NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568325758|ref|WP_024094311|]
View 

3-oxoacyl-[acyl-carrier-protein] reductase [Paenibacillus larvae]

Protein Classification

3-oxoacyl-ACP reductase family protein( domain architecture ID 11481062)

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

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0016491
PubMed:  20423462|19011750
SCOP:  4000029

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-246 4.16e-142

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


:

Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 397.64  E-value: 4.16e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK05557  82 GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHV 240
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHV 241


                 ....*.
gi 568325758 241 DGGMYM 246
Cdd:PRK05557 242 NGGMVM 247
 
Name Accession Description Interval E-value
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-246 4.16e-142

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 397.64  E-value: 4.16e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK05557  82 GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHV 240
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHV 241


                 ....*.
gi 568325758 241 DGGMYM 246
Cdd:PRK05557 242 NGGMVM 247
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 5-245 9.35e-140

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: 391.53  E-value: 9.35e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEE-AAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:cd05333   80 ILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:cd05333  160 TKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGM 239


                 .
gi 568325758 245 Y 245
Cdd:cd05333  240 Y 240
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 7-245 5.69e-139

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: 389.65  E-value: 5.69e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    7 ALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDIL 86
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568325758  167 AAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGMY 245
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 2-246 2.63e-116

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: 332.52  E-value: 2.63e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVIT-DRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:COG1028   83 RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLP--EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:COG1028  163 VGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLgaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLA 242


                 ....*..
gi 568325758 240 VDGGMYM 246
Cdd:COG1028  243 VDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 14-244 4.60e-83

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: 247.73  E-value: 4.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   14 RGIGRAIALCLAEAGADVAVNYAGNEqaAAEVVQQIEAMGrKAAMMRADVSKAQEADQLVKDTLEQLGKLDILVNNAGIT 93
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEA--LAKRVEELAEEL-GAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   94 R--DNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQRsGRIINISSVVGVLGNPGQANYVAAKAGVIGLTKAAARE 171
Cdd:pfam13561  83 PklKGPFLDTSREDFDRALDVNLYSLFLLAKAA-LPLMKEG-GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758  172 LASRGITVNAVAPGFIETDMTDQLP--EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 5-188 1.07e-23

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: 93.70  E-value: 1.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758     5 KVALVTGASRGIGRAIALCLAEAGA-DVAVNY--AGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRPmmkQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWN-LHELTAD---LPLDFFVLFSSIAGVLGSPGQANYAAANAFL 156

                          170       180
                   ....*....|....*....|....*..
gi 568325758   162 IGLtkaaARELASRGITVNAVAPGFIE 188
Cdd:smart00822 157 DAL----AEYRRARGLPALSIAWGAWA 179
 
Name Accession Description Interval E-value
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-246 4.16e-142

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 397.64  E-value: 4.16e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK05557  82 GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHV 240
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHV 241


                 ....*.
gi 568325758 241 DGGMYM 246
Cdd:PRK05557 242 NGGMVM 247
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 5-245 9.35e-140

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: 391.53  E-value: 9.35e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEE-AAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:cd05333   80 ILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:cd05333  160 TKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGM 239


                 .
gi 568325758 245 Y 245
Cdd:cd05333  240 Y 240
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 7-245 5.69e-139

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: 389.65  E-value: 5.69e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    7 ALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDIL 86
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568325758  167 AAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGMY 245
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
2-246 6.13e-127

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 359.47  E-value: 6.13e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKV-VIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK05653  82 ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVD 241
Cdd:PRK05653 162 IGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVN 241


                 ....*
gi 568325758 242 GGMYM 246
Cdd:PRK05653 242 GGMYM 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 2-246 2.63e-116

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: 332.52  E-value: 2.63e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVIT-DRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:COG1028   83 RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLP--EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:COG1028  163 VGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLgaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLA 242


                 ....*..
gi 568325758 240 VDGGMYM 246
Cdd:COG1028  243 VDGGLTA 249
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-246 3.19e-113

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 324.90  E-value: 3.19e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK12825  84 RIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVD 241
Cdd:PRK12825 164 VGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEVT 243


                 ....*
gi 568325758 242 GGMYM 246
Cdd:PRK12825 244 GGVDV 248
PRK12826 PRK12826
SDR family oxidoreductase;
2-246 9.57e-100

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 290.66  E-value: 9.57e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIV-VDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVG-VLGNPGQANYVAAKAG 160
Cdd:PRK12826  83 RLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGpRVGYPGLAHYAASKAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAK-MLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:PRK12826 163 LVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEaIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLP 242


                 ....*..
gi 568325758 240 VDGGMYM 246
Cdd:PRK12826 243 VDGGATL 249
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-245 2.50e-95

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 279.42  E-value: 2.50e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK05565  83 KIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVD 241
Cdd:PRK05565 163 NAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVD 242


                 ....
gi 568325758 242 GGMY 245
Cdd:PRK05565 243 GGWT 246
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 5-246 1.09e-94

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: 277.78  E-value: 1.09e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNEERAEAWLQEQGALGFDFRVVEGDVSSFESCKAAVAKVEAELGPVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:TIGR01829  81 VLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIGF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  165 TKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:TIGR01829 161 TKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSINGGL 240


                  ..
gi 568325758  245 YM 246
Cdd:TIGR01829 241 YM 242
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 7-241 2.13e-91

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: 268.77  E-value: 2.13e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVvqQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDIL 86
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA--AIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:cd05233   79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568325758 167 AAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLED-IPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVD 241
Cdd:cd05233  159 SLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAaIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
5-246 8.55e-85

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 252.76  E-value: 8.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:PRK12824  83 ILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:PRK12824 163 TKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISINGGL 242


                 ..
gi 568325758 245 YM 246
Cdd:PRK12824 243 YM 244
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 14-244 4.60e-83

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: 247.73  E-value: 4.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   14 RGIGRAIALCLAEAGADVAVNYAGNEqaAAEVVQQIEAMGrKAAMMRADVSKAQEADQLVKDTLEQLGKLDILVNNAGIT 93
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEA--LAKRVEELAEEL-GAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   94 R--DNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQRsGRIINISSVVGVLGNPGQANYVAAKAGVIGLTKAAARE 171
Cdd:pfam13561  83 PklKGPFLDTSREDFDRALDVNLYSLFLLAKAA-LPLMKEG-GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758  172 LASRGITVNAVAPGFIETDMTDQLP--EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
FabG-like PRK07231
SDR family oxidoreductase;
1-244 1.55e-82

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 247.05  E-value: 1.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRkAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVT-DRNEEAAERVAAEILAGGR-AIAVAADVSDEADVEAAVAAALERF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDN-LIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK07231  80 GSVDILVNNAGTTHRNgPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPE----DVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK07231 160 AVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGeptpENRAKFLATIPLGRLGTPEDIANAALFLASDEASWITG 239


                 ....*....
gi 568325758 236 QTLHVDGGM 244
Cdd:PRK07231 240 VTLVVDGGR 248
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 2-244 4.61e-82

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: 245.76  E-value: 4.61e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQR-SGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd05358   81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIPWPGHVNYAASKGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQL---PEDvKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:cd05358  161 VKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAwddPEQ-RADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTT 239


                 ....*..
gi 568325758 238 LHVDGGM 244
Cdd:cd05358  240 LFVDGGM 246
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 2-243 7.30e-82

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: 244.88  E-value: 7.30e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMmkQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd05362   81 GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDM-TDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHV 240
Cdd:cd05362  159 EAFTRVLAKELGGRGITVNAVAPGPVDTDMfYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRA 238


                 ...
gi 568325758 241 DGG 243
Cdd:cd05362  239 NGG 241
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-246 2.66e-81

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 243.73  E-value: 2.66e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK12939   4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFN-DGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK12939  83 GGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED-VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:PRK12939 163 VIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADeRHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLP 242


                 ....*..
gi 568325758 240 VDGGMYM 246
Cdd:PRK12939 243 VNGGFVM 249
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 4-246 1.71e-80

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: 242.28  E-value: 1.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:cd05366   82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLgHGGKIINASSIAGVQGFPNLGAYSASKFAVR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDV-----------KAKMLEDIPLAKLGQPEDVAKTVLFLASADSS 231
Cdd:cd05366  162 GLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVgeiagkpegegFAEFSSSIPLGRLSEPEDVAGLVSFLASEDSD 241

                        250
                 ....*....|....*
gi 568325758 232 YMTGQTLHVDGGMYM 246
Cdd:cd05366  242 YITGQTILVDGGMVY 256
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 2-246 1.39e-79

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 239.52  E-value: 1.39e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK12935  84 KVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASaDSSYMTGQTLHVD 241
Cdd:PRK12935 164 LGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCR-DGAYITGQQLNIN 242


                 ....*
gi 568325758 242 GGMYM 246
Cdd:PRK12935 243 GGLYM 247
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 2-244 1.33e-78

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: 236.87  E-value: 1.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVIN-SRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd05347   82 KIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVK--AKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:cd05347  162 AGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEfnDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIF 241


                 ....*
gi 568325758 240 VDGGM 244
Cdd:cd05347  242 VDGGW 246
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 2-246 1.75e-77

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 234.04  E-value: 1.75e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQqieaMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAE----LGERVKIFPANLSDRDEVKALGQKAEADLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK12936  80 GVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVD 241
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVN 239


                 ....*
gi 568325758 242 GGMYM 246
Cdd:PRK12936 240 GGMAM 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 5-199 1.68e-76

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 229.81  E-value: 1.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    5 KVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLV-DRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:pfam00106  80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568325758  165 TKAAARELASRGITVNAVAPGFIETDMTDQLPEDV 199
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 7-243 6.41e-76

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: 229.93  E-value: 6.41e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDIL 86
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:cd05359   81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568325758 167 AAARELASRGITVNAVAPGFIETDMTDQLP--EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:cd05359  161 YLAVELGPRGIRVNAVSPGVIDTDALAHFPnrEDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDGG 239
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-243 3.23e-74

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 226.15  E-value: 3.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEqaAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTN--WDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06935  91 KIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVK--AKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:PRK06935 171 AGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNrnDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILA 250


                 ....
gi 568325758 240 VDGG 243
Cdd:PRK06935 251 VDGG 254
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-244 1.07e-73

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 224.24  E-value: 1.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK12937   2 TLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMmkQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK12937  82 GRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDM-TDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:PRK12937 160 VEGLVHVLANELRGRGITVNAVAPGPVATELfFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLR 239


                 ....*
gi 568325758 240 VDGGM 244
Cdd:PRK12937 240 VNGGF 244
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 2-246 1.69e-73

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 225.30  E-value: 1.69e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITR-DNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGrIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK06701 124 RLDILVNNAAFQYpQQSLEDITAEQLDKTFKTNIYSYFHMTKAAL-PHLKQGSA-IINTGSITGYEGNETLIDYSATKGA 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDM--TDQLPEDVkAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK06701 202 IHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLipSDFDEEKV-SQFGSNTPMQRPGQPEELAPAYVFLASPDSSYITGQML 280


                 ....*...
gi 568325758 239 HVDGGMYM 246
Cdd:PRK06701 281 HVNGGVIV 288
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 5-244 2.29e-73

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


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 223.87  E-value: 2.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADL-NEETAKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRS-GRIINISSVVGVLGNPGQANYVAAKAGVIG 163
Cdd:TIGR02415  80 VMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAGHEGNPILSAYSSTKFAVRG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  164 LTKAAARELASRGITVNAVAPGFIETDMTDQLPED-VKAKMLE----------DIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:TIGR02415 160 LTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEEtSEIAGKPigegfeefssEIALGRPSEPEDVAGLVSFLASEDSDY 239

                         250
                  ....*....|..
gi 568325758  233 MTGQTLHVDGGM 244
Cdd:TIGR02415 240 ITGQSILVDGGM 251
PRK12743 PRK12743
SDR family oxidoreductase;
5-244 2.78e-73

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 223.76  E-value: 2.78e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAGVIG 163
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHALGG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 164 LTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK12743 163 LTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVDGG 242


                 .
gi 568325758 244 M 244
Cdd:PRK12743 243 F 243
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 2-244 3.95e-73

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 223.06  E-value: 3.95e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNY----AGNEQAAAeVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTL 77
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADA-VAAGIEAAGGKALGLAFDVRDFAATRAALDAGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  78 EQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMK-QRSGRIINISSVVGVLGNPGQANYVA 156
Cdd:PRK12827  83 EEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAkmLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK12827 163 SKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHL--LNPVPVQRLGEPDEVAALVAFLVSDAASYVTGQ 240


                 ....*...
gi 568325758 237 TLHVDGGM 244
Cdd:PRK12827 241 VIPVDGGF 248
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 1-246 9.37e-72

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 219.76  E-value: 9.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIA-DLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK12429  80 GGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTD-QLPEDVKAK-----------MLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:PRK12429 160 LIGLTKVVALEGATHGVTVNAICPGYVDTPLVRkQIPDLAKERgiseeevledvLLPLVPQKRFTTVEEIADYALFLASF 239

                        250
                 ....*....|....*...
gi 568325758 229 DSSYMTGQTLHVDGGMYM 246
Cdd:PRK12429 240 AAKGVTGQAWVVDGGWTA 257
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 2-244 1.96e-71

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 219.05  E-value: 1.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLS-ARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKA-ATRPMMKQRSGRIINISSVVGVLGNP----GQANYVA 156
Cdd:PRK08213  89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAvAKRSMIPRGYGRIINVASVAGLGGNPpevmDTIAYNT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK08213 169 SKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASKHITGQ 248


                 ....*...
gi 568325758 237 TLHVDGGM 244
Cdd:PRK08213 249 ILAVDGGV 256
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 3-228 2.94e-70

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: 215.43  E-value: 2.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIeamGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVL-AARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:COG4221   80 LDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:COG4221  160 GLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQ 225
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
3-244 5.84e-70

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 215.36  E-value: 5.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAV-NYagNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIvDY--NEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK08643  79 DLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLgHGGKIINATSQAGVVGNPELAVYSSTKFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDV---KAKMLE--------DIPLAKLGQPEDVAKTVLFLASAD 229
Cdd:PRK08643 159 VRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVgenAGKPDEwgmeqfakDITLGRLSEPEDVANCVSFLAGPD 238

                        250
                 ....*....|....*
gi 568325758 230 SSYMTGQTLHVDGGM 244
Cdd:PRK08643 239 SDYITGQTIIVDGGM 253
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-243 1.09e-69

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: 214.62  E-value: 1.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAM-GRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:cd08940   82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAK------------MLEDIPLAKLGQPEDVAKTVLFLASADS 230
Cdd:cd08940  162 GLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALAQKngvpqeqaarelLLEKQPSKQFVTPEQLGDTAVFLASDAA 241

                        250
                 ....*....|...
gi 568325758 231 SYMTGQTLHVDGG 243
Cdd:cd08940  242 SQITGTAVSVDGG 254
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-243 8.13e-69

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: 212.19  E-value: 8.13e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGN--PGQANYVAAKA 159
Cdd:cd05352   86 KIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNrpQPQAAYNASKA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:cd05352  166 AVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDLI 245


                 ....
gi 568325758 240 VDGG 243
Cdd:cd05352  246 IDGG 249
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 2-243 1.40e-67

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 209.53  E-value: 1.40e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMgrKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDV-SEAALAATAARLPGA--KVTATVADVADPAQVERVFDTAVERFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGIT-RDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGR-IINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK12829  86 GLDVLVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTPYAASKW 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLP-----------EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:PRK12829 166 AVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIearaqqlgiglDEMEQEYLEKISLGRMVEPEDIAATALFLASP 245

                        250
                 ....*....|....*
gi 568325758 229 DSSYMTGQTLHVDGG 243
Cdd:PRK12829 246 AARYITGQAISVDGN 260
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 2-243 2.00e-67

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: 209.07  E-value: 2.00e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQ-IEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEETKKlIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAG--ITRDNlIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSgRIINISSVVGVLGNPGQANYVAAK 158
Cdd:cd05355  104 GKLDILVNNAAyqHPQES-IEDITTEQLEKTFRTNIFSMFYLTKAAL-PHLKKGS-SIINTTSVTAYKGSPHLLDYAATK 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDM-TDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:cd05355  181 GAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLiPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQV 260


                 ....*.
gi 568325758 238 LHVDGG 243
Cdd:cd05355  261 LHVNGG 266
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-246 5.00e-67

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 207.51  E-value: 5.00e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLAL-IDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKE---------EEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVlGNPGQ 151
Cdd:PRK08217  82 QLNGLINNAGILRDGLLVKAKDgkvtskmslEQFQSVIDVNLTGVFLCGREAAAKMIESgSKGVIINISSIARA-GNMGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 152 ANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADss 231
Cdd:PRK08217 161 TNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTVRFIIEND-- 238

                        250
                 ....*....|....*
gi 568325758 232 YMTGQTLHVDGGMYM 246
Cdd:PRK08217 239 YVTGRVLEIDGGLRL 253
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
2-223 6.64e-67

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 207.41  E-value: 6.64e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAG-NEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVL--VArDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:COG0300   81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEdiplaklgqPEDVAKTVL 223
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLS---------PEEVARAIL 214
PRK06172 PRK06172
SDR family oxidoreductase;
1-243 3.38e-66

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 205.76  E-value: 3.38e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK06172   4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVA-DRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDN-LIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK06172  83 GRLDYAFNNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPE---DVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK06172 163 AVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEadpRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGASFTTGH 242


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:PRK06172 243 ALMVDGG 249
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 4-243 5.77e-66

(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: 204.86  E-value: 5.77e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVN--------YAGNEQAAAEVVQQIEAMGRKAAmmrADVSKAQEADQLVKD 75
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVNdlggdrkgSGKSSSAADKVVDEIKAAGGKAV---ANYDSVEDGEKIVKT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  76 TLEQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYV 155
Cdd:cd05353   82 AIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGfIETDMT-DQLPEDVKAKMlediplaklgQPEDVAKTVLFLASADSSyMT 234
Cdd:cd05353  162 AAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRMTeTVMPEDLFDAL----------KPEYVAPLVLYLCHESCE-VT 229


                 ....*....
gi 568325758 235 GQTLHVDGG 243
Cdd:cd05353  230 GGLFEVGAG 238
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 4-245 1.22e-64

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: 201.73  E-value: 1.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAIC-ARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIG 163
Cdd:cd05344   80 DILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 164 LTKAAARELASRGITVNAVAPGFIETDMTDQL-----------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:cd05344  160 LVKTLSRELAPDGVTVNSVLPGYIDTERVRRLlearaekegisVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKASY 239

                        250
                 ....*....|...
gi 568325758 233 MTGQTLHVDGGMY 245
Cdd:cd05344  240 ITGQAILVDGGLT 252
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 2-243 1.39e-63

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: 198.76  E-value: 1.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVA---VNYAGNEQAAAEVvqqieamGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVlsdILDEEGQAAAAEL-------GDAARFFHLDVTDEDGWTAVVDTARE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:cd05341   76 AFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASR--GITVNAVAPGFIETDMTDQLPEDVKAKMLEDI-PLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:cd05341  156 GAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEMGNYPNtPMGRAGEPDEIAYAVVYLASDESSFVTG 235


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:cd05341  236 SELVVDGG 243
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-242 2.15e-63

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 204.30  E-value: 2.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADV-AVNYAGNEQAAAEVVQQIeamgrKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVvCLDVPAAGEALAAVANRV-----GGTALALDITAPDAPARIAEHLAERH 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK08261 283 GGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAG 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLP---EDVKAKMLEdipLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK08261 363 VIGLVQALAPLLAERGITINAVAPGFIETQMTAAIPfatREAGRRMNS---LQQGGLPVDVAETIAWLASPASGGVTGNV 439


                 ....*
gi 568325758 238 LHVDG 242
Cdd:PRK08261 440 VRVCG 444
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-243 3.71e-63

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 197.63  E-value: 3.71e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDM------TDQLPEDVKAKMlediPLAKLGQPEDVAKTVLFLASADSSYMT 234
Cdd:PRK08063 161 LEALTRYLAVELAPKGIAVNAVSGGAVDTDAlkhfpnREELLEDARAKT----PAGRMVEPEDVANAVLFLCSPEADMIR 236


                 ....*....
gi 568325758 235 GQTLHVDGG 243
Cdd:PRK08063 237 GQTIIVDGG 245
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 5-246 5.13e-63

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: 197.30  E-value: 5.13e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIeamGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEA---GERAIAIQADVRDRDQVQAMIEEAKNHFGPVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAgiTRDNLIMRMKEEEFDTV--------IATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVA 156
Cdd:cd05349   78 TIVNNA--LIDFPFDPDQRKTFDTIdwedyqqqLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFI-ETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:cd05349  156 AKAALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTG 235

                        250
                 ....*....|.
gi 568325758 236 QTLHVDGGMYM 246
Cdd:cd05349  236 QNLVVDGGLVM 246
PRK06114 PRK06114
SDR family oxidoreductase;
2-243 5.93e-62

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 194.62  E-value: 5.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPG--QANYVAAKA 159
Cdd:PRK06114  86 ALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllQAHYNASKA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQlPEDVKAKML--EDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK06114 166 GVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR-PEMVHQTKLfeEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVD 244


                 ....*.
gi 568325758 238 LHVDGG 243
Cdd:PRK06114 245 LLVDGG 250
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 6-246 1.97e-61

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: 193.45  E-value: 1.97e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGIT----RDnlIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQR------SGRIINISSVVGVLGNPGQANYV 155
Cdd:cd05337   83 LVNNAGIAvrprGD--LLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPdrfdgpHRSIIFVTSINAYLVSPNRGEYC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLED-IPLAKLGQPEDVAKTVLFLASADSSYMT 234
Cdd:cd05337  161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAGlVPIRRWGQPEDIAKAVRTLASGLLPYST 240

                        250
                 ....*....|..
gi 568325758 235 GQTLHVDGGMYM 246
Cdd:cd05337  241 GQPINIDGGLSM 252
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 2-246 4.39e-61

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: 192.42  E-value: 4.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAG-NEQAAAEVVQQIE-AMGRKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAI--AGrKPEVLEAAAEEISsATGGRAHPIQCDVRDPEAVEAAVDETLKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGitrDNLIM---RMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRS-GRIINISSVVGVLGNPGQANYV 155
Cdd:cd05369   79 FGKIDILINNAA---GNFLApaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETD--MTDQLPEDV-KAKMLEDIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:cd05369  156 AAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTegMERLAPSGKsEKKMIERVPLGRLGTPEEIANLALFLLSDAASY 235

                        250
                 ....*....|....
gi 568325758 233 MTGQTLHVDGGMYM 246
Cdd:cd05369  236 INGTTLVVDGGQWL 249
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-244 1.20e-60

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 193.07  E-value: 1.20e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKdTLEQLG 81
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAGDISQRATADELVA-TAVGLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAAT---RPMMKQRS----GRIINISSVVGVLGNPGQANY 154
Cdd:PRK07792  89 GLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGgpvyGRIVNTSSEAGLVGPVGQANY 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGfIETDMTDQLPEDVKAKMLEDI-PLAklgqPEDVAKTVLFLASADSSYM 233
Cdd:PRK07792 169 GAAKAGITALTLSAARALGRYGVRANAICPR-ARTAMTADVFGDAPDVEAGGIdPLS----PEHVVPLVQFLASPAAAEV 243

                        250
                 ....*....|.
gi 568325758 234 TGQTLHVDGGM 244
Cdd:PRK07792 244 NGQVFIVYGPM 254
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 2-246 4.78e-60

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 190.11  E-value: 4.78e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAeVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANA-VADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMK-QRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK13394  84 SVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTAKHG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTD-QLP----------EDVKAK-MLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:PRK13394 164 LLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDkQIPeqakelgiseEEVVKKvMLGKTVDGVFTTVEDVAQTVLFLSSF 243

                        250
                 ....*....|....*...
gi 568325758 229 DSSYMTGQTLHVDGGMYM 246
Cdd:PRK13394 244 PSAALTGQSFVVSHGWFM 261
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 2-243 5.72e-60

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: 189.54  E-value: 5.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMG---RKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALT-GRDAERLEETRQSCLQAGvseKKILLVVADLTEEEGQDRIISTTLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:cd05364   80 KFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAV-PHLIKTKGEIVNVSSVAGGRSFPGVLYYCISK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQ--LPEDVKAKML----EDIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:cd05364  159 AALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRmgMPEEQYIKFLsrakETHPLGRPGTVDEVAEAIAFLASDASSF 238

                        250
                 ....*....|.
gi 568325758 233 MTGQTLHVDGG 243
Cdd:cd05364  239 ITGQLLPVDGG 249
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-243 8.69e-60

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 189.35  E-value: 8.69e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGAD-VAVNYAGneqaAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADiVGVGVAE----APETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRS-GRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK12481  82 GHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVPSYTASKS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL--PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK12481 162 AVMGLTRALATELSQYNINVNAIAPGYMATDNTAALraDTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTGYT 241


                 ....*.
gi 568325758 238 LHVDGG 243
Cdd:PRK12481 242 LAVDGG 247
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 1-244 1.75e-59

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 189.50  E-value: 1.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVN--------YAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQL 72
Cdd:PRK07791   3 LLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNdigvgldgSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  73 VKDTLEQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATR------PMMKQRSGRIINISSVVGVL 146
Cdd:PRK07791  83 VDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAywraesKAGRAVDARIINTSSGAGLQ 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 147 GNPGQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGfIETDMTDQLPEDVKAKMLEDipLAKLGQPEDVAKTVLFLA 226
Cdd:PRK07791 163 GSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-ARTRMTETVFAEMMAKPEEG--EFDAMAPENVSPLVVWLG 239

                        250
                 ....*....|....*...
gi 568325758 227 SADSSYMTGQTLHVDGGM 244
Cdd:PRK07791 240 SAESRDVTGKVFEVEGGK 257
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 2-244 3.96e-59

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 187.63  E-value: 3.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK08936  85 TLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAASKGG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK08936 165 VKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADpkQRADVESMIPMGYIGKPEEIAAVAAWLASSEASYVTGITL 244


                 ....*.
gi 568325758 239 HVDGGM 244
Cdd:PRK08936 245 FADGGM 250
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
2-246 4.53e-59

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 187.14  E-value: 4.53e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK12938  81 EIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVD 241
Cdd:PRK12938 161 HGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFSLN 240


                 ....*
gi 568325758 242 GGMYM 246
Cdd:PRK12938 241 GGLHM 245
PRK06124 PRK06124
SDR family oxidoreductase;
1-244 7.05e-59

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 186.84  E-value: 7.05e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK06124   8 SLAGQVALVTGSARGLGFEIARALAGAGAHVLVN-GRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK06124  87 GRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK06124 167 LTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADpaVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVL 246


                 ....*.
gi 568325758 239 HVDGGM 244
Cdd:PRK06124 247 AVDGGY 252
PRK06138 PRK06138
SDR family oxidoreductase;
2-243 7.74e-59

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 186.90  E-value: 7.74e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVV--ADRDAEAAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQL------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIfarhadPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:PRK06138 241 TTLVVDGG 248
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
2-246 1.01e-58

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 186.77  E-value: 1.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVvqqieamGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIadiKPARARLAALEI-------GPAAIAVSLDVTRQDSIDRIVAAAVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:PRK07067  77 RFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCAT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL-----------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLA 226
Cdd:PRK07067 157 KAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVdalfaryenrpPGEKKRLVGEAVPLGRMGVPDDLTGMALFLA 236

                        250       260
                 ....*....|....*....|
gi 568325758 227 SADSSYMTGQTLHVDGGMYM 246
Cdd:PRK07067 237 SADADYIVAQTYNVDGGNWM 256
PRK07063 PRK07063
SDR family oxidoreductase;
2-243 1.02e-58

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 186.80  E-value: 1.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVVQQIEamGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALadlDAALAERAAAAIARDVA--GARVLAVPADVTDAASVAAAVAAAEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGIT--RDNLimRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVA 156
Cdd:PRK07063  83 AFGPLDVLVNNAGINvfADPL--AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADS 230
Cdd:PRK07063 161 AKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWwnaqpdPAAARAETLALQPMKRIGRPEEVAMTAVFLASDEA 240

                        250
                 ....*....|...
gi 568325758 231 SYMTGQTLHVDGG 243
Cdd:PRK07063 241 PFINATCITIDGG 253
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-246 7.62e-58

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 184.39  E-value: 7.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGI---TRDNLiMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGR------IINISSVVGVLGNPGQANYV 155
Cdd:PRK12745  83 CLVNNAGVgvkVRGDL-LDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVSPNRGEYC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTdqlpEDVKAKMLEDI-----PLAKLGQPEDVAKTVLFLASADS 230
Cdd:PRK12745 162 ISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMT----APVTAKYDALIakglvPMPRWGEPEDVARAVAALASGDL 237

                        250
                 ....*....|....*.
gi 568325758 231 SYMTGQTLHVDGGMYM 246
Cdd:PRK12745 238 PYSTGQAIHVDGGLSI 253
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 2-244 8.03e-58

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: 184.19  E-value: 8.03e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVkDTLEQL- 80
Cdd:cd05329    4 LEGKTALVTGGTKGIGYAIVEELAGLGAEV-YTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELM-DTVASHf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 -GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:cd05329   82 gGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLA-HPLLKAsGNGNIVFISSVAGVIAVPSGAPYGATK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTD---QLPEDVKaKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:cd05329  161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEpviQQKENLD-KVIERTPLKRFGEPEEVAALVAFLCMPAASYITG 239


                 ....*....
gi 568325758 236 QTLHVDGGM 244
Cdd:cd05329  240 QIIAVDGGL 248
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-243 1.55e-57

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 183.54  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGAD-VAVNYAgneqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDiVGINIV----EPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK08993  84 GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIRVPSYTASKS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL--PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK08993 164 GVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLraDEQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYT 243


                 ....*.
gi 568325758 238 LHVDGG 243
Cdd:PRK08993 244 IAVDGG 249
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
2-243 3.50e-57

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 182.69  E-value: 3.50e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEqaAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPE--IEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVG-VLGNPGQANYVAAKAG 160
Cdd:PRK08226  82 RIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQL--------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:PRK08226 162 IVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIarqsnpedPESVLTEMAKAIPLRRLADPLEVGELAAFLASDESSY 241

                        250
                 ....*....|.
gi 568325758 233 MTGQTLHVDGG 243
Cdd:PRK08226 242 LTGTQNVIDGG 252
PRK08589 PRK08589
SDR family oxidoreductase;
2-243 3.88e-57

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 183.06  E-value: 3.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLA--VDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGItrDNLIMRMKE---EEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:PRK08589  82 RVDVLFNNAGV--DNAAGRIHEypvDVFDKIMAVDMRGTFLMTKMLL-PLMMEQGGSIINTSSFSGQAADLYRSGYNAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL---PEDVKAKMLED-----IPLAKLGQPEDVAKTVLFLASADS 230
Cdd:PRK08589 159 GAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLtgtSEDEAGKTFREnqkwmTPLGRLGKPEEVAKLVVFLASDDS 238

                        250
                 ....*....|...
gi 568325758 231 SYMTGQTLHVDGG 243
Cdd:PRK08589 239 SFITGETIRIDGG 251
PRK09730 PRK09730
SDR family oxidoreductase;
5-243 4.75e-57

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 181.97  E-value: 4.75e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGIT-RDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGR---IINISSVVGVLGNPGQ-ANYVAAKA 159
Cdd:PRK09730  82 ALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGAPGEyVDYAASKG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKA-KMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK09730 162 AIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRVdRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSFI 241


                 ....*
gi 568325758 239 HVDGG 243
Cdd:PRK09730 242 DLAGG 246
PRK07035 PRK07035
SDR family oxidoreductase;
2-244 9.17e-57

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 181.37  E-value: 9.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAeVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQA-VADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGItrdNL----IMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:PRK07035  85 RLDILVNNAAA---NPyfghILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL--PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK07035 162 KAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALfkNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTG 241


                 ....*....
gi 568325758 236 QTLHVDGGM 244
Cdd:PRK07035 242 ECLNVDGGY 250
PRK06128 PRK06128
SDR family oxidoreductase;
2-243 1.26e-56

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 182.75  E-value: 1.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQA-AAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQdAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKEL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAG--ITRDNlIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQrSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:PRK06128 133 GGLDILVNIAGkqTAVKD-IADITTEQFDATFKTNVYAMFWLCKAAI-PHLPP-GASIINTGSIQSYQPSPTLLDYASTK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMT---DQLPEDVKaKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK06128 210 AAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQpsgGQPPEKIP-DFGSETPMKRPGQPVEMAPLYVLLASQESSYVTG 288


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:PRK06128 289 EVFGVTGG 296
PRK05867 PRK05867
SDR family oxidoreductase;
2-243 1.75e-56

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 181.00  E-value: 1.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIA-ARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGN-PGQ-ANYVAAK 158
Cdd:PRK05867  86 GIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINvPQQvSHYCASK 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLpEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK05867 166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPY-TEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMTGSDI 244


                 ....*
gi 568325758 239 HVDGG 243
Cdd:PRK05867 245 VIDGG 249
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 2-243 4.24e-56

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 179.85  E-value: 4.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAamMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVAL--LDRSEDVAEVAAQLLGGNAKG--LVCDVSDSQSVEAAVAAVISAFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06841  89 RIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDM-----TDQLPEDVKAKmledIPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK06841 169 VGMTKVLALEWGPYGITVNAISPTVVLTELgkkawAGEKGERAKKL----IPAGRFAYPEEIAAAALFLASDAAAMITGE 244


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:PRK06841 245 NLVIDGG 251
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 3-244 1.49e-55

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: 178.05  E-value: 1.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAVNyagneQAAAEVVQQIEAMGRKAAMmRADVSKAQEADQLVKDtleqLGK 82
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIAT-----DINEEKLKELERGPGITTR-VLDVTDKEQVAALAKE----EGR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVG-VLGNPGQANYVAAKAGV 161
Cdd:cd05368   71 IDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTKAAV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQL------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:cd05368  151 IGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERiqaqpdPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTG 230


                 ....*....
gi 568325758 236 QTLHVDGGM 244
Cdd:cd05368  231 TAVVIDGGW 239
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-243 1.71e-55

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 178.44  E-value: 1.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQqieamgRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK06463   4 RFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELRE------KGVFTIKCDVGNRDQVKKSKEVVEKEF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGV-LGNPGQANYVAAKA 159
Cdd:PRK06463  78 GRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAITKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDI-----PLAKLGQPEDVAKTVLFLASADSSYMT 234
Cdd:PRK06463 158 GIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKLRELfrnktVLKTTGKPEDIANIVLFLASDDARYIT 237


                 ....*....
gi 568325758 235 GQTLHVDGG 243
Cdd:PRK06463 238 GQVIVADGG 246
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 3-243 2.12e-55

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: 177.91  E-value: 2.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVVQQieaMGRKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILadiNAPALEQLKEELTNL---YKNRVIALELDITSKESIKELIESYLEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGITRDNLIMR---MKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGnPGQ----- 151
Cdd:cd08930   78 FGRIDILINNAYPSPKVWGSRfeeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIA-PDFriyen 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 152 ------ANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIetdmTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFL 225
Cdd:cd08930  157 tqmyspVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGI----LNNQPSEFLEKYTKKCPLKRMLNPEDLRGAIIFL 232

                        250
                 ....*....|....*...
gi 568325758 226 ASADSSYMTGQTLHVDGG 243
Cdd:cd08930  233 LSDASSYVTGQNLVIDGG 250
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 2-243 5.49e-55

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: 176.81  E-value: 5.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVvqqieamGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:cd05345    3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIadiNADGAERVAADI-------GEAAIAIQADVTKRADVEAMVEAALS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIM-RMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:cd05345   76 KFGRLDILVNNAGITHRNKPMlEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNAS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAP-----GFIETDMTDQLPEdVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:cd05345  156 KGWVVTATKAMAVELAPRNIRVNCLCPvagetPLLSMFMGEDTPE-NRAKFRATIPLGRLSTPDDIANAALYLASDEASF 234

                        250
                 ....*....|.
gi 568325758 233 MTGQTLHVDGG 243
Cdd:cd05345  235 ITGVALEVDGG 245
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 2-244 5.85e-55

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 177.18  E-value: 5.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDI-NQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK07097  87 VIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAK--------MLEDIPLAKLGQPEDVAKTVLFLASADSSYM 233
Cdd:PRK07097 167 KMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGsrhpfdqfIIAKTPAARWGDPEDLAGPAVFLASDASNFV 246

                        250
                 ....*....|.
gi 568325758 234 TGQTLHVDGGM 244
Cdd:PRK07097 247 NGHILYVDGGI 257
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-243 6.59e-55

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 176.66  E-value: 6.59e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVG-ARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRD-NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGV-LGNPGQANYVAAK 158
Cdd:PRK07478  82 GGLDIAFNNAGTLGEmGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHtAGFPGMAAYAASK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAK-MLEDI-PLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK07478 162 AGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALaFVAGLhALKRMAQPEEIAQAALFLASDAASFVTGT 241


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:PRK07478 242 ALLVDGG 248
PRK07814 PRK07814
SDR family oxidoreductase;
2-244 1.82e-54

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 175.74  E-value: 1.82e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIA-ARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQR-SGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK07814  87 RLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTAKAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRgITVNAVAPGFIETDMTDQLP--EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK07814 167 LAHYTRLAALDLCPR-IRVNAIAPGSILTSALEVVAanDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTL 245


                 ....*.
gi 568325758 239 HVDGGM 244
Cdd:PRK07814 246 EVDGGL 251
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-246 1.19e-53

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 173.35  E-value: 1.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIeamGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEHF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GK-LDILVNNA-------GITRDNLiMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSvvGVLGNPGQA 152
Cdd:PRK08642  79 GKpITTVVNNAladfsfdGDARKKA-DDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGT--NLFQNPVVP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 153 --NYVAAKAGVIGLTKAAARELASRGITVNAVAPGFI-ETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASAD 229
Cdd:PRK08642 156 yhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPW 235

                        250
                 ....*....|....*..
gi 568325758 230 SSYMTGQTLHVDGGMYM 246
Cdd:PRK08642 236 ARAVTGQNLVVDGGLVM 252
PRK07774 PRK07774
SDR family oxidoreductase;
1-243 1.27e-53

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 173.39  E-value: 1.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07774   3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADI-NAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRD---NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVL-GNPgqanYVA 156
Cdd:PRK07774  82 GGIDYLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLySNF----YGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL-PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK07774 158 AKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVtPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITG 237


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:PRK07774 238 QIFNVDGG 245
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 2-243 1.66e-53

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: 173.06  E-value: 1.66e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIeamGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADI-DGGAAQAVVAQI---AGGALALRVDVTDEQQVAALFERAVEEFG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITR-DNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd08944   77 GLDLLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMT-------DQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYM 233
Cdd:cd08944  157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLLlaklagfEGALGPGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFI 236

                        250
                 ....*....|
gi 568325758 234 TGQTLHVDGG 243
Cdd:cd08944  237 TGQVLCVDGG 246
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 2-243 1.65e-52

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 169.98  E-value: 1.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK12828   5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLP---GVPADALRIGGIDLVDPQAARRAVDEVNRQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK12828  82 RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMtdqlpedvkakMLEDIPLAKLG---QPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVLPSIIDTPP-----------NRADMPDADFSrwvTPEQIAAVIAFLLSDEAQAITGASI 230


                 ....*
gi 568325758 239 HVDGG 243
Cdd:PRK12828 231 PVDGG 235
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-243 2.73e-52

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 176.96  E-value: 2.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAvnyaGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVV----VADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNL--IMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGR-IINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK06484  81 DVLVNNAGVTDPTMtaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVK---AKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK06484 161 VISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKldpSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGST 240


                 ....*.
gi 568325758 238 LHVDGG 243
Cdd:PRK06484 241 LVVDGG 246
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 2-244 3.15e-52

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 169.93  E-value: 3.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIIN-DITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK08085  86 PIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:PRK08085 166 KMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDeaFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLF 245


                 ....*
gi 568325758 240 VDGGM 244
Cdd:PRK08085 246 VDGGM 250
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-243 3.88e-52

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 169.58  E-value: 3.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASR--GIGRAIALCLAEAGADVAVNY---------AGNEQ-AAAEVVQQIEAMGRKAAMMRADVSKAQEA 69
Cdd:PRK12859   4 LKNKVAVVTGVSRldGIGAAICKELAEAGADIFFTYwtaydkempWGVDQdEQIQLQEELLKNGVKVSSMELDLTQNDAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  70 DQLVKDTLEQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNP 149
Cdd:PRK12859  84 KELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 150 GQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETD-MTDQLPEDVKAKMlediPLAKLGQPEDVAKTVLFLASA 228
Cdd:PRK12859 164 GELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTEEIKQGLLPMF----PFGRIGEPKDAARLIKFLASE 239

                        250
                 ....*....|....*
gi 568325758 229 DSSYMTGQTLHVDGG 243
Cdd:PRK12859 240 EAEWITGQIIHSEGG 254
PRK09135 PRK09135
pteridine reductase; Provisional
 1-243 4.67e-52

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 169.34  E-value: 4.67e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAM-GRKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:PRK09135   3 TDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAELNALrPGSAAALQADLLDPDALPELVAACVAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK09135  83 FGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAA-PQLRKQRGAIVNITDIHAERPLKGYPVYCAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRgITVNAVAPGFIE-TDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLAsADSSYMTGQTL 238
Cdd:PRK09135 162 ALEMLTRSLALELAPE-VRVNAVAPGAILwPEDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLL-ADASFITGQIL 239


                 ....*
gi 568325758 239 HVDGG 243
Cdd:PRK09135 240 AVDGG 244
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 5-243 4.98e-52

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: 168.61  E-value: 4.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:cd05357   81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELASRgITVNAVAPGFI--ETDMTDQLPEDVKAKmledIPLAKLGQPEDVAKTVLFLasADSSYMTGQTLHVDG 242
Cdd:cd05357  161 TRSAALELAPN-IRVNGIAPGLIllPEDMDAEYRENALRK----VPLKRRPSAEEIADAVIFL--LDSNYITGQIIKVDG 233


                 .
gi 568325758 243 G 243
Cdd:cd05357  234 G 234
PRK07856 PRK07856
SDR family oxidoreductase;
2-243 1.53e-51

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 168.19  E-value: 1.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEvvqqieamGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVV-CGRRAPETVD--------GRPAEFHAADVRDPDQVAALVDAIVERHG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRS-GRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK07856  75 RLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRRPSPGTAAYGAAKAG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRgITVNAVAPGFIETDMTDQL---PEDVkAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK07856 155 LLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSELHygdAEGI-AAVAATVPLGRLATPADIAWACLFLASDLASYVSGAN 232


                 ....*.
gi 568325758 238 LHVDGG 243
Cdd:PRK07856 233 LEVHGG 238
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 3-246 1.56e-51

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 168.29  E-value: 1.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEA-MGRKAAM-MRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADI-NSEKAANVAQEINAeYGEGMAYgFGADATSEQSVLALSRGVDEIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQR-SGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK12384  80 GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPG-FIETDMTDQL-----------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLAS 227
Cdd:PRK12384 160 GGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQSLlpqyakklgikPDEVEQYYIDKVPLKRGCDYQDVLNMLLFYAS 239

                        250
                 ....*....|....*....
gi 568325758 228 ADSSYMTGQTLHVDGGMYM 246
Cdd:PRK12384 240 PKASYCTGQSINVTGGQVM 258
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-243 1.72e-51

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 167.75  E-value: 1.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADV-AVNYAGNEQAaaevvqqieamGRKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:PRK08220   5 DFSGKTVWVTGAAQGIGYAVALAFVEAGAKViGFDQAFLTQE-----------DYPFATFVLDVSDAAAVAQVCQRLLAE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK08220  74 TGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL------PEDVKAKMLED----IPLAKLGQPEDVAKTVLFLASAD 229
Cdd:PRK08220 154 ALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLwvdedgEQQVIAGFPEQfklgIPLGKIARPQEIANAVLFLASDL 233

                        250
                 ....*....|....
gi 568325758 230 SSYMTGQTLHVDGG 243
Cdd:PRK08220 234 ASHITLQDIVVDGG 247
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 2-244 2.86e-51

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: 167.25  E-value: 2.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAmgRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADI-DDDAGQAVAAELGD--PDISFVHCDVTVEADVRAAVDTAVARFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGI--TRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:cd05326   79 RLDIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQ--LPEDVKAKMLED---IPLAKLGQPEDVAKTVLFLASADSSYMT 234
Cdd:cd05326  159 AVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAgfGVEDEAIEEAVRgaaNLKGTALRPEDIAAAVLYLASDDSRYVS 238

                        250
                 ....*....|
gi 568325758 235 GQTLHVDGGM 244
Cdd:cd05326  239 GQNLVVDGGL 248
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 2-243 3.55e-51

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: 167.31  E-value: 3.55e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGAD---VAVNYAGNEQAAAEVVQQIEAMgrKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKlslVDLNEEGLEAAKAALLEIAPDA--EVLLIKADVSDEAQVEAYVDATVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGIT-RDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:cd05330   79 QFGRIDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTD----QL----PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASAD 229
Cdd:cd05330  159 KHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEgslkQLgpenPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDD 238

                        250
                 ....*....|....
gi 568325758 230 SSYMTGQTLHVDGG 243
Cdd:cd05330  239 AGYVNAAVVPIDGG 252
PRK06123 PRK06123
SDR family oxidoreductase;
5-243 4.24e-51

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 166.88  E-value: 4.24e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGItrdnLIMRMKEEEFDT-----VIATNLKGVFNCVKAATRPMMKQRSGR---IINISSVVGVLGNPGQ-ANYV 155
Cdd:PRK06123  83 ALVNNAGI----LEAQMRLEQMDAarltrIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEyIDYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLED-IPLAKLGQPEDVAKTVLFLASADSSYMT 234
Cdd:PRK06123 159 ASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVKAgIPMGRGGTAEEVARAILWLLSDEASYTT 238


                 ....*....
gi 568325758 235 GQTLHVDGG 243
Cdd:PRK06123 239 GTFIDVSGG 247
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-243 1.54e-50

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 165.66  E-value: 1.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMmkQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06077  84 VADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRgITVNAVAPGFIETDMTDQLP------EDVKAKmlEDIPLAKLGQPEDVAKTVLFLASADSsyMTG 235
Cdd:PRK06077 162 INLTKYLALELAPK-IRVNAIAPGFVKTKLGESLFkvlgmsEKEFAE--KFTLMGKILDPEEVAEFVAAILKIES--ITG 236


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:PRK06077 237 QVFVLDSG 244
PRK09242 PRK09242
SDR family oxidoreductase;
2-244 1.58e-50

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 165.69  E-value: 1.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQI--EAMGRKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLI-VARDADALAQARDELaeEFPEREVHGLAADVSDDEDRRAILDWVEDH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQR-SGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:PRK09242  86 WDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYA-HPLLKQHaSSAIVNIGSVSGLTHVRSGAPYGMTK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVK--AKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK09242 165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDyyEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQ 244


                 ....*...
gi 568325758 237 TLHVDGGM 244
Cdd:PRK09242 245 CIAVDGGF 252
PRK07326 PRK07326
SDR family oxidoreductase;
1-225 7.24e-50

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 163.26  E-value: 7.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRkAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAI-TARDQKELEEAAAELNNKGN-VLGLAADVRDEADVQRAVDAIVAAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK07326  81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAV-PALKRGGGYIINISSLAGTNFFAGGAAYNASKFG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLediplaklgQPEDVAKTVLFL 225
Cdd:PRK07326 160 LVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDAWKI---------QPEDIAQLVLDL 215
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 2-244 9.83e-50

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 163.40  E-value: 9.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILN-GRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK07523  87 PIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVK--AKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:PRK07523 167 GNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEfsAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHVLY 246


                 ....*
gi 568325758 240 VDGGM 244
Cdd:PRK07523 247 VDGGI 251
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 2-243 1.64e-49

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 163.26  E-value: 1.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV-NYAGNEQAAaEVVQQIEAmgrkaammraDVSKAQEADQLVKDTLEQL 80
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNaDIHGGDGQH-ENYQFVPT----------DVSSAEEVNHTVAEIIEKF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEE---------FDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQ 151
Cdd:PRK06171  76 GRIDGLVNNAGINIPRLLVDEKDPAgkyelneaaFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 152 ANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIE-TDM------------TDQLPEDVKAKMLED--IPLAKLGQPE 216
Cdd:PRK06171 156 SCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLrtpeyeealaytRGITVEQLRAGYTKTstIPLGRSGKLS 235

                        250       260
                 ....*....|....*....|....*..
gi 568325758 217 DVAKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK06171 236 EVADLVCYLLSDRASYITGVTTNIAGG 262
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-243 2.17e-49

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 169.26  E-value: 2.17e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNyagnEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLII----DRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRL 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGItrdNLIMRMKEEE----FDTVIATNLKGVFNCVKAATRPMMKqrSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK06484 345 DVLVNNAGI---AEVFKPSLEQsaedFTRVYDVNLSGAFACARAAARLMSQ--GGVIVNLGSIASLLALPPRNAYCASKA 419

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKM---LEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK06484 420 AVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALKASGRADFdsiRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGA 499


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:PRK06484 500 TLTVDGG 506
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 2-243 3.15e-49

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 162.32  E-value: 3.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDI-NADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNlIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06113  88 KVDILVNNAGGGGPK-PFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETD-MTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHV 240
Cdd:PRK06113 167 SHLVRNMAFDLGEKNIRVNGIAPGAILTDaLKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTV 246


                 ...
gi 568325758 241 DGG 243
Cdd:PRK06113 247 SGG 249
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 2-246 7.33e-49

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: 161.25  E-value: 7.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQqieaMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAE----IGPAACAISLDVTDQASIDRCVAALVDRWG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd05363   77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQ----------LPEDVKAKML-EDIPLAKLGQPEDVAKTVLFLASAD 229
Cdd:cd05363  157 VISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGvdakfaryenRPRGEKKRLVgEAVPFGRMGRAEDLTGMAIFLASTD 236

                        250
                 ....*....|....*..
gi 568325758 230 SSYMTGQTLHVDGGMYM 246
Cdd:cd05363  237 ADYIVAQTYNVDGGNWM 253
PRK12746 PRK12746
SDR family oxidoreductase;
2-243 9.30e-49

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 160.97  E-value: 9.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL- 80
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELq 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 -----GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKaATRPMMKQRsGRIINISSVVGVLGNPGQANYV 155
Cdd:PRK12746  84 irvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQ-QTLPLLRAE-GRVINISSAEVRLGFTGSIAYG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYM 233
Cdd:PRK12746 162 LSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDpeIRNFATNSSVFGRIGQVEDIADAVAFLASSDSRWV 241

                        250
                 ....*....|
gi 568325758 234 TGQTLHVDGG 243
Cdd:PRK12746 242 TGQIIDVSGG 251
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 6-243 1.21e-48

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: 160.43  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADL-KSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGIT-RDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:cd05365   80 LVNNAGGGgPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETD-MTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:cd05365  160 TRNLAFDLGPKGIRVNAVAPGAVKTDaLASVLTPEIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-241 1.96e-48

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 160.17  E-value: 1.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRS-GRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK06198  84 RLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQL-------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYM 233
Cdd:PRK06198 164 LATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIqrefhgaPDDWLEKAAATQPFGRLLDPDEVARAVAFLLSDESGLM 243


                 ....*...
gi 568325758 234 TGQTLHVD 241
Cdd:PRK06198 244 TGSVIDFD 251
PRK06947 PRK06947
SDR family oxidoreductase;
5-243 2.02e-48

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 159.97  E-value: 2.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVskAQEADQL-VKDTLEQ-LGK 82
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDV--ANEADVIaMFDAVQSaFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNL-IMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGR---IINISSVVGVLGNPGQ-ANYVAA 157
Cdd:PRK06947  81 LDALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGSPNEyVDYAGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKML-EDIPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK06947 161 KGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLgAQTPLGRAGEADEVAETIVWLLSDAASYVTGA 240


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:PRK06947 241 LLDVGGG 247
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 5-244 2.24e-48

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: 160.01  E-value: 2.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFV-CARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKA--ATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:cd08945   83 VLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEvlKAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMTDQL-----------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSS 231
Cdd:cd08945  163 GFTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAA 242

                        250
                 ....*....|...
gi 568325758 232 YMTGQTLHVDGGM 244
Cdd:cd08945  243 AVTAQALNVCGGL 255
PRK09134 PRK09134
SDR family oxidoreductase;
1-243 3.28e-48

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 159.71  E-value: 3.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK09134   6 MAAPRAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIIN-ISSVVGVLgNPGQANYVAAKA 159
Cdd:PRK09134  86 GPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNmIDQRVWNL-NPDFLSYTLSKA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRgITVNAVAPGfIETDMTDQLPEDVkAKMLEDIPLAKLGQPEDVAKTVLFLASADSsyMTGQTLH 239
Cdd:PRK09134 165 ALWTATRTLAQALAPR-IRVNAIGPG-PTLPSGRQSPEDF-ARQHAATPLGRGSTPEEIAAAVRYLLDAPS--VTGQMIA 239


                 ....
gi 568325758 240 VDGG 243
Cdd:PRK09134 240 VDGG 243
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 7-243 4.97e-48

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: 158.79  E-value: 4.97e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAvnyagneqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDIL 86
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVI--------ALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:cd05331   73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 167 AAARELASRGITVNAVAPGFIETDMTDQL------PEDVKAKMLED----IPLAKLGQPEDVAKTVLFLASADSSYMTGQ 236
Cdd:cd05331  153 CLGLELAPYGVRCNVVSPGSTDTAMQRTLwhdedgAAQVIAGVPEQfrlgIPLGKIAQPADIANAVLFLASDQAGHITMH 232


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:cd05331  233 DLVVDGG 239
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 2-244 8.67e-48

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 158.35  E-value: 8.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVvqqieamgrKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVgdiDPEAGKAAADEV---------GGLFVPTDVTDEDAVNALFDTAAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGIT--RDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNP-GQANYV 155
Cdd:PRK06057  76 TYGSVDIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSAtSQISYT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL----PEDVkAKMLEDIPLAKLGQPEDVAKTVLFLASADSS 231
Cdd:PRK06057 156 ASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELfakdPERA-ARRLVHVPMGRFAEPEEIAAAVAFLASDDAS 234

                        250
                 ....*....|...
gi 568325758 232 YMTGQTLHVDGGM 244
Cdd:PRK06057 235 FITASTFLVDGGI 247
PRK07069 PRK07069
short chain dehydrogenase; Validated
 7-244 1.60e-47

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 157.56  E-value: 1.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAM--GRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAEINAAhgEGVAFAAVQDVTDEAQWQALLAQAADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:PRK07069  82 VLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELASRGITV--NAVAPGFIETDMTDQL-----PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK07069 162 TKSIALDCARRGLDVrcNSIHPTFIRTGIVDPIfqrlgEEEATRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVTGAE 241


                 ....*..
gi 568325758 238 LHVDGGM 244
Cdd:PRK07069 242 LVIDGGI 248
PRK06398 PRK06398
aldose dehydrogenase; Validated
 2-244 1.91e-47

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 157.69  E-value: 1.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAevvqqieamgrKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNV-INFDIKEPSYN-----------DVDYFKVDVSNKEQVIKGIDYVISKYG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06398  72 RIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRgITVNAVAPGFIETDMTDQL--------PEDVKAKMLE---DIPLAKLGQPEDVAKTVLFLASADS 230
Cdd:PRK06398 152 LGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLEWAaelevgkdPEHVERKIREwgeMHPMKRVGKPEEVAYVVAFLASDLA 230

                        250
                 ....*....|....
gi 568325758 231 SYMTGQTLHVDGGM 244
Cdd:PRK06398 231 SFITGECVTVDGGL 244
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-243 2.34e-47

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 157.54  E-value: 2.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASR--GIGRAIALCLAEAGADVAVNY---------AGNEQAAAEVVQQ-IEAMGRKAAMMRADVSKAQEA 69
Cdd:PRK12748   3 LMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYwspydktmpWGMHDKEPVLLKEeIESYGVRCEHMEIDLSQPYAP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  70 DQLVKDTLEQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNP 149
Cdd:PRK12748  83 NRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 150 GQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETD-MTDQLPEDVKAKMlediPLAKLGQPEDVAKTVLFLASA 228
Cdd:PRK12748 163 DELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGwITEELKHHLVPKF----PQGRVGEPVDAARLIAFLVSE 238

                        250
                 ....*....|....*
gi 568325758 229 DSSYMTGQTLHVDGG 243
Cdd:PRK12748 239 EAKWITGQVIHSEGG 253
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-244 2.63e-47

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 156.80  E-value: 2.63e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGrkaamMRADVSKAQEADqlvkDTLEQLGK 82
Cdd:PRK07060   8 SGKSVLVTGASSGIGRACAVALAQRGARV-VAAARNAAALDRLAGETGCEP-----LRLDVGDDAAIR----AALAAAGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK07060  78 FDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgRGGSIVNVSSQAALVGLPDHLAYCASKAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAK--MLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLH 239
Cdd:PRK07060 158 DAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSgpMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLP 237


                 ....*
gi 568325758 240 VDGGM 244
Cdd:PRK07060 238 VDGGY 242
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 2-244 4.41e-47

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: 156.93  E-value: 4.41e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVS-SRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGItrdNL----IMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:cd08936   87 GVDILVSNAAV---NPffgnILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:cd08936  164 KTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDkaVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITG 243


                 ....*....
gi 568325758 236 QTLHVDGGM 244
Cdd:cd08936  244 ETVVVGGGT 252
PRK07831 PRK07831
SDR family oxidoreductase;
1-240 6.36e-47

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 156.35  E-value: 6.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGAS-RGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAM--GRKAAMMRADVSKAQEADQLVKDTL 77
Cdd:PRK07831  14 LLAGKVVLVTAAAgTGIGSATARRALEEGARVVISDI-HERRLGETADELAAElgLGRVEAVVCDVTSEAQVDALIDAAV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  78 EQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVA 156
Cdd:PRK07831  93 ERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARgHGGVIVNNASVLGWRAQHGQAHYAA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL-PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK07831 173 AKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVtSAELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTG 252


                 ....*
gi 568325758 236 QTLHV 240
Cdd:PRK07831 253 EVVSV 257
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 2-223 7.19e-47

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: 156.21  E-value: 7.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMG-RKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLS-ARREERLEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd05332   80 GGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTD-QLPEDVKAKMLEDIPLAKLGQPEDVAKTVL 223
Cdd:cd05332  160 LQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMnALSGDGSMSAKMDDTTANGMSPEECALEIL 223
PRK08628 PRK08628
SDR family oxidoreductase;
2-243 1.12e-46

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 155.89  E-value: 1.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVI--FGRSAPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITrDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK08628  83 RIDGLVNNAGVN-DGVGLEAGREAFVASLERNLIHYYVMAHYCL-PHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQL------PEDVKAKMLEDIPLAK-LGQPEDVAKTVLFLASADSSYMT 234
Cdd:PRK08628 161 LALTREWAVALAKDGVRVNAVIPAEVMTPLYENWiatfddPEAKLAAITAKIPLGHrMTTAEEIADTAVFLLSERSSHTT 240


                 ....*....
gi 568325758 235 GQTLHVDGG 243
Cdd:PRK08628 241 GQWLFVDGG 249
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 3-246 1.24e-46

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 155.52  E-value: 1.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAaaevvQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPG-----ETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKE------EEFDTVIATNLKGVFNCVKAATRPMMK-------QRsGRIINISSVVGVLGNP 149
Cdd:cd05371   76 LDIVVNCAGIAVAAKTYNKKGqqphslELFQRVINVNLIGTFNVIRLAAGAMGKnepdqggER-GVIINTASVAAFEGQI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 150 GQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIP-LAKLGQPEDVAKTVLFLasA 228
Cdd:cd05371  155 GQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPfPSRLGDPAEYAHLVQHI--I 232

                        250
                 ....*....|....*...
gi 568325758 229 DSSYMTGQTLHVDGGMYM 246
Cdd:cd05371  233 ENPYLNGEVIRLDGAIRM 250
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-223 4.45e-46

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 153.69  E-value: 4.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGL-LARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK07666  84 SIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGV 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDM------TDQLPEdvkakmlediplaKLGQPEDVAKTVL 223
Cdd:PRK07666 164 LGLTESLMQEVRKHNIRVTALTPSTVATDMavdlglTDGNPD-------------KVMQPEDLAEFIV 218
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 2-243 4.59e-46

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 153.79  E-value: 4.59e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMmRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIIS-ARKAEACADAAEELSAYGECIAI-PADLSSEEGIEALVARVAERSD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMK-----QRSGRIINISSVVGVLGNPGQA-NYV 155
Cdd:cd08942   82 RLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALL-PLLRaaataENPARVINIGSIAGIVVSGLENySYG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAK--MLEDIPLAKLGQPEDVAKTVLFLASADSSYM 233
Cdd:cd08942  161 ASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALeaEEKSIPLGRWGRPEDMAGLAIMLASRAGAYL 240

                        250
                 ....*....|
gi 568325758 234 TGQTLHVDGG 243
Cdd:cd08942  241 TGAVIPVDGG 250
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 4-246 4.65e-46

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 154.07  E-value: 4.65e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVIT-GRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGitrDNLIMR---MKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK07677  80 DALINNAA---GNFICPaedLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKgIKGNIINMVATYAWDAGPGVIHSAAAKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASR-GITVNAVAPGFIE-TDMTDQLPEDVKA--KMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK07677 157 GVLAMTRTLAVEWGRKyGIRVNAIAPGPIErTGGADKLWESEEAakRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYING 236

                        250
                 ....*....|.
gi 568325758 236 QTLHVDGGMYM 246
Cdd:PRK07677 237 TCITMDGGQWL 247
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 2-243 2.60e-45

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: 152.61  E-value: 2.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAA-LGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAG-----ITRDNLIMR---------MKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLG 147
Cdd:cd08935   82 TVDILINGAGgnhpdATTDPEHYEpeteqnffdLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 148 NPGQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDM-------TDQLPEDVKAKMLEDIPLAKLGQPEDVAK 220
Cdd:cd08935  162 LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQnrkllinPDGSYTDRSNKILGRTPMGRFGKPEELLG 241

                        250       260
                 ....*....|....*....|....
gi 568325758 221 TVLFLASAD-SSYMTGQTLHVDGG 243
Cdd:cd08935  242 ALLFLASEKaSSFVTGVVIPVDGG 265
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 2-243 3.02e-45

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: 151.91  E-value: 3.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLL--VDRSELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITrdnLIMR----MKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVV--GVLGNPgqanYV 155
Cdd:cd08937   80 RVDVLINNVGGT---IWAKpyehYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIYRIP----YS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIET----------DMTDQLPE---DVKAKMLEDIPLAKLGQPEDVAKTV 222
Cdd:cd08937  153 AAKGGVNALTASLAFEHARDGIRVNAVAPGGTEApprkiprnaaPMSEQEKVwyqRIVDQTLDSSLMGRYGTIDEQVRAI 232

                        250       260
                 ....*....|....*....|.
gi 568325758 223 LFLASADSSYMTGQTLHVDGG 243
Cdd:cd08937  233 LFLASDEASYITGTVLPVGGG 253
PRK07985 PRK07985
SDR family oxidoreductase;
2-246 3.08e-45

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 153.23  E-value: 3.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQ-IEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAQDVKKiIEECGRKAVLLPGDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGI-TRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGrIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK07985 127 GGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAI-PLLPKGAS-IITTSSIQAYQPSPHLLDYAATKA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIET--DMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK07985 205 AILNYSRGLAKQVAEKGIRVNIVAPGPIWTalQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYVTAEV 284


                 ....*....
gi 568325758 238 LHVDGGMYM 246
Cdd:PRK07985 285 HGVCGGEHL 293
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 4-246 1.07e-44

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: 150.69  E-value: 1.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEA-MGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:cd05322    2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADI-NSENAEKVADEINAeYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRS-GRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPG-FIETDMTDQL-----------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASAD 229
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSLlpqyakklgikESEVEQYYIDKVPLKRGCDYQDVLNMLLFYASPK 240

                        250
                 ....*....|....*..
gi 568325758 230 SSYMTGQTLHVDGGMYM 246
Cdd:cd05322  241 ASYCTGQSINITGGQVM 257
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 2-236 2.25e-44

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: 149.47  E-value: 2.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV--------NYAGN---EQAAAEVVQQIEAMGRKAAMMRADVSKAQEAD 70
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVaaktasegDNGSAkslPGTIEETAEEIEAAGGQALPIVVDVRDEDQVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  71 QLVKDTLEQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPG 150
Cdd:cd05338   81 ALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 151 QANYVAAKAGVIGLTKAAARELASRGITVNAVAPG-FIETDMTDQLPEDVKAKMLEDiplaklgqPEDVAKTVLFLASAD 229
Cdd:cd05338  161 DVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIETPAATELSGGSDPARARS--------PEILSDAVLAILSRP 232


                 ....*..
gi 568325758 230 SSYMTGQ 236
Cdd:cd05338  233 AAERTGL 239
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 6-220 2.42e-44

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: 149.31  E-value: 2.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVI-LDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLT 165
Cdd:cd05339   80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 166 KAAARELAS---RGITVNAVAPGFIETDMTdqlpEDVKAKMledIPLAKLGQPEDVAK 220
Cdd:cd05339  160 ESLRLELKAygkPGIKTTLVCPYFINTGMF----QGVKTPR---PLLAPILEPEYVAE 210
PRK06500 PRK06500
SDR family oxidoreductase;
2-244 2.55e-44

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 149.34  E-value: 2.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyaGNEQAAAEVVQqiEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAIT--GRDPASLEAAR--AELGESALVIRADAGDVAAQKALAQALAEAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINiSSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06500  80 RLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALL-PLLANPASIVLN-GSINAHIGMPNSSVYAASKAAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQL--PEDVKAKMLEDI----PLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK06500 158 LSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLglPEATLDAVAAQIqalvPLGRFGTPEEIAKAVLYLASDESAFIVG 237


                 ....*....
gi 568325758 236 QTLHVDGGM 244
Cdd:PRK06500 238 SEIIVDGGM 246
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 1-243 5.49e-44

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 148.68  E-value: 5.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK12747   1 MLKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 ------GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSgRIINISSVVGVLGNPGQANY 154
Cdd:PRK12747  81 qnrtgsTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQAL-SRLRDNS-RIINISSAATRISLPDFIAY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLA--KLGQPEDVAKTVLFLASADSSY 232
Cdd:PRK12747 159 SMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAfnRLGEVEDIADTAAFLASPDSRW 238

                        250
                 ....*....|.
gi 568325758 233 MTGQTLHVDGG 243
Cdd:PRK12747 239 VTGQLIDVSGG 249
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 5-192 7.26e-44

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: 147.38  E-value: 7.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRM-KEEEFDTVIATNLKGVFNCVKAATrPMMKQRS-GRIINISSVVGVLGNPgqanYVAAKAGVI 162
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTpTREQARETMKTNFFGTVDVTQALL-PLLKKSPaGRIVNVSSGLGSLTSA----YGVSKAALN 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMT 192
Cdd:cd05324  156 ALTRILAKELKETGIKVNACCPGWVKTDMG 185
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 2-243 1.16e-43

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 148.51  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAI-LDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAG-----ITRDNL----------IMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISS----- 141
Cdd:PRK08277  87 PCDILINGAGgnhpkATTDNEfhelieptktFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSmnaft 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 142 ----VVGvlgnpgqanYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL-------PEDVKAKMLEDIPLA 210
Cdd:PRK08277 167 pltkVPA---------YSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALlfnedgsLTERANKILAHTPMG 237

                        250       260       270
                 ....*....|....*....|....*....|....
gi 568325758 211 KLGQPEDVAKTVLFLASAD-SSYMTGQTLHVDGG 243
Cdd:PRK08277 238 RFGKPEELLGTLLWLADEKaSSFVTGVVLPVDGG 271
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 4-244 1.85e-43

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: 146.96  E-value: 1.85e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKV-VFADIDEERGADFA---EAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIG 163
Cdd:cd09761   77 DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYC-RDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 164 LTKAAARELaSRGITVNAVAPGFIETdmTDQLPEDVKAKMLED---IPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHV 240
Cdd:cd09761  156 LTHALAMSL-GPDIRVNCISPGWINT--TEQQEFTAAPLTQEDhaqHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIV 232


                 ....
gi 568325758 241 DGGM 244
Cdd:cd09761  233 DGGM 236
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-243 2.44e-43

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 146.26  E-value: 2.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVavnYAGNEQAAAEVVQQIEAMgrkaammRADVSKAQEAdqlvkdTLEQLG 81
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQV---YGVDKQDKPDLSGNFHFL-------QLDLSDDLEP------LFDWVP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRD-NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK06550  67 SVDILCNTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMT--DQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK06550 147 LAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTaaDFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTIV 226


                 ....*
gi 568325758 239 HVDGG 243
Cdd:PRK06550 227 PIDGG 231
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 1-246 4.15e-43

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 146.64  E-value: 4.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07890   2 LLKGKVVVVSGVGPGLGRTLAVRAARAGADV-VLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAgiTRDNLIMRMKEEEFDT---VIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:PRK07890  81 GRVDALVNNA--FRVPSMKPLADADFAHwraVIELNVLGTLRLTQAFT-PALAESGGSIVMINSMVLRHSQPKYGAYKMA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL-----------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLA 226
Cdd:PRK07890 158 KGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGYfrhqagkygvtVEQIYAETAANSDLKRLPTDDEVASAVLFLA 237

                        250       260
                 ....*....|....*....|
gi 568325758 227 SADSSYMTGQTLHVDGGMYM 246
Cdd:PRK07890 238 SDLARAITGQTLDVNCGEYH 257
PRK07577 PRK07577
SDR family oxidoreductase;
2-243 6.09e-43

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 145.25  E-value: 6.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADV---AVNYAGNeqaaaevvqqieamgRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVigiARSAIDD---------------FPGELFACDLADIEQTAATLAQINE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QlGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVvGVLGNPGQANYVAAK 158
Cdd:PRK07577  66 I-HPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSR-AIFGALDRTSYSAAK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDM---TDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK07577 144 SALVGCTRTWALELAEYGITVNAVAPGPIETELfrqTRPVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITG 223


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:PRK07577 224 QVLGVDGG 231
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 3-243 1.50e-42

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 145.09  E-value: 1.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVL--VDRSELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITrdnliMRMK------EEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVV--GVLGNPgqanY 154
Cdd:PRK12823  85 IDVLINNVGGT-----IWAKpfeeyeEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIAtrGINRVP----Y 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDM------TDQLPEDVKAKM-------LEDIPLAKLGQPEDVAKT 221
Cdd:PRK12823 156 SAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPPrrvprnAAPQSEQEKAWYqqivdqtLDSSLMKRYGTIDEQVAA 235

                        250       260
                 ....*....|....*....|..
gi 568325758 222 VLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK12823 236 ILFLASDEASYITGTVLPVGGG 257
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 2-246 1.52e-42

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 145.10  E-value: 1.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAeVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDA-AVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK07576  86 PIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAY-PLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAGV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIE-TDMTDQL--PEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK07576 165 DMLTRTLALEWGPEGIRVNSIVPGPIAgTEGMARLapSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVVL 244


                 ....*...
gi 568325758 239 HVDGGMYM 246
Cdd:PRK07576 245 PVDGGWSL 252
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-243 2.79e-42

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 152.31  E-value: 2.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVVQQIEAMGrkaamMRADVSKAQEADQLVKDTLE 78
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLadlDEEAAEAAAAELGGPDRALG-----VACDVTDEAAVQAAFEEAAL 494

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRS-GRIINISSVVGVLGNPGQANYVAA 157
Cdd:PRK08324 495 AFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNPGPNFGAYGAA 574

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAP------------GFIETDMT------DQLPEDVKAKMLediplakLGQ---PE 216
Cdd:PRK08324 575 KAAELHLVRQLALELGPDGIRVNGVNPdavvrgsgiwtgEWIEARAAayglseEELEEFYRARNL-------LKRevtPE 647

                        250       260
                 ....*....|....*....|....*..
gi 568325758 217 DVAKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK08324 648 DVAEAVVFLASGLLSKTTGAIITVDGG 674
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 2-245 2.81e-42

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 144.28  E-value: 2.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADV---AVNYAGNEQAAAEVVQqieamgrkaammrADVSKAQEADQLVKDTLE 78
Cdd:PRK06523   7 LAGKRALVTGGTKGIGAATVARLLEAGARVvttARSRPDDLPEGVEFVA-------------ADLTTAEGCAAVARAVLE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNL--IMRMKEEEFDTVIATNLKgvfncvkAATR------PMM-KQRSGRIINISSVVGVLGNP 149
Cdd:PRK06523  74 RLGGVDILVHVLGGSSAPAggFAALTDEEWQDELNLNLL-------AAVRldrallPGMiARGSGVIIHVTSIQRRLPLP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 150 GQ-ANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKM--------------LEDIPLAKLGQ 214
Cdd:PRK06523 147 EStTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERLAEAAgtdyegakqiimdsLGGIPLGRPAE 226

                        250       260       270
                 ....*....|....*....|....*....|.
gi 568325758 215 PEDVAKTVLFLASADSSYMTGQTLHVDGGMY 245
Cdd:PRK06523 227 PEEVAELIAFLASDRAASITGTEYVIDGGTV 257
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 5-243 4.08e-42

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: 143.60  E-value: 4.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGrKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKV-KATFVQCDVTSWEQLAAAFKKAIEKFGRVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDN--LIMRMKEEEFDTVIATNLKGVFNCVKAATRPM---MKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:cd05323   80 ILINNAGILDEKsyLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMdknKGGKGGVIVNIGSVAGLYPAPQFPVYSASKH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASR-GITVNAVAPGFIETDMtdqLPEDVK--AKMLEDIPLAKlgqPEDVAKTVLFLASADSsyMTGQ 236
Cdd:cd05323  160 GVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL---LPDLVAkeAEMLPSAPTQS---PEVVAKAIVYLIEDDE--KNGA 231


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:cd05323  232 IWIVDGG 238
PRK12744 PRK12744
SDR family oxidoreductase;
2-243 7.26e-42

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 143.34  E-value: 7.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGAD-VAVNY--AGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKaVAIHYnsAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMmkQRSGRIINIssVVGVLG--NPGQANYVA 156
Cdd:PRK12744  86 AFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTL--VTSLLGafTPFYSAYAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFIETDM--TDQLPEDV----KAKMLEDIPLAKLGQPEDVAKTVLFLASaDS 230
Cdd:PRK12744 162 SKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFfyPQEGAEAVayhkTAAALSPFSKTGLTDIEDIVPFIRFLVT-DG 240

                        250
                 ....*....|...
gi 568325758 231 SYMTGQTLHVDGG 243
Cdd:PRK12744 241 WWITGQTILINGG 253
PRK08416 PRK08416
enoyl-ACP reductase;
4-243 8.37e-42

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 143.37  E-value: 8.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEA-MGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:PRK08416   8 GKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEANKIAEDLEQkYGIKAKAYPLNILEPETYKELFKKIDEDFDR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLI------MRMKEEEFDTV-IATNLKGVFNCVKAATRpMMKQRSGRIINISSVVGVLGNPGQANYV 155
Cdd:PRK08416  88 VDFFISNAIISGRAVVggytkfMRLKPKGLNNIyTATVNAFVVGAQEAAKR-MEKVGGGSIISLSSTGNLVYIENYAGHG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLP--EDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYM 233
Cdd:PRK08416 167 TSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTnyEEVKAKTEELSPLNRMGQPEDLAGACLFLCSEKASWL 246

                        250
                 ....*....|
gi 568325758 234 TGQTLHVDGG 243
Cdd:PRK08416 247 TGQTIVVDGG 256
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-244 1.22e-41

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 142.79  E-value: 1.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQieaMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK06200   3 WLHGQVALITGGGSGIGRALVERFLAEGARVAV-LERSAEKLASLRQR---FGDHVLVVEGDVTSYADNQRAVDQTVDAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGI----TRdnlIMRMKEEE----FDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQA 152
Cdd:PRK06200  79 GKLDCFVGNAGIwdynTS---LVDIPAETldtaFDEIFNVNVKGYLLGAKAAL-PALKASGGSMIFTLSNSSFYPGGGGP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 153 NYVAAKAGVIGLTKAAARELASRgITVNAVAPGFIETD--------MTDQLPEDV--KAKMLEDI-PLAKLGQPEDVAKT 221
Cdd:PRK06200 155 LYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDlrgpaslgQGETSISDSpgLADMIAAItPLQFAPQPEDHTGP 233

                        250       260
                 ....*....|....*....|....
gi 568325758 222 VLFLAS-ADSSYMTGQTLHVDGGM 244
Cdd:PRK06200 234 YVLLASrRNSRALTGVVINADGGL 257
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 4-244 1.46e-41

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 142.46  E-value: 1.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    4 GKVALVTGASRGIGRAIALCLAEAGAD-VAVNYAGNEQA-------AAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKD 75
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRvVAVDLCADDPAvgyplatRAELDAVAAACPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   76 TLEQLGKLDILVNNAG-ITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ---RSGRIINISSVVGVLGNPGQ 151
Cdd:TIGR04504  81 AVERWGRLDAAVAAAGvIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARpdpRGGRFVAVASAAATRGLPHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  152 ANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMtdqLPEDVKAKMLEDI-------PLAKLGQPEDVAKTVLF 224
Cdd:TIGR04504 161 AAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAM---LAATARLYGLTDVeefaghqLLGRLLEPEEVAAAVAW 237

                         250       260
                  ....*....|....*....|
gi 568325758  225 LASADSSYMTGQTLHVDGGM 244
Cdd:TIGR04504 238 LCSPASSAVTGSVVHADGGF 257
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 2-243 1.48e-41

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 142.46  E-value: 1.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQqiEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK08265   4 LAGKVAIVTGGATLIGAAVARALVAAGARVAI--VDIDADNGAAVA--ASLGERARFIATDITDDAAIERAVATVVARFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTvIATNLKGVFNCVKAAtRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK08265  80 RVDILVNLACTYLDDGLASSRADWLAA-LDVNLVSAAMLAQAA-HPHLARGGGAIVNFTSISAKFAQTGRWLYPASKAAI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMleDI------PLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK08265 158 RQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGGDRAKA--DRvaapfhLLGRVGDPEEVAQVVAFLCSDAASFVTG 235


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:PRK08265 236 ADYAVDGG 243
PRK06949 PRK06949
SDR family oxidoreductase;
2-244 2.19e-41

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 142.21  E-value: 2.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAaEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLK-ELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVK-AATRPMMKQRS-------GRIINISSVVGVLGNPGQAN 153
Cdd:PRK06949  86 TIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQeVAKRMIARAKGagntkpgGRIINIASVAGLRVLPQIGL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 154 YVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPE-DVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:PRK06949 166 YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWEtEQGQKLVSMLPRKRVGKPEDLDGLLLLLAADESQF 245

                        250
                 ....*....|..
gi 568325758 233 MTGQTLHVDGGM 244
Cdd:PRK06949 246 INGAIISADDGF 257
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 7-230 2.19e-41

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: 139.96  E-value: 2.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGAD-VAVNYagneqaaaevvqqieamgrkaammradvskaqeadqlvkdtleqlgKLDI 85
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSPkVLVVS----------------------------------------------RRDV 34

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLT 165
Cdd:cd02266   35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758 166 KAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADS 230
Cdd:cd02266  115 QQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDRPK 179
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 2-243 2.51e-41

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: 141.45  E-value: 2.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADV---AVNYAGNEQAAAEVVQQIEAMGrkaammraDVSKAQEadqlVKDTLE 78
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVvavSRTQADLDSLVRECPGIEPVCV--------DLSDWDA----TEEALG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMM-KQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:cd05351   73 SVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIaRGVPGSIVNVSSQASQRALTNHTVYCST 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:cd05351  153 KAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDpeKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTG 232


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:cd05351  233 STLPVDGG 240
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 2-228 2.59e-41

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: 141.52  E-value: 2.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAI-AARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd08934   80 RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPE-DVKAKMLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:cd08934  160 NAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHtITKEAYEERISTIRKLQAEDIAAAVRYAVTA 227
PLN02253 PLN02253
xanthoxin dehydrogenase
 2-243 5.46e-41

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 141.88  E-value: 5.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEqAAAEVVQQIEAmGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDD-LGQNVCDSLGG-EPNVCFFHCDVTVEDDVSRAVDFTVDKFG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNL--IMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PLN02253  94 TLDIMVNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSKH 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMT-DQLPEDVKAK--------------MLEDIPLAklgqPEDVAKTVLF 224
Cdd:PLN02253 174 AVLGLTRSVAAELGKHGIRVNCVSPYAVPTALAlAHLPEDERTEdalagfrafagknaNLKGVELT----VDDVANAVLF 249

                        250
                 ....*....|....*....
gi 568325758 225 LASADSSYMTGQTLHVDGG 243
Cdd:PLN02253 250 LASDEARYISGLNLMIDGG 268
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 2-222 1.14e-40

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 140.46  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyaGN--EQAAAEVVQQIeamgRKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAI---GDldEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEAD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK07825  76 LGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKH 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEdiplaklgqPEDVAKTV 222
Cdd:PRK07825 156 AVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGAKGFKNVE---------PEDVAAAI 209
PRK06181 PRK06181
SDR family oxidoreductase;
4-228 1.44e-40

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 140.11  E-value: 1.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLA-ARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEE-FDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:PRK06181  80 DILVNNAGITMWSRFDELTDLSvFERVMRVNYLGAVYCTHAAL-PHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDmTDQLPEDVKAKMLEDIPL--AKLGQPEDVAKTVLFLASA 228
Cdd:PRK06181 159 GFFDSLRIELADDGVAVTVVCPGFVATD-IRKRALDGDGKPLGKSPMqeSKIMSAEECAEAILPAIAR 225
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 4-243 6.60e-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: 138.44  E-value: 6.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAM-MRADVSKAQEADQLVKDTLEQLGK 82
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKV-VFCARGEAAGQALESELNRAGPGSCKfVPCDVTKEEDIKTLISVTVERFGR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGI-TRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd08933   88 IDCLVNNAGWhPPHQTTDETSAQEFRDLLNLNLISYFLASKYAL-PHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLP---EDVKAKMLEDI---PLAKLGQPEDVAKTVLFLAsADSSYMTG 235
Cdd:cd08933  167 TAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAaqtPDTLATIKEGElaqLLGRMGTEAESGLAALFLA-AEATFCTG 245


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:cd08933  246 IDLLLSGG 253
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 5-193 7.22e-39

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: 135.05  E-value: 7.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAvnyagneqAAAEVVQQIEAMGRKAAM----MRADVSKAQEADQLVKDTLEQL 80
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVI--------ATARNPDKLESLGELLNDnlevLELDVTDEESIKAAVKEVIERF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd05374   73 GRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAA 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTD 193
Cdd:cd05374  153 LEALSESLRLELAPFGIKVTIIEPGPVRTGFAD 185
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 5-225 1.21e-38

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: 134.03  E-value: 1.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVvqqieAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALS-----ASGGDVEAVPYDARDPEDARALVDALRDRFGRID 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:cd08932   76 VLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRAL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETDMTDQLPEDVkakmleDIPLAKLGQPEDVAKTVLFL 225
Cdd:cd08932  156 AHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVG------AFPPEEMIQPKDIANLVRMV 210
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 2-238 1.36e-38

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: 134.88  E-value: 1.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLV-KDTLEQL 80
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFeRVAREQQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNA-------GITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQAn 153
Cdd:cd09763   81 GRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVA- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 154 YVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLG--QPEDVAKTVLFLAS-ADS 230
Cdd:cd09763  160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKERDAFLNgeTTEYSGRCVVALAAdPDL 239


                 ....*...
gi 568325758 231 SYMTGQTL 238
Cdd:cd09763  240 MELSGRVL 247
PRK07074 PRK07074
SDR family oxidoreductase;
3-244 1.50e-38

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 134.90  E-value: 1.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGaDVAVNYAGNEQAAAEVVQQIEAmGRKAAMMrADVSKAQEADQLVKDTLEQLGK 82
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAG-DRVLALDIDAAALAAFADALGD-ARFVPVA-CDLTDAASLAAALANAAAERGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVG--VLGNPGqanYVAAKAG 160
Cdd:PRK07074  78 VDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGmaALGHPA---YSAAKAG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIET-------DMTDQLPEDVKAKMlediPLAKLGQPEDVAKTVLFLASADSSYM 233
Cdd:PRK07074 155 LIHYTKLLAVEYGRFGIRANAVAPGTVKTqawearvAANPQVFEELKKWY----PLQDFATPDDVANAVLFLASPAARAI 230

                        250
                 ....*....|.
gi 568325758 234 TGQTLHVDGGM 244
Cdd:PRK07074 231 TGVCLPVDGGL 241
PRK05650 PRK05650
SDR family oxidoreductase;
8-195 1.57e-38

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 135.17  E-value: 1.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDILV 87
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADV-NEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  88 NNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTKA 167
Cdd:PRK05650  83 NNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSET 162

                        170       180
                 ....*....|....*....|....*...
gi 568325758 168 AARELASRGITVNAVAPGFIETDMTDQL 195
Cdd:PRK05650 163 LLVELADDEIGVHVVCPSFFQTNLLDSF 190
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 1-244 6.51e-38

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: 132.86  E-value: 6.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVnyagNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAV----LDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEE-----FDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYV 155
Cdd:cd05348   77 GKLDCFIGNAGIWDYSTSLVDIPEEkldeaFDELFHINVKGYILGAKAAL-PALYATEGSVIFTVSNAGFYPGGGGPLYT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRgITVNAVAPGFIETDM------------TDQLPEDvkaKMLEDI-PLAKLGQPEDVAKTV 222
Cdd:cd05348  156 ASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLrgpaslgqgetsISTPPLD---DMLKSIlPLGFAPEPEDYTGAY 231

                        250       260
                 ....*....|....*....|...
gi 568325758 223 LFLAS-ADSSYMTGQTLHVDGGM 244
Cdd:cd05348  232 VFLASrGDNRPATGTVINYDGGM 254
PRK12742 PRK12742
SDR family oxidoreductase;
2-243 1.13e-37

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 131.80  E-value: 1.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIeamgrKAAMMRADVSkaqEADQLVkDTLEQLG 81
Cdd:PRK12742   4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQET-----GATAVQTDSA---DRDAVI-DVVRKSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMmkQRSGRIINISSVVG-VLGNPGQANYVAAKAG 160
Cdd:PRK12742  75 ALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIIIGSVNGdRMPVAGMAAYAASKSA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTdqlPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTL 238
Cdd:PRK12742 153 LQGMARGLARDFGPRGITINVVQPGPIDTDAN---PANgpMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMH 229


                 ....*
gi 568325758 239 HVDGG 243
Cdd:PRK12742 230 TIDGA 234
PRK07454 PRK07454
SDR family oxidoreductase;
5-226 1.37e-37

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 131.62  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLAL-VARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:PRK07454  86 VLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETDMTDQlpEDVKA-----KMLediplaklgQPEDVAKTVLFLA 226
Cdd:PRK07454 166 TKCLAEEERSHGIRVCTITLGAVNTPLWDT--ETVQAdfdrsAML---------SPEQVAQTILHLA 221
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 4-220 2.96e-37

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: 130.84  E-value: 2.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADV---AVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANViivARSESKLEEAVEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQ----LPEDVKAKMLEDIPLaklgQPEDVAK 220
Cdd:cd08939  161 LRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEenktKPEETKAIEGSSGPI----TPEEAAR 220
PRK05855 PRK05855
SDR family oxidoreductase;
4-193 1.11e-36

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 135.88  E-value: 1.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGAD-VAVNYagNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEvVASDI--DEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGV 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRpMMKQRS--GRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK05855 393 PDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGR-QMVERGtgGHIVNVASAAAYAPSRSLPAYATSKAA 471

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTD 193
Cdd:PRK05855 472 VLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
PRK08267 PRK08267
SDR family oxidoreductase;
8-223 2.02e-36

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 129.29  E-value: 2.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAmmRADVSKAQEADQLVKD-TLEQLGKLDIL 86
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGA-YDINEAGLAALAAELGAGNAWTG--ALDVTDRAAWDAALADfAAATGGRLDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSG-RIINISSVVGVLGNPGQANYVAAKAGVIGLT 165
Cdd:PRK08267  82 FNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAAL-PYLKATPGaRVINTSSASAIYGQPGLAVYSATKFAVRGLT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 166 KAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLaKLgQPEDVAKTVL 223
Cdd:PRK08267 161 EALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTKRLGV-RL-TPEDVAEAVW 216
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 5-225 3.50e-36

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: 127.62  E-value: 3.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNyagnEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGIC----ARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:cd08929   77 ALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETDMTDQlPEDVKAKMlediplaklgQPEDVAKTVLFL 225
Cdd:cd08929  157 SEAAMLDLREANIRVVNVMPGSVDTGFAGS-PEGQAWKL----------APEDVAQAVLFA 206
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 6-226 2.93e-35

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: 125.57  E-value: 2.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKV-VLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLT 165
Cdd:cd05360   81 WVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568325758 166 KAAARELASRG--ITVNAVAPGFIETDMtdqlPEDVKAKM-LEDIPLAKLGQPEDVAKTVLFLA 226
Cdd:cd05360  161 ESLRAELAHDGapISVTLVQPTAMNTPF----FGHARSYMgKKPKPPPPIYQPERVAEAIVRAA 220
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-226 2.12e-34

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 125.80  E-value: 2.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVL-LARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK07109  84 GPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568325758 161 VIGLTKAAARELASRG--ITVNAVAPGFIETdmtdQLPEDVKAKM-LEDIPLAKLGQPEDVAKTVLFLA 226
Cdd:PRK07109 164 IRGFTDSLRCELLHDGspVSVTMVQPPAVNT----PQFDWARSRLpVEPQPVPPIYQPEVVADAILYAA 228
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 1-228 5.47e-34

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 123.09  E-value: 5.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADV--AVNYAGNEQAAAEVVqqieamgrkaaMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK06179   1 MSNSKVALVTGASSGIGRATAEKLARAGYRVfgTSRNPARAAPIPGVE-----------LLELDVTDDASVQAAVDEVIA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITrdnLIMRMKE---EEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYV 155
Cdd:PRK06179  70 RAGRIDVLVNNAGVG---LAGAAEEssiAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPE-------------DVKAKMLEDIPLAKLgqPEDVAKTV 222
Cdd:PRK06179 147 ASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEpdsplaeydreraVVSKAVAKAVKKADA--PEVVADTV 224


                 ....*.
gi 568325758 223 LFLASA 228
Cdd:PRK06179 225 VKAALG 230
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 6-246 1.03e-33

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: 121.91  E-value: 1.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAmmradvsKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQAFESENPGTKAL-------SEQKPEELVDAVLQAGGAIDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRD-NLIMRMKEEEF-DTVIATNLKGvFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIG 163
Cdd:cd05361   76 LVSNDYIPRPmNPIDGTSEADIrQAFEALSIFP-FALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 164 LTKAAARELASRGITVNAVAPGFIE------TDMTDQLPEDVkAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:cd05361  155 LAESLAKELSRDNILVYAIGPNFFNsptyfpTSDWENNPELR-ERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQF 233


                 ....*....
gi 568325758 238 LHVDGGMYM 246
Cdd:cd05361  234 FAFAGGYLP 242
PRK07062 PRK07062
SDR family oxidoreductase;
2-243 4.33e-33

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 120.53  E-value: 4.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMM--RADVSKAQEADQLVKDTLEQ 79
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAI-CGRDEERLASAEARLREKFPGARLLaaRCDVLDEADVAAFAAAVEAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAG----ITRDNLIMRMKEEEFDtviatnLK--GVFNCVKAAtRPMMKQRS-GRIINISSVVGVLGNPGQA 152
Cdd:PRK07062  85 FGGVDMLVNNAGqgrvSTFADTTDDAWRDELE------LKyfSVINPTRAF-LPLLRASAaASIVCVNSLLALQPEPHMV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 153 NYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDM----------TDQLPEDVKAKMLED--IPLAKLGQPEDVAK 220
Cdd:PRK07062 158 ATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQwrrryearadPGQSWEAWTAALARKkgIPLGRLGRPDEAAR 237

                        250       260
                 ....*....|....*....|...
gi 568325758 221 TVLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK07062 238 ALFFLASPLSSYTTGSHIDVSGG 260
PRK07201 PRK07201
SDR family oxidoreductase;
2-178 5.81e-33

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 125.83  E-value: 5.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK07201 369 LVGKVVLITGASSGIGRATAIKVAEAGATV-FLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHG 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAG--ITR--DNLIMRMkeEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSvVGVLGN-PGQANYVA 156
Cdd:PRK07201 448 HVDYLVNNAGrsIRRsvENSTDRF--HDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSS-IGVQTNaPRFSAYVA 524

                        170       180
                 ....*....|....*....|..
gi 568325758 157 AKAGVIGLTKAAARELASRGIT 178
Cdd:PRK07201 525 SKAALDAFSDVAASETLSDGIT 546
PRK07832 PRK07832
SDR family oxidoreductase;
5-193 3.87e-32

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 118.22  E-value: 3.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAAMMRA-DVSKAQEADQLVKDTLEQLGKL 83
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDR-DADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAHGSM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAgRGGHLVNVSSAAGLVALPWHAAYSASKFGLR 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMTD 193
Cdd:PRK07832 160 GLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 7-193 5.74e-32

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: 117.05  E-value: 5.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAqEADQLVKDTLE-QLGKLDI 85
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALA-ARRTDRLDELKAELLNPNPSVEVEILDVTDE-ERNQLVIAELEaELGGLDL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLT 165
Cdd:cd05350   79 VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLA 158

                        170       180
                 ....*....|....*....|....*...
gi 568325758 166 KAAARELASRGITVNAVAPGFIETDMTD 193
Cdd:cd05350  159 ESLRYDVKKRGIRVTVINPGFIDTPLTA 186
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 5-227 1.09e-31

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: 116.61  E-value: 1.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQ--IEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLIL--TGRRAERLQELADelGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRD-NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd05346   79 IDILVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMT------DQlpeDVKAKMLEDI-PLaklgQPEDVAKTVLFLAS 227
Cdd:cd05346  159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEFSlvrfhgDK---EKADKVYEGVePL----TPEDIAETILWVAS 224
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 4-243 1.65e-31

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 116.34  E-value: 1.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVV--ADIDPEIAEKVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:cd08943   79 DIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQgIGGNIVFNASKNAVAPGPNAAAYSAAKAAEA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 163 GLTKAAARELASRGITVNAVAP-----GFIETDM---------TDQLPEDVKAKMLediplakLGQ---PEDVAKTVLFL 225
Cdd:cd08943  159 HLARCLALEGGEDGIRVNTVNPdavfrGSKIWEGvwraarakaYGLLEEEYRTRNL-------LKRevlPEDVAEAVVAM 231

                        250
                 ....*....|....*...
gi 568325758 226 ASADSSYMTGQTLHVDGG 243
Cdd:cd08943  232 ASEDFGKTTGAIVTVDGG 249
PRK07775 PRK07775
SDR family oxidoreductase;
7-228 5.35e-31

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 115.62  E-value: 5.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDIL 86
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALG-ARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:PRK07775  92 VSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVT 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 167 AAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDipLAKLGQ--------PEDVAKTVLFLASA 228
Cdd:PRK07775 172 NLQMELEGTGVRASIVHPGPTLTGMGWSLPAEVIGPMLED--WAKWGQarhdyflrASDLARAITFVAET 239
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 1-238 7.50e-31

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: 114.21  E-value: 7.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRA---DVSKAQEADQLVKDTL 77
Cdd:cd05340    1 LLNDRIILVTGASDGIGREAALTYARYGATV-ILLGRNEEKLRQVADHINEEGGRQPQWFIldlLTCTSENCQQLAQRIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  78 EQLGKLDILVNNAGITRDnlIMRMKE---EEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANY 154
Cdd:cd05340   80 VNYPRLDGVLHNAGLLGD--VCPLSEqnpQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMtdqlpedvKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMT 234
Cdd:cd05340  158 AVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAM--------RASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKT 229


                 ....
gi 568325758 235 GQTL 238
Cdd:cd05340  230 GMTF 233
PRK09072 PRK09072
SDR family oxidoreductase;
2-223 8.34e-31

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 114.65  E-value: 8.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSkAQEADQLVKDTLEQLG 81
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLL--VGRNAEKLEALAARLPYPGRHRWVVADLT-SEAGREAVLARAREMG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK09072  80 GINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMledipLAKLGQPEDVAKTVL 223
Cdd:PRK09072 160 RGFSEALRRELADTGVRVLYLAPRATRTAMNSEAVQALNRAL-----GNAMDDPEDVAAAVL 216
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 6-244 1.73e-30

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: 113.87  E-value: 1.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    6 VALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMM-RADVSKAQ----EADQLVKDTLEQL 80
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTcQADLSNSAtlfsRCEAIIDACFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   81 GKLDILVNNAGITRDNLIMRMKEEE-------FDTVIA----TNLKGVFNCVKA------ATRPMMKQRSGRIINISSVV 143
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLRGDAGEgvgdkksLEVQVAelfgSNAIAPYFLIKAfaqrqaGTRAEQRSTNLSIVNLCDAM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  144 GVLGNPGQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFieTDMTDQLPEDVKAKMLEDIPLAKL-GQPEDVAKTV 222
Cdd:TIGR02685 163 TDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL--SLLPDAMPFEVQEDYRRKVPLGQReASAEQIADVV 240

                         250       260
                  ....*....|....*....|..
gi 568325758  223 LFLASADSSYMTGQTLHVDGGM 244
Cdd:TIGR02685 241 IFLVSPKAKYITGTCIKVDGGL 262
PRK05717 PRK05717
SDR family oxidoreductase;
4-244 2.36e-30

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 113.45  E-value: 2.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAaevvQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGS----KVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGIT--RDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK05717  86 DALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCA-PYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRgITVNAVAPGFIET-DMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHV 240
Cdd:PRK05717 165 LALTHALAISLGPE-IRVNAVSPGWIDArDPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVV 243


                 ....
gi 568325758 241 DGGM 244
Cdd:PRK05717 244 DGGM 247
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 2-243 2.43e-30

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 113.41  E-value: 2.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQI-EAMGRKAAMMRADVSKAQEADQLVKDtLEQL 80
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVIL-LSRNEENLKKAREKIkSESNVDVSYIVADLTKREDLERTVKE-LKNI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK08339  84 GEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRIS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDV---KAKMLE--------DIPLAKLGQPEDVAKTVLFLASAD 229
Cdd:PRK08339 164 MAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRakrEGKSVEealqeyakPIPLGRLGEPEEIGYLVAFLASDL 243

                        250
                 ....*....|....
gi 568325758 230 SSYMTGQTLHVDGG 243
Cdd:PRK08339 244 GSYINGAMIPVDGG 257
PRK09186 PRK09186
flagellin modification protein A; Provisional
 1-243 2.73e-30

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 113.16  E-value: 2.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVA---VNYAGNEQAAAEVVQQIEAmgRKAAMMRADVSKAQEADQLVKDTL 77
Cdd:PRK09186   1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIaadIDKEALNELLESLGKEFKS--KKLSLVELDITDQESLEEFLSKSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  78 EQLGKLDILVNNAGITRDN---LIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVL-------- 146
Cdd:PRK09186  79 EKYGKIDGAVNCAYPRNKDygkKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVapkfeiye 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 147 GNPGQA--NYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIetdmTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLF 224
Cdd:PRK09186 159 GTSMTSpvEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGI----LDNQPEAFLNAYKKCCNGKGMLDPDDICGTLVF 234

                        250
                 ....*....|....*....
gi 568325758 225 LASADSSYMTGQTLHVDGG 243
Cdd:PRK09186 235 LLSDQSKYITGQNIIVDDG 253
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 4-192 6.05e-30

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: 111.93  E-value: 6.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEA-MGRKAAMMRADVSKAQEADQLVKDTLEQLgK 82
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVIL-ISRTQEKLDAVAKEIEEkYGVETKTIAADFSAGDDIYERIEKELEGL-D 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRD--NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd05356   79 IGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAF 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETDMT 192
Cdd:cd05356  159 LDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-190 1.78e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 111.55  E-value: 1.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK06180   1 MSSMKTWLITGVSSGFGRALAQAALAAGHRVVGT-VRSEAARADFE---ALHPDRALARLLDVTDFDAIDAVVADAEATF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK06180  77 GPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFA 156

                        170       180       190
                 ....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIETD 190
Cdd:PRK06180 157 LEGISESLAKEVAPFGIHVTAVEPGSFRTD 186
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 2-212 2.02e-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: 2.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAG-NEQAAAEVVQQIEAMgrkaAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:COG3967    3 LTGNTILITGGTSGIGLALAKRLHARGNTVII--TGrREEKLEEAAAANPGL----HTIVLDVADPASIAALAEQVTAEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITR--DNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:COG3967   77 PDLNVLINNAGIMRaeDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAkmledIPLAKL 212
Cdd:COG3967  157 AALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRA-----MPLDEF 205
PRK06914 PRK06914
SDR family oxidoreductase;
4-228 2.21e-29

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 111.27  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMG--RKAAMMRADVSkAQEADQLVKDTLEQLG 81
Cdd:PRK06914   3 KKIAIVTGASSGFGLLTTLELAKKGYLVIAT-MRNPEKQENLLSQATQLNlqQNIKVQQLDVT-DQNSIHNFQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDM--------TDQLPEDVK-----AKMLEDIP--LAKLGQPEDVAKTVLFLA 226
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIwevgkqlaENQSETTSPykeymKKIQKHINsgSDTFGNPIDVANLIVEIA 240


                 ..
gi 568325758 227 SA 228
Cdd:PRK06914 241 ES 242
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 4-230 1.72e-28

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 108.85  E-value: 1.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAVnyAG-NEQAAAEVVQQIEAMGRKAAM--MRADVSKAQEADQLVKDTLEQL 80
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVII--ACrNEEKGEEAAAEIKKETGNAKVevIQLDLSSLASVRQFAEEFLARF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGitrdnlIMRMKEEE----FDTVIATNLKGVFncvkAATR---P-MMKQRSGRIINISSVVGVLGN---- 148
Cdd:cd05327   79 PRLDILINNAG------IMAPPRRLtkdgFELQFAVNYLGHF----LLTNlllPvLKASAPSRIVNVSSIAHRAGPidfn 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 149 -----------PGQAnYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIetdMTDQLPEDVKAKMLEDI--PLAKLGqP 215
Cdd:cd05327  149 dldlennkeysPYKA-YGQSKLANILFTRELARRLEGTGVTVNALHPGVV---RTELLRRNGSFFLLYKLlrPFLKKS-P 223

                        250
                 ....*....|....*
gi 568325758 216 EDVAKTVLFLASADS 230
Cdd:cd05327  224 EQGAQTALYAATSPE 238
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 2-244 1.79e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 108.59  E-value: 1.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGAD---VAVNYAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEADQLVkdtlE 78
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHlhlVARDADALEALAADLR---AAHGVDVAVHALDLSSPEAREQLA----A 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINissVVGVLGNPGQANYVAAK 158
Cdd:PRK06125  78 EAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVN---VIGAAGENPDADYICGS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 159 AG---VIGLTKAAARELASRGITVNAVAPGFIETDMTDQL----------PEDVKAKMLEDIPLAKLGQPEDVAKTVLFL 225
Cdd:PRK06125 155 AGnaaLMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLlkgraraelgDESRWQELLAGLPLGRPATPEEVADLVAFL 234

                        250
                 ....*....|....*....
gi 568325758 226 ASADSSYMTGQTLHVDGGM 244
Cdd:PRK06125 235 ASPRSGYTSGTVVTVDGGI 253
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-243 4.63e-28

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 106.77  E-value: 4.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGrKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCIN-SRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEeeFDTVIATNLKGVFNCVKAATrPMMKQRSGrIINISSVVGVL-GNPGQANYVAAKAG 160
Cdd:PRK05786  81 AIDGLVVTVGGYVEDTVEEFSG--LEEMLTNHIKIPLYAVNASL-RFLKEGSS-IVLVSSMSGIYkASPDQLSYAVAKAG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELASRGITVNAVAPGFIetdMTDQLPEDVKAKmledipLAKLGQ----PEDVAKTVLFLASADSSYMTGQ 236
Cdd:PRK05786 157 LAKAVEILASELLGRGIRVNGIAPTTI---SGDFEPERNWKK------LRKLGDdmapPEDFAKVIIWLLTDEADWVDGV 227


                 ....*..
gi 568325758 237 TLHVDGG 243
Cdd:PRK05786 228 VIPVDGG 234
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 1-244 5.25e-28

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: 107.03  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGA--SRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRkAAMMRADVSKAQEADQLVKDTLE 78
Cdd:COG0623    2 LLKGKRGLITGVanDRSIAWGIAKALHEEGAELAFTYQ-GEALKKRVEPLAEELGS-ALVLPCDVTDDEQIDALFDEIKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILV-------NNAG------ITRDNLIMRMkeeefdTVIATNLKGVfncVKAAtRPMMKQRsGRIINISsvvgv 145
Cdd:COG0623   80 KWGKLDFLVhsiafapKEELggrfldTSREGFLLAM------DISAYSLVAL---AKAA-EPLMNEG-GSIVTLT----- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 146 lgnpgqanYVAA-KA----GVIGLTKAA--------ARELASRGITVNAVAPGFIETdmtdqlpedVKA-------KMLE 205
Cdd:COG0623  144 --------YLGAeRVvpnyNVMGVAKAAleasvrylAADLGPKGIRVNAISAGPIKT---------LAAsgipgfdKLLD 206

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568325758 206 DI----PLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:COG0623  207 YAeeraPLGRNVTIEEVGNAAAFLLSDLASGITGEIIYVDGGY 249
PRK07024 PRK07024
SDR family oxidoreductase;
9-196 6.27e-28

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 106.94  E-value: 6.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   9 VTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRkAAMMRADVSKAQEADQLVKDTLEQLGKLDILVN 88
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGL-VARRTDALQAFAARLPKAAR-VSVYAADVRDADALAAAAADFIAAHGLPDVVIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  89 NAGITRDNLI-MRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTKA 167
Cdd:PRK07024  85 NAGISVGTLTeEREDLAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLES 164

                        170       180
                 ....*....|....*....|....*....
gi 568325758 168 AARELASRGITVNAVAPGFIETDMTDQLP 196
Cdd:PRK07024 165 LRVELRPAGVRVVTIAPGYIRTPMTAHNP 193
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 2-243 6.92e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 107.20  E-value: 6.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAG-NEQAAAEVVQQIEAMGRKAAMMR--ADVSKAQEADQLVKDTLE 78
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMI--VGrNPDKLAAAAEEIEALKGAGAVRYepADVTDEDQVARAVDAATA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRD-NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:PRK05875  83 WHGRLHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPED--VKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:PRK05875 163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESpeLSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITG 242


                 ....*...
gi 568325758 236 QTLHVDGG 243
Cdd:PRK05875 243 QVINVDGG 250
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 2-228 7.62e-28

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: 106.44  E-value: 7.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADV---AVNYAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:cd05343    4 WRGRVALVTGASVGIGAAVARALVQHGMKVvgcARRVDKIEALAAECQ---SAGYPTLFPYQCDLSNEEQILSMFSAIRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPmMKQRS---GRIINISSVVG--VLGNPGQAN 153
Cdd:cd05343   81 QHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQS-MKERNvddGHIININSMSGhrVPPVSVFHF 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568325758 154 YVAAKAGVIGLTKAAAREL--ASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:cd05343  160 YAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYVLST 236
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 5-222 7.72e-28

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: 106.00  E-value: 7.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAmmRADVSKAQEADQLVKDTLEQLG-KL 83
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGL-YDIDEDGLAALAAELGAENVVAG--ALDVTDRAAWAAALADFAAATGgRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSG-RIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:cd08931   78 DALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAAL-PYLKATPGaRVINTASSSAIYGQPDLAVYSATKFAVR 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMTDQLPE--DVKAKMLEDIPlaklgqPEDVAKTV 222
Cdd:cd08931  157 GLTEALDVEWARHGIRVADVWPWFVDTPILTKGETgaAPKKGLGRVLP------VSDVAKVV 212
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 2-192 1.80e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 106.59  E-value: 1.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLAL--VDLEEAELAALAAELGGDDRVLTVVADVTDLAAMQAAAEEAVERFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK05872  85 GIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATL-PALIERRGYVLQVSSLAAFAAAPGMAAYCASKAGV 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFIETDMT 192
Cdd:PRK05872 164 EAFANALRLEVAHHGVTVGSAYLSWIDTDLV 194
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 2-196 1.02e-26

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: 103.16  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAG-NEQAAAEVVQQIEAMGrkaaMMRADVSKAQEADQLVKDTLEQL 80
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVII--TGrREERLAEAKKELPNIH----TIVLDVGDAESVEALAEALLSEY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKE--EEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:cd05370   77 PNLDILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATK 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLP 196
Cdd:cd05370  157 AALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERR 194
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 3-190 1.04e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 103.96  E-value: 1.04e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGaDVAVNYAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERG-DRVVATARDTATLADLA---EKYGDRLLPLALDVTDRAAVFAAVETAVEHFGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:PRK08263  78 LDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALE 157

                        170       180
                 ....*....|....*....|....*...
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETD 190
Cdd:PRK08263 158 GMSEALAQEVAEFGIKVTLVEPGGYSTD 185
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-214 7.88e-26

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: 100.83  E-value: 7.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEvvqqIEAMGRKAAMMR---ADVSK-AQEADQLVKDTLEQlGK 82
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATE----LAALGASHSRLHileLDVTDeIAESAEAVAERLGD-AG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMR-MKEEEFDTVIATNLKGVFNCVKAaTRPMMKQ-RSGRIINISSVVGVLG-NP--GQANYVAA 157
Cdd:cd05325   76 LDVLINNAGILHSYGPASeVDSEDLLEVFQVNVLGPLLLTQA-FLPLLLKgARAKIINISSRVGSIGdNTsgGWYSYRAS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQL--------PEDVKAKMLEDIPLAKLGQ 214
Cdd:cd05325  155 KAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFaknkgpitPEESVAGLLKVIDNLNEED 219
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 8-244 1.20e-25

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: 100.65  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGAdvavnyagneqaaaevvqQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGK-LDIL 86
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGH------------------TVIGIDLREADVIADLSTPEGRAAAIADVLARCSGvLDGL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLImrmkeeefDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGN------------------ 148
Cdd:cd05328   65 VNCAGVGGTTVA--------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAqdklelakalaagteara 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 149 ---------PGQANYVAAKAGVIGLTKAAARE-LASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDI---PLAKLGQP 215
Cdd:cd05328  137 valaehagqPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGGESVDAfvtPMGRRAEP 216

                        250       260
                 ....*....|....*....|....*....
gi 568325758 216 EDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:cd05328  217 DEIAPVIAFLASDAASWINGANLFVDGGL 245
PRK08264 PRK08264
SDR family oxidoreductase;
1-223 4.21e-25

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 98.81  E-value: 4.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVnyagneqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVkdtlEQL 80
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAAKVY-------AAARDPESVTDLGPRVVPLQLDVTDPASVAAAA----EAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITR-DNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK08264  72 SDVTILVNNAGIFRtGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDvKAKmlediplaklgqPEDVAKTVL 223
Cdd:PRK08264 152 AAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLDAP-KAS------------PADVARQIL 202
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 2-238 4.68e-25

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 99.18  E-value: 4.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMG-RKAAMMRADVSKAQEAD-QLVKDTLE- 78
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATV-ILLGRTEEKLEAVYDEIEAAGgPQPAIIPLDLLTATPQNyQQLADTIEe 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNLIMRMKEEE-FDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:PRK08945  89 QFGRLDGVLHNAGLLGELGPMEQQDPEvWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMTdqlpedVKAKMLEDIplAKLGQPEDVAKTVLFLASADSSYMTGQT 237
Cdd:PRK08945 169 KFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMR------ASAFPGEDP--QKLKTPEDIMPLYLYLMGDDSRRKNGQS 240


                 .
gi 568325758 238 L 238
Cdd:PRK08945 241 F 241
PRK06194 PRK06194
hypothetical protein; Provisional
 2-193 6.45e-25

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 99.70  E-value: 6.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAG-----ADVavnyagNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDT 76
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGmklvlADV------QQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  77 LEQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQR-------SGRIINISSVVGVLGNP 149
Cdd:PRK06194  78 LERFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFT-PLMLAAaekdpayEGHIVNTASMAGLLAPP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568325758 150 GQANYVAAKAGVIGLTKAAARELASRGITVNA--VAPGFIETDMTD 193
Cdd:PRK06194 157 AMGIYNVSKHAVVSLTETLYQDLSLVTDQVGAsvLCPYFVPTGIWQ 202
PRK06182 PRK06182
short chain dehydrogenase; Validated
 5-190 7.72e-25

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 99.26  E-value: 7.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVavnYAGNEQAaaEVVQQIEAMGRKAamMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTV---YGAARRV--DKMEDLASLGVHP--LSLDVTDEASIKAAVDTIIAEEGRID 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:PRK06182  77 VLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGF 156

                        170       180
                 ....*....|....*....|....*.
gi 568325758 165 TKAAARELASRGITVNAVAPGFIETD 190
Cdd:PRK06182 157 SDALRLEVAPFGIDVVVIEPGGIKTE 182
PRK06139 PRK06139
SDR family oxidoreductase;
2-189 1.90e-24

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 99.02  E-value: 1.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARL-VLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGItrdNLIMRMKE---EEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAK 158
Cdd:PRK06139  84 RIDVWVNNVGV---GAVGRFEEtpiEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568325758 159 AGVIGLTKAAARELAS-RGITVNAVAPGFIET 189
Cdd:PRK06139 161 FGLRGFSEALRGELADhPDIHVCDVYPAFMDT 192
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 6-241 1.02e-23

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: 95.43  E-value: 1.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDnlIMRMKE---EEFDTVIATNLkGVFNCVKAATRPMMKQRS--GRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:cd05367   81 LINNAGSLGP--VSKIEFidlDELQKYFDLNL-TSPVCLTSTLLRAFKKRGlkKTVVNVSSGAAVNPFKGWGLYCSSKAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARELasRGITVNAVAPGFIETDMTDQLPEDVKA----KMLEDIP-LAKLGQPEDVAKTVLFLASADsSYMTG 235
Cdd:cd05367  158 RDMFFRVLAAEE--PDVRVLSYAPGVVDTDMQREIRETSADpetrSRFRSLKeKGELLDPEQSAEKLANLLEKD-KFESG 234


                 ....*.
gi 568325758 236 QtlHVD 241
Cdd:cd05367  235 A--HVD 238
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 5-188 1.07e-23

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: 93.70  E-value: 1.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758     5 KVALVTGASRGIGRAIALCLAEAGA-DVAVNY--AGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRPmmkQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWN-LHELTAD---LPLDFFVLFSSIAGVLGSPGQANYAAANAFL 156

                          170       180
                   ....*....|....*....|....*..
gi 568325758   162 IGLtkaaARELASRGITVNAVAPGFIE 188
Cdd:smart00822 157 DAL----AEYRRARGLPALSIAWGAWA 179
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 2-207 1.09e-23

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: 95.17  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGAdvAVNYAG--NEQAAAEVVqqiEAMGRKAAMMRADVSKAQEadqlVKDTLEQ 79
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGA--KKVYAAvrDPGSAAHLV---AKYGDKVVPLRLDVTDPES----IKAAAAQ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGITRDNLIMrmKEEEFDTV---IATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVA 156
Cdd:cd05354   72 AKDVDVVINNAGVLKPATLL--EEGALEALkqeMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSA 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGFIETDMT------DQLPEDVKAKMLEDI 207
Cdd:cd05354  150 SKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAagaggpKESPETVAEAVLKAL 206
PRK07041 PRK07041
SDR family oxidoreductase;
8-243 3.17e-23

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 93.95  E-value: 3.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTleqlGKLDILV 87
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTI--ASRSRDRLAAAARALGGGAPVRTAALDITDEAAVDAFFAEA----GPFDHVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  88 NNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPmmkqRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLTKA 167
Cdd:PRK07041  75 ITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAARIA----PGGSLTFVSGFAAVRPSASGVLQGAINAALEALARG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 168 AARELASrgITVNAVAPGFIETDMTDQLPEDVKAKML----EDIPLAKLGQPEDVAKTVLFLASadSSYMTGQTLHVDGG 243
Cdd:PRK07041 151 LALELAP--VRVNTVSPGLVDTPLWSKLAGDAREAMFaaaaERLPARRVGQPEDVANAILFLAA--NGFTTGSTVLVDGG 226
PRK05693 PRK05693
SDR family oxidoreductase;
5-189 6.66e-23

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 94.09  E-value: 6.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVavnYAGNEQAaaEVVQQIEAMGRKAAMMraDVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEV---WATARKA--EDVEALAAAGFTAVQL--DVNDGAALARLAEELEAEHGGLD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:PRK05693  75 VLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVG-VTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHAL 153

                        170       180
                 ....*....|....*....|....*
gi 568325758 165 TKAAARELASRGITVNAVAPGFIET 189
Cdd:PRK05693 154 SDALRLELAPFGVQVMEVQPGAIAS 178
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 6-234 3.94e-22

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: 91.29  E-value: 3.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLT 165
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 166 KAAARELASRGITV-NAVAPGFIETDMTDQLPEDVKAKMLEDIPLaklgQPEDVAKTVLFLASADSSYMT 234
Cdd:cd05373  161 QSMARELGPKGIHVaHVIIDGGIDTDFIRERFPKRDERKEEDGIL----DPDAIAEAYWQLHTQPRSAWT 226
PRK05866 PRK05866
SDR family oxidoreductase;
2-191 4.68e-22

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 92.11  E-value: 4.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVA-VARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITrdnlIMRMKEE------EFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSvVGVLGN--PGQAN 153
Cdd:PRK05866 117 GVDILINNAGRS----IRRPLAEsldrwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVAT-WGVLSEasPLFSV 191

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568325758 154 YVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDM 191
Cdd:PRK05866 192 YNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 4-244 5.76e-22

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: 91.10  E-value: 5.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAGnEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd05372    1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQP-EALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRDNlimRMKEEEFDTVIATNLKGV------FNCVKAATRPMMKqRSGRIINISsvvgvlgnpgqanYV 155
Cdd:cd05372   80 KLDGLVHSIAFAPKV---QLKGPFLDTSRKGFLKALdisaysLVSLAKAALPIMN-PGGSIVTLS-------------YL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AA-KA----GVIGLTKAA--------ARELASRGITVNAVAPGFIETDMTDQLPeDVKaKMLE----DIPLAKLGQPEDV 218
Cdd:cd05372  143 GSeRVvpgyNVMGVAKAAlessvrylAYELGRKGIRVNAISAGPIKTLAASGIT-GFD-KMLEyseqRAPLGRNVTAEEV 220

                        250       260
                 ....*....|....*....|....*.
gi 568325758 219 AKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:cd05372  221 GNTAAFLLSDLSSGITGEIIYVDGGY 246
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 3-183 2.64e-21

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: 91.66  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAE-AGADVAV----NYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTL 77
Cdd:cd08953  204 PGGVYLVTGGAGGIGRALARALARrYGARLVLlgrsPLPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVR 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  78 EQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRPMmkqRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:cd08953  284 ERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLN-LAQALADE---PLDFFVLFSSVSAFFGGAGQADYAAA 359

                        170       180
                 ....*....|....*....|....*.
gi 568325758 158 KAgvigLTKAAARELASRGITVNAVA 183
Cdd:cd08953  360 NA----FLDAFAAYLRQRGPQGRVLS 381
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 2-238 3.04e-21

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: 89.04  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---------NYAGNEQAAAEvvqQIEAMGRKAAMMRADVSKAQEADQL 72
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIaaktaephpKLPGTIYTAAE---EIEAAGGKALPCIVDIRDEDQVRAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  73 VKDTLEQLGKLDILVNNAGIT--RDNLIMRMKeeEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVlgNP- 149
Cdd:cd09762   78 VEKAVEKFGGIDILVNNASAIslTGTLDTPMK--RYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNL--NPk 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 150 ---GQANYVAAKAGVIGLTKAAARELASRGITVNAVAP-GFIETDMTDQLPEDVKAKMLEdiplaklgQPEDVAKTVLFL 225
Cdd:cd09762  154 wfkNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPrTAIATAAMNMLGGVDVAACCR--------KPEIMADAAYAI 225

                        250
                 ....*....|...
gi 568325758 226 ASADSSYMTGQTL 238
Cdd:cd09762  226 LTKPSSEFTGNFL 238
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 4-191 3.38e-21

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 89.63  E-value: 3.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVA---VNYAGNEQAaaevVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVlgdVDKPGLRQA----VNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSG-RIINISSVVGVLGNPGQANYVAAKA 159
Cdd:PRK05876  82 GHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGgHVVFTASFAGLVPNAGLGAYGVAKY 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDM 191
Cdd:PRK05876 162 GVVGLAETLAREVTADGIGVSVLCPMVVETNL 193
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 4-235 3.89e-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: 88.15  E-value: 3.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVA-VNYAGNEQAAAEVVQqieamgrkaammRADVSKAQEADQLVKDTLEQLGK 82
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVAsIDLAENEEADASIIV------------LDSDSFTEQAKQVVASVARLSGK 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAG-ITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKqrSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd05334   69 VDALICVAGgWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLS--GGLLVLTGAKAALEPTPGMIGYGAAKAAV 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568325758 162 IGLTKAAAREL--ASRGITVNAVAPGFIETDMTdqlpedvkAKMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTG 235
Cdd:cd05334  147 HQLTQSLAAENsgLPAGSTANAILPVTLDTPAN--------RKAMPDADFSSWTPLEFIAELILFWASGAARPKSG 214
PRK07806 PRK07806
SDR family oxidoreductase;
1-90 4.10e-21

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 88.62  E-value: 4.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK07806   3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEF 82

                         90
                 ....*....|
gi 568325758  81 GKLDILVNNA 90
Cdd:PRK07806  83 GGLDALVLNA 92
PRK08278 PRK08278
SDR family oxidoreductase;
2-238 8.62e-21

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 88.42  E-value: 8.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVnyAGN------------EQAAAEvvqqIEAMGRKAAMMRADVSKAQEA 69
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVI--AAKtaephpklpgtiHTAAEE----IEAAGGQALPLVGDVRDEDQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  70 DQLVKDTLEQLGKLDILVNNAGITR----DNLIMRmkeeEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGV 145
Cdd:PRK08278  78 AAAVAKAVERFGGIDICVNNASAINltgtEDTPMK----RFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 146 lgNP----GQANYVAAKAGVIGLTKAAARELASRGITVNAVAP-GFIETDMTDQLP---EDVKAKMlediplaklgQPED 217
Cdd:PRK08278 154 --DPkwfaPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrTTIATAAVRNLLggdEAMRRSR----------TPEI 221

                        250       260
                 ....*....|....*....|.
gi 568325758 218 VAKTVLFLASADSSYMTGQTL 238
Cdd:PRK08278 222 MADAAYEILSRPAREFTGNFL 242
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 7-241 1.92e-20

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: 85.71  E-value: 1.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAvnyagneqaaaevvqqieAMGRKAAMMRADVSKAQEadqlVKDTLEQLGKLDIL 86
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVI------------------TAGRSSGDYQVDITDEAS----IKALFEKVGHFDAI 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQRsGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:cd11731   59 VSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHG-LPYLNDG-GSITLTSGILAQRPIPGGAAAATVNGALEGFVR 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568325758 167 AAARELaSRGITVNAVAPGFIETDMtdqlpedvkaKMLED-IPLAKLGQPEDVAKTvlFLASADSSYmTGQTLHVD 241
Cdd:cd11731  137 AAAIEL-PRGIRINAVSPGVVEESL----------EAYGDfFPGFEPVPAEDVAKA--YVRSVEGAF-TGQVLHVD 198
PRK08340 PRK08340
SDR family oxidoreductase;
8-244 1.05e-19

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 85.24  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEAMGrKAAMMRADVSKAQEADQLVKDTLEQLGKLDILV 87
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVIS-SRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDALV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  88 NNAGITRDNLIMRMKEEEFDTVIATNLKGV---FNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGL 164
Cdd:PRK08340  82 WNAGNVRCEPCMLHEAGYSDWLEAALLHLVapgYLTTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELASRGITVNAVAPGFIET------------DMTDQLPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:PRK08340 162 AKGVSRTYGGKGIRAYTVLLGSFDTpgarenlariaeERGVSFEETWEREVLERTPLKRTGRWEELGSLIAFLLSENAEY 241

                        250
                 ....*....|..
gi 568325758 233 MTGQTLHVDGGM 244
Cdd:PRK08340 242 MLGSTIVFDGAM 253
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 2.19e-19

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 84.22  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAgNEQAAAEV---VQQIEAmgrkAAMMRADVSKAQEADQLVKD 75
Cdd:PRK07533   7 PLAGKRGLVVGIAneQSIAWGCARAFRALGAELAVTYL-NDKARPYVeplAEELDA----PIFLPLDVREPGQLEAVFAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  76 TLEQLGKLDILVNN-AGITRDNLIMRM---KEEEFDTVIATNLKGVFNCVKAAtRPMMKQrSGRIINISsvvgVLGnpgq 151
Cdd:PRK07533  82 IAEEWGRLDFLLHSiAFAPKEDLHGRVvdcSREGFALAMDVSCHSFIRMARLA-EPLMTN-GGSLLTMS----YYG---- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 152 ANYVAAKAGVIGLTKAA--------ARELASRGITVNAVAPGFIET------DMTDQLPEDVKAKMlediPLAKLGQPED 217
Cdd:PRK07533 152 AEKVVENYNLMGPVKAAlessvrylAAELGPKGIRVHAISPGPLKTraasgiDDFDALLEDAAERA----PLRRLVDIDD 227

                        250       260
                 ....*....|....*....|....*..
gi 568325758 218 VAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:PRK07533 228 VGAVAAFLASDAARRLTGNTLYIDGGY 254
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 4-229 1.84e-18

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: 82.13  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVV---QQIEAMGRKaammrADVSKAQEADQLVKDTL 77
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMacrDMAKCEEAAAEIRrdtLNHEVIVRH-----LDLASLKSIRAFAAEFL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  78 EQLGKLDILVNNAGITRdnlIMRMKEEE-FDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLG--------- 147
Cdd:cd09807   76 AEEDRLDVLINNAGVMR---CPYSKTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGkinfddlns 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 148 ----NPGQAnYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTD--QLPEDVKAKMLEDIPLAKLGQPEDVAKT 221
Cdd:cd09807  153 eksyNTGFA-YCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRhtGIHHLFLSTLLNPLFWPFVKTPREGAQT 231


                 ....*...
gi 568325758 222 VLFLASAD 229
Cdd:cd09807  232 SIYLALAE 239
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 8-183 2.63e-18

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: 79.53  E-value: 2.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    8 LVTGASRGIGRAIALCLAEAGA-DVAV---NYAGNEqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLlsrSAAPRP-DAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   84 DILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRPmmkqRSGR-IINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:pfam08659  83 RGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWN-LHEATPD----EPLDfFVLFSSIAGLLGSPGQANYAAANAFLD 157

                         170       180
                  ....*....|....*....|.
gi 568325758  163 GLtkaaARELASRGITVNAVA 183
Cdd:pfam08659 158 AL----AEYRRSQGLPATSIN 174
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 5-200 2.63e-18

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: 81.56  E-value: 2.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVavnYAG---NEQAAAEVVQQIEAMGRKAAMMraDVSKAQEADQLVKDTLEQLG 81
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTV---LAGcltKNGPGAKELRRVCSDRLRTLQL--DVTKPEQIKRAAQWVKEHVG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDI--LVNNAGIT---RDNLIMRMkeEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQANYVA 156
Cdd:cd09805   76 EKGLwgLVNNAGILgfgGDEELLPM--DDYRKCMEVNLFGTVEVTKAFL-PLLRRAKGRVVNVSSMGGRVPFPAGGAYCA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 157 AKAGVIGLTKAAARELASRGITVNAVAPGF--------------IETDMTDQLPEDVK 200
Cdd:cd09805  153 SKAAVEAFSDSLRRELQPWGVKVSIIEPGNfktgitgnselwekQAKKLWERLPPEVK 210
PRK08219 PRK08219
SDR family oxidoreductase;
5-228 8.92e-18

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 79.21  E-value: 8.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEagADVAVNYAGNEQAAAEVVQQIEAmgrkAAMMRADVSKAQEadqlVKDTLEQLGKLD 84
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP--THTLLLGGRPAERLDELAAELPG----ATPFPVDLTDPEA----IAAAVEQLGRLD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITRDNLIMRMKEEEFDTVIATNLKGvfncVKAATR---PMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK08219  74 VLVHNAGVADLGPVAESTVDEWRATLEVNVVA----PAELTRlllPALRAAHGHVVFINSGAGLRANPGWGSYAASKFAL 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568325758 162 IGLTKAAARELASRgITVNAVAPGFIETDMTdqlpEDVKAKMLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:PRK08219 150 RALADALREEEPGN-VRVTSVHPGRTDTDMQ----RGLVAQEGGEYDPERYLRPETVAKAVRFAVDA 211
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
5-225 1.45e-17

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 78.96  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVavnYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLD 84
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHV---ISISRTENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 I----LVNNAGITRDnlIMRMKEEEFDTVIAT---NLkgvfncvkaaTRPMM---------KQRSG--RIINISSvvGVL 146
Cdd:PRK06924  79 VssihLINNAGMVAP--IKPIEKAESEELITNvhlNL----------LAPMIltstfmkhtKDWKVdkRVINISS--GAA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 147 GNP--GQANYVAAKAGVIGLTKAAA--RELASRGITVNAVAPGFIETDMTDQLPEDVKakmlEDIP----------LAKL 212
Cdd:PRK06924 145 KNPyfGWSAYCSSKAGLDMFTQTVAteQEEEEYPVKIVAFSPGVMDTNMQAQIRSSSK----EDFTnldrfitlkeEGKL 220

                        250
                 ....*....|...
gi 568325758 213 GQPEDVAKTVLFL 225
Cdd:PRK06924 221 LSPEYVAKALRNL 233
PRK08251 PRK08251
SDR family oxidoreductase;
3-196 1.92e-17

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 78.82  E-value: 1.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAM--GRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKGRDLAL-CARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPG-QANYVAAKA 159
Cdd:PRK08251  80 GGLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGvKAAYAASKA 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568325758 160 GVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLP 196
Cdd:PRK08251 160 GVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAK 196
PRK09291 PRK09291
SDR family oxidoreductase;
3-197 2.47e-17

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 78.50  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAvnyagneqAAAEVVQQIEAMGRKAAMM-------------RADVSKAQEA 69
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNVI--------AGVQIAPQVTALRAEAARRglalrvekldltdAIDRAQAAEW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  70 DqlvkdtleqlgkLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNP 149
Cdd:PRK09291  73 D------------VDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGP 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568325758 150 GQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPE 197
Cdd:PRK09291 141 FTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGFNDTMAE 188
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
2-243 2.59e-17

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 78.60  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAGNEQAAAEV-VQQIEAMGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK07370   4 LTGKKALVTGIAnnRSIAWGIAQQLHAAGAELGITYLPDEKGRFEKkVRELTEPLNPSLFLPCDVQDDAQIEETFETIKQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNN-AGITRDNLI---MRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQrSGRIINISSVVGVLGNPGQANY 154
Cdd:PRK07370  84 KWGKLDILVHClAFAGKEELIgdfSATSREGFARALEISAYSLAPLCKAA-KPLMSE-GGSIVTLTYLGGVRAIPNYNVM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGFIET----------DMTDQLPEdvKAkmlediPLAKLGQPEDVAKTVLF 224
Cdd:PRK07370 162 GVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTlassavggilDMIHHVEE--KA------PLRRTVTQTEVGNTAAF 233

                        250
                 ....*....|....*....
gi 568325758 225 LASADSSYMTGQTLHVDGG 243
Cdd:PRK07370 234 LLSDLASGITGQTIYVDAG 252
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 2-185 3.82e-17

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 80.35  E-value: 3.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVVQQIeAMGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:COG3347  423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVadlDGEAAEAAAAELGGGY-GADAVDATDVDVTAEAAVAAAFGFAGLD 501

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 qLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ-RSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:COG3347  502 -IGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQgLGGSSVFAVSKNAAAAAYGAAAAATA 580

                        170       180
                 ....*....|....*....|....*...
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPG 185
Cdd:COG3347  581 KAAAQHLLRALAAEGGANGINANRVNPD 608
PRK06482 PRK06482
SDR family oxidoreductase;
3-231 5.11e-17

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 77.85  E-value: 5.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQieaMGRKAAMMRADVSKAQEADQLVKDTLEQLGK 82
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVR-RPDALDDLKAR---YGDRLWVLQLDVTDSAAVRAVVDRAFAALGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMT------------DQLPEDVKAKMLEDIPLAKLGQPEDVAKTVlfLASADS 230
Cdd:PRK06482 157 GFVEAVAQEVAPFGIEFTIVEPGPARTNFGagldrgapldayDDTPVGDLRRALADGSFAIPGDPQKMVQAM--IASADQ 234


                 .
gi 568325758 231 S 231
Cdd:PRK06482 235 T 235
PRK08017 PRK08017
SDR family oxidoreductase;
5-218 1.22e-16

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 76.66  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVavnYAGNEQAaaEVVQQIEAMGRKAAMMRAD--VSKAQEADQLVKDTLeqlGK 82
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRV---LAACRKP--DDVARMNSLGFTGILLDLDdpESVERAADEVIALTD---NR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAG---------ITRDNLimrmkEEEFdtviATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQAN 153
Cdd:PRK08017  75 LYGLFNNAGfgvygplstISRQQM-----EQQF----STNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGA 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 154 YVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDIPLAK---LGqPEDV 218
Cdd:PRK08017 146 YAASKYALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNVNQTQSDKPVENPGIAArftLG-PEAV 212
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 7-206 5.14e-16

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: 74.10  E-value: 5.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVvqqieAMGRKAAMMRADVSKAQEadqlVKDTLEQLGKLDIL 86
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLS-GRDAGALAGL-----AAEVGALARPADVAAELE----VWALAQELGPLDLL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  87 VNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQrsGRIINISSVVGVLGNPGQANYVAAKAGVIGLTK 166
Cdd:cd11730   71 VYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAG--ARLVFLGAYPELVMLPGLSAYAAAKAALEAYVE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568325758 167 AAARELASRGITVnaVAPGFIETDMTDQL---------PEDVKAKMLED 206
Cdd:cd11730  149 VARKEVRGLRLTL--VRPPAVDTGLWAPPgrlpkgalsPEDVAAAILEA 195
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
2-243 6.31e-16

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 74.76  E-value: 6.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAGnEQAAAEVVQQIEAMGRKAAMMRA-DVSKAQEADQLVKDTLE 78
Cdd:PRK08594   5 LEGKTYVVMGVAnkRSIAWGIARSLHNAGAKLVFTYAG-ERLEKEVRELADTLEGQESLLLPcDVTSDEEITACFETIKE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNN-AGITRDNLIMRMKEEEFDT-VIATNLKGV-FNCVKAATRPMMKQrSGRIINISSVVGVLGNPGQANYV 155
Cdd:PRK08594  84 EVGVIHGVAHCiAFANKEDLRGEFLETSRDGfLLAQNISAYsLTAVAREAKKLMTE-GGSIVTLTYLGGERVVQNYNVMG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAAARELASRGITVNAVAPGFIET-------DMTDQLPEdvkakMLEDIPLAKLGQPEDVAKTVLFLASA 228
Cdd:PRK08594 163 VAKASLEASVKYLANDLGKDGIRVNAISAGPIRTlsakgvgGFNSILKE-----IEERAPLRRTTTQEEVGDTAAFLFSD 237

                        250
                 ....*....|....*
gi 568325758 229 DSSYMTGQTLHVDGG 243
Cdd:PRK08594 238 LSRGVTGENIHVDSG 252
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 5-223 6.74e-16

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: 74.80  E-value: 6.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEagadvavnyagNEQAAAEVVQQIEAMGRKAAMMRAdvskaqeADQLVKDTLEQL---- 80
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLAS-----------DPSKRFKVYATMRDLKKKGRLWEA-------AGALAGGTLETLqldv 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 ---------------GKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGV 145
Cdd:cd09806   63 cdsksvaaavervteRHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 146 LGNPGQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDV-----------KAKMLEDIPLA---- 210
Cdd:cd09806  143 QGLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPeevldrtaddiTTFHFFYQYLAhskq 222

                        250
                 ....*....|....*..
gi 568325758 211 ---KLGQ-PEDVAKTVL 223
Cdd:cd09806  223 vfrEAAQnPEEVAEVFL 239
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 2-191 8.38e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 75.04  E-value: 8.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV----------NYAGNEqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQ 71
Cdd:PRK08303   6 LRGKVALVAGATRGAGRGIAVELGAAGATVYVtgrstrarrsEYDRPE-TIEETAELVTAAGGRGIAVQVDHLVPEQVRA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  72 LVKDTLEQLGKLDILVNN--AGitrDNLI--------------MRMKEEEFDTVIATNlkgvfncvKAATRPMMKQRSGR 135
Cdd:PRK08303  85 LVERIDREQGRLDILVNDiwGG---EKLFewgkpvwehsldkgLRMLRLAIDTHLITS--------HFALPLLIRRPGGL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568325758 136 IINISSvvgvlgnpGQANYVA-----------AKAGVIGLTKAAARELASRGITVNAVAPGFIETDM 191
Cdd:PRK08303 154 VVEITD--------GTAEYNAthyrlsvfydlAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEM 212
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 8-243 1.08e-15

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 73.81  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVNYAgNEQAAaevVQQIEAMGrkAAMMRADVSKAQEADQLVKDTLEQLGKLDILV 87
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVSYR-THYPA---IDGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDGLRAII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  88 NNA--------GITRDNLIMRMKEEEFDTVIATNLkgvfncvkAATRPMMKQRSGR--IINISSVVGVLGNPGQANYVAA 157
Cdd:PRK06483  80 HNAsdwlaekpGAPLADVLARMMQIHVNAPYLLNL--------ALEDLLRGHGHAAsdIIHITDYVVEKGSDKHIAYAAS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 158 KAGVIGLTKAAARELASRgITVNAVAPGFI---ETDmtdqlPEDVKAKMLEDIPLAKLGQPEDVAKTVLFLAsaDSSYMT 234
Cdd:PRK06483 152 KAALDNMTLSFAAKLAPE-VKVNSIAPALIlfnEGD-----DAAYRQKALAKSLLKIEPGEEEIIDLVDYLL--TSCYVT 223


                 ....*....
gi 568325758 235 GQTLHVDGG 243
Cdd:PRK06483 224 GRSLPVDGG 232
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 8-190 2.22e-15

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: 74.34  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGAD--VAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDtLEQLGKLDI 85
Cdd:cd05274  154 LITGGLGGLGLLVARWLAARGARhlVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAE-LAAGGPLAG 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRpmmKQRSGRIINISSVVGVLGNPGQANYVAAKAGVIGLt 165
Cdd:cd05274  233 VIHAAGVLRDALLAELTPAAFAAVLAAKVAGALN-LHELTP---DLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDAL- 307

                        170       180
                 ....*....|....*....|....*
gi 568325758 166 kaaARELASRGITVNAVAPGFIETD 190
Cdd:cd05274  308 ---AAQRRRRGLPATSVQWGAWAGG 329
PRK06720 PRK06720
hypothetical protein; Provisional
 2-152 9.27e-15

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 69.62  E-value: 9.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAeVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06720  14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQA-TVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFS 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568325758  82 KLDILVNNAGITRDNLIMRMKEEEFDTVIATNlkGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQA 152
Cdd:PRK06720  93 RIDMLFQNAGLYKIDSIFSRQQENDSNVLCIN--DVWIEIKQLTSSFMKQQEEVVLSDLPIFGIIGTKGQS 161
PRK06101 PRK06101
SDR family oxidoreductase;
6-194 1.15e-14

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 71.05  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAaaeVVQQIEAMGRKAAMMRADVSKAQEAdqlvKDTLEQLGKL-D 84
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIA--CGRNQS---VLDELHTQSANIFTLAFDVTDHPGT----KAALSQLPFIpE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITR--DNLIMRMKEeeFDTVIATNLKGVFNCVKAAtRPMMkQRSGRIINISSVVGVLGNPGQANYVAAKAGVI 162
Cdd:PRK06101  74 LWIFNAGDCEymDDGKVDATL--MARVFNVNVLGVANCIEGI-QPHL-SCGHRVVIVGSIASELALPRAEAYGASKAAVA 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568325758 163 GLTKAAARELASRGITVNAVAPGFIETDMTDQ 194
Cdd:PRK06101 150 YFARTLQLDLRPKGIEVVTVFPGFVATPLTDK 181
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
2-243 1.66e-14

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 70.77  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTG--ASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAaMMRADVSKAQEADQLVKDTLEQ 79
Cdd:PRK08690   4 LQGKKILITGmiSERSIAYGIAKACREQGAELAFTYV-VDKLEERVRKMAAELDSEL-VFRCDVASDDEINQVFADLGKH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGIT-----RDNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQRSGRIINISSVVGVLGNPGQANY 154
Cdd:PRK08690  82 WDGLDGLVHSIGFApkealSGDFLDSISREAFNTAHEISAYSLPALAKAA-RPMMRGRNSAIVALSYLGAVRAIPNYNVM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPEDVK-AKMLED-IPLAKLGQPEDVAKTVLFLASADSSY 232
Cdd:PRK08690 161 GMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKlLGHVAAhNPLRRNVTIEEVGNTAAFLLSDLSSG 240

                        250
                 ....*....|.
gi 568325758 233 MTGQTLHVDGG 243
Cdd:PRK08690 241 ITGEITYVDGG 251
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 4-192 6.19e-14

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 69.89  E-value: 6.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKL 83
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNL-VLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIEGL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 D--ILVNNAGITRD--NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVL--GNPGQANYVAA 157
Cdd:PLN02780 132 DvgVLINNVGVSYPyaRFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVipSDPLYAVYAAT 211

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568325758 158 KAGVIGLTKAAARELASRGITVNAVAPGFIETDMT 192
Cdd:PLN02780 212 KAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMA 246
PRK05993 PRK05993
SDR family oxidoreductase;
1-192 2.70e-13

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 67.74  E-value: 2.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASRGIGRAIALCLAEAGADVavnYAGNEQAaaEVVQQIEAMGRKAAMMraDVSKAQEADQLVKDTLEQL 80
Cdd:PRK05993   1 MDMKRSILITGCSSGIGAYCARALQSDGWRV---FATCRKE--EDVAALEAEGLEAFQL--DYAEPESIAALVAQVLELS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 -GKLDILVNN-----AGITRDnLIMRMKEEEFDTviatNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANY 154
Cdd:PRK05993  74 gGRLDALFNNgaygqPGAVED-LPTEALRAQFEA----NFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAY 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMT 192
Cdd:PRK05993 149 NASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRFR 186
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 6-187 9.21e-13

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 65.93  E-value: 9.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   6 VALVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQieAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIA--TGRRQERLQELKD--ELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITrdnLIM----RMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAGV 161
Cdd:PRK10538  78 LVNNAGLA---LGLepahKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFV 154

                        170       180
                 ....*....|....*....|....*.
gi 568325758 162 IGLTKAAARELASRGITVNAVAPGFI 187
Cdd:PRK10538 155 RQFSLNLRTDLHGTAVRVTDIEPGLV 180
PRK07102 PRK07102
SDR family oxidoreductase;
8-223 9.34e-13

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 65.72  E-value: 9.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRkaammrADVSKAQ-EADQLVK--DTLEQL-GKL 83
Cdd:PRK07102   5 LIIGATSDIARACARRYAAAGARLYL-AARDVERLERLADDLRARGA------VAVSTHElDILDTAShaAFLDSLpALP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNlimRMKEEEFD---TVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPgqANYV--AAK 158
Cdd:PRK07102  78 DIVLIAVGTLGDQ---AACEADPAlalREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRA--SNYVygSAK 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758 159 AGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPedvkakmledIPLAKLGQPEDVAKTVL 223
Cdd:PRK07102 153 AALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTAGLK----------LPGPLTAQPEEVAKDIF 207
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 6-241 1.14e-12

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: 65.70  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    6 VALVTGASRGIGRAIAL----CLAEAGADVaVNYAGNEQAAAEVVQQIEAM--GRKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQelakCLKSPGSVL-VLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLKALREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   80 LGKLD----ILVNNAGiTRDNLIMRMKE-EEFDTV---IATNLKG--VFNCVKAATRPMMKQRSGRIINISSVVGVLGNP 149
Cdd:TIGR01500  81 PRPKGlqrlLLINNAG-TLGDVSKGFVDlSDSTQVqnyWALNLTSmlCLTSSVLKAFKDSPGLNRTVVNISSLCAIQPFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  150 GQANYVAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPE-----DVKAKMLEDIPLAKLGQPEDVAKTVLF 224
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREesvdpDMRKGLQELKAKGKLVDPKVSAQKLLS 239

                         250
                  ....*....|....*..
gi 568325758  225 LASADsSYMTGQtlHVD 241
Cdd:TIGR01500 240 LLEKD-KFKSGA--HVD 253
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 5-243 1.30e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 65.81  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASrGIGRAIALCLAEAGADVAVNYagNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVkDTLEQLGKLD 84
Cdd:PRK06940   3 EVVVVIGAG-GIGQAIARRVGAGKKVLLADY--NEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALA-ATAQTLGPVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  85 ILVNNAGITR-----------DNLIMRMKEEEFDTVIATNLKGVFNCVKAATR-PMMKQRSGRIINISSV---------- 142
Cdd:PRK06940  79 GLVHTAGVSPsqaspeailkvDLYGTALVLEEFGKVIAPGGAGVVIASQSGHRlPALTAEQERALATTPTeellslpflq 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 143 VGVLGNPGQANYVAAKAGVIgLTKAAARELASRGITVNAVAPGFIETDMT-DQLPEDVKA---KMLEDIPLAKLGQPEDV 218
Cdd:PRK06940 159 PDAIEDSLHAYQIAKRANAL-RVMAEAVKWGERGARINSISPGIISTPLAqDELNGPRGDgyrNMFAKSPAGRPGTPDEI 237

                        250       260
                 ....*....|....*....|....*
gi 568325758 219 AKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK06940 238 AALAEFLMGPRGSFITGSDFLVDGG 262
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
154-244 1.85e-12

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 64.64  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 154 YVAAKAGVIGLTKAAARE-LASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEDI--PLAKLGQPEDVAKTVLFLASADS 230
Cdd:PRK12428 137 YQLSKEALILWTMRQAQPwFGARGIRVNCVAPGPVFTPILGDFRSMLGQERVDSDakRMGRPATADEQAAVLVFLCSDAA 216

                         90
                 ....*....|....
gi 568325758 231 SYMTGQTLHVDGGM 244
Cdd:PRK12428 217 RWINGVNLPVDGGL 230
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 8-170 3.25e-12

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


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 65.38  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGAD--VAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLEQLGKLDI 85
Cdd:cd08955  153 LITGGLGGLGLLVAEWLVERGARhlVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQIRASLPPLRG 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRpmmkqrsGRIINI----SSVVGVLGNPGQANYVAAKAGV 161
Cdd:cd08955  233 VIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWN-LHQLTQ-------DLPLDFfvlfSSVASLLGSPGQANYAAANAFL 304


                 ....*....
gi 568325758 162 IGLtkAAAR 170
Cdd:cd08955  305 DAL--AHYR 311
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 4-231 5.86e-12

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: 63.77  E-value: 5.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVVQqiEAMGRKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMvcrNQTRAEEARKEIET--ESGNQNIFLHIVDMSDPKQVWEFVEEFKEEG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGITRDNliMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSvVGVL------GN------ 148
Cdd:cd09808   79 KKLHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS-GGMLvqklntNNlqsert 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 149 --PGQANYVAAKAGVIGLTKAAARelASRGITVNAVAPGFIETDMTDQLPEDVKAKMLEdiplaKLGQPEDVAKTVLFLA 226
Cdd:cd09808  156 afDGTMVYAQNKRQQVIMTEQWAK--KHPEIHFSVMHPGWADTPAVRNSMPDFHARFKD-----RLRSEEQGADTVVWLA 228


                 ....*
gi 568325758 227 SADSS 231
Cdd:cd09808  229 LSSAA 233
PRK05854 PRK05854
SDR family oxidoreductase;
2-197 1.69e-11

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 62.78  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAV---NYAGNEQAAAEVVQqiEAMGRKAAMMRADVSKAQEADQLvKDTLE 78
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILpvrNRAKGEAAVAAIRT--AVPDAKLSLRALDLSSLASVAAL-GEQLR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGK-LDILVNNAGitrdnlIMRMKEEE-----FDTVIATNLKGVFNCVkAATRPMMKQRSGRIINISSVVgvlGNPGQA 152
Cdd:PRK05854  89 AEGRpIHLLINNAG------VMTPPERQttadgFELQFGTNHLGHFALT-AHLLPLLRAGRARVTSQSSIA---ARRGAI 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568325758 153 N---------YVAAKAgvIGLTKAA----ARELASR------GITVNAVAPGFIETDMTDQLPE 197
Cdd:PRK05854 159 NwddlnwersYAGMRA--YSQSKIAvglfALELDRRsraagwGITSNLAHPGVAPTNLLAARPE 220
PRK08703 PRK08703
SDR family oxidoreductase;
2-240 9.11e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 59.95  E-value: 9.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADV---AVNYAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEA--DQLVKDT 76
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVilvARHQKKLEKVYDAIV---EAGHPEPFAIRFDLMSAEEKefEQFAATI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  77 LEQL-GKLDILVNNAG-------ITRDNLIMRMKEEEFDTVIATNLkgvfncvKAATRPMMKQR-SGRIINISSVVGVLG 147
Cdd:PRK08703  81 AEATqGKLDGIVHCAGyfyalspLDFQTVAEWVNQYRINTVAPMGL-------TRALFPLLKQSpDASVIFVGESHGETP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 148 NPGQANYVAAKAGVIGLTKAAARELASRG-ITVNAVAPGFIETdmtdqlPEDVKAKMLEDipLAKLGQPEDVAKTVLFLA 226
Cdd:PRK08703 154 KAYWGGFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINS------PQRIKSHPGEA--KSERKSYGDVLPAFVWWA 225

                        250
                 ....*....|....
gi 568325758 227 SADSSYMTGQTLHV 240
Cdd:PRK08703 226 SAESKGRSGEIVYL 239
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
1-243 9.22e-11

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 60.54  E-value: 9.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAGNeqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK08159   7 LMAGKRGLILGVAnnRSIAWGIAKACRAAGAELAFTYQGD--ALKKRVEPLAAELGAFVAGHCDVTDEASIDAVFETLEK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGIT-RDNLIMRMKEEEFDTVIATNLKGVFNCVKAATR--PMMKQrSGRIINISSVvgvlgnpgQANYV 155
Cdd:PRK08159  85 KWGKLDFVVHAIGFSdKDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRaeKLMTD-GGSILTLTYY--------GAEKV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAA--------ARELASRGITVNAVAPGFIETdmtdqlpedVKAKMLEDI-----------PLAKLGQPE 216
Cdd:PRK08159 156 MPHYNVMGVAKAAleasvkylAVDLGPKNIRVNAISAGPIKT---------LAASGIGDFryilkwneynaPLRRTVTIE 226

                        250       260
                 ....*....|....*....|....*..
gi 568325758 217 DVAKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK08159 227 EVGDSALYLLSDLSRGVTGEVHHVDSG 253
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
8-246 4.38e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 58.45  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVQQIEamgrKAAMMRADVSKAQEADQLVKDTleqlgklDILV 87
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVG--LDRSPPGAANLAALP----GVEFVRGDLRDPEALAAALAGV-------DAVV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  88 NNAGITRDNlimrmkEEEFDTVIATNLKGVFNCVKAATRpmmkQRSGRIINISSvVGVLGNPGQA---NYVAAKAGVIGL 164
Cdd:COG0451   70 HLAAPAGVG------EEDPDETLEVNVEGTLNLLEAARA----AGVKRFVYASS-SSVYGDGEGPideDTPLRPVSPYGA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 165 TKAAARELA-----SRGITVNAV-APGFIETDMTDQLPEDVKAkMLEDIPLAKLGQP---------EDVAKTVLFLASAD 229
Cdd:COG0451  139 SKLAAELLArayarRYGLPVTILrPGNVYGPGDRGVLPRLIRR-ALAGEPVPVFGDGdqrrdfihvDDVARAIVLALEAP 217

                        250
                 ....*....|....*..
gi 568325758 230 SSymTGQTLHVDGGMYM 246
Cdd:COG0451  218 AA--PGGVYNVGGGEPV 232
PRK07023 PRK07023
SDR family oxidoreductase;
7-229 6.57e-10

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 57.72  E-value: 6.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAG-ADVAVNYAGNEQAAAevvqqieAMGRKAAMMRADVSKAQEADQ-LVKDTLEQLG--- 81
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGiAVLGVARSRHPSLAA-------AAGERLAEVELDLSDAAAAAAwLAGDLLAAFVdga 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITRD-NLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGQANYVAAKAG 160
Cdd:PRK07023  77 SRVLLINNAGTVEPiGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 161 VIGLTKAAARElASRGITVNAVAPGFIETDM--------TDQLP-----EDVKAKmlediplAKLGQPEDVA-KTVLFLA 226
Cdd:PRK07023 157 LDHHARAVALD-ANRALRIVSLAPGVVDTGMqatiratdEERFPmrerfRELKAS-------GALSTPEDAArRLIAYLL 228


                 ...
gi 568325758 227 SAD 229
Cdd:PRK07023 229 SDD 231
PRK08177 PRK08177
SDR family oxidoreductase;
5-199 9.62e-10

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 56.96  E-value: 9.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADV---AVNYAGNEQAAAEVVQQIEamgrkaammRADVSKAQEADQLVKDTLEQlg 81
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVtatVRGPQQDTALQALPGVHIE---------KLDMNDPASLDQLLQRLQGQ-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGIT--RDNLIMRMKEEEFDTVIATNlkgVFNCVKAATR--PMMKQRSGRIINISSVVGVLGNPGQAN---Y 154
Cdd:PRK08177  71 RFDLLFVNAGISgpAHQSAADATAAEIGQLFLTN---AIAPIRLARRllGQVRPGQGVLAFMSSQLGSVELPDGGEmplY 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568325758 155 VAAKAGVIGLTKAAARELASRGITVNAVAPGFIETDM-TDQLPEDV 199
Cdd:PRK08177 148 KASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMgGDNAPLDV 193
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 4-185 2.27e-09

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 56.45  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   4 GKVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVVQQI--EAMGRKAAMMRADVSKAQEADQLVKDTLEQLG 81
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHV-ILACRNMSRASAAVSRIleEWHKARVEAMTLDLASLRSVQRFAEAFKAKNS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  82 KLDILVNNAGITrdNLIMRMKEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISS-------VVGVLGN------ 148
Cdd:cd09809   80 PLHVLVCNAAVF--ALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSeshrftdLPDSCGNldfsll 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568325758 149 -PGQANYVA------AKAGVIGLTKAAARELASRGITVNAVAPG 185
Cdd:cd09809  158 sPPKKKYWSmlaynrAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK06196 PRK06196
oxidoreductase; Provisional
 2-141 2.79e-09

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 56.23  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGASRGIGRAIALCLAEAGADVAVNyAGNEQAAAEVVQQIEamGRKAAMMraDVSKAQEADQLVKDTLEQLG 81
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVP-ARRPDVAREALAGID--GVEVVML--DLADLESVRAFAERFLDSGR 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758  82 KLDILVNNAGI-----TRDnlimrmkEEEFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISS 141
Cdd:PRK06196  99 RIDILINNAGVmacpeTRV-------GDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSS 156
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-201 5.65e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 55.42  E-value: 5.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   3 TGKVALVTGASRGIGRAIALCLAEAGADV--AV-NYAGNEQAAAEVVQQieAMGRKAAMMRADVSKAQE----ADQLVKD 75
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVvlAVrNLDKGKAAAARITAA--TPGADVTLQELDLTSLASvraaADALRAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  76 tleqLGKLDILVNNAGI-------TRDNlimrmkeeeFDTVIATNLKGVFNCVKAATRPMMKQRSGRIINISSvvgvlgn 148
Cdd:PRK06197  93 ----YPRIDLLINNAGVmytpkqtTADG---------FELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSS------- 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568325758 149 pgQANYVAA--------------KAGVIGLTKAA--------ARELASRGITVNAVA--PGFIETDMTDQLPEDVKA 201
Cdd:PRK06197 153 --GGHRIRAaihfddlqwerrynRVAAYGQSKLAnllftyelQRRLAAAGATTIAVAahPGVSNTELARNLPRALRP 227
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
1-243 1.85e-08

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 53.59  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAaMMRADVSKAQEADQLvKDTLE 78
Cdd:PRK08415   2 IMKGKKGLIVGVAnnKSIAYGIAKACFEQGAELAFTYL-NEALKKRVEPIAQELGSDY-VYELDVSKPEHFKSL-AESLK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 Q-LGKLDILVNNAGITR----DNLIMRMKEEEFDTVIATNLKGVFNCVKAaTRPMMKQrSGRIINISSVvgvlgnpGQAN 153
Cdd:PRK08415  79 KdLGKIDFIVHSVAFAPkealEGSFLETSKEAFNIAMEISVYSLIELTRA-LLPLLND-GASVLTLSYL-------GGVK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 154 YVAaKAGVIGLTKAA--------ARELASRGITVNAVAPGFIETDMTDQLpEDVKaKMLE----DIPLAKLGQPEDVAKT 221
Cdd:PRK08415 150 YVP-HYNVMGVAKAAlessvrylAVDLGKKGIRVNAISAGPIKTLAASGI-GDFR-MILKwneiNAPLKKNVSIEEVGNS 226

                        250       260
                 ....*....|....*....|..
gi 568325758 222 VLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK08415 227 GMYLLSDLSSGVTGEIHYVDAG 248
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
1-246 3.67e-08

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 52.64  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTG--ASRGIGRAIALCLAEAGADVAVNYAGNeqaAAEVVQQI-EAMGRKAAMMRADVSKAQEADQLVKDTL 77
Cdd:PRK07889   4 LLEGKRILVTGviTDSSIAFHVARVAQEQGAEVVLTGFGR---ALRLTERIaKRLPEPAPVLELDVTNEEHLASLADRVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  78 EQLGKLDILVNNAGIT-RDNLIMRMKEEEFDTVI------ATNLKGVfncvKAATRPMMKQRSgriinisSVVGVLGNPG 150
Cdd:PRK07889  81 EHVDGLDGVVHSIGFApQSALGGNFLDAPWEDVAtalhvsAYSLKSL----AKALLPLMNEGG-------SIVGLDFDAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 151 QA----NYV-AAKAGVIGLTKAAARELASRGITVNAVAPGFIETDMTDQLPedvKAKMLEDI-----PLA-KLGQPEDVA 219
Cdd:PRK07889 150 VAwpayDWMgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAIP---GFELLEEGwderaPLGwDVKDPTPVA 226

                        250       260
                 ....*....|....*....|....*..
gi 568325758 220 KTVLFLASADSSYMTGQTLHVDGGMYM 246
Cdd:PRK07889 227 RAVVALLSDWFPATTGEIVHVDGGAHA 253
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 8-241 5.52e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 51.35  E-value: 5.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAeagadvavnyagneqAAAEVVQqieaMGRKAAMMRADVSKAQEADQLvkdtLEQLGKLDILV 87
Cdd:PRK07578   4 LVIGASGTIGRAVVAELS---------------KRHEVIT----AGRSSGDVQVDITDPASIRAL----FEKVGKVDAVV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  88 NNAGITRDNLIMRMKEEEFDTVIATNLKGVFNCVKAAtRPMMKQRsGRIINISSVVGVLGNPGQANYVAAKAGVIGLTKA 167
Cdd:PRK07578  61 SAAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIG-QHYLNDG-GSFTLTSGILSDEPIPGGASAATVNGALEGFVKA 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568325758 168 AARELaSRGITVNAVAPGFIETDMtdqlpedvkAKMLEDIPLAKLGQPEDVAKTvlFLASADSSyMTGQTLHVD 241
Cdd:PRK07578 139 AALEL-PRGIRINVVSPTVLTESL---------EKYGPFFPGFEPVPAARVALA--YVRSVEGA-QTGEVYKVG 199
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 8-191 6.33e-08

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: 52.11  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVqqiEAMGRKAAMMRADVSKAQEADQLVkDTLEQLGKLDILV 87
Cdd:cd08951   11 FITGSSDGLGLAAARTLLHQGHEVVL-HARSQKRAADAK---AACPGAAGVLIGDLSSLAETRKLA-DQVNAIGRFDAVI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  88 NNAGITRDNLImRMKEEEFDTVIATNLKGVFNCVKAATRPMmkqrsgRIINISS--------------VVGVLGNPGQAn 153
Cdd:cd08951   86 HNAGILSGPNR-KTPDTGIPAMVAVNVLAPYVLTALIRRPK------RLIYLSSgmhrggnaslddidWFNRGENDSPA- 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568325758 154 YVAAKAGVIGLTKAAARELASrgITVNAVAPGFIETDM 191
Cdd:cd08951  158 YSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKM 193
PRK06953 PRK06953
SDR family oxidoreductase;
5-191 7.42e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 51.61  E-value: 7.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVaVNYAGNEQAAAEVvqqiEAMGRKAAMMraDVSKAQEADQLvkdtLEQLG--K 82
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRV-IATARDAAALAAL----QALGAEALAL--DVADPASVAGL----AWKLDgeA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  83 LDILVNNAGI--TRDNLIMRMKEEEFDTVIATNLKGVFNCVKAATrPMMKQRSGRIINISSVVGVLGNPGQAN---YVAA 157
Cdd:PRK06953  71 LDAAVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILL-PLVEAAGGVLAVLSSRMGSIGDATGTTgwlYRAS 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568325758 158 KAGVIGLTKAAARElaSRGITVNAVAPGFIETDM 191
Cdd:PRK06953 150 KAALNDALRAASLQ--ARHATCIALHPGWVRTDM 181
PRK08862 PRK08862
SDR family oxidoreductase;
8-184 1.42e-07

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 50.49  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVnYAGNEQAAAEVVQQIEAMGRKAAMMRADvSKAQEADQLVKDTLE-QLGK-LDI 85
Cdd:PRK08862   9 LITSAGSVLGRTISCHFARLGATLIL-CDQDQSALKDTYEQCSALTDNVYSFQLK-DFSQESIRHLFDAIEqQFNRaPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  86 LVNNagITRDNLIMRMKEEEFDTVI------ATNLkgvFNCVKAATRPMMKQRS-GRIINISS------VVGVlgnpgqa 152
Cdd:PRK08862  87 LVNN--WTSSPLPSLFDEQPSESFIqqlsslASTL---FTYGQVAAERMRKRNKkGVIVNVIShddhqdLTGV------- 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568325758 153 nyVAAKAGVIGLTKAAARELASRGITVNAVAP 184
Cdd:PRK08862 155 --ESSNALVSGFTHSWAKELTPFNIRVGGVVP 184
PRK07984 PRK07984
enoyl-ACP reductase FabI;
2-243 1.76e-07

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 50.67  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTG--ASRGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGrKAAMMRADVSKAQEADQLVKDTLEQ 79
Cdd:PRK07984   4 LSGKRILVTGvaSKLSIAYGIAQAMHREGAELAFTYQ-NDKLKGRVEEFAAQLG-SDIVLPCDVAEDASIDAMFAELGKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  80 LGKLDILVNNAGITRDNlimRMKEEEFDTVIATNLKgVFNCVKAATRPMMKQRSGRIINISSVVGVLGNPGqANYVAAKA 159
Cdd:PRK07984  82 WPKFDGFVHSIGFAPGD---QLDGDYVNAVTREGFK-IAHDISSYSFVAMAKACRSMLNPGSALLTLSYLG-AERAIPNY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 160 GVIGLTKAA--------ARELASRGITVNAVAPGFIETDMTDQLpEDVKaKMLED----IPLAKLGQPEDVAKTVLFLAS 227
Cdd:PRK07984 157 NVMGLAKASleanvrymANAMGPEGVRVNAISAGPIRTLAASGI-KDFR-KMLAHceavTPIRRTVTIEDVGNSAAFLCS 234

                        250
                 ....*....|....*.
gi 568325758 228 ADSSYMTGQTLHVDGG 243
Cdd:PRK07984 235 DLSAGISGEVVHVDGG 250
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
 2-245 2.11e-07

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 50.59  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGAS--RGIGRAIALCLAEAGADVAVnyaGNEQAAAEVVQQIEAMGR----------------KAAMMRADV 63
Cdd:PRK06300   6 LTGKIAFIAGIGddQGYGWGIAKALAEAGATILV---GTWVPIYKIFSQSLELGKfdasrklsngslltfaKIYPMDASF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  64 SKAQE----------------------ADQLVKDtleqLGKLDILVNNagitrdnliMRMKEEEFDTVIATNLKGVFNCV 121
Cdd:PRK06300  83 DTPEDvpeeirenkrykdlsgytisevAEQVKKD----FGHIDILVHS---------LANSPEISKPLLETSRKGYLAAL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 122 KAATRPM--MKQRSGRIIN----------ISSVVGVLGNPGQANyvAAKAGVIGLTKAAARELASR-GITVNAV------ 182
Cdd:PRK06300 150 STSSYSFvsLLSHFGPIMNpggstisltyLASMRAVPGYGGGMS--SAKAALESDTKVLAWEAGRRwGIRVNTIsagpla 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568325758 183 -----APGFIEtDMTDQlpedvkakMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGMY 245
Cdd:PRK06300 228 sragkAIGFIE-RMVDY--------YQDWAPLPEPMEAEQVGAAAAFLVSPLASAITGETLYVDHGAN 286
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
1-243 2.55e-07

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 50.13  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAGNeqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK06505   4 LMQGKRGLIMGVAndHSIAWGIAKQLAAQGAELAFTYQGE--ALGKRVKPLAESLGSDFVLPCDVEDIASVDAVFEALEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDN-LIMRMKEEEFDTVIATNLKGVFNCVKAATR--PMMKQrSGRIINISSvvgvlgnpGQANYV 155
Cdd:PRK06505  82 KWGKLDFVVHAIGFSDKNeLKGRYADTTRENFSRTMVISCFSFTEIAKRaaKLMPD-GGSMLTLTY--------GGSTRV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAA----ARELAS----RGITVNAVAPGFIETdMTDQLPEDVKAK---MLEDIPLAKLGQPEDVAKTVLF 224
Cdd:PRK06505 153 MPNYNVMGVAKAAleasVRYLAAdygpQGIRVNAISAGPVRT-LAGAGIGDARAIfsyQQRNSPLRRTVTIDEVGGSALY 231

                        250
                 ....*....|....*....
gi 568325758 225 LASADSSYMTGQTLHVDGG 243
Cdd:PRK06505 232 LLSDLSSGVTGEIHFVDSG 250
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
2-243 3.26e-07

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 49.82  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTG--ASRGIGRAIALCLAEAGADVAVNYAGNE------QAAAEVVQQIeamgrkaaMMRADVSKAQEADQLV 73
Cdd:PRK06997   4 LAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVGDRfkdritEFAAEFGSDL--------VFPCDVASDEQIDALF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  74 KDTLEQLGKLDILVNNAGIT-RD----NLIMRMKEEEFDtvIATNLKGV-FNCVKAATRPMMKqRSGRIINISsvvgVLG 147
Cdd:PRK06997  76 ASLGQHWDGLDGLVHSIGFApREaiagDFLDGLSRENFR--IAHDISAYsFPALAKAALPMLS-DDASLLTLS----YLG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 148 npgqANYVAAKAGVIGLTKAA--------ARELASRGITVNAVAPGFIETDMTDQLPEDVKA-KMLEDI-PLAKLGQPED 217
Cdd:PRK06997 149 ----AERVVPNYNTMGLAKASleasvrylAVSLGPKGIRANGISAGPIKTLAASGIKDFGKIlDFVESNaPLRRNVTIEE 224

                        250       260
                 ....*....|....*....|....*.
gi 568325758 218 VAKTVLFLASADSSYMTGQTLHVDGG 243
Cdd:PRK06997 225 VGNVAAFLLSDLASGVTGEITHVDSG 250
PRK05884 PRK05884
SDR family oxidoreductase;
8-243 3.74e-07

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 49.42  E-value: 3.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVnyAGNEQAAAEVVqqieamgrkaammradvSKAQEADQLVKDT-----LEQL-- 80
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTL--VGARRDDLEVA-----------------AKELDVDAIVCDNtdpasLEEArg 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 ---GKLDILVN------NAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRPMmkqRSGriiniSSVVGVL--GNP 149
Cdd:PRK05884  65 lfpHHLDTIVNvpapswDAGDPRTYSLADTANAWRNALDATVLSAVLT-VQSVGDHL---RSG-----GSIISVVpeNPP 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 150 GQANYVAAKAGVIGLTKAAARELASRGITVNAVAPG-FIET--DMTDQLPEDVKAkmlediplaklgqpeDVAKTVLFLA 226
Cdd:PRK05884 136 AGSAEAAIKAALSNWTAGQAAVFGTRGITINAVACGrSVQPgyDGLSRTPPPVAA---------------EIARLALFLT 200

                        250
                 ....*....|....*..
gi 568325758 227 SADSSYMTGQTLHVDGG 243
Cdd:PRK05884 201 TPAARHITGQTLHVSHG 217
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 5-189 1.87e-06

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: 47.90  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   5 KVALVTGASRGIGRAIALCLAEAGADVAV----NYAGNEQAAAEVVQQIEamgrKAAMMRADVSKAQEADQLVKDTLEQL 80
Cdd:cd09810    2 GTVVITGASSGLGLAAAKALARRGEWHVVmacrDFLKAEQAAQEVGMPKD----SYSVLHCDLASLDSVRQFVDNFRRTG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 GKLDILVNNAGI--TRDNLIMRmKEEEFDTVIATNLKGVFncvkAATRPMMK--QRSG----RIINISSVVG----VLGN 148
Cdd:cd09810   78 RPLDALVCNAAVylPTAKEPRF-TADGFELTVGVNHLGHF----LLTNLLLEdlQRSEnaspRIVIVGSITHnpntLAGN 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568325758 149 PGQANYVAAKAGVIGLTKAA-------------------------ARELASR-----GITVNAVAPGFIET 189
Cdd:cd09810  153 VPPRATLGDLEGLAGGLKGFnsmidggefegakaykdskvcnmltTYELHRRlheetGITFNSLYPGCIAE 223
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 7-183 3.08e-06

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


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 47.55  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGAD--VAVNYAGNE-QAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVkDTLEQLGKL 83
Cdd:cd08952  233 VLVTGGTGALGAHVARWLARRGAEhlVLTSRRGPDaPGAAELVAELTALGARVTVAACDVADRDALAALL-AALPAGHPL 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  84 DILVNNAGITRDNLIMRMKEEEFDTVI------ATNLKgvfncvkAATRPmmkQRSGRIINISSVVGVLGNPGQANYVAA 157
Cdd:cd08952  312 TAVVHAAGVLDDGPLDDLTPERLAEVLrakvagARHLD-------ELTRD---RDLDAFVLFSSIAGVWGSGGQGAYAAA 381

                        170       180
                 ....*....|....*....|....*.
gi 568325758 158 KAGVIGLtkaaARELASRGITVNAVA 183
Cdd:cd08952  382 NAYLDAL----AERRRARGLPATSVA 403
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-246 1.18e-04

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 42.40  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGAS--RGIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAmgrKAAMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK06079   4 ILSGKKIVVMGVAnkRSIAWGCAQAIKDQGATVIYTYQ-NDRMKKSLQKLVDE---EDLLVECDVASDESIERAFATIKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGI----TRDNLIMRMKEEEFDtvIATNLKGV-FNCVKAATRPMMKQRSGrIINISSVVGVLGNPgqaN 153
Cdd:PRK06079  80 RVGKIDGIVHAIAYakkeELGGNVTDTSRDGYA--LAQDISAYsLIAVAKYARPLLNPGAS-IVTLTYFGSERAIP---N 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 154 YvaakaGVIGLTKAA--------ARELASRGITVNAVAPGFIETDMT------DQLPEDVKAKMLEDIPLAKlgqpEDVA 219
Cdd:PRK06079 154 Y-----NVMGIAKAAlessvrylARDLGKKGIRVNAISAGAVKTLAVtgikghKDLLKESDSRTVDGVGVTI----EEVG 224

                        250       260
                 ....*....|....*....|....*..
gi 568325758 220 KTVLFLASADSSYMTGQTLHVDGGMYM 246
Cdd:PRK06079 225 NTAAFLLSDLSTGVTGDIIYVDKGVHL 251
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 2-244 2.23e-04

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 41.68  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   2 LTGKVALVTGA--SRGIGRAIALCLAEAGADVAVN-----------------------------------YAGNE--QAA 42
Cdd:PLN02730   7 LRGKRAFIAGVadDNGYGWAIAKALAAAGAEILVGtwvpalnifetslrrgkfdesrklpdgslmeitkvYPLDAvfDTP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  43 AEVVQQIEAMGRKAAMMRADVSKAQEAdqlVKdtlEQLGKLDILVNNagitrdnliMRMKEEEFDTVIATNLKGVFNCVK 122
Cdd:PLN02730  87 EDVPEDVKTNKRYAGSSNWTVQEVAES---VK---ADFGSIDILVHS---------LANGPEVTKPLLETSRKGYLAAIS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 123 AATRPM--MKQRSGRIINissvvgvlgnPGQA----NYVA--------------AKAGVIGLTKAAARElASR--GITVN 180
Cdd:PLN02730 152 ASSYSFvsLLQHFGPIMN----------PGGAsislTYIAseriipgygggmssAKAALESDTRVLAFE-AGRkyKIRVN 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758 181 -----------AVAPGFIEtDMTDQlpedvkakMLEDIPLAKLGQPEDVAKTVLFLASADSSYMTGQTLHVDGGM 244
Cdd:PLN02730 221 tisagplgsraAKAIGFID-DMIEY--------SYANAPLQKELTADEVGNAAAFLASPLASAITGATIYVDNGL 286
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
 8-203 3.41e-04

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


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 41.10  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEA------------GADVAvnyagneqAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVkD 75
Cdd:cd08956  197 LITGGTGTLGALLARHLVTEhgvrhlllvsrrGPDAP--------GAAELVAELAALGAEVTVAACDVADRAALAALL-A 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  76 TLEQLGKLDILVNNAGITRDNLIMRMKEEEFDTVIATNLKGVFNcVKAATRPMmkqRSGRIINISSVVGVLGNPGQANYV 155
Cdd:cd08956  268 AVPADHPLTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWH-LHELTRDL---DLAAFVLFSSAAGVLGSPGQANYA 343

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAgvigLTKAAARELASRGITVNAVAPGFIE--TDMTDQLPEDVKAKM 203
Cdd:cd08956  344 AANA----FLDALAQHRRARGLPATSLAWGLWAqaSGMTAHLSDADLARL 389
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
1-243 5.43e-04

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 40.38  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   1 MLTGKVALVTGASR--GIGRAIALCLAEAGADVAVNYAgNEQAAAEVVQQIEAMGRKAaMMRADVSKAQEADQLVKDTLE 78
Cdd:PRK06603   5 LLQGKKGLITGIANnmSISWAIAQLAKKHGAELWFTYQ-SEVLEKRVKPLAEEIGCNF-VSELDVTNPKSISNLFDDIKE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  79 QLGKLDILVNNAGITRDNlimRMKEEEFDTviatNLKGVFNCVKAATRPMMK-QRSGRII--NISSVVgVLGNPGqANYV 155
Cdd:PRK06603  83 KWGSFDFLLHGMAFADKN---ELKGRYVDT----SLENFHNSLHISCYSLLElSRSAEALmhDGGSIV-TLTYYG-AEKV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758 156 AAKAGVIGLTKAA--------ARELASRGITVNAVAPGFIETDMTDQLPEdvKAKMLED----IPLAKLGQPEDVAKTVL 223
Cdd:PRK06603 154 IPNYNVMGVAKAAleasvkylANDMGENNIRVNAISAGPIKTLASSAIGD--FSTMLKShaatAPLKRNTTQEDVGGAAV 231

                        250       260
                 ....*....|....*....|
gi 568325758 224 FLASADSSYMTGQTLHVDGG 243
Cdd:PRK06603 232 YLFSELSKGVTGEIHYVDCG 251
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 7-187 1.15e-03

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: 39.58  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   7 ALVTGASRGIGRAIALCLAEAGADVAV------NYAGNEQAAAEVVQqieamgrkaammrADVSKAQEADQLVKDTleql 80
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQGYRVRAlvrsgsDAVLLDGLPVEVVE-------------GDLTDAASLAAAMKGC---- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  81 gklDILVNNAGITRDNlimRMKEEEFDtviATNLKGVFNCVKAAtrpmMKQRSGRIINISSvVGVLG-NPGQA------- 152
Cdd:cd05228   64 ---DRVFHLAAFTSLW---AKDRKELY---RTNVEGTRNVLDAA----LEAGVRRVVHTSS-IAALGgPPDGRidettpw 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568325758 153 -------NYVAAKAgvigLTKAAARELASRGITVNAVAPGFI 187
Cdd:cd05228  130 nerpfpnDYYRSKL----LAELEVLEAAAEGLDVVIVNPSAV 167
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
 8-156 1.97e-03

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 38.50  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEvvQQIEAMGRKAAMMRA---DVSKAQeADQLVKDTLEQLGKLD 84
Cdd:cd05263    2 FVTGGTGFLGRHLVKRLLENGFKVLVLVRSESLGEAH--ERIEEAGLEADRVRVlegDLTQPN-LGLSAAASRELAGKVD 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568325758  85 ILVNNAGITRDNLimrmkeeEFDTVIATNLKGVFNCVKAATRpmmkQRSGRIINISSvVGVLGNPGQANYVA 156
Cdd:cd05263   79 HVIHCAASYDFQA-------PNEDAWRTNIDGTEHVLELAAR----LDIQRFHYVST-AYVAGNREGNIRET 138
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 7-226 2.39e-03

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: 38.05  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758    7 ALVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAaevvqqiEAMGRKAAMMRADVSKAQEADQLVKDTleqlgKLDIL 86
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASN-------TARLADLRFVEGDLTDRDALEKLLADV-----RPDAV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   87 VNNAGIT--RDNLimrmkeEEFDTVIATNLKGVFNCVKAATrpmmKQRSGRIINISSvVGVLGNPGQAN----------- 153
Cdd:pfam01370  69 IHLAAVGgvGASI------EDPEDFIEANVLGTLNLLEAAR----KAGVKRFLFASS-SEVYGDGAEIPqeettltgpla 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758  154 ----YVAAKAGVIGLTKAAARELASRGITV---NAVAPGFIETDMTDQLPEDVkAKMLEDIPLAKLGQ---------PED 217
Cdd:pfam01370 138 pnspYAAAKLAGEWLVLAYAAAYGLRAVILrlfNVYGPGDNEGFVSRVIPALI-RRILEGKPILLWGDgtqrrdflyVDD 216


                  ....*....
gi 568325758  218 VAKTVLFLA 226
Cdd:pfam01370 217 VARAILLAL 225
PLN00015 PLN00015
protochlorophyllide reductase
 8-153 3.08e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 38.15  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568325758   8 LVTGASRGIGRAIALCLAEAGADVAVNYAGNEQAAAEVVQQIEAMGRKAAMMRADVSKAQEADQLVkDTLEQLGK-LDIL 86
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACRDFLKAERAAKSAGMPKDSYTVMHLDLASLDSVRQFV-DNFRRSGRpLDVL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568325758  87 VNNAGITRDNLIM-RMKEEEFDTVIATNLKGVFNCVKAATRPMMKQ--RSGRIINISSVVG----VLGN-PGQAN 153
Cdd:PLN00015  80 VCNAAVYLPTAKEpTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSdyPSKRLIIVGSITGntntLAGNvPPKAN 154
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH