASDEAPFINAT 246


                  ....*..
gi 1482408268 234 ALAVDGG 240
Cdd:PRK07063  247 CITIDGG 253
PRK06484 PRK06484
short chain dehydrogenase; Validated
 9-240 3.37e-42

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 150.38  E-value: 3.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:PRK06484    8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVERAReradslgPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVNNA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGA--VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH-ASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:PRK06484   88 GVTDptMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHgAAIVNVASGAGLVALPKRTAYSASKAAVISLTRS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTPWVSRLLDGAddpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVD 238
Cdd:PRK06484  168 LACEWAAKGIRVNAVLPGYVRTQMVAELERAG---KLDPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTLVVD 244


                  ..
gi 1482408268 239 GG 240
Cdd:PRK06484  245 GG 246
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-241 4.42e-42

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 143.93  E-value: 4.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVL-----DLDPSGVHGPLTGIRA-----DVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK08213   11 SGKTALVTGGSRGLGLQIAEALGEAGARVVLSarkaeELEEAAAHLEALGIDAlwiaaDVADEADIERLAEETLERFGHV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPH--LRRSAhASVVNVCSIAATAGLPQRAL----YSAT 148
Cdd:PRK08213   91 DILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsmIPRGY-GRIINVASVAGLGGNPPEVMdtiaYNTS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 149 KGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaddpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK08213  170 KGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTL------ERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASK 243

                         250
                  ....*....|...
gi 1482408268 229 SVTGTALAVDGGM 241
Cdd:PRK08213  244 HITGQILAVDGGV 256
PRK08628 PRK08628
SDR family oxidoreductase;
10-252 7.77e-42

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 143.56  E-value: 7.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH---------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNN 80
Cdd:PRK08628   11 IVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEfaeelralqPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLVNN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIG-AVGTveDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:PRK08628   91 AGVNdGVGL--EAGREAFVASLERNLIHYYVMAHYCLPHLKAS-RGAIVNISSKTALTGQGGTSGYAAAKGAQLALTREW 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 160 AADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARQPLG-RLVTADEVAAAVLYLAGPSAGSVTGTALAVD 238
Cdd:PRK08628  168 AVALAKDGVRVNAVIPAEVMTPLYENWIATFDDPEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHTTGQWLFVD 247

                         250
                  ....*....|....
gi 1482408268 239 GGMQGLrlrpvDRA 252
Cdd:PRK08628  248 GGYVHL-----DRA 256
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-240 1.18e-41

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 143.11  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK13394    2 MSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANavadeinkagGKAIGVAMDVTNEDAVNAGIDKVAER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVV-NVCSIAATAGLPQRALYSATK 149
Cdd:PRK13394   82 FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVViYMGSVHSHEASPLKSAYVTAK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLD------GADDPEAERAALNARQPLGRLVTADEVAAAVLYLA 223
Cdd:PRK13394  162 HGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPeqakelGISEEEVVKKVMLGKTVDGVFTTVEDVAQTVLFLS 241

                         250
                  ....*....|....*..
gi 1482408268 224 GPSAGSVTGTALAVDGG 240
Cdd:PRK13394  242 SFPSAALTGQSFVVSHG 258
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-241 1.44e-41

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 142.55  E-value: 1.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH--------------GPLTGIRADVSDDVGVRAAVAA 66
Cdd:PRK12827    1 MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRaeadavaagieaagGKALGLAFDVRDFAATRAALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  67 AAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHA-SVVNVCSIAATAGLPQRALY 145
Cdd:PRK12827   81 GVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGgRIVNIASVAGVRGNRGQVNY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 146 SATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPwvsrlldGADDPEAERAALNArQPLGRLVTADEVAAAVLYLAGP 225
Cdd:PRK12827  161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTP-------MADNAAPTEHLLNP-VPVQRLGEPDEVAALVAFLVSD 232

                         250
                  ....*....|....*.
gi 1482408268 226 SAGSVTGTALAVDGGM 241
Cdd:PRK12827  233 AASYVTGQVIPVDGGF 248
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 9-240 2.45e-41

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: 141.76  E-value: 2.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSG---VHGPLTG------IRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:cd08943     4 ALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIaekVAEAAQGgpralgVQCDVTSEAQVQSAFEQAVLEFGGLDIVVS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSA-HASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:cd08943    84 NAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPgtvdtpwvSRLLDGADDPEAERAALNARQP------------LGRLVTADEVAAAVLYLAGPS 226
Cdd:cd08943   164 LALEGGEDGIRVNTVNP--------DAVFRGSKIWEGVWRAARAKAYglleeeyrtrnlLKREVLPEDVAEAVVAMASED 235

                         250
                  ....*....|....
gi 1482408268 227 AGSVTGTALAVDGG 240
Cdd:cd08943   236 FGKTTGAIVTVDGG 249
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 9-241 1.08e-40

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: 140.28  E-value: 1.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNN 80
Cdd:cd05326     7 AIITGGASGIGEATARLFAKHGARVVIADIdDDAGQAvaaelgdPDISFVHCDVTVEADVRAAVDTAVARFGRLDIMFNN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGI-GA-VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:cd05326    87 AGVlGApCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLGLTRS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTPWVsRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVD 238
Cdd:cd05326   167 AATELGEHGIRVNCVSPYGVATPLL-TAGFGVEDEAIEEAVRGAANLKGTALRPEDIAAAVLYLASDDSRYVSGQNLVVD 245


                  ...
gi 1482408268 239 GGM 241
Cdd:cd05326   246 GGL 248
PRK06484 PRK06484
short chain dehydrogenase; Validated
 9-240 1.47e-40

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 145.76  E-value: 1.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:PRK06484  272 VAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKklaealgDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNNA 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAV-GTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMA 160
Cdd:PRK06484  352 GIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGG--VIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLA 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 161 ADHVREGIRVNCVNPGTVDTPWVSRLLDGAddpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK06484  430 CEWAPAGIRVNTVAPGYIETPAVLALKASG---RADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGG 506
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 9-240 2.30e-40

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: 139.02  E-value: 2.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVA-------------VLDLDPSGVHGplTGIRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVinyrkskdaaaevAAEIEELGGKA--VVVRADVSQPQDVEEMFAAVKERFGRLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:cd05359    79 VLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgadDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:cd05359   159 VRYLAVELGPRGIRVNAVSPGVIDTDALAHFP----NREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTL 234


                  ....*
gi 1482408268 236 AVDGG 240
Cdd:cd05359   235 VVDGG 239
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-240 3.24e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 139.29  E-value: 3.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAER 70
Cdd:PRK07478    1 MMRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAeggeavalagDVRDEAYAKALVALAVER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCS-IAATAGLPQRALYSAT 148
Cdd:PRK07478   81 FGGLDIAFNNAGTlGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTfVGHTAGFPGMAAYAAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 149 KGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrllDGADDPEAeRAALNARQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK07478  161 KAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGR---AMGDTPEA-LAFVAGLHALKRMAQPEEIAQAALFLASDAAS 236

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:PRK07478  237 FVTGTALLVDGG 248
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 4-243 3.53e-40

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: 139.20  E-value: 3.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSgVHGPLTGIR----------ADVSDDVGVRAAVAAAAERLGG 73
Cdd:cd08937     2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSEL-VHEVLAEILaagdaahvhtADLETYAGAQGVVRAAVERFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGigavGTV-----EDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLpqRALYSAT 148
Cdd:cd08937    81 VDVLINNVG----GTIwakpyEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIY--RIPYSAA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 149 KGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALN-------ARQPLGRLVTADEVAAAVLY 221
Cdd:cd08937   155 KGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEQEKVWYQrivdqtlDSSLMGRYGTIDEQVRAILF 234

                         250       260
                  ....*....|....*....|..
gi 1482408268 222 LAGPSAGSVTGTALAVDGGMQG 243
Cdd:cd08937   235 LASDEASYITGTVLPVGGGDLG 256
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 2-240 4.30e-40

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: 139.21  E-value: 4.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   2 TEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSG-----------VHGPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:cd08933     5 LRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAgqaleselnraGPGSCKFVPCDVTKEEDIKTLISVTVER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAV-GTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATK 149
Cdd:cd08933    85 FGRIDCLVNNAGWHPPhQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS-QGNIINLSSLVGSIGQKQAAPYVATK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAE-RAALNArQPLGRLVTADEVAAAVLYLAGpSAG 228
Cdd:cd08933   164 GAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATiKEGELA-QLLGRMGTEAESGLAALFLAA-EAT 241

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:cd08933   242 FCTGIDLLLSGG 253
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 4-242 6.43e-40

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: 138.10  E-value: 6.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDP-----------SGVHGPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPevleaaaeeisSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH-ASVVNVCSIAATAGLPQRALYSATKGA 151
Cdd:cd05369    81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAAAKAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 152 VLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAEraaLNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:cd05369   161 VDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKK---MIERVPLGRLGTPEEIANLALFLLSDAASYIN 237

                         250
                  ....*....|.
gi 1482408268 232 GTALAVDGGMQ 242
Cdd:cd05369   238 GTTLVVDGGQW 248
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-240 6.55e-40

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 138.38  E-value: 6.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVL---------DLDPSGVhgpLTgIRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK06463    5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLynsaeneakELREKGV---FT-IKCDVGNRDQVKKSKEVVEKEFGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNvcsIAATAGLPQRA----LYSATKG 150
Cdd:PRK06463   81 DVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVN---IASNAGIGTAAegttFYAITKA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVsrlLDGADDPEAE--RAALNARQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK06463  158 GIIILTRRLAFELGKYGIRVNAVAPGWVETDMT---LSGKSQEEAEklRELFRNKTVLKTTGKPEDIANIVLFLASDDAR 234

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:PRK06463  235 YITGQVIVADGG 246
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 9-241 1.36e-39

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: 137.18  E-value: 1.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAvldldpSGVHG-----------------PLTGIRADVSDDVGVRAAVAAAAERL 71
Cdd:TIGR01829   3 ALVTGGMGGIGTAICQRLAKDGYRVA------ANCGPneeraeawlqeqgalgfDFRVVEGDVSSFESCKAAVAKVEAEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  72 GGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGA 151
Cdd:TIGR01829  77 GPVDVLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 152 VLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:TIGR01829 157 MIGFTKALAQEGATKGVTVNTISPGYIATDMVMAM------REDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYIT 230

                         250
                  ....*....|
gi 1482408268 232 GTALAVDGGM 241
Cdd:TIGR01829 231 GATLSINGGL 240
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 11-219 2.55e-39

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: 136.04  E-value: 2.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLDPSGV--------HGPLTGIRADVSDDVGVRAAVAAAAERLGG-LDILVNNA 81
Cdd:cd08931     5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLaalaaelgAENVVAGALDVTDRAAWAAALADFAAATGGrLDALFNNA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:cd08931    85 GVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDV 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1482408268 162 DHVREGIRVNCVNPGTVDTPWVSRLLDGAddpeaeraalNARQPLGRLVTADEVAAAV 219
Cdd:cd08931   165 EWARHGIRVADVWPWFVDTPILTKGETGA----------APKKGLGRVLPVSDVAKVV 212
PRK07326 PRK07326
SDR family oxidoreductase;
1-181 3.42e-39

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 135.91  E-value: 3.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV---------HGPLTGIRADVSDDVGVRAAVAAAAERL 71
Cdd:PRK07326    1 MMSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELeeaaaelnnKGNVLGLAADVRDEADVQRAVDAIVAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  72 GGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHAsVVNVCSIAATAGLPQRALYSATKGA 151
Cdd:PRK07326   81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGY-IINISSLAGTNFFAGGAAYNASKFG 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1482408268 152 VLSLTLAMAADHVREGIRVNCVNPGTVDTP 181
Cdd:PRK07326  160 LVGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
PRK12743 PRK12743
SDR family oxidoreductase;
8-241 3.96e-39

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 136.32  E-value: 3.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVL-DLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK12743    4 VAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEVRShgvraeirqlDLSDLPEGAQALDKLIQRLGRIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHAS-VVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:PRK12743   84 LVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGrIINITSVHEHTPLPGASAYTAAKHALGGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSrlLDGADDPEAERAALnarqPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:PRK12743  164 TKAMALELVEHGILVNAVAPGAIATPMNG--MDDSDVKPDSRPGI----PLGRPGDTHEIASLVAWLCSEGASYTTGQSL 237


                  ....*.
gi 1482408268 236 AVDGGM 241
Cdd:PRK12743  238 IVDGGF 243
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-180 4.01e-39

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 135.97  E-value: 4.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVL-----DLDPSGVHGPLTGIR-----ADVSDDVGVRAAVAAAAER 70
Cdd:PRK07666    2 AQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLarteeNLKAVAEEVEAYGVKvviatADVSDYEEVTAAIEQLKNE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:PRK07666   82 LGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKF 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDT 180
Cdd:PRK07666  162 GVLGLTESLMQEVRKHNIRVTALTPSTVAT 191
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 4-240 8.95e-39

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: 135.31  E-value: 8.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSG-------VHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAaqavvaqIAGGALALRVDVTDEQQVAALFERAVEEFGGLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:cd08944    81 LVNNAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDP-EAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:cd08944   161 TRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGAlGPGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFITGQV 240


                  ....*.
gi 1482408268 235 LAVDGG 240
Cdd:cd08944   241 LCVDGG 246
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
1-240 9.38e-39

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 135.70  E-value: 9.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS---------GVHGPLTGIRADVSDDVGVRAAVAAAAERL 71
Cdd:PRK08226    1 MGKLTGKTALITGALQGIGEGIARVFARHGANLILLDISPEiekladelcGRGHRCTAVVADVRDPASVAAAIKRAKEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  72 GGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAAT-AGLPQRALYSATKG 150
Cdd:PRK08226   81 GRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDmVADPGETAYALTKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGA--DDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK08226  161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSnpEDPESVLTEMAKAIPLRRLADPLEVGELAAFLASDESS 240

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:PRK08226  241 YLTGTQNVIDGG 252
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 2-241 1.82e-38

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 134.85  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   2 TEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK08936    3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANdvaeeikkagGEAIAVKGDVTVESDVVNLIQTAVKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPH-LRRSAHASVVNVCSIAATAGLPQRALYSATK 149
Cdd:PRK08936   83 FGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYfVEHDIKGNIINMSSVHEQIPWPLFVHYAASK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEaERAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK08936  163 GGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKF---ADPK-QRADVESMIPMGYIGKPEEIAAVAAWLASSEASY 238

                         250
                  ....*....|..
gi 1482408268 230 VTGTALAVDGGM 241
Cdd:PRK08936  239 VTGITLFADGGM 250
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 9-241 2.16e-38

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 134.10  E-value: 2.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTG-----------IRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK12937    8 AIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAeieaaggraiaVQADVADAAAVTRLFDAAETAFGRIDVL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHasVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK12937   88 VNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGGR--IINLSTSVIALPLPGYGPYAASKAAVEGLVH 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTpwvSRLLDGADDPEAERaaLNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAV 237
Cdd:PRK12937  166 VLANELRGRGITVNAVAPGPVAT---ELFFNGKSAEQIDQ--LAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLRV 240


                  ....
gi 1482408268 238 DGGM 241
Cdd:PRK12937  241 NGGF 244
PRK07774 PRK07774
SDR family oxidoreductase;
1-240 3.64e-38

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 133.72  E-value: 3.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK07774    1 MGRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAErvakqivadgGTAIAVQVDVSDPDSAKAMADATVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGI--GAVGTVEDHTD-EQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSiaaTAGLPQRALYSA 147
Cdd:PRK07774   81 FGGIDYLVNNAAIygGMKLDLLITVPwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSS---TAAWLYSNFYGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaddPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSA 227
Cdd:PRK07774  158 AKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVT-----PKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEA 232

                         250
                  ....*....|...
gi 1482408268 228 GSVTGTALAVDGG 240
Cdd:PRK07774  233 SWITGQIFNVDGG 245
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 10-240 4.97e-38

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: 133.41  E-value: 4.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGP------------LTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd05330     7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAkaalleiapdaeVLLIKADVSDEAQVEAYVDATVEQFGRIDGF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:cd05330    87 FNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVGLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTPWVSRLLD--GADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:cd05330   167 RNSAVEYGQYGIRINAIAPGAILTPMVEGSLKqlGPENPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAGYVNAAV 246


                  ....*.
gi 1482408268 235 LAVDGG 240
Cdd:cd05330   247 VPIDGG 252
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 3-241 6.10e-38

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 133.35  E-value: 6.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLG 72
Cdd:PRK07523    7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGqglsahalafDVTDHDAVRAAIDAFEAEIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK07523   87 PIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEAErAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK07523  167 GNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALV---ADPEFS-AWLEKRTPAGRWGKVEELVGACVFLASDASSFVNG 242


                  ....*....
gi 1482408268 233 TALAVDGGM 241
Cdd:PRK07523  243 HVLYVDGGI 251
PRK06114 PRK06114
SDR family oxidoreductase;
9-240 1.90e-37

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 131.83  E-value: 1.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSG-----------VHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK06114   11 AFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDglaetaehieaAGRRAIQIAADVTSKADLRAAVARTEAELGALTLA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATA---GLPQrALYSATKGAVLS 154
Cdd:PRK06114   91 VNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIvnrGLLQ-AHYNASKAGVIH 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRlldgaddPE-AERAALNARQ-PLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK06114  170 LSKSLAMEWVGRGIRVNSISPGYTATPMNTR-------PEmVHQTKLFEEQtPMQRMAKVDEMVGPAVFLLSDAASFCTG 242


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:PRK06114  243 VDLLVDGG 250
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 1-241 3.18e-37

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 131.19  E-value: 3.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVavldldpsGVHG----PLTGIRADVSDDVG-----------VRAAVA 65
Cdd:PRK12936    1 MFDLSGRKALVTGASGGIGEEIARLLHAQGAIV--------GLHGtrveKLEALAAELGERVKifpanlsdrdeVKALGQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  66 AAAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALY 145
Cdd:PRK12936   73 KAEADLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 146 SATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDgaddpeAERAALNARQPLGRLVTADEVAAAVLYLAGP 225
Cdd:PRK12936  153 CASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLND------KQKEAIMGAIPMKRMGTGAEVASAVAYLASS 226

                         250
                  ....*....|....*.
gi 1482408268 226 SAGSVTGTALAVDGGM 241
Cdd:PRK12936  227 EAAYVTGQTIHVNGGM 242
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 9-240 3.22e-37

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: 131.45  E-value: 3.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV---------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:cd08942     9 VLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACadaaeelsaYGECIAIPADLSSEEGIEALVARVAERSDRLDVLVN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH----ASVVNVCSIAATAGLPQRAL-YSATKGAVLS 154
Cdd:cd08942    89 NAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGLENYsYGASKAAVHQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGtvdtPWVSRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:cd08942   169 LTRKLAKELAGEHITVNAIAPG----RFPSKMTAFLLNDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAYLTGAV 244


                  ....*.
gi 1482408268 235 LAVDGG 240
Cdd:cd08942   245 IPVDGG 250
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 9-240 3.55e-37

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: 130.77  E-value: 3.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05365     2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEavaaaiqqagGQAIGLECNVTSEQDLEAVVKATVSQFGGITILV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVE-DHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:cd05365    82 NNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMTR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTPWVSRLLdgadDPEAERAALnARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAV 237
Cdd:cd05365   162 NLAFDLGPKGIRVNAVAPGAVKTDALASVL----TPEIERAML-KHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTV 236


                  ...
gi 1482408268 238 DGG 240
Cdd:cd05365   237 SGG 239
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 1-241 4.52e-37

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 130.89  E-value: 4.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVA-------------VLDLDPSGvhGPLTGIRADVSDDVGVRAAVAAA 67
Cdd:PRK12935    1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVinynsskeaaenlVNELGKEG--HDVYAVQADVSKVEDANRLVEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  68 AERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSA 147
Cdd:PRK12935   79 VNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVsrlldgADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSA 227
Cdd:PRK12935  159 AKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMV------AEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDGA 232

                         250
                  ....*....|....
gi 1482408268 228 gSVTGTALAVDGGM 241
Cdd:PRK12935  233 -YITGQQLNINGGL 245
PRK07074 PRK07074
SDR family oxidoreductase;
9-241 5.13e-37

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 131.05  E-value: 5.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH--------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNN 80
Cdd:PRK07074    5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAafadalgdARFVPVACDLTDAASLAAALANAAAERGPVDVLVAN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRAlYSATKGAVLSLTLAMA 160
Cdd:PRK07074   85 AGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPA-YSAAKAGLIHYTKLLA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 161 ADHVREGIRVNCVNPGTVDTP-WVSRLldgADDPEAERAAlNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDG 239
Cdd:PRK07074  164 VEYGRFGIRANAVAPGTVKTQaWEARV---AANPQVFEEL-KKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVDG 239


                  ..
gi 1482408268 240 GM 241
Cdd:PRK07074  240 GL 241
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 9-241 9.06e-37

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: 130.35  E-value: 9.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPL----------TGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd08945     6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVkelreagveaDGRTCDVRSVPEIEALVAAAVARYGPIDVLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPH--LRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:cd08945    86 NNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVGFT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADD-----PEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:cd08945   166 KALGLELARTGITVNAVCPGFVETPMAASVREHYADiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAAAVT 245

                         250
                  ....*....|
gi 1482408268 232 GTALAVDGGM 241
Cdd:cd08945   246 AQALNVCGGL 255
PRK05650 PRK05650
SDR family oxidoreductase;
8-216 9.34e-37

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 130.55  E-value: 9.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK05650    2 RVMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggdgfyqrcDVRDYSQLTALAQACEEKWGGIDVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK05650   82 VNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTpwvsRLLDGADDP----EAERAALNARQPLgrlvTADEVA 216
Cdd:PRK05650  162 TLLVELADDEIGVHVVCPSFFQT----NLLDSFRGPnpamKAQVGKLLEKSPI----TAADIA 216
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 10-240 1.77e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 129.69  E-value: 1.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAV-------LD-----LDPSGVHGplTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK07890    9 VVSGVGPGLGRTLAVRAARAGADVVLaartaerLDevaaeIDDLGRRA--LAVPTDITDEDQCANLVALALERFGRVDAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNA-GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:PRK07890   87 VNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES-GGSIVMINSMVLRHSQPKYGAYKMAKGALLAAS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTP----WVSRLLDGADDPEAE-RAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:PRK07890  166 QSLATELGPQGIRVNSVAPGYIWGDplkgYFRHQAGKYGVTVEQiYAETAANSDLKRLPTDDEVASAVLFLASDLARAIT 245


                  ....*....
gi 1482408268 232 GTALAVDGG 240
Cdd:PRK07890  246 GQTLDVNCG 254
PRK07832 PRK07832
SDR family oxidoreductase;
8-221 2.22e-36

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 129.78  E-value: 2.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA-----------DVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK07832    2 RCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARAlggtvpehralDISDYDAVAAFAADIHAAHGSMDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHL---RRSAHasVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK07832   82 VMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvaaGRGGH--LVNVSSAAGLVALPWHAAYSASKFGLR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLY 221
Cdd:PRK07832  160 GLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAGVDREDPRVQKWVDRFRGHAVTPEKAAEKILA 227
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 2-240 2.35e-36

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: 128.74  E-value: 2.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   2 TEFTGLRAVVTGGASGIGRAVAERLAERGANVAVL-----DLDPSGVHGP-LTGIRADVSDDVGVRAAVAAaaerLGGLD 75
Cdd:cd05351     3 LDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVsrtqaDLDSLVRECPgIEPVCVDLSDWDATEEALGS----VGPVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLR-RSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd05351    79 LLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIaRGVPGSIVNVSSQASQRALTNHTVYCSTKAALDM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTpwvSRLLDGADDPEAERAALNaRQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:cd05351   159 LTKVMALELGPHKIRVNSVNPTVVMT---DMGRDNWSDPEKAKKMLN-RIPLGKFAEVEDVVNAILFLLSDKSSMTTGST 234


                  ....*.
gi 1482408268 235 LAVDGG 240
Cdd:cd05351   235 LPVDGG 240
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 9-181 2.51e-36

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 129.64  E-value: 2.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVhGPLTGIR---ADVSDDVGVRAAVAAAAERLGGLDILVNNAGIGA 85
Cdd:PRK06179    7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPARA-APIPGVElleLDVTDDASVQAAVDEVIARAGRIDVLVNNAGVGL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  86 VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV--LSLTLamaaDH 163
Cdd:PRK06179   86 AGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVegYSESL----DH 161

                         170       180
                  ....*....|....*....|
gi 1482408268 164 -VRE-GIRVNCVNPGTVDTP 181
Cdd:PRK06179  162 eVRQfGIRVSLVEPAYTKTN 181
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 9-181 6.38e-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: 127.74  E-value: 6.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSG-------VHGPLTGIRA---DVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05339     2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGaeetannVRKAGGKVHYykcDVSKREEVYEAAKKIKKEVGDVTILI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL--T 156
Cdd:cd05339    82 NNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFheS 161

                         170       180
                  ....*....|....*....|....*.
gi 1482408268 157 LAMAADH-VREGIRVNCVNPGTVDTP 181
Cdd:cd05339   162 LRLELKAyGKPGIKTTLVCPYFINTG 187
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 3-240 1.10e-35

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: 127.96  E-value: 1.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:cd08935     2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDkvakeitalgGRAIALAADVLDRASLERAREEIVAQFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAG--------------IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAG 138
Cdd:cd08935    82 TVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 139 LPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERA-ALNARQPLGRLVTADEVAA 217
Cdd:cd08935   162 LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPDGSYTDRSnKILGRTPMGRFGKPEELLG 241

                         250       260
                  ....*....|....*....|....
gi 1482408268 218 AVLYLAGPSAGS-VTGTALAVDGG 240
Cdd:cd08935   242 ALLFLASEKASSfVTGVVIPVDGG 265
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 1-243 1.73e-35

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 126.98  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLD---------LDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERL 71
Cdd:PRK12823    3 NQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDrselvhevaAELRAAGGEALALTADLETYAGAQAAMAAAVEAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  72 GGLDILVNNAGigavGTV-----EDHTDEQwhhvldvnVVGMVRVT--------RAALPHLRRSAHASVVNVCSIaATAG 138
Cdd:PRK12823   83 GRIDVLINNVG----GTIwakpfEEYEEEQ--------IEAEIRRSlfptlwccRAVLPHMLAQGGGAIVNVSSI-ATRG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 139 LpQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTP--WVSRllDGADDPEAERAALN-------ARQPLGRL 209
Cdd:PRK12823  150 I-NRVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPprRVPR--NAAPQSEQEKAWYQqivdqtlDSSLMKRY 226

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1482408268 210 VTADEVAAAVLYLAGPSAGSVTGTALAVDGGMQG 243
Cdd:PRK12823  227 GTIDEQVAAILFLASDEASYITGTVLPVGGGDLG 260
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 9-220 1.99e-35

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: 126.21  E-value: 1.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANV------------AVLDLDPSGVHGP--LTGIRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:cd08939     4 VLITGGSSGIGKALAKELVKEGANViivarseskleeAVEEIEAEANASGqkVSYISADLSDYEEVEQAFAQAVEKGGPP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd08939    84 DLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRG 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRllDGADDPEAERAALNARQPlgrlVTADEVAAAVL 220
Cdd:cd08939   164 LAESLRQELKPYNIRVSVVYPPDTDTPGFEE--ENKTKPEETKAIEGSSGP----ITPEEAARIIV 223
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 9-241 2.45e-35

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: 126.42  E-value: 2.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV---LDLDPSGVHGPLTG-----IRADVSDDVGVRAAVAAAAERLGGLDILVNN 80
Cdd:cd05349     3 VLVTGASRGLGAAIARSFAREGARVVVnyyRSTESAEAVAAEAGeraiaIQADVRDRDQVQAMIEEAKNHFGPVDTIVNN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIG------AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd05349    83 ALIDfpfdpdQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAALLG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSrlldgADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:cd05349   163 FTRNMAKELGPYGITVNMVSGGLLKVTDAS-----AATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQN 237


                  ....*..
gi 1482408268 235 LAVDGGM 241
Cdd:cd05349   238 LVVDGGL 244
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-221 2.57e-35

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: 126.11  E-value: 2.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAV----------LDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:cd08934     2 QGKVALVTGASSGIGEATARALAAEGAAVAIaarrvdrleaLADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd08934    82 DILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDgaddpEAERAALNARQPLGRLVTADEVAAAVLY 221
Cdd:cd08934   162 FSEGLRQEVTERGVRVVVIEPGTVDTELRDHITH-----TITKEAYEERISTIRKLQAEDIAAAVRY 223
PRK07856 PRK07856
SDR family oxidoreductase;
1-240 3.87e-35

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 125.82  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTG--IRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK07856    1 NLDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRPAefHAADVRDPDQVAALVDAIVERHGRLDVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGiGAVGTVEDHTDEQWHH-VLDVNVVGMVRVTRAALPHLRR-SAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:PRK07856   81 NNAG-GSPYALAAEASPRFHEkIVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREgIRVNCVNPGTVDTPWVSRLLDGADDPeaerAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALA 236
Cdd:PRK07856  160 RSLAVEWAPK-VRVNAVVVGLVRTEQSELHYGDAEGI----AAVAATVPLGRLATPADIAWACLFLASDLASYVSGANLE 234


                  ....
gi 1482408268 237 VDGG 240
Cdd:PRK07856  235 VHGG 238
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 1-240 4.98e-35

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 125.84  E-value: 4.98e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV----------HGPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK07576    4 MFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVdaavaqlqqaGPEGLGVSADVRDYAAVEAAFAQIADE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:PRK07576   84 FGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISAPQAFVPMPMQAHVCAAKA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTV-DTPWVSRLldgADDPEAeRAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK07576  163 GVDMLTRTLALEWGPEGIRVNSIVPGPIaGTEGMARL---APSPEL-QAAVAQSVPLKRNGTKQDIANAALFLASDMASY 238

                         250
                  ....*....|.
gi 1482408268 230 VTGTALAVDGG 240
Cdd:PRK07576  239 ITGVVLPVDGG 249
PRK06124 PRK06124
SDR family oxidoreductase;
5-241 8.72e-35

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 125.21  E-value: 8.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK06124   10 AGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAaggaaealafDIADEEAVAAAFARIDAEHGRL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK06124   90 DILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgADDPEAErAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:PRK06124  170 LMRALAAEFGPHGITSNAIAPGYFATETNAAM---AADPAVG-PWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHV 245


                  ....*..
gi 1482408268 235 LAVDGGM 241
Cdd:PRK06124  246 LAVDGGY 252
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-241 8.96e-35

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 125.17  E-value: 8.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLT-----GIRA-----DVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK07097    9 KGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAayrelGIEAhgyvcDVTDEDGVQAMVSQIEKEVGVI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK07097   89 DILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGLKM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDpeAERAALN----ARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:PRK07097  169 LTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQAD--GSRHPFDqfiiAKTPAARWGDPEDLAGPAVFLASDASNFV 246

                         250
                  ....*....|.
gi 1482408268 231 TGTALAVDGGM 241
Cdd:PRK07097  247 NGHILYVDGGI 257
PRK06181 PRK06181
SDR family oxidoreductase;
9-220 9.36e-35

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 125.09  E-value: 9.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV----------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK06181    4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLaslaqeladhGGEALVVPTDVSDAEACERLIEAAVARFGGIDILV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQW-HHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATKGAVL---- 153
Cdd:PRK06181   84 NNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHALHgffd 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 154 SLTLAMAADhvreGIRVNCVNPGTVDTPWVSRLLDGADDPEAERaalnaRQPLGRLVTADEVAAAVL 220
Cdd:PRK06181  163 SLRIELADD----GVAVTVVCPGFVATDIRKRALDGDGKPLGKS-----PMQESKIMSAEECAEAIL 220
PRK07035 PRK07035
SDR family oxidoreductase;
5-241 1.00e-34

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 124.74  E-value: 1.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRAD----------VSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK07035    7 TGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAggkaealachIGEMEQIDALFAHIRERHGRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGA-VGTVEDhTDE-QWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK07035   87 DILVNNAAANPyFGHILD-TDLgAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEAERAALnARQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK07035  166 ISMTKAFAKECAPFGIRVNALLPGLTDTKFASALF---KNDAILKQAL-AHIPLRRHAEPSEMAGAVLYLASDASSYTTG 241


                  ....*....
gi 1482408268 233 TALAVDGGM 241
Cdd:PRK07035  242 ECLNVDGGY 250
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 9-240 1.47e-34

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 124.57  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK06113   14 AIITGAGAGIGKEIAITFATAGASVVVSDINADAANhvvdeiqqlgGQAFACRCDITSEQELSALADFALSKLGKVDILV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDE-QWHHVLdvNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK06113   94 NNAGGGGPKPFDMPMADfRRAYEL--NVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTPWVSRLLdgadDPEAERAALNaRQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAV 237
Cdd:PRK06113  172 NMAFDLGEKNIRVNGIAPGAILTDALKSVI----TPEIEQKMLQ-HTPIRRLGQPQDIANAALFLCSPAASWVSGQILTV 246


                  ...
gi 1482408268 238 DGG 240
Cdd:PRK06113  247 SGG 249
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-241 2.97e-34

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 123.53  E-value: 2.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PRK08217    9 VITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEeavaecgalgTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGLIN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGI---GAVGTVEDH------TDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASV-VNVCSIaATAGLPQRALYSATK 149
Cdd:PRK08217   89 NAGIlrdGLLVKAKDGkvtskmSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGViINISSI-ARAGNMGQTNYSASK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVsrlldGADDPEAeRAALNARQPLGRLVTADEVAAAVLYLAgpSAGS 229
Cdd:PRK08217  168 AGVAAMTVTWAKELARYGIRVAAIAPGVIETEMT-----AAMKPEA-LERLEKMIPVGRLGEPEEIAHTVRFII--ENDY 239

                         250
                  ....*....|..
gi 1482408268 230 VTGTALAVDGGM 241
Cdd:PRK08217  240 VTGRVLEIDGGL 251
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 5-240 6.70e-34

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 123.20  E-value: 6.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGP-LTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:PRK06171    8 QGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQHEnYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAVGTVEDHTDEQWHHVLD---------VNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK06171   88 NIPRLLVDEKDPAGKYELNeaafdkmfnINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCYAATKAALNS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTpwvsrllDGADDPEAERAALNARQ----------------PLGRLVTADEVAAA 218
Cdd:PRK06171  168 FTRSWAKELGKHNIRVVGVAPGILEA-------TGLRTPEYEEALAYTRGitveqlragytktstiPLGRSGKLSEVADL 240

                         250       260
                  ....*....|....*....|..
gi 1482408268 219 VLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK06171  241 VCYLLSDRASYITGVTTNIAGG 262
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 9-222 1.07e-33

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 121.32  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTG------IRADVSDDVGVRAAVAAAAERLGGLDILVNNAG 82
Cdd:cd08932     3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASggdveaVPYDARDPEDARALVDALRDRFGRIDVLVHNAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  83 IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAAD 162
Cdd:cd08932    83 IGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 163 HVREGIRVNCVNPGTVDTPWvsrlldgaddpeAERAALNARQPLGRLVTADEVAAAVLYL 222
Cdd:cd08932   163 GWDHGVRVSAVCPGFVDTPM------------AQGLTLVGAFPPEEMIQPKDIANLVRMV 210
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 9-222 1.95e-33

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: 120.69  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV-------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLaaaaaqeLEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:cd08929    83 GVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAML 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482408268 162 DHVREGIRVNCVNPGTVDTpwvsrllDGADDPEAEraalnarqplGRLVTADEVAAAVLYL 222
Cdd:cd08929   163 DLREANIRVVNVMPGSVDT-------GFAGSPEGQ----------AWKLAPEDVAQAVLFA 206
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 6-240 2.69e-33

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: 121.19  E-value: 2.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH------GPLT-GIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05363     3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARataaeiGPAAcAISLDVTDQASIDRCVAALVDRWGSIDILV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH-ASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:cd05363    83 NNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRgGKIINMASQAGRRGEALVGVYCATKAAVISLTQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTP-WV---SRLLDGADDPEAERAALNARQ-PLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:cd05363   163 SAGLNLIRHGINVNAIAPGVVDGEhWDgvdAKFARYENRPRGEKKRLVGEAvPFGRMGRAEDLTGMAIFLASTDADYIVA 242


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:cd05363   243 QTYNVDGG 250
PRK07454 PRK07454
SDR family oxidoreductase;
8-223 5.16e-33

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 120.06  E-value: 5.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPS---GVHGPL--TGIRA-----DVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK07454    8 RALITGASSGIGKATALAFAKAGWDLALVARSQDaleALAAELrsTGVKAaaysiDLSNPEAIAPGIAELLEQFGCPDVL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK07454   88 INNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTK 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTP-WvsrlldgadDPEAERAALNARQPLgrlvTADEVAAAVLYLA 223
Cdd:PRK07454  168 CLAEEERSHGIRVCTITLGAVNTPlW---------DTETVQADFDRSAML----SPEQVAQTILHLA 221
PRK06128 PRK06128
SDR family oxidoreductase;
1-240 5.20e-33

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 121.50  E-value: 5.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAV--LDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAA 68
Cdd:PRK06128   50 FGRLQGRKALITGADSGIGRATAIAFAREGADIALnyLPEEEQDAAEVVQLIQAegrkavalpgDLKDEAFCRQLVERAV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  69 ERLGGLDILVNNAGIG-AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRrsAHASVVNVCSIAATAGLPQRALYSA 147
Cdd:PRK06128  130 KELGGLDILVNIAGKQtAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLP--PGASIINTGSIQSYQPSPTLLDYAS 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPwvsrLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSA 227
Cdd:PRK06128  208 TKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTP----LQPSGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQES 283

                         250
                  ....*....|...
gi 1482408268 228 GSVTGTALAVDGG 240
Cdd:PRK06128  284 SYVTGEVFGVTGG 296
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-219 5.22e-33

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 120.82  E-value: 5.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK07825    2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKetaaelGLVVGGPLDVTDPASFAAFLDAVEADLGPIDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:PRK07825   82 LVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGFT 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGaddpeaeraalnarqPLGRLVTADEVAAAV 219
Cdd:PRK07825  162 DAARLELRGTGVHVSVVLPSFVNTELIAGTGGA---------------KGFKNVEPEDVAAAI 209
PRK05867 PRK05867
SDR family oxidoreductase;
3-240 9.35e-33

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 119.75  E-value: 9.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDP----------SGVHGPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK05867    6 DLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLdalekladeiGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAAL-PHLRRSAHASVVNVCSIAA-TAGLPQR-ALYSATK 149
Cdd:PRK05867   86 GIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAkAMVKQGQGGVIINTASMSGhIINVPQQvSHYCASK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVsrlldgadDPEAERAAL-NARQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK05867  166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILTELV--------EPYTEYQPLwEPKIPLGRLGRPEELAGLYLYLASEASS 237

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:PRK05867  238 YMTGSDIVIDGG 249
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 9-241 1.18e-32

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: 119.22  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDP------SGVHGP-LTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:cd09761     4 AIVTGGGHGIGKQICLDFLEAGDKVVFADIDEergadfAEAEGPnLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVNNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHAsVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:cd09761    84 ARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGR-IINIASTRAFQSEPDSEAYAASKGGLVALTHALAM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 162 DHVREgIRVNCVNPGTVDTpwvsrlldgadDPEAERAALNARQ------PLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:cd09761   163 SLGPD-IRVNCISPGWINT-----------TEQQEFTAAPLTQedhaqhPAGRVGTPKDIANLVLFLCQQDAGFITGETF 230


                  ....*.
gi 1482408268 236 AVDGGM 241
Cdd:cd09761   231 IVDGGM 236
PRK07831 PRK07831
SDR family oxidoreductase;
6-237 1.41e-32

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 119.37  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGA-SGIGRAVAERLAERGANVAVLD------------LDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK07831   17 GKVVLVTAAAgTGIGSATARRALEEGARVVISDiherrlgetadeLAAELGLGRVEAVVCDVTSEAQVDALIDAAVERLG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASV-VNVCSIAATAGLPQRALYSATKGA 151
Cdd:PRK07831   97 RLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGViVNNASVLGWRAQHGQAHYAAAKAG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 152 VLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgadDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:PRK07831  177 VMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKV-----TSAELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLT 251


                  ....*.
gi 1482408268 232 GTALAV 237
Cdd:PRK07831  252 GEVVSV 257
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 9-180 1.49e-32

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: 118.49  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANV-------------AVLDLDPSGVHgpLTGIRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:cd05324     3 ALVTGANRGIGFEIVRQLAKSGPGTviltardvergqaAVEKLRAEGLS--VRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGA-VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPqralYSATKGAVLS 154
Cdd:cd05324    81 ILVNNAGIAFkGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVSKAALNA 156

                         170       180
                  ....*....|....*....|....*.
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDT 180
Cdd:cd05324   157 LTRILAKELKETGIKVNACCPGWVKT 182
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 9-240 2.29e-32

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: 118.15  E-value: 2.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV------LDLDP-----SGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd05357     3 ALVTGAAKRIGRAIAEALAAEGYRVVVhynrseAEAQRlkdelNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:cd05357    83 VNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREgIRVNCVNPGTVdtpwvsrlLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAgpSAGSVTGTALAV 237
Cdd:cd05357   163 SAALELAPN-IRVNGIAPGLI--------LLPEDMDAEYRENALRKVPLKRRPSAEEIADAVIFLL--DSNYITGQIIKV 231


                  ...
gi 1482408268 238 DGG 240
Cdd:cd05357   232 DGG 234
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 9-241 2.53e-32

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: 118.80  E-value: 2.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANV------------AVLDLDPSGVHgpLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:cd08936    13 ALVTASTDGIGLAIARRLAQDGAHVvvssrkqqnvdrAVATLQGEGLS--VTGTVCHVGKAEDRERLVATAVNLHGGVDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAV-GTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:cd08936    91 LVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLGL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNARqplgRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:cd08936   171 TKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEESMKETLRIR----RLGQPEDCAGIVSFLCSEDASYITGETV 246


                  ....*.
gi 1482408268 236 AVDGGM 241
Cdd:cd08936   247 VVGGGT 252
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 9-240 3.87e-32

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: 117.82  E-value: 3.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd08930     5 ILITGAAGLIGKAFCKALLSAGARLILADINAPALEqlkeeltnlykNRVIALELDITSKESIKELIESYLEKFGRIDIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGT---VEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQR----------AL 144
Cdd:cd08930    85 INNAYPSPKVWgsrFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAPDFRiyentqmyspVE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 YSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVdtpwvsrlLDGADDPEAERaaLNARQPLGRLVTADEVAAAVLYLAG 224
Cdd:cd08930   165 YSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGI--------LNNQPSEFLEK--YTKKCPLKRMLNPEDLRGAIIFLLS 234

                         250
                  ....*....|....*.
gi 1482408268 225 PSAGSVTGTALAVDGG 240
Cdd:cd08930   235 DASSYVTGQNLVIDGG 250
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 9-197 4.36e-32

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: 117.88  E-value: 4.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV----LDLDPSGVHGPLTG------------------IRADVSDDVGVRAAVAA 66
Cdd:cd05338     6 AFVTGASRGIGRAIALRLAKAGATVVVaaktASEGDNGSAKSLPGtieetaeeieaaggqalpIVVDVRDEDQVRALVEA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  67 AAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYS 146
Cdd:cd05338    86 TVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDVAYA 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1482408268 147 ATKGAVLSLTLAMAADHVREGIRVNCVNPGT-VDTPWVSRLLDGADDPEAER 197
Cdd:cd05338   166 AGKAGMSRLTLGLAAELRRHGIAVNSLWPSTaIETPAATELSGGSDPARARS 217
PRK07985 PRK07985
SDR family oxidoreductase;
8-240 4.90e-32

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 118.94  E-value: 4.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDL-----DPSGVHGPL--TGIRA-----DVSDDVGVRAAVAAAAERLGGLD 75
Cdd:PRK07985   51 KALVTGGDSGIGRAAAIAYAREGADVAISYLpveeeDAQDVKKIIeeCGRKAvllpgDLSDEKFARSLVHEAHKALGGLD 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIG-AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRrsAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK07985  131 IMALVAGKQvAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLP--KGASIITTSSIQAYQPSPHLLDYAATKAAILN 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVdtpWVSRLLDGAdDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTA 234
Cdd:PRK07985  209 YSRGLAKQVAEKGIRVNIVAPGPI---WTALQISGG-QTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYVTAEV 284


                  ....*.
gi 1482408268 235 LAVDGG 240
Cdd:PRK07985  285 HGVCGG 290
PRK05855 PRK05855
SDR family oxidoreductase;
3-220 7.60e-32

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 122.40  E-value: 7.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLG 72
Cdd:PRK05855  312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAagavahayrvDVSDADAMEAFAEWVRAEHG 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLR-RSAHASVVNVCSIAATAglPQRAL--YSATK 149
Cdd:PRK05855  392 VPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVeRGTGGHIVNVASAAAYA--PSRSLpaYATSK 469

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWV-SRLLDGADDPEAERAALNARQPLG-RLVTADEVAAAVL 220
Cdd:PRK05855  470 AAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVaTTRFAGADAEDEARRRGRADKLYQrRGYGPEKVAKAIV 542
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 9-181 4.31e-31

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 117.33  E-value: 4.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK07109   11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEalaaeiraagGEALAVVADVADAEAVQAAADRAEEELGPIDTWV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:PRK07109   91 NNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTDS 170

                         170       180
                  ....*....|....*....|....*
gi 1482408268 159 MAAD--HVREGIRVNCVNPGTVDTP 181
Cdd:PRK07109  171 LRCEllHDGSPVSVTMVQPPAVNTP 195
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 10-223 9.38e-31

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: 114.02  E-value: 9.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIR----------ADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:cd05360     4 VITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRelggeaiavvADVADAAQVERAADTAVERFGRIDTWVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:cd05360    84 NAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESL 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 160 AAD--HVREGIRVNCVNPGTVDTPWvsrlldgaddPEAERAALNAR-QPLGRLVTADEVAAAVLYLA 223
Cdd:cd05360   164 RAElaHDGAPISVTLVQPTAMNTPF----------FGHARSYMGKKpKPPPPIYQPERVAEAIVRAA 220
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-240 1.02e-30

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 114.43  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAV----------------LDLDPSGVhgpltGIRADVSDDVGVRAAV 64
Cdd:PRK06077    1 MYSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVnakkraeemnetlkmvKENGGEGI-----GVLADVSTREGCETLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  65 AAAAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSahASVVNVCSIAATAGLPQRAL 144
Cdd:PRK06077   76 KATIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREG--GAIVNIASVAGIRPAYGLSI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 YSATKGAVLSLTLAMAADhVREGIRVNCVNPGTVDTPWVSRLLD--GADDPE-AERAALnarqpLGRLVTADEVAAAVLY 221
Cdd:PRK06077  154 YGAMKAAVINLTKYLALE-LAPKIRVNAIAPGFVKTKLGESLFKvlGMSEKEfAEKFTL-----MGKILDPEEVAEFVAA 227

                         250
                  ....*....|....*....
gi 1482408268 222 LAgpSAGSVTGTALAVDGG 240
Cdd:PRK06077  228 IL--KIESITGQVFVLDSG 244
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-246 1.04e-30

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 114.29  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGVHGPLTGIR----------ADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK12745    5 ALVTGGRRGIGLGIARALAAAGFDLAINDRpDDEELAATQQELRalgveviffpADVADLSAHEAMLDAAQAAWGRIDCL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAV--GTVEDHTDEQWHHVLDVNVVGMVRVTRA------ALPHLRRSAHASVVNVCSIAATAGLPQRALYSATK 149
Cdd:PRK12745   85 VNNAGVGVKvrGDLLDLTPESFDRVLAINLRGPFFLTQAvakrmlAQPEPEELPHRSIVFVSSVNAIMVSPNRGEYCISK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADdpeaeRAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:PRK12745  165 AGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYD-----ALIAKGLVPMPRWGEPEDVARAVAALASGDLPY 239

                         250
                  ....*....|....*..
gi 1482408268 230 VTGTALAVDGGMQGLRL 246
Cdd:PRK12745  240 STGQAIHVDGGLSIPRL 256
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 4-242 1.95e-30

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 113.60  E-value: 1.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDpsgvHGPLTGIRADVSDDVGVRAAVAAA-----------AERLG 72
Cdd:PRK06125    5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARD----ADALEALAADLRAAHGVDVAVHALdlsspeareqlAAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK06125   81 DIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADYICGSAGNAAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDG----ADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK06125  161 MAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGraraELGDESRWQELLAGLPLGRPATPEEVADLVAFLASPRSG 240

                         250
                  ....*....|....
gi 1482408268 229 SVTGTALAVDGGMQ 242
Cdd:PRK06125  241 YTSGTVVTVDGGIS 254
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 8-244 2.49e-30

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: 113.36  E-value: 2.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHgpltgirADVSDDVGVRAAVAAAAERLGG-LDILVNNAGIGAV 86
Cdd:cd05328     1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVI-------ADLSTPEGRAAAIADVLARCSGvLDGLVNCAGVGGT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  87 GTVEDhtdeqwhhVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAA--------------TAGLPQRAL-------- 144
Cdd:cd05328    74 TVAGL--------VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGagwaqdklelakalAAGTEARAValaehagq 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 -----YSATKGAVLSLTLAMAAD-HVREGIRVNCVNPGTVDTPWvsrLLDGADDPEAERAALNARQPLGRLVTADEVAAA 218
Cdd:cd05328   146 pgylaYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPI---LQAFLQDPRGGESVDAFVTPMGRRAEPDEIAPV 222

                         250       260
                  ....*....|....*....|....*.
gi 1482408268 219 VLYLAGPSAGSVTGTALAVDGGMQGL 244
Cdd:cd05328   223 IAFLASDAASWINGANLFVDGGLDAS 248
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 3-240 5.16e-30

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 113.07  E-value: 5.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK08277    7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEavvaeikaagGEALAVKADVLDKESLEQARQQILEDFG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAG---IGAVGTVEDHTD------------EQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATA 137
Cdd:PRK08277   87 PCDILINGAGgnhPKATTDNEFHELieptktffdldeEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 138 GLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERA-ALNARQPLGRLVTADEVA 216
Cdd:PRK08277  167 PLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALLFNEDGSLTERAnKILAHTPMGRFGKPEELL 246

                         250       260
                  ....*....|....*....|....*
gi 1482408268 217 AAVLYLAGPSAGS-VTGTALAVDGG 240
Cdd:PRK08277  247 GTLLWLADEKASSfVTGVVLPVDGG 271
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 11-182 9.38e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 112.44  E-value: 9.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:PRK08263    8 ITGASRGFGRAWTEAALERGDRVVATARDTATLAdlaekygDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAGY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV--LSLTLAMAA 161
Cdd:PRK08263   88 GLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALegMSEALAQEV 167

                         170       180
                  ....*....|....*....|.
gi 1482408268 162 DHVreGIRVNCVNPGTVDTPW 182
Cdd:PRK08263  168 AEF--GIKVTLVEPGGYSTDW 186
PLN02253 PLN02253
xanthoxin dehydrogenase
 9-240 1.23e-29

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 112.22  E-value: 1.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDL-DPSG--VHGPLTG------IRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PLN02253   21 ALVTGGATGIGESIVRLFHKHGAKVCIVDLqDDLGqnVCDSLGGepnvcfFHCDVTVEDDVSRAVDFTVDKFGTLDIMVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGA--VGTVEDHTDEQWHHVLDVNVVG----MVRVTRAALPHLRrsahASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PLN02253  101 NAGLTGppCPDIRNVELSEFEKVFDVNVKGvflgMKHAARIMIPLKK----GSIVSLCSVASAIGGLGPHAYTGSKHAVL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPwvsrlLDGADDPEAER-----------AALNARQPlGRLVTADEVAAAVLYL 222
Cdd:PLN02253  177 GLTRSVAAELGKHGIRVNCVSPYAVPTA-----LALAHLPEDERtedalagfrafAGKNANLK-GVELTVDDVANAVLFL 250

                         250
                  ....*....|....*...
gi 1482408268 223 AGPSAGSVTGTALAVDGG 240
Cdd:PLN02253  251 ASDEARYISGLNLMIDGG 268
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 9-220 1.40e-29

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 112.37  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPS---------GVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PRK05872   12 VVVTGAARGIGAELARRLHARGAKLALVDLEEAelaalaaelGGDDRVLTVVADVTDLAAMQAAAEEAVERFGGIDVVVA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:PRK05872   92 NAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYCASKAGVEAFANAL 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 160 AADHVREGIRVNCVNPGTVDTPWVSrlldGADDPEAERAALNARQP--LGRLVTADEVAAAVL 220
Cdd:PRK05872  171 RLEVAHHGVTVGSAYLSWIDTDLVR----DADADLPAFRELRARLPwpLRRTTSVEKCAAAFV 229
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
4-240 1.71e-29

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 110.96  E-value: 1.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVL-------------DLDPSGVHGPLtgIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK08063    2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyarsrkaaeetaeEIEALGRKALA--VKANVGDVEKIKEMFAQIDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKG 150
Cdd:PRK08063   80 FGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDT------PWVSRLLDGAddpeaeraalNARQPLGRLVTADEVAAAVLYLAG 224
Cdd:PRK08063  160 ALEALTRYLAVELAPKGIAVNAVSGGAVDTdalkhfPNREELLEDA----------RAKTPAGRMVEPEDVANAVLFLCS 229

                         250
                  ....*....|....*.
gi 1482408268 225 PSAGSVTGTALAVDGG 240
Cdd:PRK08063  230 PEADMIRGQTIIVDGG 245
PRK06947 PRK06947
SDR family oxidoreductase;
10-240 1.86e-29

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 111.05  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAV--------LDLDPSGVH---GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK06947    6 LITGASRGIGRATAVLAAARGWSVGInyardaaaAEETADAVRaagGRACVVAGDVANEADVIAMFDAVQSAFGRLDALV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGT-VEDHTDEQWHHVLDVNVVGMVRVTRAALPHL---RRSAHASVVNVCSIAATAGLPQRAL-YSATKGAVL 153
Cdd:PRK06947   86 NNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLstdRGGRGGAIVNVSSIASRLGSPNEYVdYAGSKGAVD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWvsrlldGADDPEAERAA-LNARQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK06947  166 TLTLGLAKELGPHGVRVNAVRPGLIETEI------HASGGQPGRAArLGAQTPLGRAGEADEVAETIVWLLSDAASYVTG 239


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:PRK06947  240 ALLDVGGG 247
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 11-220 1.88e-29

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: 110.64  E-value: 1.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLDPS------GVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGIG 84
Cdd:COG3967    10 ITGGTSGIGLALAKRLHARGNTVIITGRREEkleeaaAANPGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  85 avgTVEDHTDEQWH-----HVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:COG3967    90 ---RAEDLLDEAEDladaeREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482408268 160 aadhvRE-----GIRVNCVNPGTVDTPWvsrlldGADDPEAERAalnarqplgrlVTADEVAAAVL 220
Cdd:COG3967   167 -----RHqlkdtSVKVIELAPPAVDTDL------TGGQGGDPRA-----------MPLDEFADEVM 210
PRK08264 PRK08264
SDR family oxidoreductase;
1-202 3.99e-29

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 109.59  E-value: 3.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGAN---VAVLDLDPSGVHGP-LTGIRADVSDDVGVRAAVaaaaERLGGLDI 76
Cdd:PRK08264    1 MMDIKGKVVLVTGANRGIGRAFVEQLLARGAAkvyAAARDPESVTDLGPrVVPLQLDVTDPASVAAAA----EAASDVTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGT-VEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:PRK08264   77 LVNNAGIFRTGSlLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEA-ERAALNA 202
Cdd:PRK08264  157 TQALRAELAPQGTRVLGVHPGPIDTDMAAGLDAPKASPADvARQILDA 204
PRK07577 PRK07577
SDR family oxidoreductase;
8-240 1.38e-28

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 108.28  E-value: 1.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGvHGPLTGIRADVSDDVGVRAAVAAAAERlGGLDILVNNAGIGAVG 87
Cdd:PRK07577    5 TVLVTGATKGIGLALSLRLANLGHQVIGIARSAID-DFPGELFACDLADIEQTAATLAQINEI-HPVDAIVNNVGIALPQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  88 TVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAaTAGLPQRALYSATKGAVLSLTLAMAADHVREG 167
Cdd:PRK07577   83 PLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSALVGCTRTWALELAEYG 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 168 IRVNCVNPGTVDTPWVSRLLDGADdpEAERAALnARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK07577  162 ITVNAVAPGPIETELFRQTRPVGS--EEEKRVL-ASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDGG 231
PRK09135 PRK09135
pteridine reductase; Provisional
 9-240 1.43e-28

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 108.48  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV-------------LDLDPSGVHGPLTgIRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:PRK09135    9 ALITGGARRIGAAIARTLHAAGYRVAIhyhrsaaeadalaAELNALRPGSAAA-LQADLLDPDALPELVAACVAAFGRLD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGI---GAVGTVedhTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK09135   88 ALVNNASSfypTPLGSI---TEAQWDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVNITDIHAERPLKGYPVYCAAKAAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREgIRVNCVNPGTVDTPwvsrlLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGpSAGSVTG 232
Cdd:PRK09135  164 EMLTRSLALELAPE-VRVNAVAPGAILWP-----EDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLLA-DASFITG 236


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:PRK09135  237 QILAVDGG 244
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 4-220 2.20e-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: 108.44  E-value: 2.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAV---------------LDLDPSGVHGpltgIRADVSDDVGVRAAVAAAA 68
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLsarreerleevksecLELGAPSPHV----VPLDMSDLEDAEQVVEEAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  69 ERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSAT 148
Cdd:cd05332    77 KLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAAS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482408268 149 KGAVL----SLTLAMAADhvreGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNArqplgRLVTADEVAAAVL 220
Cdd:cd05332   157 KHALQgffdSLRAELSEP----NISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTA-----NGMSPEECALEIL 223
PRK09730 PRK09730
SDR family oxidoreductase;
9-240 2.26e-28

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 108.01  E-value: 2.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV-------------LDLDPSGvhGPLTGIRADVSDDVGVRAAVAAAAERLGGLD 75
Cdd:PRK09730    4 ALVTGGSRGIGRATALLLAQEGYTVAVnyqqnlhaaqevvNLITQAG--GKAFVLQADISDENQVVAMFTAIDQHDEPLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALphlRRSAH------ASVVNVCSIAATAGLPQRAL-YSA 147
Cdd:PRK09730   82 ALVNNAGIlFTQCTVENLTAERINRVLSTNVTGYFLCCREAV---KRMALkhggsgGAIVNVSSAASRLGAPGEYVdYAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrllDGADDPEAERAALNArqPLGRLVTADEVAAAVLYLAGPSA 227
Cdd:PRK09730  159 SKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHA---SGGEPGRVDRVKSNI--PMQRGGQPEEVAQAIVWLLSDKA 233

                         250
                  ....*....|...
gi 1482408268 228 GSVTGTALAVDGG 240
Cdd:PRK09730  234 SYVTGSFIDLAGG 246
PRK06123 PRK06123
SDR family oxidoreductase;
9-240 4.97e-28

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 107.17  E-value: 4.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANV------------AVLDLdPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK06123    5 MIITGASRGIGAATALLAAERGYAVclnylrnrdaaeAVVQA-IRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTD-EQWHHVLDVNVVGMVRVTRAALPHLRrSAHA----SVVNVCSIAATAGLPQRAL-YSATKG 150
Cdd:PRK06123   84 LVNNAGILEAQMRLEQMDaARLTRIFATNVVGSFLCAREAVKRMS-TRHGgrggAIVNVSSMAARLGSPGEYIdYAASKG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrllDGADDPEAERaaLNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:PRK06123  163 AIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHA---SGGEPGRVDR--VKAGIPMGRGGTAEEVARAILWLLSDEASYT 237

                         250
                  ....*....|
gi 1482408268 231 TGTALAVDGG 240
Cdd:PRK06123  238 TGTFIDVSGG 247
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 9-181 5.31e-28

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 107.03  E-value: 5.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV--LDLDP-----SGVHGPLTGIRA---DVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALaaRRTDRldelkAELLNPNPSVEVeilDVTDEERNQLVIAELEAELGGLDLVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:cd05350    81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAES 160

                         170       180
                  ....*....|....*....|...
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTP 181
Cdd:cd05350   161 LRYDVKKRGIRVTVINPGFIDTP 183
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 8-241 7.41e-28

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 106.76  E-value: 7.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK08085   11 NILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQegikahaapfNVTHKQEVEAAIEHIEKDIGPIDVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK08085   91 INNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAVKMLTR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVREGIRVNCVNPGTVDTPWVSRLLDGaddpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAV 237
Cdd:PRK08085  171 GMCVELARHNIQVNGIAPGYFKTEMTKALVED----EAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFV 246


                  ....
gi 1482408268 238 DGGM 241
Cdd:PRK08085  247 DGGM 250
PRK06194 PRK06194
hypothetical protein; Provisional
 1-220 1.24e-27

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 107.02  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----------GPLTGIRADVSDDVGVRAAVAAAAER 70
Cdd:PRK06194    1 MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDravaelraqgAEVLGVRTDVSDAAQVEALADAALER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHAS------VVNVCSIAATAGLPQRAL 144
Cdd:PRK06194   81 FGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDpayeghIVNTASMAGLLAPPAMGI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 YSATKGAVLSLTLAMAADHVREGIRVNC--VNPGTVDT----PWVSRLLDGADDPEAERAALNARQPLGR-----LVTAD 213
Cdd:PRK06194  161 YNVSKHAVVSLTETLYQDLSLVTDQVGAsvLCPYFVPTgiwqSERNRPADLANTAPPTRSQLIAQAMSQKavgsgKVTAE 240


                  ....*..
gi 1482408268 214 EVAAAVL 220
Cdd:PRK06194  241 EVAQLVF 247
PRK07814 PRK07814
SDR family oxidoreductase;
9-242 1.70e-27

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 106.02  E-value: 1.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVL-----DLDPSGVHGPLTGIRA-----DVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK07814   13 AVVTGAGRGLGAAIALAFAEAGADVLIAartesQLDEVAEQIRAAGRRAhvvaaDLAHPEATAGLAGQAVEAFGRLDIVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPH-LRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:PRK07814   93 NNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLmLEHSGGGSVINISSTMGRLAGRGFAAYGTAKAALAHYTR 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADhVREGIRVNCVNPGTVDTpwvsRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAV 237
Cdd:PRK07814  173 LAALD-LCPRIRVNAIAPGSILT----SALEVVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEV 247


                  ....*
gi 1482408268 238 DGGMQ 242
Cdd:PRK07814  248 DGGLT 252
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 9-223 2.11e-27

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: 105.44  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANV-----------AVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd05346     3 VLITGASSGIGEATARRFAKAGAKLiltgrraerlqELADELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDIDIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIgAVGT--VEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:cd05346    83 VNNAGL-ALGLdpAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQF 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWvsRLLDGADDPEAERAALNARQPLgrlvTADEVAAAVLYLA 223
Cdd:cd05346   162 SLNLRKDLIGTGIRVTNIEPGLVETEF--SLVRFHGDKEKADKVYEGVEPL----TPEDIAETILWVA 223
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-240 2.65e-27

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 105.59  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEF--TGLRAVVTGGASGIGRAVAERLAERGANVAVldldpsGVHGP---------------LTGIRADVSDDVGVRAA 63
Cdd:PRK06935    8 MDFFslDGKVAIVTGGNTGLGQGYAVALAKAGADIII------TTHGTnwdetrrliekegrkVTFVQVDLTKPESAEKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  64 VAAAAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRA 143
Cdd:PRK06935   82 VKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 144 LYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaDDPEAERAALNARQPLGRLVTADEVAAAVLYLA 223
Cdd:PRK06935  162 AYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPI----RADKNRNDEILKRIPAGRWGEPDDLMGAAVFLA 237

                         250
                  ....*....|....*..
gi 1482408268 224 GPSAGSVTGTALAVDGG 240
Cdd:PRK06935  238 SRASDYVNGHILAVDGG 254
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 9-240 3.39e-27

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 105.12  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV------------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK12384    5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAanvaqeinaeygEGMAYGFGADATSEQSVLALSRGVDEIFGRVDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTR-AALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:PRK12384   85 LVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAReFSRLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGT-VDTPWVSRLLD------GADDPEAERAALNaRQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK12384  165 TQSLALDLAEYGITVHSLMLGNlLKSPMFQSLLPqyakklGIKPDEVEQYYID-KVPLKRGCDYQDVLNMLLFYASPKAS 243

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:PRK12384  244 YCTGQSINVTGG 255
PRK12746 PRK12746
SDR family oxidoreductase;
1-240 3.75e-27

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 105.12  E-value: 3.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAV-------------LDLDPSGvhGPLTGIRADVSDDVGVRAAVAAA 67
Cdd:PRK12746    1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIhygrnkqaadetiREIESNG--GKAFLIEADLNSIDGVKKLVEQL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  68 AERL------GGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRrsAHASVVNVCSIAATAGLPQ 141
Cdd:PRK12746   79 KNELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR--AEGRVINISSAEVRLGFTG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 142 RALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEAERAALNArQPLGRLVTADEVAAAVLY 221
Cdd:PRK12746  157 SIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLL---DDPEIRNFATNS-SVFGRIGQVEDIADAVAF 232

                         250
                  ....*....|....*....
gi 1482408268 222 LAGPSAGSVTGTALAVDGG 240
Cdd:PRK12746  233 LASSDSRWVTGQIIDVSGG 251
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-242 4.76e-27

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 104.77  E-value: 4.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGA--SGIGRAVAERLAERGANV---------AVLDLDPSGVHGPL-------TGIR-----ADVSDDVGVR 61
Cdd:PRK12748    4 MKKIALVTGASrlNGIGAAVCRRLAAKGIDIfftywspydKTMPWGMHDKEPVLlkeeiesYGVRcehmeIDLSQPYAPN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  62 AAVAAAAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQ 141
Cdd:PRK12748   84 RVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMPD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 142 RALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrlldgaddpEAERAALNARQPLGRLVTADEVAAAVLY 221
Cdd:PRK12748  164 ELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWIT---------EELKHHLVPKFPQGRVGEPVDAARLIAF 234

                         250       260
                  ....*....|....*....|.
gi 1482408268 222 LAGPSAGSVTGTALAVDGGMQ 242
Cdd:PRK12748  235 LVSEEAKWITGQVIHSEGGFS 255
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-241 5.40e-27

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 104.40  E-value: 5.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVaVLDLDPS---------GVHGPLTGIRADVSDDVGVRAAVAAAAERLG-GLDILV 78
Cdd:PRK08642    8 VLVTGGSRGLGAAIARAFAREGARV-VVNYHQSedaaealadELGDRAIALQADVTDREQVQAMFATATEHFGkPITTVV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIG------AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSiaataGLPQRAL-----YSA 147
Cdd:PRK08642   87 NNALADfsfdgdARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGT-----NLFQNPVvpyhdYTT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrlldgADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSA 227
Cdd:PRK08642  162 AKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDAS-----AATPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPWA 236

                         250
                  ....*....|....
gi 1482408268 228 GSVTGTALAVDGGM 241
Cdd:PRK08642  237 RAVTGQNLVVDGGL 250
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 10-248 6.36e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 104.38  E-value: 6.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAV----------LDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PRK07677    5 IITGGSSGMGKAMAKRFAEEGANVVItgrtkekleeAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALIN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPH-LRRSAHASVVN-VCSIAATAGlPQRALYSATKGAVLSLTL 157
Cdd:PRK07677   85 NAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINmVATYAWDAG-PGVIHSAAAKAGVLAMTR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 158 AMAADHVRE-GIRVNCVNPGTVD-TPWVSRLLdgaDDPEAERAALNArQPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:PRK07677  164 TLAVEWGRKyGIRVNAIAPGPIErTGGADKLW---ESEEAAKRTIQS-VPLGRLGTPEEIAGLAYFLLSDEAAYINGTCI 239

                         250
                  ....*....|...
gi 1482408268 236 AVDGGmQGLRLRP 248
Cdd:PRK07677  240 TMDGG-QWLNQYP 251
PRK06182 PRK06182
short chain dehydrogenase; Validated
 9-229 8.61e-27

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 104.66  E-value: 8.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANV--------AVLDLDPSGVHGpltgIRADVSDDVGVRAAVAAAAERLGGLDILVNN 80
Cdd:PRK06182    6 ALVTGASSGIGKATARRLAAQGYTVygaarrvdKMEDLASLGVHP----LSLDVTDEASIKAAVDTIIAEEGRIDVLVNN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMA 160
Cdd:PRK06182   82 AGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1482408268 161 ADHVREGIRVNCVNPGTVDTPWVsrllDGADDPEAERAALNARQPLgrlvtADEVAAAVLYLAGPSAGS 229
Cdd:PRK06182  162 LEVAPFGIDVVVIEPGGIKTEWG----DIAADHLLKTSGNGAYAEQ-----AQAVAASMRSTYGSGRLS 221
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 9-245 1.41e-26

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: 103.59  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV------HG-PLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNA 81
Cdd:cd05348     7 ALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVaelradFGdAVVGVEGDVRSLADNERAVARCVERFGKLDCFIGNA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GI-----GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:cd05348    87 GIwdystSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYAT-EGSVIFTVSNAGFYPGGGGPLYTASKHAVVGLV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMA---ADHvregIRVNCVNPGTVdtpwVSRLLDGADDPEAERA--------ALNARQPLGRLVTADEVAAAVLYLAGP 225
Cdd:cd05348   166 KQLAyelAPH----IRVNGVAPGGM----VTDLRGPASLGQGETSistpplddMLKSILPLGFAPEPEDYTGAYVFLASR 237

                         250       260
                  ....*....|....*....|.
gi 1482408268 226 S-AGSVTGTALAVDGGMqGLR 245
Cdd:cd05348   238 GdNRPATGTVINYDGGM-GVR 257
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 6-232 2.90e-26

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: 103.07  E-value: 2.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANV------------AVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHViiacrneekgeeAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEdhTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAG--------------L 139
Cdd:cd05327    81 LDILINNAGIMAPPRRL--TKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGpidfndldlennkeY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 140 PQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddpeaerAALNARQPLGRL---VTADEVA 216
Cdd:cd05327   159 SPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRN-----------GSFFLLYKLLRPflkKSPEQGA 227

                         250
                  ....*....|....*..
gi 1482408268 217 AAVLYLA-GPSAGSVTG 232
Cdd:cd05327   228 QTALYAAtSPELEGVSG 244
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 1-221 2.96e-26

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: 102.59  E-value: 2.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAV----------LDLDPSGVHGP-LTGIRADVSDDVGVRAAVAAAAE 69
Cdd:cd05343     1 MERWRGRVALVTGASVGIGAAVARALVQHGMKVVGcarrvdkieaLAAECQSAGYPtLFPYQCDLSNEEQILSMFSAIRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  70 RLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHL--RRSAHASVVNVCSIAATAGLPQRAL--Y 145
Cdd:cd05343    81 QHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMkeRNVDDGHIININSMSGHRVPPVSVFhfY 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1482408268 146 SATKGAVLSLTLAMaADHVREG---IRVNCVNPGTVDTPWVSRLLDgaDDPEAERAALNARQPLgrlvTADEVAAAVLY 221
Cdd:cd05343   161 AATKHAVTALTEGL-RQELREAkthIRATSISPGLVETEFAFKLHD--NDPEKAAATYESIPCL----KPEDVANAVLY 232
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 11-185 6.01e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 102.30  E-value: 6.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:PRK06180    9 ITGVSSGFGRALAQAALAAGHRVVGTVRSEAARAdfealhpDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADH 163
Cdd:PRK06180   89 GHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEV 168

                         170       180
                  ....*....|....*....|..
gi 1482408268 164 VREGIRVNCVNPGTVDTPWVSR 185
Cdd:PRK06180  169 APFGIHVTAVEPGSFRTDWAGR 190
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-248 6.08e-26

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 101.96  E-value: 6.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV------HG-PLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK06200    1 MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLaslrqrFGdHVLVVEGDVTSYADNQRAVDQTVDAFGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGI-----GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhASVVNVCSIAATAGLPQRALYSAT 148
Cdd:PRK06200   81 LDCFVGNAGIwdyntSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGGGGPLYTAS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 149 KGAVLSLTLAMAADhVREGIRVNCVNPGTVDTP--------WVSRLLDGADDPEAEraaLNARQPLGRLVTADEVAAAVL 220
Cdd:PRK06200  160 KHAVVGLVRQLAYE-LAPKIRVNGVAPGGTVTDlrgpaslgQGETSISDSPGLADM---IAAITPLQFAPQPEDHTGPYV 235

                         250       260
                  ....*....|....*....|....*....
gi 1482408268 221 YLAG-PSAGSVTGTALAVDGGMqGLRLRP 248
Cdd:PRK06200  236 LLASrRNSRALTGVVINADGGL-GIRGIR 263
PRK08219 PRK08219
SDR family oxidoreductase;
9-181 8.14e-26

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 100.78  E-value: 8.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAER------GANVAVLDLDPSGVHGpLTGIRADVSDDVGVraavAAAAERLGGLDILVNNAG 82
Cdd:PRK08219    6 ALITGASRGIGAAIARELAPThtlllgGRPAERLDELAAELPG-ATPFPVDLTDPEAI----AAAVEQLGRLDVLVHNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  83 IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLrRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAAD 162
Cdd:PRK08219   81 VADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPAL-RAAHGHVVFINSGAGLRANPGWGSYAASKFALRALADALREE 159

                         170
                  ....*....|....*....
gi 1482408268 163 HvREGIRVNCVNPGTVDTP 181
Cdd:PRK08219  160 E-PGNVRVTSVHPGRTDTD 177
PRK08278 PRK08278
SDR family oxidoreductase;
1-235 8.78e-26

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 101.90  E-value: 8.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVL--------DLdPSGVHGPLTGIRA----------DVSDDVGVRA 62
Cdd:PRK08278    1 MMSLSGKTLFITGASRGIGLAIALRAARDGANIVIAaktaephpKL-PGTIHTAAEEIEAaggqalplvgDVRDEDQVAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  63 AVAAAAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCS--IAATAGLP 140
Cdd:PRK08278   80 AVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPplNLDPKWFA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 141 QRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGT-VDTPWVSRLLDGADDPEAeraalnARQPlgrLVTADevaAAV 219
Cdd:PRK08278  160 PHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPRTtIATAAVRNLLGGDEAMRR------SRTP---EIMAD---AAY 227

                         250
                  ....*....|....*.
gi 1482408268 220 LYLAGPSAgSVTGTAL 235
Cdd:PRK08278  228 EILSRPAR-EFTGNFL 242
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-249 1.07e-25

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 102.17  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   2 TEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSG-VHGPLTGIRAD------VSDDVGVRAAVAAAAER---L 71
Cdd:PRK07792    8 TDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALdASDVLDEIRAAgakavaVAGDISQRATADELVATavgL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  72 GGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHAS-------VVNVCSIAATAGLPQRAL 144
Cdd:PRK07792   88 GGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKAAggpvygrIVNTSSEAGLVGPVGQAN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 YSATKGAVLSLTLAMAADHVREGIRVNCVNPgTVDTPWVSRLLDGADDPEAEraalnARQPLgrlvTADEVAAAVLYLAG 224
Cdd:PRK07792  168 YGAAKAGITALTLSAARALGRYGVRANAICP-RARTAMTADVFGDAPDVEAG-----GIDPL----SPEHVVPLVQFLAS 237

                         250       260
                  ....*....|....*....|....*
gi 1482408268 225 PSAGSVTGTALAVDGGMQGLRLRPV 249
Cdd:PRK07792  238 PAAAEVNGQVFIVYGPMVTLVAAPV 262
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 9-180 1.24e-25

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: 100.45  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGV---------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIATCrDPSAAtelaalgasHSRLHILELDVTDEIAESAEAVAERLGDAGLDVLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRA---LYSATKGAVLS 154
Cdd:cd05325    81 NNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDNTSGgwySYRASKAALNM 160

                         170       180
                  ....*....|....*....|....*.
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDT 180
Cdd:cd05325   161 LTKSLAVELKRDGITVVSLHPGWVRT 186
PRK09072 PRK09072
SDR family oxidoreductase;
8-220 2.06e-25

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 100.40  E-value: 2.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH---------GPLTGIRADVSDDVGvRAAVAAAAERLGGLDILV 78
Cdd:PRK09072    7 RVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEalaarlpypGRHRWVVADLTSEAG-REAVLARAREMGGINVLI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:PRK09072   86 NNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSEA 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTpwvsrlldGADDPEAEraALNarQPLG-RLVTADEVAAAVL 220
Cdd:PRK09072  166 LRRELADTGVRVLYLAPRATRT--------AMNSEAVQ--ALN--RALGnAMDDPEDVAAAVL 216
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 9-195 2.13e-25

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: 99.79  E-value: 2.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGAN---VAVLDL---------DPSGVHGpltgIRADVSDDVGVRAAVAAAAErlggLDI 76
Cdd:cd05354     6 VLVTGANRGIGKAFVESLLAHGAKkvyAAVRDPgsaahlvakYGDKVVP----LRLDVTDPESIKAAAAQAKD----VDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAV-GTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:cd05354    78 VINNAGVLKPaTLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTpwvsRLLDGADDPEA 195
Cdd:cd05354   158 TQGLRAELAAQGTLVLSVHPGPIDT----RMAAGAGGPKE 193
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 10-223 2.16e-25

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: 100.05  E-value: 2.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSgvHGPL-------------TGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:cd05367     3 ILTGASRGIGRALAEELLKRGSPSVVVLLARS--EEPLqelkeelrpglrvTTVKADLSDAAGVEQLLEAIRKLDGERDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAG-IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLR-RSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:cd05367    81 LINNAGsLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKkRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1482408268 155 LTLAMAADHvrEGIRVNCVNPGTVDTPWVSRLLDGADDPEAeRAALNARQPLGRLVTADEVAAAVLYLA 223
Cdd:cd05367   161 FFRVLAAEE--PDVRVLSYAPGVVDTDMQREIRETSADPET-RSRFRSLKEKGELLDPEQSAEKLANLL 226
PRK05717 PRK05717
SDR family oxidoreductase;
6-241 3.25e-25

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 99.96  E-value: 3.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLDLDP---SGVHGPLTG----IRADVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK05717   10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRergSKVAKALGEnawfIAMDVADEAQVAAGVAEVLGQFGRLDALV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  79 NNAGIG--AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRrsAH-ASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:PRK05717   90 CNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLR--AHnGAIVNLASTRARQSEPDTEAYAASKGGLLAL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 TLAMAADHVREgIRVNCVNPGTVDtpwvsrlldgADDPEAERA-----ALNARQPLGRLVTADEVAAAVLYLAGPSAGSV 230
Cdd:PRK05717  168 THALAISLGPE-IRVNAVSPGWID----------ARDPSQRRAeplseADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFV 236

                         250
                  ....*....|.
gi 1482408268 231 TGTALAVDGGM 241
Cdd:PRK05717  237 TGQEFVVDGGM 247
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 9-246 4.82e-25

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: 99.46  E-value: 4.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGVHGPLTGIR----------ADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd05337     4 AIVTGASRGIGRAIATELAARGFDIAINDLpDDDQATEVVAEVLaagrraiyfqADIGELSDHEALLDQAWEDFGRLDCL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAV--GTVEDHTDEQWHHVLDVNVVGMVRVTRAAL------PHLRRSAHASVVNVCSIAATAGLPQRALYSATK 149
Cdd:cd05337    84 VNNAGIAVRprGDLLDLTEDSFDRLIAINLRGPFFLTQAVArrmveqPDRFDGPHRSIIFVTSINAYLVSPNRGEYCISK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLldgadDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:cd05337   164 AGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPV-----KEKYDELIAAGLVPIRRWGQPEDIAKAVRTLASGLLPY 238

                         250
                  ....*....|....*..
gi 1482408268 230 VTGTALAVDGGMQGLRL 246
Cdd:cd05337   239 STGQPINIDGGLSMRRL 255
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 3-181 5.90e-25

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 98.53  E-value: 5.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS------GVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:cd05370     2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREErlaeakKELPNIHTIVLDVGDAESVEALAEALLSEYPNLDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIG-------AVGTVEDHTDEqwhhvLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATK 149
Cdd:cd05370    82 LINNAGIQrpidlrdPASDLDKADTE-----IDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATK 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDTP 181
Cdd:cd05370   157 AALHSYTLALRHQLKDTGVEVVEIVPPAVDTE 188
PRK12742 PRK12742
SDR family oxidoreductase;
1-240 1.50e-24

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 97.91  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVA---VLDLDPSGVHGPLTGIRAdVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK12742    1 MGAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRftyAGSKDAAERLAQETGATA-VQTDSADRDAVIDVVRKSGALDIL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVvgmvrvtraalphlRRSAHASVV---------NVCSIAATAG----LPQRAL 144
Cdd:PRK12742   80 VVNAGIAVFGDALELDADDIDRLFKINI--------------HAPYHASVEaarqmpeggRIIIIGSVNGdrmpVAGMAA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 YSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPwvsrlLDGADDPEAEraALNARQPLGRLVTADEVAAAVLYLAG 224
Cdd:PRK12742  146 YAASKSALQGMARGLARDFGPRGITINVVQPGPIDTD-----ANPANGPMKD--MMHSFMAIKRHGRPEEVAGMVAWLAG 218

                         250
                  ....*....|....*.
gi 1482408268 225 PSAGSVTGTALAVDGG 240
Cdd:PRK12742  219 PEASFVTGAMHTIDGA 234
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 9-180 4.74e-24

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: 96.52  E-value: 4.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV----------HGPLTG-IRADVSDDvgvRAAVAAAAERLGGLDI- 76
Cdd:cd05356     4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLdavakeieekYGVETKtIAADFSAG---DDIYERIEKELEGLDIg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 -LVNNAGIGAVGTVEDH--TDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:cd05356    81 iLVNNVGISHSIPEYFLetPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160

                         170       180
                  ....*....|....*....|....*..
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDT 180
Cdd:cd05356   161 FFSRALYEEYKSQGIDVQSLLPYLVAT 187
PRK06482 PRK06482
SDR family oxidoreductase;
11-193 6.53e-24

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 96.72  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLDPSGV------HGP-LTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:PRK06482    7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALddlkarYGDrLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVSNAGY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADH 163
Cdd:PRK06482   87 GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVAQEV 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 1482408268 164 VREGIRVNCVNPGTVDTPWVSRLLDGADDP 193
Cdd:PRK06482  167 APFGIEFTIVEPGPARTNFGAGLDRGAPLD 196
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-239 1.05e-23

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 98.76  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSG---------VHGplTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK08261  210 GKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGealaavanrVGG--TALALDITAPDAPARIAEHLAERHGGLDI 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:PRK08261  288 VVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLV 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTPWVSRLldgaddPEAERAA---LNARQPLGRLVtadEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK08261  368 QALAPLLAERGITINAVAPGFIETQMTAAI------PFATREAgrrMNSLQQGGLPV---DVAETIAWLASPASGGVTGN 438


                  ....*.
gi 1482408268 234 ALAVDG 239
Cdd:PRK08261  439 VVRVCG 444
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 6-240 3.06e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 94.76  E-value: 3.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAV-----LDLDPSGVH------GPLTGIRADVSDDVGVRAAVAAAAERLGG- 73
Cdd:PRK12747    4 GKVALVTGASRGIGRAIAKRLANDGALVAIhygnrKEEAEETVYeiqsngGSAFSIGANLESLHGVEALYSSLDNELQNr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 -----LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHasVVNVCSIAATAGLPQRALYSAT 148
Cdd:PRK12747   84 tgstkFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR--IINISSAATRISLPDFIAYSMT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 149 KGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgaDDPEAERAALNArQPLGRLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK12747  162 KGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELL---SDPMMKQYATTI-SAFNRLGEVEDIADTAAFLASPDSR 237

                         250
                  ....*....|..
gi 1482408268 229 SVTGTALAVDGG 240
Cdd:PRK12747  238 WVTGQLIDVSGG 249
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 11-181 3.55e-23

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: 95.04  E-value: 3.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANV--AVLDLDPSGVH-------GPLTGIRADVSDDVGVRAAVAAAAERLG--GLDILVN 79
Cdd:cd09805     5 ITGCDSGFGNLLAKKLDSLGFTVlaGCLTKNGPGAKelrrvcsDRLRTLQLDVTKPEQIKRAAQWVKEHVGekGLWGLVN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTD-EQWHHVLDVNVVGMVRVTRAALPHLRRsAHASVVNVCSIAATAGLPQRALYSATKGAVlsltlA 158
Cdd:cd09805    85 NAGILGFGGDEELLPmDDYRKCMEVNLFGTVEVTKAFLPLLRR-AKGRVVNVSSMGGRVPFPAGGAYCASKAAV-----E 158

                         170       180
                  ....*....|....*....|....*...
gi 1482408268 159 MAADHVRE-----GIRVNCVNPGTVDTP 181
Cdd:cd09805   159 AFSDSLRRelqpwGVKVSIIEPGNFKTG 186
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 4-240 8.81e-23

(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: 93.16  E-value: 8.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRADV---------------SDDV-GVRAAVAAA 67
Cdd:cd05353     3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKvvdeikaaggkavanYDSVeDGEKIVKTA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  68 AERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSA 147
Cdd:cd05353    83 IDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTvdtpwVSRLLDGADDPEaeraALNARQPlgrlvtaDEVAAAVLYLaGPSA 227
Cdd:cd05353   163 AKLGLLGLSNTLAIEGAKYNITCNTIAPAA-----GSRMTETVMPED----LFDALKP-------EYVAPLVLYL-CHES 225

                         250
                  ....*....|...
gi 1482408268 228 GSVTGTALAVDGG 240
Cdd:cd05353   226 CEVTGGLFEVGAG 238
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 3-233 3.25e-22

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 94.98  E-value: 3.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSG---VHGPLTG----IRADVSDDVGVRAAVAAAAERLGGL- 74
Cdd:COG3347   422 PLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAaeaAAAELGGgygaDAVDATDVDVTAEAAVAAAFGFAGLd 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 ----DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRS--AHASVVNVCSIAATAGLPQRALYSAT 148
Cdd:COG3347   502 iggsDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQglGGSSVFAVSKNAAAAAYGAAAAATAK 581

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 149 KGAVLSLtLAMAADHVREGIRVNCVNPGTVDTP--------WVSRLLDGADDPEAERAALNARQPLGRLVTADEVAAAVL 220
Cdd:COG3347   582 AAAQHLL-RALAAEGGANGINANRVNPDAVLDGsaiwasaaRAERAAAYGIGNLLLEEVYRKRVALAVLVLAEDIAEAAA 660

                         250
                  ....*....|...
gi 1482408268 221 YLAGPSAGSVTGT 233
Cdd:COG3347   661 FFASDGGNKATGG 673
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-240 4.10e-22

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 91.50  E-value: 4.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGAN---VAVLDLDPSGVHGPLTG-----IRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK12481    3 LFDLNGKVAIITGCNTGLGQGMAIGLAKAGADivgVGVAEAPETQAQVEALGrkfhfITADLIQQKDIDSIVSQAVEVMG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRA-ALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGA 151
Cdd:PRK12481   83 HIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAvAKQFVKQGNGGKIINIASMLSFQGGIRVPSYTASKSA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 152 VLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgADdpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:PRK12481  163 VMGLTRALATELSQYNINVNAIAPGYMATDNTAALR--AD--TARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVT 238


                  ....*....
gi 1482408268 232 GTALAVDGG 240
Cdd:PRK12481  239 GYTLAVDGG 247
PRK09134 PRK09134
SDR family oxidoreductase;
8-240 5.45e-22

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 91.14  E-value: 5.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAV-------------LDLDPSGVHGPLtgIRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK09134   11 AALVTGAARRIGRAIALDLAAHGFDVAVhynrsrdeaealaAEIRALGRRAVA--LQADLADEAEVRALVARASAALGPI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK09134   89 TLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNMIDQRVWNLNPDFLSYTLSKAALWT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 155 LTLAMAADhVREGIRVNCVNPGTVdtpwvsrlLDGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAgpSAGSVTGTA 234
Cdd:PRK09134  169 ATRTLAQA-LAPRIRVNAIGPGPT--------LPSGRQSPEDFARQHAATPLGRGSTPEEIAAAVRYLL--DAPSVTGQM 237


                  ....*.
gi 1482408268 235 LAVDGG 240
Cdd:PRK09134  238 IAVDGG 243
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-240 8.32e-22

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 90.70  E-value: 8.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDL-DPSGVHGPLTG-------IRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK08993    7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIvEPTETIEQVTAlgrrflsLTADLRKIDGIPALLERAVAEFGHI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHA-SVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK08993   87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGgKIINIASMLSFQGGIRVPSYTASKSGVM 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgADdpEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK08993  167 GVTRLMANEWAKHNINVNAIAPGYMATNNTQQLR--AD--EQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGY 242


                  ....*..
gi 1482408268 234 ALAVDGG 240
Cdd:PRK08993  243 TIAVDGG 249
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
9-242 1.25e-21

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 90.07  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVldldPSGVHGP---------------LTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:PRK12938    6 AYVTGGMGGIGTSICQRLHKDGFKVVA----GCGPNSPrrvkwledqkalgfdFIASEGNVGDWDSTKAAFDKVKAEVGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVL 153
Cdd:PRK12938   82 IDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDpeaeraALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGT 233
Cdd:PRK12938  162 GFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLE------KIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGA 235


                  ....*....
gi 1482408268 234 ALAVDGGMQ 242
Cdd:PRK12938  236 DFSLNGGLH 244
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 9-238 2.69e-21

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: 88.02  E-value: 2.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVldldpSGVHGPltGIRADVSDDVGVRAAVaaaaERLGGLDILVNNAGIGAVGT 88
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVIT-----AGRSSG--DYQVDITDEASIKALF----EKVGHFDAIVSTAGDAEFAP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  89 VEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRsaHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVReGI 168
Cdd:cd11731    70 LAELTDADFQRGLNSKLLGQINLVRHGLPYLND--GGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIELPR-GI 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 169 RVNCVNPGTVDTPWVsrlLDGADDPEAERaalnarqplgrlVTADEVAAAVLYLAGpsaGSVTGTALAVD 238
Cdd:cd11731   147 RINAVSPGVVEESLE---AYGDFFPGFEP------------VPAEDVAKAYVRSVE---GAFTGQVLHVD 198
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 8-239 7.31e-21

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: 87.38  E-value: 7.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGIGAVG 87
Cdd:cd05334     3 VVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSDSFTEQAKQVVASVARLSGKVDALICVAGGWAGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  88 TVEDHTD-EQWHHVLDVNVVGMVRVTRAALPHLRRSAHasVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADH--V 164
Cdd:cd05334    83 SAKSKSFvKNWDLMWKQNLWTSFIASHLATKHLLSGGL--LVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENsgL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1482408268 165 REGIRVNCVNPGTVDTPwvsrlLDGADDPEAERaalnarqplGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDG 239
Cdd:cd05334   161 PAGSTANAILPVTLDTP-----ANRKAMPDADF---------SSWTPLEFIAELILFWASGAARPKSGSLIPVVT 221
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 9-240 7.63e-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: 88.02  E-value: 7.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDldpsGVHGPLTGIRADVSDDVGVRAAVAAAAERL--------GGLDILVNN 80
Cdd:cd05361     4 ALVTHARHFAGPASAEALTEDGYTVVCHD----ASFADAAERQAFESENPGTKALSEQKPEELvdavlqagGAIDVLVSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIGA-VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:cd05361    80 DYIPRpMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 160 AADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAeRAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDG 239
Cdd:cd05361   160 AKELSRDNILVYAIGPNFFNSPTYFPTSDWENNPEL-RERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAG 238


                  .
gi 1482408268 240 G 240
Cdd:cd05361   239 G 239
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 4-241 8.16e-21

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: 88.16  E-value: 8.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGA--SGIGRAVAERLAERGANVAVL---------------DLDPSGVhgpltgIRADVSDDVGVRAAVAA 66
Cdd:COG0623     3 LKGKRGLITGVAndRSIAWGIAKALHEEGAELAFTyqgealkkrveplaeELGSALV------LPCDVTDDEQIDALFDE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  67 AAERLGGLDILV------NNAGIGavGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRsaHASVVNVCSIAATAGLP 140
Cdd:COG0623    77 IKEKWGKLDFLVhsiafaPKEELG--GRFLDTSREGFLLAMDISAYSLVALAKAAEPLMNE--GGSIVTLTYLGAERVVP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 141 QRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPwVSRLLDGADDPEaERAALNArqPLGRLVTADEVAAAVL 220
Cdd:COG0623   153 NYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTL-AASGIPGFDKLL-DYAEERA--PLGRNVTIEEVGNAAA 228

                         250       260
                  ....*....|....*....|.
gi 1482408268 221 YLAGPSAGSVTGTALAVDGGM 241
Cdd:COG0623   229 FLLSDLASGITGEIIYVDGGY 249
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 9-240 1.17e-20

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: 87.91  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDP-----------SGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd05322     5 AVVIGGGQTLGEFLCHGLAEAGYDVAVADINSenaekvadeinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVDLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTR-AALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:cd05322    85 VYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAReFSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREGIRVNCVNPGT-VDTPWVSRLLD------GADDPEAERAALNaRQPLGRLVTADEVAAAVLYLAGPSAGS 229
Cdd:cd05322   165 QSLALDLAEHGITVNSLMLGNlLKSPMFQSLLPqyakklGIKESEVEQYYID-KVPLKRGCDYQDVLNMLLFYASPKASY 243

                         250
                  ....*....|.
gi 1482408268 230 VTGTALAVDGG 240
Cdd:cd05322   244 CTGQSINITGG 254
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
22-246 1.22e-20

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 87.36  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  22 VAERLAERGANVAVLDLDPSGVhGPLTGIRADVSDDVGVRAAVAAAAERLgglDILVNNAGIGAVGTVEDhtdeqwhhVL 101
Cdd:PRK12428    1 TARLLRFLGARVIGVDRREPGM-TLDGFIQADLGDPASIDAAVAALPGRI---DALFNIAGVPGTAPVEL--------VA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 102 DVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAAtAGLPQRA----------------------------LYSATKGAVL 153
Cdd:PRK12428   69 RVNFLGLRHLTEALLPRMAPGG--AIVNVASLAG-AEWPQRLelhkalaatasfdegaawlaahpvalatGYQLSKEALI 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVRE-GIRVNCVNPGTVDTPWVSRLLDGADDPEAERAAlnarQPLGRLVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK12428  146 LWTMRQAQPWFGArGIRVNCVAPGPVFTPILGDFRSMLGQERVDSDA----KRMGRPATADEQAAVLVFLCSDAARWING 221

                         250
                  ....*....|....
gi 1482408268 233 TALAVDGGMQGLRL 246
Cdd:PRK12428  222 VNLPVDGGLAATYI 235
PRK06949 PRK06949
SDR family oxidoreductase;
3-180 1.46e-20

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 87.51  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAV----------LDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK06949    6 NLEGKVALVTGASSGLGARFAQVLAQAGAKVVLasrrverlkeLRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTR-AALPHLRRSAHAS-------VVNVCSIAATAGLPQRAL 144
Cdd:PRK06949   86 TIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQeVAKRMIARAKGAGntkpggrIINIASVAGLRVLPQIGL 165

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1482408268 145 YSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDT 180
Cdd:PRK06949  166 YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDT 201
PRK06914 PRK06914
SDR family oxidoreductase;
9-182 1.52e-20

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 87.77  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPS------------GVHGPLTGIRADVSDDVGVRAAVAAAAErLGGLDI 76
Cdd:PRK06914    6 AIVTGASSGFGLLTTLELAKKGYLVIATMRNPEkqenllsqatqlNLQQNIKVQQLDVTDQNSIHNFQLVLKE-IGRIDL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV---- 152
Cdd:PRK06914   85 LVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYALegfs 164

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1482408268 153 LSLTLAMAAdhvrEGIRVNCVNPGTVDTP-W 182
Cdd:PRK06914  165 ESLRLELKP----FGIDVALIEPGSYNTNiW 191
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 10-248 1.96e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 87.55  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANV------------AVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK05875   11 LVTGGGSGIGKGVAAGLVAAGAAVmivgrnpdklaaAAEEIEALKGAGAVRYEPADVTDEDQVARAVDAATAWHGRLHGV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIG-AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLt 156
Cdd:PRK05875   91 VHCAGGSeTIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAVDHL- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 157 LAMAADHVREG-IRVNCVNPGTVDTPWVSRLLDGADDPEAERAAlnarQPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:PRK05875  170 MKLAADELGPSwVRVNSIRPGLIRTDLVAPITESPELSADYRAC----TPLPRVGEVEDVANLAMFLLSDAASWITGQVI 245

                         250
                  ....*....|...
gi 1482408268 236 AVDGGmQGLRLRP 248
Cdd:PRK05875  246 NVDGG-HMLRRGP 257
PRK07201 PRK07201
SDR family oxidoreductase;
10-199 6.65e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 88.47  E-value: 6.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PRK07201  375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAkggtahaytcDLTDSAAVDHTVKDILAEHGHVDYLVN 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTD--EQWHHVLDVNVVGMVRVTRAALPHL--RRSAHasVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:PRK07201  455 NAGRSIRRSVENSTDrfHDYERTMAVNYFGAVRLILGLLPHMreRRFGH--VVNVSSIGVQTNAPRFSAYVASKAALDAF 532

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWV--SRLLDGADDPEAERAA 199
Cdd:PRK07201  533 SDVAASETLSDGITFTTIHMPLVRTPMIapTKRYNNVPTISPEEAA 578
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 10-235 1.61e-19

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: 84.17  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVldldpsgvHGPLTGIRADVSDDVG---------------------VRAAVAAAA 68
Cdd:cd05340     8 LVTGASDGIGREAALTYARYGATVIL--------LGRNEEKLRQVADHINeeggrqpqwfildlltctsenCQQLAQRIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  69 ERLGGLDILVNNAG-IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSA 147
Cdd:cd05340    80 VNYPRLDGVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADdpeaeraalnarqPLgRLVTADEVAAAVLYLAGPSA 227
Cdd:cd05340   160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTED-------------PQ-KLKTPADIMPLYLWLMGDDS 225


                  ....*...
gi 1482408268 228 GSVTGTAL 235
Cdd:cd05340   226 RRKTGMTF 233
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 10-196 3.00e-19

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: 84.05  E-value: 3.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLA----ERGANVAVL-DLDPSG---------VHGPLTGIRADVSDDVGVRAAVAAAAERlgGLD 75
Cdd:cd09806     4 LITGCSSGIGLHLAVRLAsdpsKRFKVYATMrDLKKKGrlweaagalAGGTLETLQLDVCDSKSVAAAVERVTER--HVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:cd09806    82 VLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEGL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTPWVSRLLdgADDPEAE 196
Cdd:cd09806   162 CESLAVQLLPFNVHLSLIECGPVHTAFMEKVL--GSPEEVL 200
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 9-231 3.91e-19

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: 82.18  E-value: 3.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLdpsgvhgpltgiradvsddvgvraavaaaaerlgGLDILVNNAGIGAVGT 88
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRGSPKVLVVS----------------------------------RRDVVVHNAAILDDGR 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  89 VEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGI 168
Cdd:cd02266    47 LIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASEGWGNGL 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 169 RVNCVNPGTVDTPWVsrlldgADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVT 231
Cdd:cd02266   127 PATAVACGTWAGSGM------AKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDRPKAGVC 183
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 6-241 4.47e-19

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: 83.40  E-value: 4.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGAS--GIGRAVAERLAERGANVAVLDLDPS----------GVHGPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:cd05372     1 GKRILITGIANdrSIAWGIAKALHEAGAELAFTYQPEAlrkrveklaeRLGESALVLPCDVSNDEEIKELFAEVKKDWGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAG----IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAATAGLPQRALYSATK 149
Cdd:cd05372    81 LDGLVHSIAfapkVQLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNPGG--SIVTLSYLGSERVVPGYNVMGVAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 150 GAVLSLTLAMAADHVREGIRVNCVNPGTVDT------PWVSRLLDGAddpeaeraalNARQPLGRLVTADEVAAAVLYLA 223
Cdd:cd05372   159 AALESSVRYLAYELGRKGIRVNAISAGPIKTlaasgiTGFDKMLEYS----------EQRAPLGRNVTAEEVGNTAAFLL 228

                         250
                  ....*....|....*...
gi 1482408268 224 GPSAGSVTGTALAVDGGM 241
Cdd:cd05372   229 SDLSSGITGEIIYVDGGY 246
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 9-241 6.65e-19

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 83.57  E-value: 6.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDL---------DPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAE 69
Cdd:PRK07791    9 VIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsasGGSAAQAVVDEIVAaggeavangdDIADWDGAANLVDAAVE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  70 RLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLR------RSAHASVVNVCSIAATAGLPQRA 143
Cdd:PRK07791   89 TFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRaeskagRAVDARIINTSSGAGLQGSVGQG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 144 LYSATKGAVLSLTLAMAADHVREGIRVNCVNPG--TVDTPWVSRLLDGaddpEAERAALNARQPlgrlvtaDEVAAAVLY 221
Cdd:PRK07791  169 NYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAarTRMTETVFAEMMA----KPEEGEFDAMAP-------ENVSPLVVW 237

                         250       260
                  ....*....|....*....|
gi 1482408268 222 LAGPSAGSVTGTALAVDGGM 241
Cdd:PRK07791  238 LGSAESRDVTGKVFEVEGGK 257
PRK06139 PRK06139
SDR family oxidoreductase;
10-234 2.01e-18

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 82.85  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGLDILVN 79
Cdd:PRK06139   11 VITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRAlgaevlvvptDVTDADQVKALATQAASFGGRIDVWVN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAM 159
Cdd:PRK06139   91 NVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGFSEAL 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 160 AADHVRE-GIRVNCVNPGTVDTPWVSrllDGADdpeaerAALNARQPLGRLVTADEVAAAVLYLA-GPSAGSVTGTA 234
Cdd:PRK06139  171 RGELADHpDIHVCDVYPAFMDTPGFR---HGAN------YTGRRLTPPPPVYDPRRVAKAVVRLAdRPRATTTVGAA 238
PRK05693 PRK05693
SDR family oxidoreductase;
9-180 2.59e-18

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 81.76  E-value: 2.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANV-----AVLDLDPSGVHGpLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:PRK05693    4 VLITGCSSGIGRALADAFKAAGYEVwatarKAEDVEALAAAG-FTAVQLDVNDGAALARLAEELEAEHGGLDVLINNAGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADH 163
Cdd:PRK05693   83 GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRS-RGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLEL 161

                         170
                  ....*....|....*..
gi 1482408268 164 VREGIRVNCVNPGTVDT 180
Cdd:PRK05693  162 APFGVQVMEVQPGAIAS 178
PRK07024 PRK07024
SDR family oxidoreductase;
7-181 4.09e-18

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 80.74  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   7 LRAVVTGGASGIGRAVAERLAERGANVAVL-----DLDPSGVHGPLTG----IRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK07024    3 LKVFITGASSGIGQALAREYARQGATLGLVarrtdALQAFAARLPKAArvsvYAADVRDADALAAAAADFIAAHGLPDVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIgAVGTVEDHTD--EQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSL 155
Cdd:PRK07024   83 IANAGI-SVGTLTEEREdlAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKY 161

                         170       180
                  ....*....|....*....|....*.
gi 1482408268 156 TLAMAADHVREGIRVNCVNPGTVDTP 181
Cdd:PRK07024  162 LESLRVELRPAGVRVVTIAPGYIRTP 187
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 1-184 4.89e-18

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 81.16  E-value: 4.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAER---------- 70
Cdd:PRK05876    1 MDGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVthladeafrl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  71 LGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRsaHASVVNVCSIAATAGL-PQRAL--YSA 147
Cdd:PRK05876   81 LGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLE--QGTGGHVVFTASFAGLvPNAGLgaYGV 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1482408268 148 TKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVS 184
Cdd:PRK05876  159 AKYGVVGLAETLAREVTADGIGVSVLCPMVVETNLVA 195
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-240 5.71e-18

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 80.60  E-value: 5.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGG--ASGIGRAVAERLAERGANVAVL---DLDPSGVHG------------------PLTGIRADVSDD 57
Cdd:PRK12859    1 MNQLKNKVAVVTGVsrLDGIGAAICKELAEAGADIFFTywtAYDKEMPWGvdqdeqiqlqeellkngvKVSSMELDLTQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  58 VGVRAAVAAAAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATA 137
Cdd:PRK12859   81 DAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 138 GLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrlldgaddpEAERAALNARQPLGRLVTADEVAA 217
Cdd:PRK12859  161 PMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMT---------EEIKQGLLPMFPFGRIGEPKDAAR 231

                         250       260
                  ....*....|....*....|...
gi 1482408268 218 AVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK12859  232 LIKFLASEEAEWITGQIIHSEGG 254
PRK05866 PRK05866
SDR family oxidoreductase;
3-212 1.42e-17

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 79.79  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAV-------LDLDPSGVH---GPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK05866   37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAvarredlLDAVADRITragGDAMAVPCDLSDLDAVDALVADVEKRIG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDeQWHHV---LDVNVVGMVRVTRAALPHL--RRSAHasVVNVCSIAATAG-LPQRALYS 146
Cdd:PRK05866  117 GVDILINNAGRSIRRPLAESLD-RWHDVertMVLNYYAPLRLIRGLAPGMleRGDGH--IINVATWGVLSEaSPLFSVYN 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1482408268 147 ATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWV--SRLLDGAddpeaerAALNARQPLGRLVTA 212
Cdd:PRK05866  194 ASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIapTKAYDGL-------PALTADEAAEWMVTA 254
PRK07041 PRK07041
SDR family oxidoreductase;
10-240 1.71e-17

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 78.54  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVL---------DLDPSGVHGPLTGIRADVSDDVGVRaavaAAAERLGGLDILVNN 80
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIAsrsrdrlaaAARALGGGAPVRTAALDITDEAAVD----AFFAEAGPFDHVVIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAAlphlRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMA 160
Cdd:PRK07041   77 AADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 161 ADhvREGIRVNCVNPGTVDTPWVSRLLDgaDDPEAERAALNARQPLGRLVTADEVAAAVLYLAGpsAGSVTGTALAVDGG 240
Cdd:PRK07041  153 LE--LAPVRVNTVSPGLVDTPLWSKLAG--DAREAMFAAAAERLPARRVGQPEDVANAILFLAA--NGFTTGSTVLVDGG 226
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 11-235 2.97e-17

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 78.38  E-value: 2.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANV-------------------------AVLDLDpsgvhgpLTGIRADVSDDVgvraaVA 65
Cdd:PRK08945   17 VTGAGDGIGREAALTYARHGATVillgrteekleavydeieaaggpqpAIIPLD-------LLTATPQNYQQL-----AD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  66 AAAERLGGLDILVNNAGI-GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSiaaTAGLPQRAL 144
Cdd:PRK08945   85 TIEEQFGRLDGVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSS---SVGRQGRAN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 ---YSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTpwvsrlldgaddpeAERA-ALNARQPLgRLVTADEVAAAVL 220
Cdd:PRK08945  162 wgaYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT--------------AMRAsAFPGEDPQ-KLKTPEDIMPLYL 226

                         250
                  ....*....|....*
gi 1482408268 221 YLAGPSAGSVTGTAL 235
Cdd:PRK08945  227 YLMGDDSRRKNGQSF 241
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 11-223 3.01e-16

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 75.56  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANV-------AVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:PRK10538    5 VTGATAGFGECITRRFIQQGHKViatgrrqERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 gAVGTVEDH--TDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAA 161
Cdd:PRK10538   85 -ALGLEPAHkaSVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRT 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1482408268 162 DHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAALNArQPLgrlvTADEVAAAVLYLA 223
Cdd:PRK10538  164 DLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNT-VAL----TPEDVSEAVWWVA 220
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
8-223 1.54e-15

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 74.24  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV-----HGPLTGIRADVSDDVGVRaavaaaaERLGGLDILVNNAG 82
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAanlaaLPGVEFVRGDLRDPEALA-------AALAGVDAVVHLAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  83 IGAVGTvedhtdEQWHHVLDVNVVGMVRVTRAALPH-LRRSAHAS---VVNVCSIAATAGLPQRAL--YSATKGAVLSLT 156
Cdd:COG0451    74 PAGVGE------EDPDETLEVNVEGTLNLLEAARAAgVKRFVYASsssVYGDGEGPIDEDTPLRPVspYGASKLAAELLA 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482408268 157 LAMAADHvreGIRVNCVNPGTV----DTPWVSRLLDGADDPEAERAALNARQPLGrLVTADEVAAAVLYLA 223
Cdd:COG0451   148 RAYARRY---GLPVTILRPGNVygpgDRGVLPRLIRRALAGEPVPVFGDGDQRRD-FIHVDDVARAIVLAL 214
PRK09291 PRK09291
SDR family oxidoreductase;
5-176 2.34e-15

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 73.11  E-value: 2.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAvldldpSGVH--GPLTGIRADVSD-DVGVRAavaaaaERLGGL------- 74
Cdd:PRK09291    1 MSKTILITGAGSGFGREVALRLARKGHNVI------AGVQiaPQVTALRAEAARrGLALRV------EKLDLTdaidraq 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 ------DILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSAT 148
Cdd:PRK09291   69 aaewdvDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCAS 148

                         170       180
                  ....*....|....*....|....*...
gi 1482408268 149 KGAVLSLTLAMAADHVREGIRVNCVNPG 176
Cdd:PRK09291  149 KHALEAIAEAMHAELKPFGIQVATVNPG 176
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 9-241 2.46e-15

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: 73.42  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAV----LDLDPSGVHGPLTGIRAD----VSDDVGVRAAVAAAAERL--------G 72
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLhyhrSAAAASTLAAELNARRPNsavtCQADLSNSATLFSRCEAIidacfrafG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNA---------------GIGAVGTVEDHTDEqwhhVLDVNVVGMVRVTRAALPHLR------RSAHASVVNVC 131
Cdd:TIGR02685  84 RCDVLVNNAsafyptpllrgdageGVGDKKSLEVQVAE----LFGSNAIAPYFLIKAFAQRQAgtraeqRSTNLSIVNLC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 132 SIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGtvdtpwVSRLLDgaDDPEAERAALNARQPLG-RLV 210
Cdd:TIGR02685 160 DAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPG------LSLLPD--AMPFEVQEDYRRKVPLGqREA 231

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1482408268 211 TADEVAAAVLYLAGPSAGSVTGTALAVDGGM 241
Cdd:TIGR02685 232 SAEQIADVVIFLVSPKAKYITGTCIKVDGGL 262
PRK05993 PRK05993
SDR family oxidoreductase;
10-223 4.67e-15

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 72.75  E-value: 4.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANV--------AVLDLDPSGvhgpLTGIRADVSDDVGVRAAVAAAAERLGG-LDILVNN 80
Cdd:PRK05993    8 LITGCSSGIGAYCARALQSDGWRVfatcrkeeDVAALEAEG----LEAFQLDYAEPESIAALVAQVLELSGGrLDALFNN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV--LSLTLA 158
Cdd:PRK05993   84 GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFAIegLSLTLR 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 159 MAADHvrEGIRVNCVNPGTVDT-------PWVSRLLDGADDPEAE-----RAALNARQPLGRLVTADEVAAAVLYLA 223
Cdd:PRK05993  164 MELQG--SGIHVSLIEPGPIETrfranalAAFKRWIDIENSVHRAayqqqMARLEGGGSKSRFKLGPEAVYAVLLHA 238
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 11-197 5.84e-15

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: 72.09  E-value: 5.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLD-------PSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGG 73
Cdd:cd09762     8 ITGASRGIGKAIALKAARDGANVVIAAKTaephpklPGTIYTAAEEIEAaggkalpcivDIRDEDQVRAAVEKAVEKFGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVC---SIAATAGLPQRAlYSATKG 150
Cdd:cd09762    88 IDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSpplNLNPKWFKNHTA-YTMAKY 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1482408268 151 AVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAER 197
Cdd:cd09762   167 GMSMCVLGMAEEFKPGGIAVNALWPRTAIATAAMNMLGGVDVAACCR 213
PRK09186 PRK09186
flagellin modification protein A; Provisional
 10-240 6.90e-15

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 71.94  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGV------------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK09186    8 LITGAGGLIGSALVKAILEAGGIVIAADIDKEALnelleslgkefkSKKLSLVELDITDQESLEEFLSKSAEKYGKIDGA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNA-----GIGAvgTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGlPQRALY------- 145
Cdd:PRK09186   88 VNCAyprnkDYGK--KFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVA-PKFEIYegtsmts 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 146 ----SATKGAVLSLTLAMAADHVREGIRVNCVNPGTVdtpwvsrlLDGadDPEAERAALNARQPLGRLVTADEVAAAVLY 221
Cdd:PRK09186  165 pveyAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGI--------LDN--QPEAFLNAYKKCCNGKGMLDPDDICGTLVF 234

                         250
                  ....*....|....*....
gi 1482408268 222 LAGPSAGSVTGTALAVDGG 240
Cdd:PRK09186  235 LLSDQSKYITGQNIIVDDG 253
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 6-184 8.66e-14

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 69.51  E-value: 8.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA------------DVSDDV--GVRAAVaaaaERL 71
Cdd:PLN02780   53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSkysktqiktvvvDFSGDIdeGVKRIK----ETI 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  72 GGLD--ILVNNAGIGAVGTVEDHT--DEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATA--GLPQRALY 145
Cdd:PLN02780  129 EGLDvgVLINNVGVSYPYARFFHEvdEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVipSDPLYAVY 208

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1482408268 146 SATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVS 184
Cdd:PLN02780  209 AATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMAS 247
PRK08416 PRK08416
enoyl-ACP reductase;
1-240 1.17e-13

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 68.64  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVA-------------VLDLDPSgvhgplTGIRA-----DVSDDVGVRA 62
Cdd:PRK08416    3 SNEMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAftynsnveeankiAEDLEQK------YGIKAkayplNILEPETYKE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  63 AVAAAAERLGGLDILVNNAGIGAVGTVEDHTD------EQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAAT 136
Cdd:PRK08416   77 LFKKIDEDFDRVDFFISNAIISGRAVVGGYTKfmrlkpKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 137 AGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPwvsrLLDGADDPEAERAALNARQPLGRLVTADEVA 216
Cdd:PRK08416  157 VYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTD----ALKAFTNYEEVKAKTEELSPLNRMGQPEDLA 232

                         250       260
                  ....*....|....*....|....
gi 1482408268 217 AAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK08416  233 GACLFLCSEKASWLTGQTIVVDGG 256
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 3-242 5.65e-13

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 66.80  E-value: 5.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERL----------G 72
Cdd:PRK08339    5 DLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLertvkelkniG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  73 GLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK08339   85 EPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTpwvSRLLDGADDpEAERAALNARQ---------PLGRLVTADEVAAAVLYLA 223
Cdd:PRK08339  165 AGLVRTLAKELGPKGITVNGIMPGIIRT---DRVIQLAQD-RAKREGKSVEEalqeyakpiPLGRLGEPEEIGYLVAFLA 240

                         250
                  ....*....|....*....
gi 1482408268 224 GPSAGSVTGTALAVDGGMQ 242
Cdd:PRK08339  241 SDLGSYINGAMIPVDGGRL 259
PRK08703 PRK08703
SDR family oxidoreductase;
1-232 5.92e-13

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 66.49  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV-----------HGPLTGIRADV---SDDVGVRAAVAA 66
Cdd:PRK08703    1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLekvydaiveagHPEPFAIRFDLmsaEEKEFEQFAATI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  67 AAERLGGLDILVNNAG-IGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALY 145
Cdd:PRK08703   81 AEATQGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 146 SATKGAVLSLTLAMAADHVREG-IRVNCVNPGTVDTPWVSRLLDGADdpEAERAALnarqplgrlvtaDEVAAAVLYLAG 224
Cdd:PRK08703  161 GASKAALNYLCKVAADEWERFGnLRANVLVPGPINSPQRIKSHPGEA--KSERKSY------------GDVLPAFVWWAS 226


                  ....*...
gi 1482408268 225 PSAGSVTG 232
Cdd:PRK08703  227 AESKGRSG 234
PRK07775 PRK07775
SDR family oxidoreductase;
9-228 7.31e-13

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 66.32  E-value: 7.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVA------------VLDLDPSGvhGPLTGIRADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAAAGFPVAlgarrvekceelVDKIRADG--GEAVAFPLDVTDPDSVKSFVAQAEEALGEIEV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLT 156
Cdd:PRK07775   91 LVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMV 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDTPWVSRLldgadDPEAERAALNARQPLG-----RLVTADEVAAAVLYLAGPSAG 228
Cdd:PRK07775  171 TNLQMELEGTGVRASIVHPGPTLTGMGWSL-----PAEVIGPMLEDWAKWGqarhdYFLRASDLARAITFVAETPRG 242
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 10-240 1.37e-12

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 65.34  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANV---------AVLDLDPSGVhgplTGIRADVSDDVGVRAAVAAAAERLGGLDILVNN 80
Cdd:PRK06483    6 LITGAGQRIGLALAWHLLAQGQPVivsyrthypAIDGLRQAGA----QCIQADFSTNAGIMAFIDELKQHTDGLRAIIHN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAH--ASVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:PRK06483   82 ASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHaaSDIIHITDYVVEKGSDKHIAYAASKAALDNMTLS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREgIRVNCVNPGTVdtpwvsrLLDGADDPEAERAALnARQPLGRLVTADEVAAAVLYLAGPSagSVTGTALAVD 238
Cdd:PRK06483  162 FAAKLAPE-VKVNSIAPALI-------LFNEGDDAAYRQKAL-AKSLLKIEPGEEEIIDLVDYLLTSC--YVTGRSLPVD 230


                  ..
gi 1482408268 239 GG 240
Cdd:PRK06483  231 GG 232
PRK08251 PRK08251
SDR family oxidoreductase;
10-180 1.76e-12

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 64.96  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAV-------LDLDPSGVHGPLTGIRA-----DVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK08251    6 LITGASSGLGAGMAREFAAKGRDLALcarrtdrLEELKAELLARYPGIKVavaalDVNDHDQVFEVFAEFRDELGGLDRV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIG---AVGTVEDHTDEQwhhVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQ-RALYSATKGAVL 153
Cdd:PRK08251   86 IVNAGIGkgaRLGTGKFWANKA---TAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGvKAAYAASKAGVA 162

                         170       180
                  ....*....|....*....|....*..
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVDT 180
Cdd:PRK08251  163 SLGEGLRAELAKTPIKVSTIEPGYIRS 189
PRK07806 PRK07806
SDR family oxidoreductase;
1-219 2.72e-12

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 64.74  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAV-------------LDLDPSGVHGplTGIRADVSDDVGVRAAVAAA 67
Cdd:PRK07806    1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVnyrqkaprankvvAEIEAAGGRA--SAVGADLTDEESVAALMDTA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  68 AERLGGLDILVNNAGigavGTVEDHTDEqwHHVLDVNVVGMVRVTRAALPHLRRSAHasVVNVCS-----IAATAGLPQR 142
Cdd:PRK07806   79 REEFGGLDALVLNAS----GGMESGMDE--DYAMRLNRDAQRNLARAALPLMPAGSR--VVFVTShqahfIPTVKTMPEY 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482408268 143 ALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGAdDPEAERAalnARQPLGRLVTADEVAAAV 219
Cdd:PRK07806  151 EPVARSKRAGEDALRALRPELAEKGIGFVVVSGDMIEGTVTATLLNRL-NPGAIEA---RREAAGKLYTVSEFAAEV 223
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 9-204 6.20e-12

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 62.92  E-value: 6.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPsgvhGPLTGIRADVSD-----DVGVRAAVAAAAERLGGLDILVNNAGI 83
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRLLLSGRDA----GALAGLAAEVGAlarpaDVAAELEVWALAQELGPLDLLVYAAGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATagLPQRALYSATKGAVLSLTLAMAADh 163
Cdd:cd11730    77 ILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPELVM--LPGLSAYAAAKAALEAYVEVARKE- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1482408268 164 vREGIRVNCVNPGTVDTP-W--VSRLLDGADDPE-AERAALNARQ 204
Cdd:cd11730   154 -VRGLRLTLVRPPAVDTGlWapPGRLPKGALSPEdVAAAILEAHQ 197
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 9-201 1.98e-11

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: 62.01  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVA-----------VLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd05373     2 AAVVGAGDGLGAAIARRFAAEGFSVAlaarreakleaLLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTL 157
Cdd:cd05373    82 VYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQ 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1482408268 158 AMAADHVREGIRV-NCVNPGTVDTPWVSRLLDGADDPEAERAALN 201
Cdd:cd05373   162 SMARELGPKGIHVaHVIIDGGIDTDFIRERFPKRDERKEEDGILD 206
PRK08340 PRK08340
SDR family oxidoreductase;
7-241 2.26e-11

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 62.13  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   7 LRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGV---------HGPLTGIRADVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:PRK08340    1 MNVLVTASSRGIGFNVARELLKKGARVVISSRNEENLekalkelkeYGEVYAVKADLSDKDDLKNLVKEAWELLGGIDAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGigAVGT----VEDHTDEQWHHVLDVNVVGMVRVTRAALPH-LRRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK08340   81 VWNAG--NVRCepcmLHEAGYSDWLEAALLHLVAPGYLTTLLIQAwLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLD------GADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPS 226
Cdd:PRK08340  159 VQLAKGVSRTYGGKGIRAYTVLLGSFDTPGARENLAriaeerGVSFEETWEREVLERTPLKRTGRWEELGSLIAFLLSEN 238

                         250
                  ....*....|....*
gi 1482408268 227 AGSVTGTALAVDGGM 241
Cdd:PRK08340  239 AEYMLGSTIVFDGAM 253
PRK06101 PRK06101
SDR family oxidoreductase;
11-185 2.30e-11

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 61.81  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANV-------AVLDlDPSGVHGPLTGIRADVSDDVGVRaavaaaaERLGGLDILVNNAGI 83
Cdd:PRK06101    6 ITGATSGIGKQLALDYAKQGWQViacgrnqSVLD-ELHTQSANIFTLAFDVTDHPGTK-------AALSQLPFIPELWIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  84 GAvGTVEDHTD-----EQWHHVLDVNVVGMVRVTRAALPHLRRsAHaSVVNVCSIAATAGLPQRALYSATKGAVLSLTLA 158
Cdd:PRK06101   78 NA-GDCEYMDDgkvdaTLMARVFNVNVLGVANCIEGIQPHLSC-GH-RVVIVGSIASELALPRAEAYGASKAAVAYFART 154

                         170       180
                  ....*....|....*....|....*..
gi 1482408268 159 MAADHVREGIRVNCVNPGTVDTPWVSR 185
Cdd:PRK06101  155 LQLDLRPKGIEVVTVFPGFVATPLTDK 181
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 9-224 2.67e-11

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: 62.08  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPS-GVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGG-LDI 76
Cdd:cd09763     6 ALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEArggkcipvrcDHSDDDEVEALFERVAREQQGrLDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVL----DVNVVGmVR----VTRAALPHLRRSAHASVVNVCSIAATAGLPQRAlYSAT 148
Cdd:cd09763    86 LVNNAYAAVQLILVGVAKPFWEEPPtiwdDINNVG-LRahyaCSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVA-YGVG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 149 KGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAER---AALNARQP--LGRLVTADEVAAAVLYLA 223
Cdd:cd09763   164 KAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKerdAFLNGETTeySGRCVVALAADPDLMELS 243


                  .
gi 1482408268 224 G 224
Cdd:cd09763   244 G 244
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 10-180 5.36e-11

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: 61.33  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA------------DVSDDVGVRAAVAAAAERLGGLDIL 77
Cdd:cd09807     5 IITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRdtlnhevivrhlDLASLKSIRAFAAEFLAEEDRLDVL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  78 VNNAGIGAV--GTVEDHTDEQwhhvLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAG------------LPQRA 143
Cdd:cd09807    85 INNAGVMRCpySKTEDGFEMQ----FGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGkinfddlnseksYNTGF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1482408268 144 LYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDT 180
Cdd:cd09807   161 AYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK12744 PRK12744
SDR family oxidoreductase;
1-240 8.34e-11

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 60.52  E-value: 8.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGASGIGRAVAERLAERGANVAVL----------------DLDPSGVHGPLtgIRADVSDDVGVRAAV 64
Cdd:PRK12744    3 DHSLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIhynsaaskadaeetvaAVKAAGAKAVA--FQADLTTAAAVEKLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  65 AAAAERLGGLDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLrrSAHASVVNVCSIAATAGLPQRAL 144
Cdd:PRK12744   81 DDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTLVTSLLGAFTPFYSA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 145 YSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrlldGADDPEA-----ERAALNARQPLGrLVTADEVAAAV 219
Cdd:PRK12744  159 YAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFY----PQEGAEAvayhkTAAALSPFSKTG-LTDIEDIVPFI 233

                         250       260
                  ....*....|....*....|..
gi 1482408268 220 LYLAgpSAGS-VTGTALAVDGG 240
Cdd:PRK12744  234 RFLV--TDGWwITGQTILINGG 253
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-240 9.22e-11

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 60.16  E-value: 9.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   4 FTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPS---------GVHGPLTGIRADVSDDVGVRAAVAAAAERLGGL 74
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENklkrmkktlSKYGNIHYVVGDVSSTESARNVIEKAAKVLNAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  75 DILVNNAGIGAVGTVEDHTDEQwhHVLDVNVVGMVRVTRAALPHLRRSAhaSVVNVCSIAAT-AGLPQRALYSATKGAVL 153
Cdd:PRK05786   83 DGLVVTVGGYVEDTVEEFSGLE--EMLTNHIKIPLYAVNASLRFLKEGS--SIVLVSSMSGIyKASPDQLSYAVAKAGLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 154 SLTLAMAADHVREGIRVNCVNPGTVdtpwvsrllDGADDPEAERAALnarQPLGR-LVTADEVAAAVLYLAGPSAGSVTG 232
Cdd:PRK05786  159 KAVEILASELLGRGIRVNGIAPTTI---------SGDFEPERNWKKL---RKLGDdMAPPEDFAKVIIWLLTDEADWVDG 226


                  ....*...
gi 1482408268 233 TALAVDGG 240
Cdd:PRK05786  227 VVIPVDGG 234
PRK08017 PRK08017
SDR family oxidoreductase;
10-180 1.50e-10

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 59.71  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHG----PLTGIRADVSDDVGVRAAVAAAAERLGG-LDILVNNAGIG 84
Cdd:PRK08017    6 LITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARmnslGFTGILLDLDDPESVERAADEVIALTDNrLYGLFNNAGFG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  85 AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHV 164
Cdd:PRK08017   86 VYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSDALRMELR 165

                         170
                  ....*....|....*.
gi 1482408268 165 REGIRVNCVNPGTVDT 180
Cdd:PRK08017  166 HSGIKVSLIEPGPIRT 181
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
53-241 2.71e-10

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 58.80  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  53 DVSDDVGVRAAVAAAAERLGGLDILVNNAGIGAV----GTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVV 128
Cdd:PRK07533   68 DVREPGQLEAVFARIAEEWGRLDFLLHSIAFAPKedlhGRVVDCSREGFALAMDVSCHSFIRMARLAEPLMTNGG--SLL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 129 NVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTpwvsRLLDGADDPEAERAALNARQPLGR 208
Cdd:PRK07533  146 TMSYYGAEKVVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKT----RAASGIDDFDALLEDAAERAPLRR 221

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1482408268 209 LVTADEVAAAVLYLAGPSAGSVTGTALAVDGGM 241
Cdd:PRK07533  222 LVDIDDVGAVAAFLASDAARRLTGNTLYIDGGY 254
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
1-240 3.49e-10

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 58.57  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGLRAVVTGGAS--GIGRAVAERLAERGANVAVLDL-DPSG--------VHGPLTG---IRADVSDDVGVRAAVAA 66
Cdd:PRK07370    1 MLDLTGKKALVTGIANnrSIAWGIAQQLHAAGAELGITYLpDEKGrfekkvreLTEPLNPslfLPCDVQDDAQIEETFET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  67 AAERLGGLDILVNNAGI----GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLrrSAHASVVNVCSIAATAGLPQR 142
Cdd:PRK07370   81 IKQKWGKLDILVHCLAFagkeELIGDFSATSREGFARALEISAYSLAPLCKAAKPLM--SEGGSIVTLTYLGGVRAIPNY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 143 ALYSATKGAVLSLTLAMAADHVREGIRVNCVNPG---TVDTPWVSRLLDGADDPEaERAalnarqPLGRLVTADEVAAAV 219
Cdd:PRK07370  159 NVMGVAKAALEASVRYLAAELGPKNIRVNAISAGpirTLASSAVGGILDMIHHVE-EKA------PLRRTVTQTEVGNTA 231

                         250       260
                  ....*....|....*....|.
gi 1482408268 220 LYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK07370  232 AFLLSDLASGITGQTIYVDAG 252
PRK06196 PRK06196
oxidoreductase; Provisional
 5-133 4.65e-10

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 58.54  E-value: 4.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRA------DVSDDVGVRAAVAAAAERLGGLDILV 78
Cdd:PRK06196   25 SGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDGvevvmlDLADLESVRAFAERFLDSGRRIDILI 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1482408268  79 NNAGIGAvgTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSI 133
Cdd:PRK06196  105 NNAGVMA--CPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSA 157
PRK07023 PRK07023
SDR family oxidoreductase;
8-230 4.72e-10

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 58.10  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGanVAVLDL----DPS---GVHGPLTGIRADVSDDVGVRAAVAAAAERLGGLD----I 76
Cdd:PRK07023    3 RAIVTGHSRGLGAALAEQLLQPG--IAVLGVarsrHPSlaaAAGERLAEVELDLSDAAAAAAWLAGDLLAAFVDGasrvL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAG----IGAVGTVedHTDEQWHHVLdVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAV 152
Cdd:PRK07023   81 LINNAGtvepIGPLATL--DAAAIARAVG-LNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 153 LSLTLAMAADHVReGIRVNCVNPGTVDTPWVS--RLLDGADDPEAER-AALNARqplGRLVTADEVAAAVL-YLAGPSAG 228
Cdd:PRK07023  158 DHHARAVALDANR-ALRIVSLAPGVVDTGMQAtiRATDEERFPMRERfRELKAS---GALSTPEDAARRLIaYLLSDDFG 233


                  ..
gi 1482408268 229 SV 230
Cdd:PRK07023  234 ST 235
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 10-147 6.45e-10

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: 58.53  E-value: 6.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAER-GANVAVL---DLDPSGVH------------GPLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:cd08953   209 LVTGGAGGIGRALARALARRyGARLVLLgrsPLPPEEEWkaqtlaalealgARVLYISADVTDAAAVRRLLEKVRERYGA 288

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAalphLRRSAHASVVNVCSIAATAGLPQRALYSA 147
Cdd:cd08953   289 IDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQA----LADEPLDFFVLFSSVSAFFGGAGQADYAA 358
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 14-200 3.10e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 55.20  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  14 GASG-IGRAVAERLAERGANVAVldldpsgvhGPLTG-IRADVSDDVGVRAAVaaaaERLGGLDILVNNAGIGAVGTVED 91
Cdd:PRK07578    7 GASGtIGRAVVAELSKRHEVITA---------GRSSGdVQVDITDPASIRALF----EKVGKVDAVVSAAGKVHFAPLAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  92 HTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhasvvnvcSIAATAGL------PQRALYSATKGAVLSLTLAmAADHVR 165
Cdd:PRK07578   74 MTDEDFNVGLQSKLMGQVNLVLIGQHYLNDGG--------SFTLTSGIlsdepiPGGASAATVNGALEGFVKA-AALELP 144

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1482408268 166 EGIRVNCVNPGTVDTPWVS--RLLDGADDPEAERAAL 200
Cdd:PRK07578  145 RGIRINVVSPTVLTESLEKygPFFPGFEPVPAARVAL 181
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
53-240 3.96e-09

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 55.91  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  53 DVSDDVGVRAAVAAAAERLGGLDILVNNAGI----GAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLrrSAHASVV 128
Cdd:PRK08415   63 DVSKPEHFKSLAESLKKDLGKIDFIVHSVAFapkeALEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL--NDGASVL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 129 NVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGaddpeaeRAALN---ARQP 205
Cdd:PRK08415  141 TLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKTLAASGIGDF-------RMILKwneINAP 213

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1482408268 206 LGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK08415  214 LKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAG 248
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 10-147 6.15e-09

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: 54.03  E-value: 6.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   10 VVTGGASGIGRAVAERLAERGA-NVAVL---DLDPSGVHGPLTGIRA----------DVSDDVGVRAAVAAAAERLGGLD 75
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLsrsGPDAPGAAALLAELEAagarvtvvacDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268   76 ILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPH-LRRsahasVVNVCSIAATAGLPQRALYSA 147
Cdd:smart00822  84 GVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLpLDF-----FVLFSSIAGVLGSPGQANYAA 151
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
9-180 1.49e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 53.92  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLD-------LDPSGV-HGPLTGIRADVSD--DVGVRAAVAAAAERLGGLD--I 76
Cdd:PRK06924    4 VIITGTSQGLGEAIANQLLEKGTHVISISrtenkelTKLAEQyNSNLTFHSLDLQDvhELETNFNEILSSIQEDNVSsiH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGA-VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLR-RSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK06924   84 LINNAGMVApIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKdWKVDKRVINISSGAAKNPYFGWSAYCSSKAGLDM 163

                         170       180
                  ....*....|....*....|....*...
gi 1482408268 155 LTLAMAADHVRE--GIRVNCVNPGTVDT 180
Cdd:PRK06924  164 FTQTVATEQEEEeyPVKIVAFSPGVMDT 191
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 9-222 1.75e-08

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: 53.76  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAER----GANVAVLDLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAER-----LGGLD---- 75
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAgleqlLKALRelpr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  76 -------ILVNNAG-IGAVGTVEDHTDE--QWHHVLDVNVVGMVRVTRAALPHLR--RSAHASVVNVCSIAATAGLPQRA 143
Cdd:TIGR01500  83 pkglqrlLLINNAGtLGDVSKGFVDLSDstQVQNYWALNLTSMLCLTSSVLKAFKdsPGLNRTVVNISSLCAIQPFKGWA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1482408268 144 LYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPeAERAALNARQPLGRLVTADEVAAAVLYL 222
Cdd:TIGR01500 163 LYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREESVDP-DMRKGLQELKAKGKLVDPKVSAQKLLSL 240
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 9-178 3.14e-08

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: 52.68  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVH----GPLTGIRADVSDDVGVRAAVAAAaerlgGLDILVNNAGIG 84
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNtarlADLRFVEGDLTDRDALEKLLADV-----RPDAVIHLAAVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  85 AVGTVEDHTDEQWHHvldvNVVGMVRVTRAAlphlrRSAHASVVNVCSIAATAG---------------LPQRALYSATK 149
Cdd:pfam01370  76 GVGASIEDPEDFIEA----NVLGTLNLLEAA-----RKAGVKRFLFASSSEVYGdgaeipqeettltgpLAPNSPYAAAK 146

                         170       180
                  ....*....|....*....|....*....
gi 1482408268 150 GAVLSLTLAMAADHvreGIRVNCVNPGTV 178
Cdd:pfam01370 147 LAGEWLVLAYAAAY---GLRAVILRLFNV 172
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 10-240 1.61e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 50.79  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAErGANVAVLDLDPSGVHG----------PLTGIRADVSDDVGVRAAVAAAaERLGGLDILVN 79
Cdd:PRK06940    5 VVVIGAGGIGQAIARRVGA-GKKVLLADYNEENLEAaaktlreagfDVSTQEVDVSSRESVKALAATA-QTLGPVTGLVH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 NAGIG-AVGTVEDhtdeqwhhVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQ---RALYSATKGAVLSL 155
Cdd:PRK06940   83 TAGVSpSQASPEA--------ILKVDLYGTALVLEEFGKVIAPGGAGVVIASQSGHRLPALTAeqeRALATTPTEELLSL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 156 ---------------TLAMAADHVR----------EGIRVNCVNPGTVDTPWvsrlldGADDPEAERAA----LNARQPL 206
Cdd:PRK06940  155 pflqpdaiedslhayQIAKRANALRvmaeavkwgeRGARINSISPGIISTPL------AQDELNGPRGDgyrnMFAKSPA 228

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1482408268 207 GRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK06940  229 GRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
22-240 1.88e-07

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 50.74  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  22 VAERLAERGANVAVlDLDPSGVhgpltgIRADVSDDVGVRAAVAAAAERLGGLDILVNNAGIGAVGTVE-DHTD----EQ 96
Cdd:PRK08690   40 VVDKLEERVRKMAA-ELDSELV------FRCDVASDDEINQVFADLGKHWDGLDGLVHSIGFAPKEALSgDFLDsisrEA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  97 WHHVLDVNVVGMVRVTRAALPhLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPG 176
Cdd:PRK08690  113 FNTAHEISAYSLPALAKAARP-MMRGRNSAIVALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAG 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1482408268 177 TVDTPWVSrlldGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK08690  192 PIKTLAAS----GIADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGG 251
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 10-107 4.77e-07

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: 48.71  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGA-NVAVL---------------DLDPSGVHgpLTGIRADVSDDVGVRAAVAAAAERLGG 73
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLsrsaaprpdaqaliaELEARGVE--VVVVACDVSDPDAVAALLAEIKAEGPP 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1482408268  74 LDILVNNAGIGAVGTVEDHTDEQWHHVLDVNVVG 107
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTG 115
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
53-240 9.27e-07

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 48.59  E-value: 9.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  53 DVSDDVGVRAAVAAAAERLGGLDILVNNAGIG----AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLrrSAHASVV 128
Cdd:PRK06505   65 DVEDIASVDAVFEALEKKWGKLDFVVHAIGFSdkneLKGRYADTTRENFSRTMVISCFSFTEIAKRAAKLM--PDGGSML 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 129 NVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVdtpwvsRLLDGADDPEAeRAALNARQ---P 205
Cdd:PRK06505  143 TLTYGGSTRVMPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPV------RTLAGAGIGDA-RAIFSYQQrnsP 215

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1482408268 206 LGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK06505  216 LRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDSG 250
PRK05854 PRK05854
SDR family oxidoreductase;
5-138 1.26e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 48.52  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHGPLTGIRADVSD-DVGVRAAVAAAAERLGGL--------- 74
Cdd:PRK05854   13 SGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDaKLSLRALDLSSLASVAALgeqlraegr 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482408268  75 --DILVNNAGIGAVGTvEDHTDEQWHHVLDVNVVGMVRVTRAALPhLRRSAHASVVNVCSIAATAG 138
Cdd:PRK05854   93 piHLLINNAGVMTPPE-RQTTADGFELQFGTNHLGHFALTAHLLP-LLRAGRARVTSQSSIAARRG 156
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
50-240 1.58e-06

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 47.79  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  50 IRADVSDDVGVRAAVAAAAERLGGLDILVNNAGIGA----VGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAha 125
Cdd:PRK06079   60 VECDVASDESIERAFATIKERVGKIDGIVHAIAYAKkeelGGNVTDTSRDGYALAQDISAYSLIAVAKYARPLLNPGA-- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 126 SVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERaalnARQP 205
Cdd:PRK06079  138 SIVTLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAVTGIKGHKDLLKESD----SRTV 213

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1482408268 206 LGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK06079  214 DGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK05884 PRK05884
SDR family oxidoreductase;
10-240 2.91e-06

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 46.73  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVL-----DLDPSGVHGPLTGIRADVSDDVGVRAAVAAAAERlggLDILVN----- 79
Cdd:PRK05884    4 LVTGGDTDLGRTIAEGFRNDGHKVTLVgarrdDLEVAAKELDVDAIVCDNTDPASLEEARGLFPHH---LDTIVNvpaps 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  80 -NAGIGAVGTVEDHTdEQWHHVLDVNVVGMVRVTRAALPHLRrsAHASVVNVCSIAATAGlpqrALYSATKGAVLSLTLA 158
Cdd:PRK05884   81 wDAGDPRTYSLADTA-NAWRNALDATVLSAVLTVQSVGDHLR--SGGSIISVVPENPPAG----SAEAAIKAALSNWTAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPGtvdtpwvsrlldgaddpeaeRAALNARQPLGRL--VTADEVAAAVLYLAGPSAGSVTGTALA 236
Cdd:PRK05884  154 QAAVFGTRGITINAVACG--------------------RSVQPGYDGLSRTppPVAAEIARLALFLTTPAARHITGQTLH 213


                  ....
gi 1482408268 237 VDGG 240
Cdd:PRK05884  214 VSHG 217
PRK08177 PRK08177
SDR family oxidoreductase;
9-180 4.22e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 46.56  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHG-----PLTGIRADVSDdvgvRAAVAAAAERLGG--LDILVNNA 81
Cdd:PRK08177    4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTAlqalpGVHIEKLDMND----PASLDQLLQRLQGqrFDLLFVNA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  82 GIG--AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSaHASVVNVCSIAATAGLP---QRALYSATKGAVLSLT 156
Cdd:PRK08177   80 GISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPG-QGVLAFMSSQLGSVELPdggEMPLYKASKAALNSMT 158

                         170       180
                  ....*....|....*....|....
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDT 180
Cdd:PRK08177  159 RSFVAELGEPTLTVLSMHPGWVKT 182
PRK07984 PRK07984
enoyl-ACP reductase FabI;
98-240 8.66e-06

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 45.66  E-value: 8.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  98 HHVLDVNVVGMVRVTRAALphlrrSAHASVVNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGT 177
Cdd:PRK07984  117 HDISSYSFVAMAKACRSML-----NPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGP 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1482408268 178 VDTPWVSrlldGADDPEAERAALNARQPLGRLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK07984  192 IRTLAAS----GIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGG 250
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
 8-115 1.06e-05

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. 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: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 45.67  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLD---------LDPsgVHGPLTGIRADVSDDVGVraavaaaAERLGGLDILV 78
Cdd:cd05256     1 RVLVTGGAGFIGSHLVERLLERGHEVIVLDnlstgkkenLPE--VKPNVKFIEGDIRDDELV-------EFAFEGVDYVF 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1482408268  79 NNAGIGAV-GTVEDHTdeqwhHVLDVNVVGMVRVTRAA 115
Cdd:cd05256    72 HQAAQASVpRSIEDPI-----KDHEVNVLGTLNLLEAA 104
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
1-250 1.08e-05

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 45.51  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   1 MTEFTGL----RAVVTGGAS--GIGRAVAERLAERGANVAVL--------DLDPSGVH-GPLTGIRADVSDDVGVRAAVA 65
Cdd:PRK08159    1 MAQASGLmagkRGLILGVANnrSIAWGIAKACRAAGAELAFTyqgdalkkRVEPLAAElGAFVAGHCDVTDEASIDAVFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  66 AAAERLGGLDILVNNAGIG----AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLrrSAHASVVNVCSIAATAGLPQ 141
Cdd:PRK08159   81 TLEKKWGKLDFVVHAIGFSdkdeLTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLM--TDGGSILTLTYYGAEKVMPH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 142 RALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGaddpeaeRAALNARQ---PLGRLVTADEVAAA 218
Cdd:PRK08159  159 YNVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGDF-------RYILKWNEynaPLRRTVTIEEVGDS 231

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1482408268 219 VLYLAGPSAGSVTGTALAVDGGMQGLRLRPVD 250
Cdd:PRK08159  232 ALYLLSDLSRGVTGEVHHVDSGYHVVGMKAVD 263
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-83 1.91e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 45.02  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGANV--AVLDLD----------PSGVHGPLTGIRADVSDDVGVRAAVAAAAERLG 72
Cdd:PRK06197   15 SGRVAVVTGANTGLGYETAAALAAKGAHVvlAVRNLDkgkaaaaritAATPGADVTLQELDLTSLASVRAAADALRAAYP 94

                          90
                  ....*....|.
gi 1482408268  73 GLDILVNNAGI 83
Cdd:PRK06197   95 RIDLLINNAGV 105
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
53-240 2.88e-05

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 44.23  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  53 DVSDDVGVRAAVAAAAERLGGLDILVNNAGIG----AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSVV 128
Cdd:PRK06603   66 DVTNPKSISNLFDDIKEKWGSFDFLLHGMAFAdkneLKGRYVDTSLENFHNSLHISCYSLLELSRSAEALMHDGG--SIV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 129 NVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSRLLDGADDPEAERAAlnarQPLGR 208
Cdd:PRK06603  144 TLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGDFSTMLKSHAAT----APLKR 219

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1482408268 209 LVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK06603  220 NTTQEDVGGAAVYLFSELSKGVTGEIHYVDCG 251
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
53-240 4.69e-05

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 43.66  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  53 DVSDDVGVRAAVAAAAERLGGLDILVNNAGIG-----AVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAhaSV 127
Cdd:PRK06997   64 DVASDEQIDALFASLGQHWDGLDGLVHSIGFApreaiAGDFLDGLSRENFRIAHDISAYSFPALAKAALPMLSDDA--SL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 128 VNVCSIAATAGLPQRALYSATKGAVLSLTLAMAADHVREGIRVNCVNPGTVDTPWVSrlldGADDPEAERAALNARQPLG 207
Cdd:PRK06997  142 LTLSYLGAERVVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLAAS----GIKDFGKILDFVESNAPLR 217

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1482408268 208 RLVTADEVAAAVLYLAGPSAGSVTGTALAVDGG 240
Cdd:PRK06997  218 RNVTIEEVGNVAAFLLSDLASGVTGEITHVDSG 250
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
 146-248 7.70e-05

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 42.88  E-value: 7.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 146 SATKGAVLSLTLAMAADHVRE-GIRVNCVNPGtvdtPWVSRLLD--GADDPEAERAALNArqPLGRLVTADEVAAAVLYL 222
Cdd:PRK06300  193 SSAKAALESDTKVLAWEAGRRwGIRVNTISAG----PLASRAGKaiGFIERMVDYYQDWA--PLPEPMEAEQVGAAAAFL 266

                          90       100
                  ....*....|....*....|....*.
gi 1482408268 223 AGPSAGSVTGTALAVDGGMQGLRLRP 248
Cdd:PRK06300  267 VSPLASAITGETLYVDHGANVMGIGP 292
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 146-241 8.09e-05

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 42.84  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 146 SATKGAVLSLTLAMAADHVRE-GIRVNCVNPGtvdtPWVSRLLD--GADDPEAERAALNArqPLGRLVTADEVAAAVLYL 222
Cdd:PLN02730  194 SSAKAALESDTRVLAFEAGRKyKIRVNTISAG----PLGSRAAKaiGFIDDMIEYSYANA--PLQKELTADEVGNAAAFL 267

                          90
                  ....*....|....*....
gi 1482408268 223 AGPSAGSVTGTALAVDGGM 241
Cdd:PLN02730  268 ASPLASAITGATIYVDNGL 286
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
159-240 8.75e-05

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 42.79  E-value: 8.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268 159 MAADHVREGIRVNCVNPG---TVDTPWVSRLLDGADDPEaERAalnarqPLGRLVTADEVAAAVLYLAGPSAGSVTGTAL 235
Cdd:PRK08594  175 LANDLGKDGIRVNAISAGpirTLSAKGVGGFNSILKEIE-ERA------PLRRTTTQEEVGDTAAFLFSDLSRGVTGENI 247


                  ....*
gi 1482408268 236 AVDGG 240
Cdd:PRK08594  248 HVDSG 252
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 11-178 1.91e-04

extended (e) SDRs; 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: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 41.13  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLdpsgvhgpltgiradvsddvgvraavaaaaerlggLDILVNNAGIGAVGTVE 90
Cdd:cd08946     3 VTGGAGFIGSHLVRRLLERGHEVVVIDR-----------------------------------LDVVVHLAALVGVPASW 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  91 DHTDEQWHhvldVNVVGMVRVTRAAlphlRRSAHASVVNVCSIAA-----------TAGLPQRALYSATKGAVLSLTLAM 159
Cdd:cd08946    48 DNPDEDFE----TNVVGTLNLLEAA----RKAGVKRFVYASSASVygspeglpeeeETPPRPLSPYGVSKLAAEHLLRSY 119

                         170
                  ....*....|....*....
gi 1482408268 160 AADHvreGIRVNCVNPGTV 178
Cdd:cd08946   120 GESY---GLPVVILRLANV 135
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 8-133 2.07e-04

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: 41.73  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLdldpsGVHGPLTGIRA----------------DVSDDVGVRAAVAAAAERL 71
Cdd:cd09810     3 TVVITGASSGLGLAAAKALARRGEWHVVM-----ACRDFLKAEQAaqevgmpkdsysvlhcDLASLDSVRQFVDNFRRTG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1482408268  72 GGLDILVNNAGIGAVGTVEDH-TDEQWHHVLDVNVVGMVRVTRAALPHLRRS--AHASVVNVCSI 133
Cdd:cd09810    78 RPLDALVCNAAVYLPTAKEPRfTADGFELTVGVNHLGHFLLTNLLLEDLQRSenASPRIVIVGSI 142
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 9-182 6.59e-04

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: 40.35  E-value: 6.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   9 AVVTGGASGIGRAVAERLAERGANVAVLDLDPSGVHG----PLTGIRADVSDDVGVRaavaaaaERLGGLDILVNNAGIG 84
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSGSDAVLldglPVEVVEGDLTDAASLA-------AAMKGCDRVFHLAAFT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  85 AVgtvedhTDEQWHHVLDVNVVGMVRVTRAALPH-LRRSAHASvvnvcSIAATAGLPQRA--------------LYSATK 149
Cdd:cd05228    74 SL------WAKDRKELYRTNVEGTRNVLDAALEAgVRRVVHTS-----SIAALGGPPDGRidettpwnerpfpnDYYRSK 142

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1482408268 150 gavlSLTLAMAADHVREGIRVNCVNPGTVDTPW 182
Cdd:cd05228   143 ----LLAELEVLEAAAEGLDVVIVNPSAVFGPG 171
PRK06720 PRK06720
hypothetical protein; Provisional
 3-39 8.41e-04

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 39.18  E-value: 8.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1482408268   3 EFTGLRAVVTGGASGIGRAVAERLAERGANVAVLDLD 39
Cdd:PRK06720   13 KLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDID 49
PRK07102 PRK07102
SDR family oxidoreductase;
11-181 1.37e-03

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 39.14  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  11 VTGGASGIGRAVAERLAERGANVAVLDLDPSGVhgpltgirADVSDDVGVRAAVAAAAERLGGLDI-----LVNNAG--- 82
Cdd:PRK07102    6 IIGATSDIARACARRYAAAGARLYLAARDVERL--------ERLADDLRARGAVAVSTHELDILDTashaaFLDSLPalp 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  83 ---IGAVGTVEDHTDEQWH-----HVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVLS 154
Cdd:PRK07102   78 divLIAVGTLGDQAACEADpalalREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTA 157

                         170       180
                  ....*....|....*....|....*..
gi 1482408268 155 LTLAMAADHVREGIRVNCVNPGTVDTP 181
Cdd:PRK07102  158 FLSGLRNRLFKSGVHVLTVKPGFVRTP 184
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 10-217 1.43e-03

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 39.29  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVL------------DLDPSGVHG-PLTGIRADVSDDVGVRaAVAAAAERLGGLDI 76
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGARHLVLlsrrgpapraaaRAALLRAGGaRVSVVRCDVTDPAALA-ALLAELAAGGPLAG 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEQWHHVLDVNVVGmvrvTRAALPHLRRSAHASVVNVCSIAATAGLPQRALYSATKGAVlslt 156
Cdd:cd05274   233 VIHAAGVLRDALLAELTPAAFAAVLAAKVAG----ALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFL---- 304

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482408268 157 LAMAADHVREGIRVNCVNPGTVDtpwvsrllDGADDPEAERAALNARQPLGRLVTADEVAA 217
Cdd:cd05274   305 DALAAQRRRRGLPATSVQWGAWA--------GGGMAAAAALRARLARSGLGPLAPAEALEA 357
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 5-118 1.54e-03

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. 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: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 39.14  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   5 TGLRAVVTGGASGIGRAVAERLAERGAN-VAVLDLDPSGVHGPLTGIRA-DVSDDVGVRAAVAAAAERL------GGLDI 76
Cdd:cd05237     1 KGKTILVTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSrFPHDKLRFIIGDVRDKERLrrafkeRGPDI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1482408268  77 LVNNAGIGAVGTVEDHTDEqwhhVLDVNVVGMVRVTRAALPH 118
Cdd:cd05237    81 VFHAAALKHVPSMEDNPEE----AIKTNVLGTKNVIDAAIEN 118
PLN02206 PLN02206
UDP-glucuronate decarboxylase
 6-37 2.30e-03

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 38.81  E-value: 2.30e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1482408268   6 GLRAVVTGGASGIGRAVAERLAERGANVAVLD 37
Cdd:PLN02206  119 GLRVVVTGGAGFVGSHLVDRLMARGDSVIVVD 150
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 10-183 2.90e-03

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 37.96  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  10 VVTGGASGIGRAVAERLAERGANVAVL--DLDP-----------SGVHGPLTGIrADVSDDVGVRAAVAAAAERLGGLDI 76
Cdd:cd09808     5 LITGANSGIGKAAALAIAKRGGTVHMVcrNQTRaeearkeieteSGNQNIFLHI-VDMSDPKQVWEFVEEFKEEGKKLHV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  77 LVNNAgiGAVGTVEDHTDEQWHHVLDVNVVGMVRVTRAALPHLRRSAHASVVNVCSiaatAGLPQRAL------------ 144
Cdd:cd09808    84 LINNA--GCMVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS----GGMLVQKLntnnlqsertaf 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1482408268 145 -----YSATKGAVLSLTLAMAADHvrEGIRVNCVNPGTVDTPWV 183
Cdd:cd09808   158 dgtmvYAQNKRQQVIMTEQWAKKH--PEIHFSVMHPGWADTPAV 199
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 8-194 6.20e-03

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 37.09  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268   8 RAVVTGGASGIGRAVAERLAERGANVAVLDLDPS-------GVHGPLTGIRADVSDDVGVRAAVAAAAErLGGLDILVNN 80
Cdd:cd08951     9 RIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKraadakaACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482408268  81 AGIGAVGTVEDhTDEQWHHVLDVNVVGMVRVTRAALP---------HLRRSAHASV-----VNVCSIAATAglpqralYS 146
Cdd:cd08951    88 AGILSGPNRKT-PDTGIPAMVAVNVLAPYVLTALIRRpkrliylssGMHRGGNASLddidwFNRGENDSPA-------YS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1482408268 147 ATKgaVLSLTLAMAADHVREGIRVNCVNPGtvdtpWVSRLLDGADDPE 194
Cdd:cd08951   160 DSK--LHVLTLAAAVARRWKDVSSNAVHPG-----WVPTKMGGAGAPD 200
 
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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