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Conserved domains on  [gi|446931279|ref|WP_001008535|]
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MULTISPECIES: 3-oxoacyl-ACP reductase FabG [Enterobacteriaceae]

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

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List of domain hits

Name Accession Description Interval E-value
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
1-244 3.08e-139

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


:

Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 390.32  E-value: 3.08e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAE 76
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVvINYASSEAGAEALVAEIGALGGKALAvqgDVSDAESVERAVDEAKAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK05557  81 FGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLH 240

                 ....*...
gi 446931279 237 VNGGMYMV 244
Cdd:PRK05557 241 VNGGMVMG 248
 
Name Accession Description Interval E-value
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
1-244 3.08e-139

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 390.32  E-value: 3.08e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAE 76
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVvINYASSEAGAEALVAEIGALGGKALAvqgDVSDAESVERAVDEAKAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK05557  81 FGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLH 240

                 ....*...
gi 446931279 237 VNGGMYMV 244
Cdd:PRK05557 241 VNGGMVMG 248
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
6-242 1.98e-136

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: 383.05  E-value: 1.98e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD---YLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEeikALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMY 242
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
8-242 1.10e-127

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: 360.76  E-value: 1.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    8 ALVTGASRGIGRAIAETLAARGAKVIGT-ATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITyRSSEEGAEEVVEELKALGvkaLGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446931279  164 SLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMY 242
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3-243 2.59e-104

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: 302.09  E-value: 2.59e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGgraLAVAADVTDEAAVEALVAAAVAAFGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:COG1028   84 LDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAL--SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:COG1028  164 GLTRSLALELAPRGIRVNAVAPGPIDTPMTRALlgAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAV 243

                 ....*.
gi 446931279 238 NGGMYM 243
Cdd:COG1028  244 DGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
15-241 2.83e-75

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: 228.08  E-value: 2.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   15 RGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM-LNVTDPASIESVLEKIRAEFGEVDILVNNAGITR-- 91
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLpCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFAPkl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   92 DNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVAS 171
Cdd:pfam13561  86 KGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGP 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446931279  172 RGITVNVVAPGFIETDMTRALS--DDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:pfam13561 164 RGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
9-185 9.97e-18

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: 77.91  E-value: 9.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279     9 LVTGASRGIGRAIAETLAARGAK---VIG-TATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGEVD 81
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlvLLSrSGPDAPGAAALLAELEAAGARVTVvacDVADRDALAAVLAAIPAVEGPLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKkrhgRIITIGSVVGTMGNGGQANYAAAKAgligF 161
Cdd:smart00822  84 GVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLD----FFVLFSSIAGVLGSPGQANYAAANA----F 155
                          170       180
                   ....*....|....*....|....
gi 446931279   162 SKSLAREVASRGITVNVVAPGFIE 185
Cdd:smart00822 156 LDALAEYRRARGLPALSIAWGAWA 179
 
Name Accession Description Interval E-value
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
1-244 3.08e-139

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 390.32  E-value: 3.08e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAE 76
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVvINYASSEAGAEALVAEIGALGGKALAvqgDVSDAESVERAVDEAKAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK05557  81 FGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLH 240

                 ....*...
gi 446931279 237 VNGGMYMV 244
Cdd:PRK05557 241 VNGGMVMG 248
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
6-242 1.98e-136

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: 383.05  E-value: 1.98e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD---YLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEeikALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMY 242
Cdd:cd05333  161 KSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
8-242 1.10e-127

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: 360.76  E-value: 1.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    8 ALVTGASRGIGRAIAETLAARGAKVIGT-ATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITyRSSEEGAEEVVEELKALGvkaLGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446931279  164 SLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMY 242
Cdd:TIGR01830 161 SLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-243 4.15e-121

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 344.45  E-value: 4.15e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGgeaRVLVFDVSDEAAVRALIEAAVEAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK05653  81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK05653 161 VIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPV 240

                 ....*.
gi 446931279 238 NGGMYM 243
Cdd:PRK05653 241 NGGMYM 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3-243 2.59e-104

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: 302.09  E-value: 2.59e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGgraLAVAADVTDEAAVEALVAAAVAAFGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:COG1028   84 LDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAL--SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:COG1028  164 GLTRSLALELAPRGIRVNAVAPGPIDTPMTRALlgAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAV 243

                 ....*.
gi 446931279 238 NGGMYM 243
Cdd:COG1028  244 DGGLTA 249
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-244 3.27e-103

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 299.48  E-value: 3.27e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAIS---DYLGANGKGLMLNVTDPASIESVLEKIRAE 76
Cdd:PRK12825   2 GSLMGRVALVTGAARGLGRAIALRLARAGADVvVHYRSDEEAAEELVeavEALGRRAQAVQADVTDKAALEAAVAAAVER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK12825  82 FGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIE 241

                 ....*...
gi 446931279 237 VNGGMYMV 244
Cdd:PRK12825 242 VTGGVDVI 249
PRK12826 PRK12826
SDR family oxidoreductase;
3-243 1.29e-91

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 269.86  E-value: 1.29e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK12826   4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGgkaRARQVDVRDRAALKAAVAAGVEDFGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVG-TMGNGGQANYAAAKAGL 158
Cdd:PRK12826  84 LDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGpRVGYPGLAHYAASKAGL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQ-RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK12826 164 VGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQwAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLPV 243

                 ....*.
gi 446931279 238 NGGMYM 243
Cdd:PRK12826 244 DGGATL 249
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-243 1.21e-90

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 267.40  E-value: 1.21e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGA----QAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK12824  83 ILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:PRK12824 163 TKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISINGGL 242

                 ..
gi 446931279 242 YM 243
Cdd:PRK12824 243 YM 244
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
6-243 3.70e-90

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: 266.22  E-value: 3.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    6 KIALVTGASRGIGRAIAETLAARGAKVIGT-ATSENGAQAISDYLGANGKGLMLNVTDPASIES---VLEKIRAEFGEVD 81
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANcGPNEERAEAWLQEQGALGFDFRVVEGDVSSFESckaAVAKVEAELGPVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:TIGR01829  81 VLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  162 SKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:TIGR01829 161 TKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSINGGL 240

                  ..
gi 446931279  242 YM 243
Cdd:TIGR01829 241 YM 242
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
1-244 1.83e-87

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 259.46  E-value: 1.83e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK12936   2 FDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK12936  82 DILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK12936 162 FSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVNGG 241

                 ....
gi 446931279 241 MYMV 244
Cdd:PRK12936 242 MAMI 245
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
8-238 1.31e-84

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: 251.43  E-value: 1.31e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDY--LGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIeaLGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:cd05233   81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446931279 166 AREVASRGITVNVVAPGFIETDMTRALSDDQRAG-ILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVN 238
Cdd:cd05233  161 ALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKeLAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-242 2.98e-80

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 240.90  E-value: 2.98e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAE 76
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVvIAYDINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK05565  81 FGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK05565 161 AVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIIT 240

                 ....*.
gi 446931279 237 VNGGMY 242
Cdd:PRK05565 241 VDGGWT 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
15-241 2.83e-75

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: 228.08  E-value: 2.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   15 RGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM-LNVTDPASIESVLEKIRAEFGEVDILVNNAGITR-- 91
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVLpCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFAPkl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   92 DNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVAS 171
Cdd:pfam13561  86 KGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGP 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446931279  172 RGITVNVVAPGFIETDMTRALS--DDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:pfam13561 164 RGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
FabG-like PRK07231
SDR family oxidoreductase;
1-241 1.58e-71

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 218.93  E-value: 1.58e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFG 78
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGRAIAVaaDVSDEADVEAAVAAALERFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDN-LLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK07231  81 SVDILVNNAGTTHRNgPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRAL----SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGE 233
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFmgepTPENRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGV 240

                 ....*...
gi 446931279 234 TLHVNGGM 241
Cdd:PRK07231 241 TLVVDGGR 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
6-196 5.79e-71

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 215.56  E-value: 5.79e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGgkaLFIQGDVTDRAQVKALVEQAVERLGRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 446931279  163 KSLAREVASRGITVNVVAPGFIETDMTRALSDDQ 196
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
2-241 6.10e-71

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: 217.23  E-value: 6.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIG---TATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:cd05347    2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVInsrNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05347   82 KIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:cd05347  162 AGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEfnDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIF 241

                 ....*
gi 446931279 237 VNGGM 241
Cdd:cd05347  242 VDGGW 246
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
3-243 2.01e-70

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 216.02  E-value: 2.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLMLNVTDPASIES---VLEKIRAEFG 78
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVvINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDanrLVEEAVNHFG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK12935  84 KVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDeAAYITGETLHVN 238
Cdd:PRK12935 164 LGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRD-GAYITGQQLNIN 242

                 ....*
gi 446931279 239 GGMYM 243
Cdd:PRK12935 243 GGLYM 247
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
1-225 3.09e-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: 3.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:COG4221    1 MSDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:COG4221   81 DVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASD 225
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQ 225
PRK12827 PRK12827
short chain dehydrogenase; Provisional
5-241 1.40e-67

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 208.81  E-value: 1.40e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTA----TSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAAGgkaLGLAFDVRDFAATRAALDAGVEEF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMK-KRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK12827  86 GRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVNYAASKA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRalSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK12827 166 GLIGLTKTLANELAPRGITVNAVAPGAINTPMAD--NAAPTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASYVTGQVIP 243

                 ....*
gi 446931279 237 VNGGM 241
Cdd:PRK12827 244 VDGGF 248
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
6-243 8.05e-67

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 206.79  E-value: 8.05e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGtATSENGAQAIS----------DYLGANGkglmlNVTDPASIESVLEKIRA 75
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVA-GCGPNSPRRVKwledqkalgfDFIASEG-----NVGDWDSTKAAFDKVKA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  76 EFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAK 155
Cdd:PRK12938  78 EVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 156 AGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:PRK12938 158 AGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADF 237

                 ....*...
gi 446931279 236 HVNGGMYM 243
Cdd:PRK12938 238 SLNGGLHM 245
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-239 2.01e-66

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 212.00  E-value: 2.01e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGA--QAISDYLGanGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK08261 209 AGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGEalAAVANRVG--GTALALDITAPDAPARIAEHLAERHGGLD 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK08261 287 IVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGL 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIETDMTralsddqragilAQVP-----AGRL------GG-AQEIANAVAFLASDEAAY 229
Cdd:PRK08261 367 VQALAPLLAERGITINAVAPGFIETQMT------------AAIPfatreAGRRmnslqqGGlPVDVAETIAWLASPASGG 434
                        250
                 ....*....|
gi 446931279 230 ITGETLHVNG 239
Cdd:PRK08261 435 VTGNVVRVCG 444
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-201 2.33e-65

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 203.18  E-value: 2.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM---LNVTDPASIESVLEKIRAEF 77
Cdd:COG0300    1 MSLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEvvaLDVTDPDAVAALAEAVLARF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:COG0300   81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGIL 201
Cdd:COG0300  161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL 204
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
4-241 3.83e-65

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: 202.61  E-value: 3.83e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGE 79
Cdd:cd05358    2 KGKVALVTGASSGIGKAIAIRLATAGANVvVNYRSKEDAAEEVVEEIKAVGGKAIAvqaDVSKEEDVVALFQSAIKEFGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMK-KRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05358   82 LDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIPWPGHVNYAASKGGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDD--QRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:cd05358  162 KMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDpeQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTTLF 241

                 ....*
gi 446931279 237 VNGGM 241
Cdd:cd05358  242 VDGGM 246
PRK12939 PRK12939
short chain dehydrogenase; Provisional
2-243 2.99e-63

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 197.89  E-value: 2.99e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK---GLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK12939   4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGrahAIAADLADPASVQRFFDAAAAALG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK12939  84 GLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRAL-SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK12939 164 IGMTRSLARELGGRGITVNAIAPGLTATEATAYVpADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLPV 243

                 ....*.
gi 446931279 238 NGGMYM 243
Cdd:PRK12939 244 NGGFVM 249
kduD TIGR01832
2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase ...
2-240 4.49e-63

2-deoxy-D-gluconate 3-dehydrogenase; This model describes 2-deoxy-D-gluconate 3-dehydrogenase (also called 2-keto-3-deoxygluconate oxidoreductase), a member of the family of short-chain-alcohol dehydrogenases (pfam00106). This protein has been characterized in Erwinia chrysanthemi as an enzyme of pectin degradation. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 188170 [Multi-domain]  Cd Length: 248  Bit Score: 197.29  E-value: 4.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSE-NGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:TIGR01832   2 SLEGKVALVTGANTGLGQGIAVGLAEAGADIVGAGRSEpSETQQQVEALGRRFLSLTADLSDIEAIKALVDSAVEEFGHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:TIGR01832  82 DILVNNAGIIRRADAEEFSEKDWDDVMNVNLKSVFFLTQAAAKHFLKQgRGGKIINIASMLSFQGGIRVPSYTASKHAVA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  160 GFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:TIGR01832 162 GLTKLLANEWAAKGINVNAIAPGYMATNNTQALRADEDrnAAILERIPAGRWGTPDDIGGPAVFLASSASDYVNGYTLAV 241

                  ...
gi 446931279  238 NGG 240
Cdd:TIGR01832 242 DGG 244
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
1-240 9.36e-62

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 193.95  E-value: 9.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQaisdylGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQE------DYPFATFVLDVSDAAAVAQVCQRLLAETGPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK08220  78 DVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR------AGILAQ----VPAGRLGGAQEIANAVAFLASDEAAYI 230
Cdd:PRK08220 158 LAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDgeqqviAGFPEQfklgIPLGKIARPQEIANAVLFLASDLASHI 237
                        250
                 ....*....|
gi 446931279 231 TGETLHVNGG 240
Cdd:PRK08220 238 TLQDIVVDGG 247
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3-240 4.28e-61

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: 192.55  E-value: 4.28e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKV----IGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVaiiyNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQ--ANYAAAKA 156
Cdd:cd05352   86 KIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNRPQpqAAYNASKA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:cd05352  166 AVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDLI 245

                 ....
gi 446931279 237 VNGG 240
Cdd:cd05352  246 IDGG 249
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-240 5.34e-61

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 192.26  E-value: 5.34e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSEN--GAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNwdETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK06935  92 IDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK06935 172 GLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNrnDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILAV 251

                 ...
gi 446931279 238 NGG 240
Cdd:PRK06935 252 DGG 254
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
2-241 7.98e-61

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 192.20  E-value: 7.98e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAK-VIGTATSENGAQAISDY--LGANGKGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATiVFNDINQELVDKGLAAYreLGIEAHGYVCDVTDEDGVQAMVSQIEKEVG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK07097  87 VIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAG--------ILAQVPAGRLGGAQEIANAVAFLASDEAAYI 230
Cdd:PRK07097 167 KMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGsrhpfdqfIIAKTPAARWGDPEDLAGPAVFLASDASNFV 246
                        250
                 ....*....|.
gi 446931279 231 TGETLHVNGGM 241
Cdd:PRK07097 247 NGHILYVDGGI 257
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
2-243 8.33e-61

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 192.02  E-value: 8.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDYLGANGK--GLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADlNDEAAAAAAEALQKAGGKaiGVAMDVTDEEAINAGIDYAVETFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK12429  81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAG------------ILAQVPAGRLGGAQEIANAVAFLASDE 226
Cdd:PRK12429 161 IGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDLAKErgiseeevledvLLPLVPQKRFTTVEEIADYALFLASFA 240
                        250
                 ....*....|....*..
gi 446931279 227 AAYITGETLHVNGGMYM 243
Cdd:PRK12429 241 AKGVTGQAWVVDGGWTA 257
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
4-240 1.86e-60

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: 190.56  E-value: 1.86e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGE 79
Cdd:cd05362    2 AGKVALVTGASRGIGRAIAKRLARDGASVvVNYASSKAAAEEVVAEIEAAGGKAIAvqaDVSDPSQVARLFDAAEKAFGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:cd05362   82 VDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAL-SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVN 238
Cdd:cd05362  160 AFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGkTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRAN 239

                 ..
gi 446931279 239 GG 240
Cdd:cd05362  240 GG 241
PRK12829 PRK12829
short chain dehydrogenase; Provisional
5-240 2.00e-60

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 191.04  E-value: 2.00e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG-AQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:PRK12829  11 GLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAAlAATAARLPGAKVTATVADVADPAQVERVFDTAVERFGGLDVL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGIT-RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGR-IITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK12829  91 VNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTPYAASKWAVVGL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIETDMTRALSDDQ-----------RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYI 230
Cdd:PRK12829 171 VKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARaqqlgigldemEQEYLEKISLGRMVEPEDIAATALFLASPAARYI 250
                        250
                 ....*....|
gi 446931279 231 TGETLHVNGG 240
Cdd:PRK12829 251 TGQAISVDGN 260
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
2-241 1.34e-59

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 188.62  E-value: 1.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSEN---GAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEeleEAAAHLEALGIDALWIAADVADEADIERLAEETLERFG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKR-HGRIITIGSVVGTMGNG----GQANYAA 153
Cdd:PRK08213  89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRgYGRIINVASVAGLGGNPpevmDTIAYNT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGE 233
Cdd:PRK08213 169 SKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASKHITGQ 248

                 ....*...
gi 446931279 234 TLHVNGGM 241
Cdd:PRK08213 249 ILAVDGGV 256
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
5-242 3.75e-59

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: 187.48  E-value: 3.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATS-ENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEVD 81
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNrENLERAASELRAGGAGVLAVvaDLTDPEDIDRLVEKAGDAFGRVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGS--VVGTMGNGGQANyaAAKAGLI 159
Cdd:cd05344   81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSltVKEPEPNLVLSN--VARAGLI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAL-----------SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAA 228
Cdd:cd05344  159 GLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLlearaekegisVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKAS 238
                        250
                 ....*....|....
gi 446931279 229 YITGETLHVNGGMY 242
Cdd:cd05344  239 YITGQAILVDGGLT 252
PRK06841 PRK06841
short chain dehydrogenase; Provisional
2-240 1.10e-58

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 186.40  E-value: 1.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRID 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK06841  92 ILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGM 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGIL-AQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK06841 172 TKVLALEWGPYGITVNAISPTVVLTELGKKAWAGEKGERAkKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLVIDGG 251
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
8-240 2.69e-58

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: 184.86  E-value: 2.69e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAIS---DYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVvINYRKSKDAAAEVAaeiEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:cd05359   81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446931279 164 SLAREVASRGITVNVVAPGFIETDMTRAL--SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:cd05359  161 YLAVELGPRGIRVNAVSPGVIDTDALAHFpnREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDGG 239
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-243 1.97e-57

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 183.24  E-value: 1.97e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG---AQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK08217   1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKleeAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKD---------EEWNDIIETNLSSVFRLSKAVMRAMMK-KRHGRIITIGSVvGTMGNGG 147
Cdd:PRK08217  81 GQLNGLINNAGILRDGLLVKAKDgkvtskmslEQFQSVIDVNLTGVFLCGREAAAKMIEsGSKGVIINISSI-ARAGNMG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 148 QANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEa 227
Cdd:PRK08217 160 QTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTVRFIIEND- 238
                        250
                 ....*....|....*.
gi 446931279 228 aYITGETLHVNGGMYM 243
Cdd:PRK08217 239 -YVTGRVLEIDGGLRL 253
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
8-240 4.61e-57

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: 181.90  E-value: 4.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAngkgLMLNVTDPASIESVLEKIRAEFGEVDILVNNA 87
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRL----TPLDVADAAAVREVCSRLLAEHGPIDALVNCA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 GITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAR 167
Cdd:cd05331   77 GVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 168 EVASRGITVNVVAPGFIETDMTRALSDDQR------AGILAQ----VPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:cd05331  157 ELAPYGVRCNVVSPGSTDTAMQRTLWHDEDgaaqviAGVPEQfrlgIPLGKIAQPADIANAVLFLASDQAGHITMHDLVV 236

                 ...
gi 446931279 238 NGG 240
Cdd:cd05331  237 DGG 239
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
9-241 9.52e-57

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


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 180.87  E-value: 9.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    9 LVTGASRGIGRAIAETLAARGAKVI-----GTATSENGAQAISDyLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:TIGR01831   2 LVTGASRGIGRAIANQLAADGFNIGvhyhsDAAGAQETLNAIVA-NGGNGRLLSFDVADRVACREVLEADIAQHGAYYGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHG-RIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:TIGR01831  81 VLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARQGgRIITLASVSGVMGNRGQVNYSAAKAGLIGAT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446931279  163 KSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGiLAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:TIGR01831 161 KALAIELAKRKITVNCIAPGLIDTGMIAMEESALKEA-LSMVPMKRMGQPEEVAGLASFLMSDIAGYVTRQVISVNGGM 238
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
6-243 1.57e-56

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: 180.73  E-value: 1.57e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVvVNYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAgiTRDNLLMRMK-----DEEWNDI---IETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:cd05349   81 NNA--LIDFPFDPDQrktfdTIDWEDYqqqLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFI-ETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:cd05349  159 ALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNL 238

                 ....*...
gi 446931279 236 HVNGGMYM 243
Cdd:cd05349  239 VVDGGLVM 246
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
4-240 9.46e-56

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 179.23  E-value: 9.46e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENgAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK08226   5 TGKTALITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELCGRGhrcTAVVADVRDPASVAAAIKRAKEKEGRI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTM-GNGGQANYAAAKAGLI 159
Cdd:PRK08226  84 DILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMvADPGETAYALTKAAIV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRALS------DDQRA--GILAQVPAGRLGGAQEIANAVAFLASDEAAYIT 231
Cdd:PRK08226 164 GLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIArqsnpeDPESVltEMAKAIPLRRLADPLEVGELAAFLASDESSYLT 243

                 ....*....
gi 446931279 232 GETLHVNGG 240
Cdd:PRK08226 244 GTQNVIDGG 252
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
4-241 3.01e-55

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 177.64  E-value: 3.01e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK08085   8 AGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGikaHAAPFNVTHKQEVEAAIEHIEKDIGPI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK08085  88 DVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAVKM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVN 238
Cdd:PRK08085 168 LTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAftAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVD 247

                 ...
gi 446931279 239 GGM 241
Cdd:PRK08085 248 GGM 250
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
5-240 1.32e-54

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: 176.10  E-value: 1.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDYLGANGKGLML----NVTDPASIESVLEKIRAEFGE 79
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKHGVKVLyhgaDLSKPAAIEDMVAYAQRQFGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:cd08940   82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTR----ALSDD--------QRAGILAQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:cd08940  162 GLTKVVALETAGTGVTCNAICPGWVLTPLVEkqisALAQKngvpqeqaARELLLEKQPSKQFVTPEQLGDTAVFLASDAA 241
                        250
                 ....*....|...
gi 446931279 228 AYITGETLHVNGG 240
Cdd:cd08940  242 SQITGTAVSVDGG 254
PRK09242 PRK09242
SDR family oxidoreductase;
2-241 2.46e-54

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 175.32  E-value: 2.46e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD-----YLGANGKGLMLNVTDPASIESVLEKIRAE 76
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDelaeeFPEREVHGLAADVSDDEDRRAILDWVEDH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK09242  86 WDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:PRK09242 166 ALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDyyEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQC 245

                 ....*..
gi 446931279 235 LHVNGGM 241
Cdd:PRK09242 246 IAVDGGF 252
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-240 7.88e-54

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 173.23  E-value: 7.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENgaqaisDYLGANGKGLMLNVTDPasiesvLEKIRAEFGEV 80
Cdd:PRK06550   1 QEFMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDK------PDLSGNFHFLQLDLSDD------LEPLFDWVPSV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRD-NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK06550  69 DILCNTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRA-LSDDQRAGILA-QVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK06550 149 GFTKQLALDYAKDGIQVFGIAPGAVKTPMTAAdFEPGGLADWVArETPIKRWAEPEEVAELTLFLASGKADYMQGTIVPI 228

                 ...
gi 446931279 238 NGG 240
Cdd:PRK06550 229 DGG 231
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
6-241 9.88e-54

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: 173.88  E-value: 9.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRA--MMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:cd08945   84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRAL-----------SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAY 229
Cdd:cd08945  164 FTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAAA 243
                        250
                 ....*....|..
gi 446931279 230 ITGETLHVNGGM 241
Cdd:cd08945  244 VTAQALNVCGGL 255
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
5-240 1.47e-53

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: 172.95  E-value: 1.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:cd05341    5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITrdnLLMRMKD---EEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:cd05341   85 NNAGIL---TGGTVETttlEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASR--GITVNVVAPGFIETDMTRALSDDQRA-GILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVN 238
Cdd:cd05341  162 TKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEmGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSELVVD 241

                 ..
gi 446931279 239 GG 240
Cdd:cd05341  242 GG 243
PRK07063 PRK07063
SDR family oxidoreductase;
4-240 7.69e-53

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 171.39  E-value: 7.69e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG-----LMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK07063   6 AGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGarvlaVPADVTDAASVAAAVAAAEEAFG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGIT--RDNLlmRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK07063  86 PLDVLVNNAGINvfADPL--AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQ------RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYI 230
Cdd:PRK07063 164 GLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQpdpaaaRAETLALQPMKRIGRPEEVAMTAVFLASDEAPFI 243
                        250
                 ....*....|
gi 446931279 231 TGETLHVNGG 240
Cdd:PRK07063 244 NATCITIDGG 253
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
3-243 8.36e-53

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: 171.23  E-value: 8.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATS----ENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKpevlEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGitrDNLLM---RMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAA 154
Cdd:cd05369   81 KIDILINNAA---GNFLApaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETD--MTRALSDDQ-RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYIT 231
Cdd:cd05369  158 KAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTegMERLAPSGKsEKKMIERVPLGRLGTPEEIANLALFLLSDAASYIN 237
                        250
                 ....*....|..
gi 446931279 232 GETLHVNGGMYM 243
Cdd:cd05369  238 GTTLVVDGGQWL 249
PRK06124 PRK06124
SDR family oxidoreductase;
4-241 9.59e-53

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 171.05  E-value: 9.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG---LMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK06124  10 AGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAaeaLAFDIADEEAVAAAFARIDAEHGRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK06124  90 DILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAG--ILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVN 238
Cdd:PRK06124 170 LMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGpwLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAVD 249

                 ...
gi 446931279 239 GGM 241
Cdd:PRK06124 250 GGY 252
PRK06701 PRK06701
short chain dehydrogenase; Provisional
4-243 1.13e-52

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 172.14  E-value: 1.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGE 79
Cdd:PRK06701  45 KGKVALITGGDSGIGRAVAVLFAKEGADIaIVYLDEHEDANETKQRVEKEGVKCLLipgDVSDEAFCKDAVEETVRELGR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRD-NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK06701 125 LDILVNNAAFQYPqQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSATKGAI 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRA-LSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK06701 203 HAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSdFDEEKVSQFGSNTPMQRPGQPEELAPAYVFLASPDSSYITGQMLHV 282

                 ....*.
gi 446931279 238 NGGMYM 243
Cdd:PRK06701 283 NGGVIV 288
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
2-243 1.37e-52

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 170.85  E-value: 1.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK---GLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGkaiGVAMDVTNEDAVNAGIDKVAERFG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMK-KRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK13394  84 SVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHEASPLKSAYVTAKHG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQ--RAGI----------LAQVPAGRLGGAQEIANAVAFLASD 225
Cdd:PRK13394 164 LLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQakELGIseeevvkkvmLGKTVDGVFTTVEDVAQTVLFLSSF 243
                        250
                 ....*....|....*...
gi 446931279 226 EAAYITGETLHVNGGMYM 243
Cdd:PRK13394 244 PSAALTGQSFVVSHGWFM 261
PRK12743 PRK12743
SDR family oxidoreductase;
6-241 2.43e-52

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 170.21  E-value: 2.43e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKG---LMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRSHGVRaeiRQLDLSDLPEGAQALDKLIQRLGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHEHTPLPGASAYTAAKHALGG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK12743 163 LTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVDGG 242

                 .
gi 446931279 241 M 241
Cdd:PRK12743 243 F 243
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
2-241 3.62e-52

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: 169.55  E-value: 3.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK---GLMLNVTDPASIESVLEKIRAEFG 78
Cdd:cd05329    3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFkveGSVCDVSSRSERQELMDTVASHFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 E-VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:cd05329   83 GkLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:cd05329  163 LNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKEnlDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQII 242

                 ....*.
gi 446931279 236 HVNGGM 241
Cdd:cd05329  243 AVDGGL 248
PRK06484 PRK06484
short chain dehydrogenase; Validated
1-240 6.98e-52

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 175.81  E-value: 6.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK06484   1 SKAQSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNL--LMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGR-IITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK06484  81 DVLVNNAGVTDPTMtaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDD---QRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:PRK06484 161 VISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAgklDPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGST 240

                 ....*.
gi 446931279 235 LHVNGG 240
Cdd:PRK06484 241 LVVDGG 246
PRK06172 PRK06172
SDR family oxidoreductase;
1-240 1.07e-51

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 168.39  E-value: 1.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVI----GTATSENGAQAISDylgANGKGLML--NVTDPASIESVLEKIR 74
Cdd:PRK06172   3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVvadrDAAGGEETVALIRE---AGGEALFVacDVTRDAEVKALVEQTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  75 AEFGEVDILVNNAGITRDN-LLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAA 153
Cdd:PRK06172  80 AAYGRLDYAFNNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALS---DDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYI 230
Cdd:PRK06172 160 SKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYeadPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGASFT 239
                        250
                 ....*....|
gi 446931279 231 TGETLHVNGG 240
Cdd:PRK06172 240 TGHALMVDGG 249
PRK06523 PRK06523
short chain dehydrogenase; Provisional
2-242 1.51e-51

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 168.16  E-value: 1.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDYLGANgkglmlnVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTTArSRPDDLPEGVEFVAAD-------LTTAEGCAAVARAVLERLGGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNL--LMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTM-GNGGQANYAAAKAG 157
Cdd:PRK06523  79 DILVHVLGGSSAPAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLpLPESTTAYAAAKAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDD--QRAGI------------LAQVPAGRLGGAQEIANAVAFLA 223
Cdd:PRK06523 159 LSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERlaEAAGTdyegakqiimdsLGGIPLGRPAEPEEVAELIAFLA 238
                        250
                 ....*....|....*....
gi 446931279 224 SDEAAYITGETLHVNGGMY 242
Cdd:PRK06523 239 SDRAASITGTEYVIDGGTV 257
PRK07577 PRK07577
SDR family oxidoreductase;
6-240 1.60e-51

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 167.21  E-value: 1.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSengaqAISDYlgaNGKGLMLNVTDPASIESVLEKIRAEFGeVDILVN 85
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARS-----AIDDF---PGELFACDLADIEQTAATLAQINEIHP-VDAIVN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVgTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:PRK07577  75 NVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSALVGCTRTW 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446931279 166 AREVASRGITVNVVAPGFIETDM---TRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK07577 154 ALELAEYGITVNAVAPGPIETELfrqTRPVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDGG 231
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
2-240 1.00e-50

(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: 165.96  E-value: 1.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVI---------GTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEK 72
Cdd:cd05353    2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVvndlggdrkGSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  73 IRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYA 152
Cdd:cd05353   82 AIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 153 AAKAGLIGFSKSLAREVASRGITVNVVAPGfIETDMTralsddqrAGILAQVPAGRLgGAQEIANAVAFLASDEAAyITG 232
Cdd:cd05353  162 AAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRMT--------ETVMPEDLFDAL-KPEYVAPLVLYLCHESCE-VTG 230

                 ....*...
gi 446931279 233 ETLHVNGG 240
Cdd:cd05353  231 GLFEVGAG 238
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
4-241 1.30e-50

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: 165.34  E-value: 1.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAngKGLMLNVTDPASIESVLekirAEFGEVDIL 83
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGI--TTRVLDVTDKEQVAALA----KEEGRIDVL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTM-GNGGQANYAAAKAGLIGFS 162
Cdd:cd05368   75 FNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGLT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRGITVNVVAPGFIETDMTRALSDDQ------RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:cd05368  155 KSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQpdpeeaLKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVV 234

                 ....*
gi 446931279 237 VNGGM 241
Cdd:cd05368  235 IDGGW 239
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
1-240 6.49e-50

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 164.03  E-value: 6.49e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENgaqaisDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGG------DGQHENYQFVPTDVSSAEEVNHTVAEIIEKFGRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEE---------WNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANY 151
Cdd:PRK06171  79 DGLVNNAGINIPRLLVDEKDPAgkyelneaaFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 152 AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALS-------------DDQRAGILAQ--VPAGRLGGAQEIA 216
Cdd:PRK06171 159 AATKAALNSFTRSWAKELGKHNIRVVGVAPGILEATGLRTPEyeealaytrgitvEQLRAGYTKTstIPLGRSGKLSEVA 238
                        250       260
                 ....*....|....*....|....
gi 446931279 217 NAVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK06171 239 DLVCYLLSDRASYITGVTTNIAGG 262
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
2-241 6.52e-50

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 163.79  E-value: 6.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG---LMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK07523   7 DLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSahaLAFDVTDHDAVRAAIDAFEAEIG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK07523  87 PIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK07523 167 GNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEfsAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHVLY 246

                 ....*
gi 446931279 237 VNGGM 241
Cdd:PRK07523 247 VDGGI 251
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
6-189 8.12e-50

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: 163.56  E-value: 8.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:cd05374   81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160
                        170       180
                 ....*....|....*....|....
gi 446931279 166 AREVASRGITVNVVAPGFIETDMT 189
Cdd:cd05374  161 RLELAPFGIKVTIIEPGPVRTGFA 184
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
7-190 9.36e-50

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: 163.18  E-value: 9.36e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD---YLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANnvrKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:cd05339   81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHE 160
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 164 SLAREVAS---RGITVNVVAPGFIETDMTR 190
Cdd:cd05339  161 SLRLELKAygkPGIKTTLVCPYFINTGMFQ 190
PRK12828 PRK12828
short chain dehydrogenase; Provisional
1-240 1.51e-49

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 162.27  E-value: 1.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM-LNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK12828   3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGgIDLVDPQAARRAVDEVNRQFGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK12828  83 LDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAlsdDQRAGILaqvpaGRLGGAQEIANAVAFLASDEAAYITGETLHVNG 239
Cdd:PRK12828 163 RLTEALAAELLDRGITVNAVLPSIIDTPPNRA---DMPDADF-----SRWVTPEQIAAVIAFLLSDEAQAITGASIPVDG 234

                 .
gi 446931279 240 G 240
Cdd:PRK12828 235 G 235
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
1-240 1.67e-49

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: 162.56  E-value: 1.67e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:cd05345    1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNL-LMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:cd05345   81 DILVNNAGITHRNKpMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAL----SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:cd05345  161 TATKAMAVELAPRNIRVNCLCPVAGETPLLSMFmgedTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVAL 240

                 ....*
gi 446931279 236 HVNGG 240
Cdd:cd05345  241 EVDGG 245
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
5-243 1.71e-49

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: 162.93  E-value: 1.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVI-----GTATSENGAQAISDYlGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVladlnLEEAAKSTIQEISEA-GYNAVAVGADVTDKDDVEALIDQAVEKFGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05366   81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHgGKIINASSIAGVQGFPNLGAYSASKFAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTR---------ALSDDQ--RAGILAQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:cd05366  161 RGLTQTAAQELAPKGITVNAYAPGIVKTEMWDyideevgeiAGKPEGegFAEFSSSIPLGRLSEPEDVAGLVSFLASEDS 240
                        250
                 ....*....|....*.
gi 446931279 228 AYITGETLHVNGGMYM 243
Cdd:cd05366  241 DYITGQTILVDGGMVY 256
PRK12937 PRK12937
short chain dehydrogenase; Provisional
1-241 3.03e-49

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 161.83  E-value: 3.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAE 76
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVaVNYAGSAAAADELVAEIeaaGGRAIAVQADVADAAAVTRLFDAAETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK12937  81 FGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRA-LSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPGPVATELFFNgKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVL 238

                 ....*.
gi 446931279 236 HVNGGM 241
Cdd:PRK12937 239 RVNGGF 244
PRK06138 PRK06138
SDR family oxidoreductase;
1-240 3.16e-49

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 161.86  E-value: 3.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFG 78
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAFARqgDVGSAEAVEALVDFVAARWG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTR------ALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITG 232
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRrifarhADPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240

                 ....*...
gi 446931279 233 ETLHVNGG 240
Cdd:PRK06138 241 TTLVVDGG 248
PRK06057 PRK06057
short chain dehydrogenase; Provisional
3-241 3.84e-49

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 161.82  E-value: 3.84e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGanGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVG--GLFVPTDVTDEDAVNALFDTAAETYGSVDI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGIT--RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNG-GQANYAAAKAGLI 159
Cdd:PRK06057  83 AFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSAtSQISYTASKGGVL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAL--SDDQRAGI-LAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK06057 163 AMSRELGVQFARQGIRVNALCPGPVNTPLLQELfaKDPERAARrLVHVPMGRFAEPEEIAAAVAFLASDDASFITASTFL 242

                 ....*
gi 446931279 237 VNGGM 241
Cdd:PRK06057 243 VDGGI 247
PRK06398 PRK06398
aldose dehydrogenase; Validated
3-241 3.89e-49

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 161.92  E-value: 3.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGaQAISDYLgangkglMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS-YNDVDYF-------KVDVSNKEQVIKGIDYVISKYGRIDI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:PRK06398  76 LVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRgITVNVVAPGFIETDMTRAL------SDDQRAG--IL---AQVPAGRLGGAQEIANAVAFLASDEAAYIT 231
Cdd:PRK06398 156 RSIAVDYAPT-IRCVAVCPGSIRTPLLEWAaelevgKDPEHVErkIRewgEMHPMKRVGKPEEVAYVVAFLASDLASFIT 234
                        250
                 ....*....|
gi 446931279 232 GETLHVNGGM 241
Cdd:PRK06398 235 GECVTVDGGL 244
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
3-244 3.57e-48

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: 159.50  E-value: 3.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATS----ENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAE 76
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDaerlEETRQSCLQAGVSEKKILLVvaDLTEEEGQDRIISTTLAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRhGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:cd05364   81 FGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCISKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRA--LSDDQRAGILAQ----VPAGRLGGAQEIANAVAFLASDEAAYI 230
Cdd:cd05364  160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRmgMPEEQYIKFLSRaketHPLGRPGTVDEVAEAIAFLASDASSFI 239
                        250
                 ....*....|....
gi 446931279 231 TGETLHVNGGMYMV 244
Cdd:cd05364  240 TGQLLPVDGGRHLM 253
PRK07035 PRK07035
SDR family oxidoreductase;
2-241 3.89e-48

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 159.03  E-value: 3.89e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGgkaEALACHIGEMEQIDALFAHIRERHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDE-EWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK07035  85 RLDILVNNAAANPYFGHILDTDLgAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQ--RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:PRK07035 165 VISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDaiLKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECL 244

                 ....*.
gi 446931279 236 HVNGGM 241
Cdd:PRK07035 245 NVDGGY 250
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
3-240 7.25e-48

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: 158.42  E-value: 7.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITR-DNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:cd08944   81 LVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIETDMTRALSDD----QRAGILAQVPA---GRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:cd08944  161 TRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGfegaLGPGGFHLLIHqlqGRLGRPEDVAAAVVFLLSDDASFITGQV 240

                 ....*.
gi 446931279 235 LHVNGG 240
Cdd:cd08944  241 LCVDGG 246
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
4-241 1.65e-47

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 157.97  E-value: 1.65e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGE 79
Cdd:PRK08936   6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVvINYRSDEEEANDVAEEIKKAGGEAIAvkgDVTVESDVVNLIQTAVKEFGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK08936  86 LDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAASKGGV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDD--QRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK08936 166 KLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADpkQRADVESMIPMGYIGKPEEIAAVAAWLASSEASYVTGITLF 245

                 ....*
gi 446931279 237 VNGGM 241
Cdd:PRK08936 246 ADGGM 250
PRK07478 PRK07478
short chain dehydrogenase; Provisional
1-240 1.91e-47

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 157.40  E-value: 1.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL-GANGKGLML--NVTDPASIESVLEKIRAEF 77
Cdd:PRK07478   2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIrAEGGEAVALagDVRDEAYAKALVALAVERF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRD-NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVG-TMGNGGQANYAAAK 155
Cdd:PRK07478  82 GGLDIAFNNAGTLGEmGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGhTAGFPGMAAYAASK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 156 AGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDqrAGILAQV----PAGRLGGAQEIANAVAFLASDEAAYIT 231
Cdd:PRK07478 162 AGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDT--PEALAFVaglhALKRMAQPEEIAQAALFLASDAASFVT 239

                 ....*....
gi 446931279 232 GETLHVNGG 240
Cdd:PRK07478 240 GTALLVDGG 248
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-243 2.07e-47

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 157.50  E-value: 2.07e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK07067   2 MRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHG-RIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK07067  82 DILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALVSHYCATKAAVI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDM------------TRALSDDQRAgILAQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:PRK07067 162 SYTQSAALALIRHGINVNAIAPGVVDTPMwdqvdalfaryeNRPPGEKKRL-VGEAVPLGRMGVPDDLTGMALFLASADA 240
                        250
                 ....*....|....*.
gi 446931279 228 AYITGETLHVNGGMYM 243
Cdd:PRK07067 241 DYIVAQTYNVDGGNWM 256
PRK06114 PRK06114
SDR family oxidoreductase;
2-240 2.42e-47

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 157.25  E-value: 2.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKV--IGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEF 77
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADValFDLRTDDGLAETAEHIEAAGRRAIQIaaDVTSKADLRAAVARTEAEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGG--QANYAAAK 155
Cdd:PRK06114  85 GALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllQAHYNASK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 156 AGLIGFSKSLAREVASRGITVNVVAPGFIETDM-TRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:PRK06114 165 AGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMnTRPEMVHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVD 244

                 ....*.
gi 446931279 235 LHVNGG 240
Cdd:PRK06114 245 LLVDGG 250
PRK07856 PRK07856
SDR family oxidoreductase;
1-240 2.66e-47

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 157.02  E-value: 2.66e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENgaqaiSDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK07856   2 LDLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAP-----ETVDGRPAEFHAADVRDPDQVAALVDAIVERHGRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAvMRAMMKKRHGR--IITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK07856  77 DVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQA-ANAVMQQQPGGgsIVNIGSVSGRRPSPGTAAYGAAKAGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRgITVNVVAPGFIETDMTRAL--SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK07856 156 LNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSELHygDAEGIAAVAATVPLGRLATPADIAWACLFLASDLASYVSGANLE 234

                 ....
gi 446931279 237 VNGG 240
Cdd:PRK07856 235 VHGG 238
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-243 6.20e-47

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 156.02  E-value: 6.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVvVNYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 -VDILVNNA-------GITRDNLlmrmKDEEWNDI---IETNLSSVFRLSKAVMRAMMKKRHGRIITIGSvvgtmgNGGQ 148
Cdd:PRK08642  81 pITTVVNNAladfsfdGDARKKA----DDITWEDFqqqLEGSVKGALNTIQAALPGMREQGFGRIINIGT------NLFQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 149 A------NYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFI-ETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAF 221
Cdd:PRK08642 151 NpvvpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLF 230
                        250       260
                 ....*....|....*....|..
gi 446931279 222 LASDEAAYITGETLHVNGGMYM 243
Cdd:PRK08642 231 FASPWARAVTGQNLVVDGGLVM 252
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
4-240 2.37e-46

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 155.14  E-value: 2.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG--AQAISDYLGANG-KGLML--NVTDPASIESVLEKIRAEFG 78
Cdd:cd05355   25 KGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEddAEETKKLIEEEGrKCLLIpgDLGDESFCRDLVKEVVKEFG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAG--ITRDNLLmRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:cd05355  105 KLDILVNNAAyqHPQESIE-DITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKG 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDM-TRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:cd05355  182 AIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLiPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVL 261

                 ....*
gi 446931279 236 HVNGG 240
Cdd:cd05355  262 HVNGG 266
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
6-241 4.90e-46

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: 153.76  E-value: 4.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    6 KIALVTGASRGIGRAIAETLAARGAKV----IGTATSENGAQAISDYlGANGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVavadLNEETAKETAKEINQA-GGKAVAYKLDVSDKDQVFSAIDQAAEKFGGFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:TIGR02415  80 VMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAGHEGNPILSAYSSTKFAVRG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSD-----------DQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAY 229
Cdd:TIGR02415 160 LTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEetseiagkpigEGFEEFSSEIALGRPSEPEDVAGLVSFLASEDSDY 239
                         250
                  ....*....|..
gi 446931279  230 ITGETLHVNGGM 241
Cdd:TIGR02415 240 ITGQSILVDGGM 251
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-240 7.00e-46

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 153.49  E-value: 7.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSE-NGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK08993   7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEpTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK08993  87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIASMLSFQGGIRVPSYTASKSGVM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRAL-SDDQR-AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK08993 167 GVTRLMANEWAKHNINVNAIAPGYMATNNTQQLrADEQRsAEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAV 246

                 ...
gi 446931279 238 NGG 240
Cdd:PRK08993 247 DGG 249
PRK07326 PRK07326
SDR family oxidoreductase;
1-187 8.04e-46

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 152.86  E-value: 8.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK--GLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNvlGLAADVRDEADVQRAVDAIVAAFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAmMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK07326  82 GLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPA-LKRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160
                        170       180
                 ....*....|....*....|....*....
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETD 187
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-241 9.97e-46

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 152.95  E-value: 9.97e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIgtATSENGAQAISDYLGANGKGLMLNVTDPASIESVLekirAEFGEV 80
Cdd:PRK07060   5 FDFSGKSVLVTGASSGIGRACAVALAQRGARVV--AAARNAAALDRLAGETGCEPLRLDVGDDAAIRAAL----AAAGAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK07060  79 DGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgRGGSIVNVSSQAALVGLPDHLAYCASKAALD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMT-RALSDDQ-RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK07060 159 AITRVLCVELGPHGIRVNSVNPTVTLTPMAaEAWSDPQkSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPV 238

                 ....
gi 446931279 238 NGGM 241
Cdd:PRK07060 239 DGGY 242
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-243 1.16e-45

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 152.81  E-value: 1.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARG--AKVIGTATSENGAQAISDY--LGANGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGfdLAINDRPDDEELAATQQELraLGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGIT---RDNLLmRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGR------IITIGSVVGTMGNGGQANYA 152
Cdd:PRK12745  83 CLVNNAGVGvkvRGDLL-DLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVSPNRGEYC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 153 AAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQ-VPAGRLGGAQEIANAVAFLASDEAAYIT 231
Cdd:PRK12745 162 ISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYDALIAKGlVPMPRWGEPEDVARAVAALASGDLPYST 241
                        250
                 ....*....|..
gi 446931279 232 GETLHVNGGMYM 243
Cdd:PRK12745 242 GQAIHVDGGLSI 253
PRK07074 PRK07074
SDR family oxidoreductase;
6-241 1.35e-45

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 153.00  E-value: 1.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG-KGLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARfVPVACDLTDAASLAAALANAAAERGPVDVLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGtMGNGGQANYAAAKAGLIGFSKS 164
Cdd:PRK07074  83 ANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNG-MAALGHPAYSAAKAGLIHYTKL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 165 LAREVASRGITVNVVAPGFIETDMTRAlsddqRAGILAQV--------PAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK07074 162 LAVEYGRFGIRANAVAPGTVKTQAWEA-----RVAANPQVfeelkkwyPLQDFATPDDVANAVLFLASPAARAITGVCLP 236

                 ....*
gi 446931279 237 VNGGM 241
Cdd:PRK07074 237 VDGGL 241
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-240 1.49e-45

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 152.54  E-value: 1.49e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASR--GIGRAIAETLAARGAKVIGT------ATSENGAQAISDYL--------GANGKGLMLNVTDPA 64
Cdd:PRK12748   1 LPLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTywspydKTMPWGMHDKEPVLlkeeiesyGVRCEHMEIDLSQPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  65 SIESVLEKIRAEFGEVDILVNNAGI----TRDNLLMRMKDEEWndiiETNLSSVFRLSKAVMRAMMKKRHGRII--TIGS 138
Cdd:PRK12748  81 APNRVFYAVSERLGDPSILINNAAYsthtRLEELTAEQLDKHY----AVNVRATMLLSSAFAKQYDGKAGGRIInlTSGQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 139 VVGTMGngGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGfiETDmTRALSDDQRAGILAQVPAGRLGGAQEIANA 218
Cdd:PRK12748 157 SLGPMP--DELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG--PTD-TGWITEELKHHLVPKFPQGRVGEPVDAARL 231
                        250       260
                 ....*....|....*....|..
gi 446931279 219 VAFLASDEAAYITGETLHVNGG 240
Cdd:PRK12748 232 IAFLVSEEAKWITGQVIHSEGG 253
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
4-240 1.93e-45

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: 152.10  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK----GLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnrviALELDITSKESIKELIESYLEKFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMR---MKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMG-------NGGQ- 148
Cdd:cd08930   81 IDILINNAYPSPKVWGSRfeeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIApdfriyeNTQMy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 149 --ANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRagilAQVPAGRLGGAQEIANAVAFLASDE 226
Cdd:cd08930  161 spVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEFLEKYT----KKCPLKRMLNPEDLRGAIIFLLSDA 236
                        250
                 ....*....|....
gi 446931279 227 AAYITGETLHVNGG 240
Cdd:cd08930  237 SSYVTGQNLVIDGG 250
PRK06484 PRK06484
short chain dehydrogenase; Validated
5-240 2.22e-45

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 158.47  E-value: 2.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLV 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNL-LMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKrhGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:PRK06484 349 NNAGIAEVFKpSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG--GVIVNLGSIASLLALPPRNAYCASKAAVTMLSR 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 164 SLAREVASRGITVNVVAPGFIETDMTRALSDDQR---AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK06484 427 SLACEWAPAGIRVNTVAPGYIETPAVLALKASGRadfDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGG 506
PRK07774 PRK07774
SDR family oxidoreductase;
1-240 4.54e-45

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 151.44  E-value: 4.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK07774   2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadGGTAIAVQVDVSDPDSAKAMADATVSAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRD---NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGgqaNYAAA 154
Cdd:PRK07774  82 GGIDYLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYSN---FYGLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALS-DDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGE 233
Cdd:PRK07774 159 KVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTpKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQ 238

                 ....*..
gi 446931279 234 TLHVNGG 240
Cdd:PRK07774 239 IFNVDGG 245
PRK05867 PRK05867
SDR family oxidoreductase;
2-240 4.59e-45

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 151.34  E-value: 4.59e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM---LNVTDPASIESVLEKIRAEFG 78
Cdd:PRK05867   6 DLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVpvcCDVSQHQQVTSMLDQVTAELG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQ--ANYAAAK 155
Cdd:PRK05867  86 GIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVPQqvSHYCASK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 156 AGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGiLAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:PRK05867 166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLW-EPKIPLGRLGRPEELAGLYLYLASEASSYMTGSDI 244

                 ....*
gi 446931279 236 HVNGG 240
Cdd:PRK05867 245 VIDGG 249
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
6-240 6.57e-45

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: 150.51  E-value: 6.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGEVD 81
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYnRSEAEAQRLKDELNALRNSAVLvqaDLSDFAACADLVAAAFRAFGRCD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:cd05357   81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446931279 162 SKSLAREVASRgITVNVVAPGFIETDMtrALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEaaYITGETLHVNGG 240
Cdd:cd05357  161 TRSAALELAPN-IRVNGIAPGLILLPE--DMDAEYRENALRKVPLKRRPSAEEIADAVIFLLDSN--YITGQIIKVDGG 234
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
7-240 8.04e-45

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: 150.41  E-value: 8.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK---GLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGqaiGLECNVTSEQDLEAVVKATVSQFGGITIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGIT-RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:cd05365   81 VNNAGGGgPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446931279 163 KSLAREVASRGITVNVVAPGFIETD-MTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:cd05365  161 RNLAFDLGPKGIRVNAVAPGAVKTDaLASVLTPEIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-240 1.07e-44

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 150.44  E-value: 1.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSE-NGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK12481   5 DLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEaPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK12481  85 DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVPSYTASKSAVM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRALSDD--QRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK12481 165 GLTRALATELSQYNINVNAIAPGYMATDNTAALRADtaRNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTGYTLAV 244

                 ...
gi 446931279 238 NGG 240
Cdd:PRK12481 245 DGG 247
PRK08589 PRK08589
SDR family oxidoreductase;
4-240 1.23e-44

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 150.70  E-value: 1.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSE---NGAQAISDYlGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK08589   5 ENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEavsETVDKIKSN-GGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGItrDNLLMRMKD---EEWNDIIETNLSSVFRLSKAVMRAMMKKrHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK08589  84 DVLFNNAGV--DNAAGRIHEypvDVFDKIMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTSSFSGQAADLYRSGYNAAKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALS--DDQRAGILAQ------VPAGRLGGAQEIANAVAFLASDEAAY 229
Cdd:PRK08589 161 VINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTgtSEDEAGKTFRenqkwmTPLGRLGKPEEVAKLVVFLASDDSSF 240
                        250
                 ....*....|.
gi 446931279 230 ITGETLHVNGG 240
Cdd:PRK08589 241 ITGETIRIDGG 251
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
6-189 1.83e-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: 148.92  E-value: 1.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGA-KVIGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLraeGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKD-EEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGgqanYAAAKAGLIG 160
Cdd:cd05324   81 ILVNNAGIAFKGFDDSTPTrEQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVSKAALNA 156
                        170       180
                 ....*....|....*....|....*....
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMT 189
Cdd:cd05324  157 LTRILAKELKETGIKVNACCPGWVKTDMG 185
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
4-243 5.20e-44

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 148.64  E-value: 5.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD-----YLGANGKGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQeinaeYGEGMAYGFGADATSEQSVLALSRGVDEIFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPG-FIETDMTRALSDD--QRAGI---------LAQVPAGRLGGAQEIANAVAFLASD 225
Cdd:PRK12384 161 GVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQSLLPQyaKKLGIkpdeveqyyIDKVPLKRGCDYQDVLNMLLFYASP 240
                        250
                 ....*....|....*...
gi 446931279 226 EAAYITGETLHVNGGMYM 243
Cdd:PRK12384 241 KASYCTGQSINVTGGQVM 258
PRK09135 PRK09135
pteridine reductase; Provisional
1-240 6.17e-44

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 148.15  E-value: 6.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDYLGANGKG----LMLNVTDPASIESVLEKIRA 75
Cdd:PRK09135   2 MTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYhRSAAEADALAAELNALRPGsaaaLQADLLDPDALPELVAACVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  76 EFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMrAMMKKRHGRIITIGSVVGTMGNGGQANYAAAK 155
Cdd:PRK09135  82 AFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAA-PQLRKQRGAIVNITDIHAERPLKGYPVYCAAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 156 AGLIGFSKSLAREVASRgITVNVVAPGFIE-TDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLAsDEAAYITGET 234
Cdd:PRK09135 161 AALEMLTRSLALELAPE-VRVNAVAPGAILwPEDGNSFDEEARQAILARTPLKRIGTPEDIAEAVRFLL-ADASFITGQI 238

                 ....*.
gi 446931279 235 LHVNGG 240
Cdd:PRK09135 239 LAVDGG 244
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
2-240 1.00e-43

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: 148.37  E-value: 1.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVI----GTATSENGAQAISDYlGANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:cd08935    2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAalgrNQEKGDKVAKEITAL-GGRAIALAADVLDRASLERAREEIVAQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAG------ITRDNLLMR--------MKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTM 143
Cdd:cd08935   81 GTVDILINGAGgnhpdaTTDPEHYEPeteqnffdLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 144 GNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQ------RAG-ILAQVPAGRLGGAQEIA 216
Cdd:cd08935  161 PLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPdgsytdRSNkILGRTPMGRFGKPEELL 240
                        250       260
                 ....*....|....*....|....*
gi 446931279 217 NAVAFLASDEAA-YITGETLHVNGG 240
Cdd:cd08935  241 GALLFLASEKASsFVTGVVIPVDGG 265
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-240 1.16e-43

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 148.01  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDylgangKGLML---NVTDPASIESVLEKIRAE 76
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKELRE------KGVFTikcDVGNRDQVKKSKEVVEKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGtMGNG--GQANYAAA 154
Cdd:PRK06463  77 FGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAG-IGTAaeGTTFYAIT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGR-----LGGAQEIANAVAFLASDEAAY 229
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKLRELFRNKtvlktTGKPEDIANIVLFLASDDARY 235
                        250
                 ....*....|.
gi 446931279 230 ITGETLHVNGG 240
Cdd:PRK06463 236 ITGQVIVADGG 246
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
2-241 1.22e-43

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: 147.60  E-value: 1.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLG-ANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:cd05326    1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGdPDISFVHCDVTVEADVRAAVDTAVARFGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGI--TRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05326   81 DIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQV-----PAGRLGGAQEIANAVAFLASDEAAYITGE 233
Cdd:cd05326  161 LGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVrgaanLKGTALRPEDIAAAVLYLASDDSRYVSGQ 240

                 ....*...
gi 446931279 234 TLHVNGGM 241
Cdd:cd05326  241 NLVVDGGL 248
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
6-227 1.24e-43

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: 146.74  E-value: 1.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVigTATSENGaQAISDYLGANGKGLMLN--VTDPASIESVLEKIRAEFGEVDIL 83
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRV--SLGLRNP-EDLAALSASGGDVEAVPydARDPEDARALVDALRDRFGRIDVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:cd08932   78 VHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAH 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446931279 164 SLAREVASRGITVNVVAPGFIETDMTRALSDDQragilaQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:cd08932  158 ALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVG------AFPPEEMIQPKDIANLVRMVIELPE 215
PRK07890 PRK07890
short chain dehydrogenase; Provisional
1-243 2.48e-43

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 147.03  E-value: 2.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAK-VIGTATSEN--GAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK07890   1 MLLKGKVVVVSGVGPGLGRTLAVRAARAGADvVLAARTAERldEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNA-------GITRDNLlmrmkdEEWNDIIETNLSSVFRLSKAVMRAMmKKRHGRIITIGSVVGTMGNGGQAN 150
Cdd:PRK07890  81 GRVDALVNNAfrvpsmkPLADADF------AHWRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 151 YAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRAL-----------SDDQRAGILAQVPAGRLGGAQEIANAV 219
Cdd:PRK07890 154 YKMAKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGYfrhqagkygvtVEQIYAETAANSDLKRLPTDDEVASAV 233
                        250       260
                 ....*....|....*....|....
gi 446931279 220 AFLASDEAAYITGETLHVNGGMYM 243
Cdd:PRK07890 234 LFLASDLARAITGQTLDVNCGEYH 257
PRK06500 PRK06500
SDR family oxidoreductase;
3-241 3.10e-43

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 146.64  E-value: 3.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:PRK06500  84 VFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL--ANPASIVLNGSINAHIGMPNSSVYAASKAALLSLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRGITVNVVAPGFIETD------MTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLH 236
Cdd:PRK06500 162 KTLSGELLPRGIRVNAVSPGPVQTPlygklgLPEATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEII 241

                 ....*
gi 446931279 237 VNGGM 241
Cdd:PRK06500 242 VDGGM 246
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-192 4.29e-43

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 145.99  E-value: 4.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEF 77
Cdd:PRK07666   3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIataDVSDYEEVTAAIEQLKNEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK07666  83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFG 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRAL 192
Cdd:PRK07666 163 VLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDL 197
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
3-220 4.56e-43

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: 146.19  E-value: 4.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG----LMLNVTDPASIESVLEKIRAEFG 78
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPsphvVPLDMSDLEDAEQVVEEALKLFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05332   81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHAL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMT-RALSDDqrAGILAQVPAGRLGG------AQEIANAVA 220
Cdd:cd05332  161 QGFFDSLRAELSEPNISVTVVCPGLIDTNIAmNALSGD--GSMSAKMDDTTANGmspeecALEILKAIA 227
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
4-240 1.02e-42

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 145.37  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD---YLGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK06113  10 DGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDeiqQLGGQAFACRCDITSEQELSALADFALSKLGKV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLL-MRMKDEEWndIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK06113  90 DILVNNAGGGGPKPFdMPMADFRR--AYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAAS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETD-MTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVN 238
Cdd:PRK06113 168 HLVRNMAFDLGEKNIRVNGIAPGAILTDaLKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVS 247

                 ..
gi 446931279 239 GG 240
Cdd:PRK06113 248 GG 249
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
5-240 1.19e-42

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: 144.93  E-value: 1.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd08942    6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIAIpaDLSSEEGIEALVARVAERSDRLDV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVM----RAMMKKRHGRIITIGSVVGTMGNGGQA-NYAAAKAG 157
Cdd:cd08942   86 LVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLpllrAAATAENPARVINIGSIAGIVVSGLENySYGASKAA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQ--RAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:cd08942  166 VHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPaaLEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAYLTGAVI 245

                 ....*
gi 446931279 236 HVNGG 240
Cdd:cd08942  246 PVDGG 250
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
6-224 1.79e-42

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: 144.35  E-value: 1.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG----LMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVkvlpLQLDVSDRESIEAALENLPEEFRDID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRD-NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:cd05346   81 ILVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQ 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETD--MTRALSDDQRA-----GILAQVPagrlggaQEIANAVAFLAS 224
Cdd:cd05346  161 FSLNLRKDLIGTGIRVTNIEPGLVETEfsLVRFHGDKEKAdkvyeGVEPLTP-------EDIAETILWVAS 224
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
2-241 2.11e-42

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: 144.61  E-value: 2.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGK--GLMLNVTDPASIESVLEKIRAEFG 78
Cdd:cd08936    7 PLANKVALVTASTDGIGLAIARRLAQDGAHVvVSSRKQQNVDRAVATLQGEGLSvtGTVCHVGKAEDRERLVATAVNLHG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGItrdNL----LMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAA 154
Cdd:cd08936   87 GVDILVSNAAV---NPffgnILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDD--QRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITG 232
Cdd:cd08936  164 KTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDkaVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITG 243

                 ....*....
gi 446931279 233 ETLHVNGGM 241
Cdd:cd08936  244 ETVVVGGGT 252
PRK08265 PRK08265
short chain dehydrogenase; Provisional
4-240 3.45e-42

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 144.00  E-value: 3.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:PRK08265   5 AGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGRVDIL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLmRMKDEEWNDIIETNLSSVFRLSKAVmRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:PRK08265  85 VNLACTYLDDGL-ASSRADWLAALDVNLVSAAMLAQAA-HPHLARGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 164 SLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQV----PAGRLGGAQEIANAVAFLASDEAAYITGETLHVNG 239
Cdd:PRK08265 163 SMAMDLAPDGIRVNSVSPGWTWSRVMDELSGGDRAKADRVAapfhLLGRVGDPEEVAQVVAFLCSDAASFVTGADYAVDG 242

                 .
gi 446931279 240 G 240
Cdd:PRK08265 243 G 243
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
3-240 4.51e-42

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: 143.82  E-value: 4.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEV 80
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDAAHVHtaDLETYAGAQGVVRAAVERFGRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGIT-RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVvgTMGNGGQANYAAAKAGLI 159
Cdd:cd08937   82 DVLINNVGGTiWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSI--ATRGIYRIPYSAAKGGVN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTR------ALSDDQRA---GILAQ----VPAGRLGGAQEIANAVAFLASDE 226
Cdd:cd08937  160 ALTASLAFEHARDGIRVNAVAPGGTEAPPRKiprnaaPMSEQEKVwyqRIVDQtldsSLMGRYGTIDEQVRAILFLASDE 239
                        250
                 ....*....|....
gi 446931279 227 AAYITGETLHVNGG 240
Cdd:cd08937  240 ASYITGTVLPVGGG 253
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-240 8.24e-42

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 143.00  E-value: 8.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASR--GIGRAIAETLAARGAKVIGTATSE-----------NGAQAISDYLGANG---KGLMLNVTDPASIES 68
Cdd:PRK12859   6 NKVAVVTGVSRldGIGAAICKELAEAGADIFFTYWTAydkempwgvdqDEQIQLQEELLKNGvkvSSMELDLTQNDAPKE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  69 VLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITI--GSVVGTMGng 146
Cdd:PRK12859  86 LLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMtsGQFQGPMV-- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 147 GQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGfiETDmTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDE 226
Cdd:PRK12859 164 GELAYAATKGAIDALTSSLAAEVAHLGITVNAINPG--PTD-TGWMTEEIKQGLLPMFPFGRIGEPKDAARLIKFLASEE 240
                        250
                 ....*....|....
gi 446931279 227 AAYITGETLHVNGG 240
Cdd:PRK12859 241 AEWITGQIIHSEGG 254
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
4-241 1.22e-41

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 142.56  E-value: 1.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLskdGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHG-RIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK08643  81 NVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGgKIINATSQAGVVGNPELAVYSSTKFAVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDM----TRALSDDqrAG---------ILAQVPAGRLGGAQEIANAVAFLASDE 226
Cdd:PRK08643 161 GLTQTAARDLASEGITVNAYAPGIVKTPMmfdiAHQVGEN--AGkpdewgmeqFAKDITLGRLSEPEDVANCVSFLAGPD 238
                        250
                 ....*....|....*
gi 446931279 227 AAYITGETLHVNGGM 241
Cdd:PRK08643 239 SDYITGQTIIVDGGM 253
PRK07825 PRK07825
short chain dehydrogenase; Provisional
1-189 1.94e-41

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 142.39  E-value: 1.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKV-IG---TATSENGAQAISdylgaNGKGLMLNVTDPASIESVLEKIRAE 76
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGARVaIGdldEALAKETAAELG-----LVVGGPLDVTDPASFAAFLDAVEAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK07825  76 LGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKH 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMT 189
Cdd:PRK07825 156 AVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
4-243 2.73e-41

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 141.66  E-value: 2.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISdyLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVvILDLPNSPGETVAK--LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKD------EEWNDIIETNLSSVFRLSKAVMRAMMK------KRHGRIITIGSVVGTMGNGGQAN 150
Cdd:cd05371   79 VVNCAGIAVAAKTYNKKGqqphslELFQRVINVNLIGTFNVIRLAAGAMGKnepdqgGERGVIINTASVAAFEGQIGQAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 151 YAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPA-GRLGGAQEIANAVAFLASDEaaY 229
Cdd:cd05371  159 YSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFpSRLGDPAEYAHLVQHIIENP--Y 236
                        250
                 ....*....|....
gi 446931279 230 ITGETLHVNGGMYM 243
Cdd:cd05371  237 LNGEVIRLDGAIRM 250
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
2-244 2.94e-41

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 141.40  E-value: 2.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAK-VIGTATSENGAQAISDYLGANG-KGLML--NVTDPASIESVLEKIRAEF 77
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDiAVNYARSRKAAEETAEEIEALGrKALAVkaNVGDVEKIKEMFAQIDEEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSvvgtMGNGGQ-ANYAA--- 153
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSS----LGSIRYlENYTTvgv 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTR------ALSDDQRagilAQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:PRK08063 157 SKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKhfpnreELLEDAR----AKTPAGRMVEPEDVANAVLFLCSPEA 232
                        250
                 ....*....|....*..
gi 446931279 228 AYITGETLHVNGGMYMV 244
Cdd:PRK08063 233 DMIRGQTIIVDGGRSLL 249
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
7-244 3.42e-41

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: 141.45  E-value: 3.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRGIGRAIAETLAARGAKVIGTATSENGA----QAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQatevVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGIT---RDNLLmRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKR------HGRIITIGSVVGTMGNGGQANYAA 153
Cdd:cd05337   83 LVNNAGIAvrpRGDLL-DLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPdrfdgpHRSIIFVTSINAYLVSPNRGEYCI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILA-QVPAGRLGGAQEIANAVAFLASDEAAYITG 232
Cdd:cd05337  162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAgLVPIRRWGQPEDIAKAVRTLASGLLPYSTG 241
                        250
                 ....*....|..
gi 446931279 233 ETLHVNGGMYMV 244
Cdd:cd05337  242 QPINIDGGLSMR 253
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-240 8.82e-41

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 148.07  E-value: 8.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK--GLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK08324 420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRalGVACDVTDEAAVQAAFEEAALAFGGV 499
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRH---GRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK08324 500 DIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIM--KAQglgGSIVFIASKNAVNPGPNFGAYGAAKAA 577
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAP------------GFIETDM-TRALSDDQ-----RAGILAQVPAGrlggAQEIANAV 219
Cdd:PRK08324 578 ELHLVRQLALELGPDGIRVNGVNPdavvrgsgiwtgEWIEARAaAYGLSEEEleefyRARNLLKREVT----PEDVAEAV 653
                        250       260
                 ....*....|....*....|.
gi 446931279 220 AFLASDEAAYITGETLHVNGG 240
Cdd:PRK08324 654 VFLASGLLSKTTGAIITVDGG 674
PRK07069 PRK07069
short chain dehydrogenase; Validated
8-241 1.84e-40

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 139.46  E-value: 1.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGT-ATSENGAQAISDYLGAN-GKGL----MLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTdINDAAGLDAFAAEINAAhGEGVafaaVQDVTDEAQWQALLAQAADAMGGLS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK07069  82 VLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITV--NVVAPGFIETD----MTRALSDDQRAGILA-QVPAGRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:PRK07069 162 TKSIALDCARRGLDVrcNSIHPTFIRTGivdpIFQRLGEEEATRKLArGVPLGRLGEPDDVAHAVLYLASDESRFVTGAE 241

                 ....*..
gi 446931279 235 LHVNGGM 241
Cdd:PRK07069 242 LVIDGGI 248
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
2-240 3.85e-40

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 139.26  E-value: 3.85e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK08277   7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGgeaLAVKADVLDKESLEQARQQILEDFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAG------ITRDNLLMR---------MKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGS----- 138
Cdd:PRK08277  87 PCDILINGAGgnhpkaTTDNEFHELieptktffdLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSmnaft 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 139 ----VVGtmgnggqanYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRAL------SDDQRAG-ILAQVPAG 207
Cdd:PRK08277 167 pltkVPA---------YSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALlfnedgSLTERANkILAHTPMG 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 446931279 208 RLGGAQEIANAVAFLASDEAA-YITGETLHVNGG 240
Cdd:PRK08277 238 RFGKPEELLGTLLWLADEKASsFVTGVVLPVDGG 271
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-241 5.45e-40

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 139.92  E-value: 5.45e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVI--GTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEkIRAEFGE 79
Cdd:PRK07792  11 SGKVAVVTGAAAGLGRAEALGLARLGATVVvnDVASALDASDVLDEIRAAGAKAVAVagDISQRATADELVA-TAVGLGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSK---AVMRAMMK----KRHGRIITIGSVVGTMGNGGQANYA 152
Cdd:PRK07792  90 LDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRnaaAYWRAKAKaaggPVYGRIVNTSSEAGLVGPVGQANYG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 153 AAKAGLIGFSKSLAREVASRGITVNVVAPGfIETDMTralsddqrAGILAQVPAGRLGG-----AQEIANAVAFLASDEA 227
Cdd:PRK07792 170 AAKAGITALTLSAARALGRYGVRANAICPR-ARTAMT--------ADVFGDAPDVEAGGidplsPEHVVPLVQFLASPAA 240
                        250
                 ....*....|....
gi 446931279 228 AYITGETLHVNGGM 241
Cdd:PRK07792 241 AEVNGQVFIVYGPM 254
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
3-243 1.26e-39

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 137.36  E-value: 1.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:cd05363   81 LVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKAAVISL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIETDM------------TRALSDDQRAgILAQVPAGRLGGAQEIANAVAFLASDEAAY 229
Cdd:cd05363  161 TQSAGLNLIRHGINVNAIAPGVVDGEHwdgvdakfaryeNRPRGEKKRL-VGEAVPFGRMGRAEDLTGMAIFLASTDADY 239
                        250
                 ....*....|....
gi 446931279 230 ITGETLHVNGGMYM 243
Cdd:cd05363  240 IVAQTYNVDGGNWM 253
PRK06179 PRK06179
short chain dehydrogenase; Provisional
4-207 1.28e-39

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 137.73  E-value: 1.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYlgangKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGV-----ELLELDVTDDASVQAAVDEVIARAGRIDVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITrdnLLMRMKD---EEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK06179  78 VNNAGVG---LAGAAEEssiAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGF---------IETDMTRALSDDQRAG----ILAQVPAG 207
Cdd:PRK06179 155 YSESLDHEVRQFGIRVSLVEPAYtktnfdanaPEPDSPLAEYDRERAVvskaVAKAVKKA 214
PRK07831 PRK07831
SDR family oxidoreductase;
4-237 2.72e-39

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 136.70  E-value: 2.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGAS-RGIGRAIAETLAARGAKVIGTATSE----NGAQAISDYLG-ANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK07831  16 AGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHErrlgETADELAAELGlGRVEAVVCDVTSEAQVDALIDAAVERL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK07831  96 GRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHgGVIVNNASVLGWRAQHGQAHYAAAKA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIetdMTRALSDDQRAGILAQVPA----GRLGGAQEIANAVAFLASDEAAYITG 232
Cdd:PRK07831 176 GVMALTRCSALEAAEYGVRINAVAPSIA---MHPFLAKVTSAELLDELAAreafGRAAEPWEVANVIAFLASDYSSYLTG 252

                 ....*
gi 446931279 233 ETLHV 237
Cdd:PRK07831 253 EVVSV 257
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
3-240 1.09e-38

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 134.96  E-value: 1.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL-----GANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapDAEVLLIKADVSDEAQVEAYVDATVEQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGIT-RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:cd05330   81 GRIDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRAL------SDDQRAGI-LAQV-PAGRLGGAQEIANAVAFLASDEAA 228
Cdd:cd05330  161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkqlgpENPEEAGEeFVSVnPMKRFGEPEEVAAVVAFLLSDDAG 240
                        250
                 ....*....|..
gi 446931279 229 YITGETLHVNGG 240
Cdd:cd05330  241 YVNAAVVPIDGG 252
PRK06180 PRK06180
short chain dehydrogenase; Provisional
4-191 1.26e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 135.43  E-value: 1.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:PRK06180  83 VNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISE 162
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 164 SLAREVASRGITVNVVAPGFIETD-----MTRA 191
Cdd:PRK06180 163 SLAKEVAPFGIHVTAVEPGSFRTDwagrsMVRT 195
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
1-240 5.19e-38

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 132.98  E-value: 5.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIgtATSENGAQAISdyLGANGKGLMLNVTDPASIESVLEKIrAEFGEV 80
Cdd:cd05351    3 LDFAGKRALVTGAGKGIGRATVKALAKAGARVV--AVSRTQADLDS--LVRECPGIEPVCVDLSDWDATEEAL-GSVGPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:cd05351   78 DLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHTVYCSTKAALD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMTRA-LSDDQRAG-ILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:cd05351  158 MLTKVMALELGPHKIRVNSVNPTVVMTDMGRDnWSDPEKAKkMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPV 237

                 ...
gi 446931279 238 NGG 240
Cdd:cd05351  238 DGG 240
PRK07791 PRK07791
short chain dehydrogenase; Provisional
4-241 8.20e-38

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 133.64  E-value: 8.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVI---------GTATSENGAQAISDYLGANGKGLMLN---VTDPASIESVLE 71
Cdd:PRK07791   5 DGRVVIVTGAGGGIGRAHALAFAAEGARVVvndigvgldGSASGGSAAQAVVDEIVAAGGEAVANgddIADWDGAANLVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  72 KIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVF---RLSKAVMRAMMK---KRHGRIITIGSVVGTMGN 145
Cdd:PRK07791  85 AAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFatlRHAAAYWRAESKagrAVDARIINTSSGAGLQGS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 146 GGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGfIETDMTralsDDQRAGILAQVPAGRLGG--AQEIANAVAFLA 223
Cdd:PRK07791 165 VGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-ARTRMT----ETVFAEMMAKPEEGEFDAmaPENVSPLVVWLG 239
                        250
                 ....*....|....*...
gi 446931279 224 SDEAAYITGETLHVNGGM 241
Cdd:PRK07791 240 SAESRDVTGKVFEVEGGK 257
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
5-241 1.12e-37

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: 131.93  E-value: 1.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKaVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKS 164
Cdd:cd09761   81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSR-YCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVALTHA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446931279 165 LAREVaSRGITVNVVAPGFIETDMTRALSDDQRAGI-LAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:cd09761  160 LAMSL-GPDIRVNCISPGWINTTEQQEFTAAPLTQEdHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDGGM 236
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
6-240 3.10e-37

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: 130.88  E-value: 3.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISdyLGA-NGKG----LMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAE--LQAiNPKVkatfVQCDVTSWEQLAAAFKKAIEKFGRV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEE--WNDIIETNLSSVFRLSKAVMRAMMKKRH---GRIITIGSVVGTMGNGGQANYAAAK 155
Cdd:cd05323   79 DILINNAGILDEKSYLFAGKLPppWEKTIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQFPVYSASK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 156 AGLIGFSKSLAREVASR-GITVNVVAPGFIETDMtraLSDDQRAGILAQVPAGRLgGAQEIANAVAFLASDEAAyiTGET 234
Cdd:cd05323  159 HGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPL---LPDLVAKEAEMLPSAPTQ-SPEVVAKAIVYLIEDDEK--NGAI 232

                 ....*.
gi 446931279 235 LHVNGG 240
Cdd:cd05323  233 WIVDGG 238
PRK08628 PRK08628
SDR family oxidoreductase;
1-240 4.42e-37

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 130.85  E-value: 4.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGA--KVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK08628   3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAipVIFGRSAPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITrDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK08628  83 RIDGLVNNAGVN-DGVGLEAGREAFVASLERNLIHYYVMAHYCLPHL-KASRGAIVNISSKTALTGQGGTSGYAAAKGAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDM------TRALSDDQRAGILAQVPAG-RLGGAQEIANAVAFLASDEAAYIT 231
Cdd:PRK08628 161 LALTREWAVALAKDGVRVNAVIPAEVMTPLyenwiaTFDDPEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHTT 240

                 ....*....
gi 446931279 232 GETLHVNGG 240
Cdd:PRK08628 241 GQWLFVDGG 249
PRK06123 PRK06123
SDR family oxidoreductase;
6-240 4.48e-37

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 130.67  E-value: 4.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARG-AKVIGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGyAVCLNYLRNRDAAEAVVQAIRRQGGEALAvaaDVADEADVLRLFEAVDRELGRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNL-LMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGR---IITIGSVVGTMGNGGQ-ANYAAAKA 156
Cdd:PRK06123  83 ALVNNAGILEAQMrLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEyIDYAASKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGIL-AQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:PRK06123 163 AIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVkAGIPMGRGGTAEEVARAILWLLSDEASYTTGTFI 242

                 ....*
gi 446931279 236 HVNGG 240
Cdd:PRK06123 243 DVSGG 247
PRK07814 PRK07814
SDR family oxidoreductase;
4-241 5.03e-37

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 131.05  E-value: 5.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG---LMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK07814   9 DDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRahvVAADLAHPEATAGLAGQAVEAFGRL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKR-HGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK07814  89 DIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTAKAALA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRgITVNVVAPGFIetdMTRAL-----SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:PRK07814 169 HYTRLAALDLCPR-IRVNAIAPGSI---LTSALevvaaNDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKT 244

                 ....*..
gi 446931279 235 LHVNGGM 241
Cdd:PRK07814 245 LEVDGGL 251
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
8-231 2.98e-36

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: 126.48  E-value: 2.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGA-KVIGTATSengaqaisdylgangkglmlnvtdpasiesvlekiraefgevDILVNN 86
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSRR------------------------------------------DVVVHN 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  87 AGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLA 166
Cdd:cd02266   39 AAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQQWA 118
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446931279 167 REVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLA---SDEAAYIT 231
Cdd:cd02266  119 SEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALdrpKAGVCYII 186
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
4-243 5.29e-36

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: 127.97  E-value: 5.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKV----IGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVavadINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDgIQGRIIQINSKSGKVGSKHNSGYSAAKFGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPG-FIETDMTRALSDD--QRAGI---------LAQVPAGRLGGAQEIANAVAFLASDE 226
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSLLPQyaKKLGIkeseveqyyIDKVPLKRGCDYQDVLNMLLFYASPK 240
                        250
                 ....*....|....*..
gi 446931279 227 AAYITGETLHVNGGMYM 243
Cdd:cd05322  241 ASYCTGQSINITGGQVM 257
PRK07062 PRK07062
SDR family oxidoreductase;
1-240 6.67e-36

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 127.85  E-value: 6.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNF--EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG-AQAISDYLGANGKGLML----NVTDPASIESVLEKI 73
Cdd:PRK07062   2 MQIqlEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERlASAEARLREKFPGARLLaarcDVLDEADVAAFAAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  74 RAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAA 153
Cdd:PRK07062  82 EARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDM---------TRALSDDQRAGILAQ---VPAGRLGGAQEIANAVAF 221
Cdd:PRK07062 162 ARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQwrrryearaDPGQSWEAWTAALARkkgIPLGRLGRPDEAARALFF 241
                        250
                 ....*....|....*....
gi 446931279 222 LASDEAAYITGETLHVNGG 240
Cdd:PRK07062 242 LASPLSSYTTGSHIDVSGG 260
PRK06949 PRK06949
SDR family oxidoreductase;
1-241 1.06e-35

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 127.19  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG---LMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK06949   5 INLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAahvVSLDVTDYQSIKAAVAHAETEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMM--------KKRHGRIITIGSVVGTMGNGGQA 149
Cdd:PRK06949  85 GTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIarakgagnTKPGGRIINIASVAGLRVLPQIG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 150 NYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRAL-SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAA 228
Cdd:PRK06949 165 LYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHwETEQGQKLVSMLPRKRVGKPEDLDGLLLLLAADESQ 244
                        250
                 ....*....|...
gi 446931279 229 YITGETLHVNGGM 241
Cdd:PRK06949 245 FINGAIISADDGF 257
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
4-221 1.09e-35

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


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 126.88  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG---LMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:cd08934    2 QGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKalvLELDVTDEQQVDAAVERTVEALGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:cd08934   82 DILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRALSD-DQRAGILAQVPAGRLGGAQEIANAVAF 221
Cdd:cd08934  162 FSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHtITKEAYEERISTIRKLQAEDIAAAVRY 223
PRK09072 PRK09072
SDR family oxidoreductase;
1-188 1.22e-35

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 127.37  E-value: 1.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG--KGLMLNVTDPASIESVLEKIRaEFG 78
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGrhRWVVADLTSEAGREAVLARAR-EMG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK09072  80 GINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFAL 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDM 188
Cdd:PRK09072 160 RGFSEALRRELADTGVRVLYLAPRATRTAM 189
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
5-189 1.23e-35

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: 126.56  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG-LMLNVTDPASIESVLEKIRAEFG--EVD 81
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVeTKTIAADFSAGDDIYERIEKELEglDIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRD--NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:cd05356   81 ILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDMT 189
Cdd:cd05356  161 FFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
5-240 1.24e-35

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: 126.74  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQ--AISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEkvAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMK-KRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:cd08943   81 VVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSqGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 162 SKSLAREVASRGITVNVVAP-----GFIETDM----TRALSDDQ-----RAGILAQVPAgrlgGAQEIANAVAFLASDEA 227
Cdd:cd08943  161 ARCLALEGGEDGIRVNTVNPdavfrGSKIWEGvwraARAKAYGLleeeyRTRNLLKREV----LPEDVAEAVVAMASEDF 236
                        250
                 ....*....|...
gi 446931279 228 AYITGETLHVNGG 240
Cdd:cd08943  237 GKTTGAIVTVDGG 249
PRK07677 PRK07677
short chain dehydrogenase; Provisional
5-243 1.63e-35

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 126.72  E-value: 1.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDYLGANGKGL--MLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGrTKEKLEEAKLEIEQFPGQVLtvQMDVRNPEDVQKMVEQIDEKFGRID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGitrDNLLMRMKD---EEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK07677  81 ALINNAA---GNFICPAEDlsvNGWNSVIDIVLNGTFYCSQAVGKYWIEKgIKGNIINMVATYAWDAGPGVIHSAAAKAG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASR-GITVNVVAPGFIE-TDMTRALSDDQRAG--ILAQVPAGRLGGAQEIANAVAFLASDEAAYITGE 233
Cdd:PRK07677 158 VLAMTRTLAVEWGRKyGIRVNAIAPGPIErTGGADKLWESEEAAkrTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGT 237
                        250
                 ....*....|
gi 446931279 234 TLHVNGGMYM 243
Cdd:PRK07677 238 CITMDGGQWL 247
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
5-188 1.90e-35

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 126.21  E-value: 1.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSEN----GAQAISDYLGANGKGLM---LNVTDPASIESVLEKIRAEF 77
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESkleeAVEEIEAEANASGQKVSyisADLSDYEEVEQAFAQAVEKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFA 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDM 188
Cdd:cd08939  161 LRGLAESLRQELKPYNIRVSVVYPPDTDTPG 191
PRK09730 PRK09730
SDR family oxidoreductase;
6-240 1.96e-35

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 126.12  E-value: 1.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQ-AISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVaVNYQQNLHAAQeVVNLITQAGGKAFVLqaDISDENQVVAMFTAIDQHDEPLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGIT-RDNLLMRMKDEEWNDIIETNLSSVFRLSK-AVMRamMKKRHG----RIITIGSVVGTMGNGGQ-ANYAAA 154
Cdd:PRK09730  82 ALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCReAVKR--MALKHGgsggAIVNVSSAASRLGAPGEyVDYAAS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAG-ILAQVPAGRLGGAQEIANAVAFLASDEAAYITGE 233
Cdd:PRK09730 160 KGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRVDrVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGS 239

                 ....*..
gi 446931279 234 TLHVNGG 240
Cdd:PRK09730 240 FIDLAGG 246
PRK07454 PRK07454
SDR family oxidoreductase;
6-209 2.81e-35

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 125.84  E-value: 2.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELrstGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:PRK07454  87 LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446931279 163 KSLAREVASRGITVNVVAPGFIET------------DMTRALSDDQRAGIL---AQVPAGRL 209
Cdd:PRK07454 167 KCLAEEERSHGIRVCTITLGAVNTplwdtetvqadfDRSAMLSPEQVAQTIlhlAQLPPSAV 228
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
8-189 2.94e-35

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: 125.52  E-value: 2.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGL---MLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVeveILDVTDEERNQLVIAELEAELGGLDLVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKS 164
Cdd:cd05350   81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAES 160
                        170       180
                 ....*....|....*....|....*
gi 446931279 165 LAREVASRGITVNVVAPGFIETDMT 189
Cdd:cd05350  161 LRYDVKKRGIRVTVINPGFIDTPLT 185
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
1-198 2.99e-35

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 125.66  E-value: 2.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG-AQAISDYLGAngKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:COG3967    1 MKLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKlEEAAAANPGL--HTIVLDVADPASIAALAEQVTAEFPD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRmKDEEWNDI---IETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:COG3967   79 LNVLINNAGIMRAEDLLD-EAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRA 198
Cdd:COG3967  158 ALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRA 199
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
3-240 3.26e-35

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 126.21  E-value: 3.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLnVTD---PASIESVLEKIRAEFGE 79
Cdd:PRK12823   6 FAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRAAGGEALAL-TADletYAGAQAAMAAAVEAFGR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITrdnllMRMK------DEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSvVGTMG-NggQANYA 152
Cdd:PRK12823  85 IDVLINNVGGT-----IWAKpfeeyeEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSS-IATRGiN--RVPYS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 153 AAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTR------ALSDDQRA---GILAQVPA----GRLGGAQEIANAV 219
Cdd:PRK12823 157 AAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPPRRvprnaaPQSEQEKAwyqQIVDQTLDsslmKRYGTIDEQVAAI 236
                        250       260
                 ....*....|....*....|.
gi 446931279 220 AFLASDEAAYITGETLHVNGG 240
Cdd:PRK12823 237 LFLASDEASYITGTVLPVGGG 257
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
3-240 3.90e-35

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: 125.73  E-value: 3.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG----LMLNVTDPASIESVLEKIRAEFG 78
Cdd:cd08933    7 YADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGsckfVPCDVTKEEDIKTLISVTVERFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGI-----TRDNllmrMKDEEWNDIIETNLSSVFRLSKAVMrAMMKKRHGRIITIGSVVGTMGNGGQANYAA 153
Cdd:cd08933   87 RIDCLVNNAGWhpphqTTDE----TSAQEFRDLLNLNLISYFLASKYAL-PHLRKSQGNIINLSSLVGSIGQKQAAPYVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDM---TRALSDDQRA----GILAQvPAGRLGGAQEIANAVAFLASdE 226
Cdd:cd08933  162 TKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLweeLAAQTPDTLAtikeGELAQ-LLGRMGTEAESGLAALFLAA-E 239
                        250
                 ....*....|....
gi 446931279 227 AAYITGETLHVNGG 240
Cdd:cd08933  240 ATFCTGIDLLLSGG 253
PRK06198 PRK06198
short chain dehydrogenase; Provisional
3-236 5.79e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 125.50  E-value: 5.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAK-VIGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFG 78
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFvqaDLSDVEDCRRVVAAADEAFG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKR-HGRIITIGSvvgTMGNGGQ---ANYAAA 154
Cdd:PRK06198  84 RLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGS---MSAHGGQpflAAYCAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRAL-------SDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:PRK06198 161 KGALATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIqrefhgaPDDWLEKAAATQPFGRLLDPDEVARAVAFLLSDES 240

                 ....*....
gi 446931279 228 AYITGETLH 236
Cdd:PRK06198 241 GLMTGSVID 249
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
5-241 1.17e-34

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: 124.74  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    5 GKIALVTGASRGIGRAIAETLAARGAKVIGT-------------ATSENGAQAISDYlGANGKGLMLNVTDPASIESVLE 71
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVdlcaddpavgyplATRAELDAVAAAC-PDQVLPVIADVRDPAALAAAVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   72 KIRAEFGEVDILVNNAG-ITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK---RHGRIITIGSVVGTMGNGG 147
Cdd:TIGR04504  80 LAVERWGRLDAAVAAAGvIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARpdpRGGRFVAVASAAATRGLPH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  148 QANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDM---TRALSDDQRAGILA-QVPAGRLGGAQEIANAVAFLA 223
Cdd:TIGR04504 160 LAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMlaaTARLYGLTDVEEFAgHQLLGRLLEPEEVAAAVAWLC 239
                         250
                  ....*....|....*...
gi 446931279  224 SDEAAYITGETLHVNGGM 241
Cdd:TIGR04504 240 SPASSAVTGSVVHADGGF 257
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
6-187 1.20e-34

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: 123.77  E-value: 1.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:cd08929   81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAA 160
                        170       180
                 ....*....|....*....|..
gi 446931279 166 AREVASRGITVNVVAPGFIETD 187
Cdd:cd08929  161 MLDLREANIRVVNVMPGSVDTG 182
PRK12742 PRK12742
SDR family oxidoreductase;
1-240 2.93e-34

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 122.94  E-value: 2.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGT-ATSENGAQAISDYLGANGkglmlNVTDPASIESVLEKIRaEFGE 79
Cdd:PRK12742   2 GAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDAAERLAQETGATA-----VQTDSADRDAVIDVVR-KSGA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGT-MGNGGQANYAAAKAGL 158
Cdd:PRK12742  76 LDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIIIGSVNGDrMPVAGMAAYAASKSAL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRAlSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVN 238
Cdd:PRK12742 154 QGMARGLARDFGPRGITINVVQPGPIDTDANPA-NGPMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMHTID 232

                 ..
gi 446931279 239 GG 240
Cdd:PRK12742 233 GA 234
PLN02253 PLN02253
xanthoxin dehydrogenase
4-240 2.96e-34

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 124.17  E-value: 2.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEVD 81
Cdd:PLN02253  17 LGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFhcDVTVEDDVSRAVDFTVDKFGTLD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGIT-------RDNLLmrmkdEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAA 154
Cdd:PLN02253  97 IMVNNAGLTgppcpdiRNVEL-----SEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRA-LSDDQR-----AGILAQVPA-GRLGG----AQEIANAVAFLA 223
Cdd:PLN02253 172 KHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAhLPEDERtedalAGFRAFAGKnANLKGveltVDDVANAVLFLA 251
                        250
                 ....*....|....*..
gi 446931279 224 SDEAAYITGETLHVNGG 240
Cdd:PLN02253 252 SDEARYISGLNLMIDGG 268
PRK12746 PRK12746
SDR family oxidoreductase;
2-240 9.76e-34

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 122.06  E-value: 9.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLE--------- 71
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVaIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKlveqlknel 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  72 KIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANY 151
Cdd:PRK12746  83 QIRVGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 152 AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPA--GRLGGAQEIANAVAFLASDEAAY 229
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFATNSSvfGRIGQVEDIADAVAFLASSDSRW 240
                        250
                 ....*....|.
gi 446931279 230 ITGETLHVNGG 240
Cdd:PRK12746 241 VTGQIIDVSGG 251
PRK06125 PRK06125
short chain dehydrogenase; Provisional
1-241 1.25e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 122.07  E-value: 1.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG-AQAISDYLGANGKGLMLNVTDPASIESVlEKIRAEFGE 79
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADAlEALAADLRAAHGVDVAVHALDLSSPEAR-EQLAAEAGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIItigSVVGTMGNGGQANY---AAAKA 156
Cdd:PRK06125  82 IDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIV---NVIGAAGENPDADYicgSAGNA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETD------MTRA---LSDDQR-AGILAQVPAGRLGGAQEIANAVAFLASDE 226
Cdd:PRK06125 159 ALMAFTRALGGKSLDDGVRVVGVNPGPVATDrmltllKGRAraeLGDESRwQELLAGLPLGRPATPEEVADLVAFLASPR 238
                        250
                 ....*....|....*
gi 446931279 227 AAYITGETLHVNGGM 241
Cdd:PRK06125 239 SGYTSGTVVTVDGGI 253
PRK05650 PRK05650
SDR family oxidoreductase;
9-188 2.82e-33

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 121.30  E-value: 2.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLaLADVNEEGGEETLKLLREAGGDGFYQrcDVRDYSQLTALAQACEEKWGGIDVIVN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:PRK05650  84 NAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETL 163
                        170       180
                 ....*....|....*....|...
gi 446931279 166 AREVASRGITVNVVAPGFIETDM 188
Cdd:PRK05650 164 LVELADDEIGVHVVCPSFFQTNL 186
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
5-182 4.05e-33

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: 120.19  E-value: 4.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD---------------YLGANGKGLMLNVTDPASIESV 69
Cdd:cd05338    3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNGSAkslpgtieetaeeieAAGGQALPIVVDVRDEDQVRAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  70 LEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQA 149
Cdd:cd05338   83 VEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDV 162
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 150 NYAAAKAGLIGFSKSLAREVASRGITVNVVAPG 182
Cdd:cd05338  163 AYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS 195
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
8-190 4.82e-33

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 119.71  E-value: 4.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARG-AKVIGTATSENGAQAISDyLGANGKGLM---LNVTDP--ASIESVleKIRAEFGEVD 81
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAA-LGASHSRLHileLDVTDEiaESAEAV--AERLGDAGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMR-MKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGN---GGQANYAAAKAG 157
Cdd:cd05325   78 VLINNAGILHSYGPASeVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDntsGGWYSYRASKAA 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTR 190
Cdd:cd05325  158 LNMLTKSLAVELKRDGITVVSLHPGWVRTDMGG 190
PRK06128 PRK06128
SDR family oxidoreductase;
5-240 6.60e-33

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 121.12  E-value: 6.60e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGT--ATSENGAQAISDYLGANG-KGLML--NVTDPASIESVLEKIRAEFGE 79
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIALNylPEEEQDAAEVVQLIQAEGrKAVALpgDLKDEAFCRQLVERAVKELGG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAG--ITRDNLlMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK06128 135 LDILVNIAGkqTAVKDI-ADITTEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTGSIQSYQPSPTLLDYASTKAA 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDM--TRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:PRK06128 212 IVAFTKALAKQVAEKGIRVNAVAPGPVWTPLqpSGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQESSYVTGEVF 291

                 ....*
gi 446931279 236 HVNGG 240
Cdd:PRK06128 292 GVTGG 296
PRK06947 PRK06947
SDR family oxidoreductase;
6-240 6.79e-33

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 119.52  E-value: 6.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVgINYARDAAAAEETADAVRAAGGRACVvagDVANEADVIAMFDAVQSAFGRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNL-LMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGR---IITIGSVVGTMGNGGQ-ANYAAAKA 156
Cdd:PRK06947  83 ALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGSPNEyVDYAGSKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGIL-AQVPAGRLGGAQEIANAVAFLASDEAAYITGETL 235
Cdd:PRK06947 163 AVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLgAQTPLGRAGEADEVAETIVWLLSDAASYVTGALL 242

                 ....*
gi 446931279 236 HVNGG 240
Cdd:PRK06947 243 DVGGG 247
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-240 8.99e-33

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 119.44  E-value: 8.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVI-----GTATSENGAQAISDYlGANGKGLMLNVTDPASIESVLEKIRA 75
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVvnakkRAEEMNETLKMVKEN-GGEGIGVLADVSTREGCETLAKATID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  76 EFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAK 155
Cdd:PRK06077  81 RYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 156 AGLIGFSKSLAREVASRgITVNVVAPGFIETDMTRAL------SDDQRAGILAQVpaGRLGGAQEIANAVAFLASDEAay 229
Cdd:PRK06077 159 AAVINLTKYLALELAPK-IRVNAIAPGFVKTKLGESLfkvlgmSEKEFAEKFTLM--GKILDPEEVAEFVAAILKIES-- 233
                        250
                 ....*....|.
gi 446931279 230 ITGETLHVNGG 240
Cdd:PRK06077 234 ITGQVFVLDSG 244
PRK08263 PRK08263
short chain dehydrogenase; Provisional
5-208 9.50e-33

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 120.14  E-value: 9.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKS 164
Cdd:PRK08263  83 NNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSEA 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446931279 165 LAREVASRGITVNVVAPGFIETD-----MTRALSDDQRAGILAQVPAGR 208
Cdd:PRK08263 163 LAQEVAEFGIKVTLVEPGGYSTDwagtsAKRATPLDAYDTLREELAEQW 211
PRK06182 PRK06182
short chain dehydrogenase; Validated
6-187 1.01e-32

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 119.68  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYlgaNGKGLMLNVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASL---GVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:PRK06182  81 NAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDAL 160
                        170       180
                 ....*....|....*....|..
gi 446931279 166 AREVASRGITVNVVAPGFIETD 187
Cdd:PRK06182 161 RLEVAPFGIDVVVIEPGGIKTE 182
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-243 1.26e-32

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 119.29  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK07576   5 FDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLqqaGPEGLGVSADVRDYAAVEAAFAQIADEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMrAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK07576  85 GPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAY-PLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIE-TD-MTR-ALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:PRK07576 164 VDMLTRTLALEWGPEGIRVNSIVPGPIAgTEgMARlAPSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVV 243

                 ....*....
gi 446931279 235 LHVNGGMYM 243
Cdd:PRK07576 244 LPVDGGWSL 252
PRK05872 PRK05872
short chain dehydrogenase; Provisional
4-199 4.50e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 118.92  E-value: 4.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK05872   8 AGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLTVvaDVTDLAAMQAAAEEAVERFGGID 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRhGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK05872  88 VVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYCASKAGVEAF 166
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAG 199
Cdd:PRK05872 167 ANALRLEVAHHGVTVGSAYLSWIDTDLVRDADADLPAF 204
PRK06181 PRK06181
SDR family oxidoreductase;
5-219 5.30e-32

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 117.77  E-value: 5.30e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSE----NGAQAISDYlGANGKGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNEtrlaSLAQELADH-GGEALVVPTDVSDAEACERLIEAAVARFGGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEW-NDIIETNLSSVFRLSKAVMrAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLI 159
Cdd:PRK06181  80 DILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAAL-PHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALH 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446931279 160 GFSKSLAREVASRGITVNVVAPGFIETDM-TRALSDDQRAgiLAQVPA--GRLGGAQEIANAV 219
Cdd:PRK06181 159 GFFDSLRIELADDGVAVTVVCPGFVATDIrKRALDGDGKP--LGKSPMqeSKIMSAEECAEAI 219
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
5-190 5.58e-32

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: 117.71  E-value: 5.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG-----LMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNakvevIQLDLSSLASVRQFAEEFLARFPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGItrdnllMRMKDEEWNDIIE----TNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGN---------- 145
Cdd:cd05327   81 LDILINNAGI------MAPPRRLTKDGFElqfaVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPidfndldlen 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446931279 146 ----GGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTR 190
Cdd:cd05327  155 nkeySPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLR 203
PRK06914 PRK06914
SDR family oxidoreductase;
4-224 8.59e-32

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 117.43  E-value: 8.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGA-----QAISDYLGANGKGLMLNVTDPASIESVLEKIRaEFG 78
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQenllsQATQLNLQQNIKVQQLDVTDQNSIHNFQLVLK-EIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDM--------TRALSDD-----QRAGILAQVPAG--RLGGAQEIANAVAFLA 223
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIwevgkqlaENQSETTspykeYMKKIQKHINSGsdTFGNPIDVANLIVEIA 240

                 .
gi 446931279 224 S 224
Cdd:PRK06914 241 E 241
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
5-224 2.09e-30

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: 113.38  E-value: 2.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML----NVTDPASIESVLEKIRAEFGEV 80
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFpyqcDLSNEEQILSMFSAIRTQHQGV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDIIETN---LSSVFRLSKAVMRAmMKKRHGRIITIGSVVG-TMGNGGQAN-YAAAK 155
Cdd:cd05343   86 DVCINNAGLARPEPLLSGKTEGWKEMFDVNvlaLSICTREAYQSMKE-RNVDDGHIININSMSGhRVPPVSVFHfYAATK 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446931279 156 AGLIGFSKSLAREV--ASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLAS 224
Cdd:cd05343  165 HAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANAVLYVLS 235
PRK08416 PRK08416
enoyl-ACP reductase;
2-240 3.68e-30

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 112.94  E-value: 3.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATS-----ENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAE 76
Cdd:PRK08416   5 EMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSnveeaNKIAEDLEQKYGIKAKAYPLNILEPETYKELFKKIDED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNL------LMRMKDEEWNDI-IETNLSSVFRLSKAVMRaMMKKRHGRIITIGSVVGTMGNGGQA 149
Cdd:PRK08416  85 FDRVDFFISNAIISGRAVvggytkFMRLKPKGLNNIyTATVNAFVVGAQEAAKR-MEKVGGGSIISLSSTGNLVYIENYA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 150 NYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSD--DQRAGILAQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:PRK08416 164 GHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNyeEVKAKTEELSPLNRMGQPEDLAGACLFLCSEKA 243
                        250
                 ....*....|...
gi 446931279 228 AYITGETLHVNGG 240
Cdd:PRK08416 244 SWLTGQTIVVDGG 256
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
1-202 4.63e-30

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: 111.63  E-value: 4.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDylGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd05370    1 MKLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGrREERLAEAKKE--LPNIHTIVLDVGDAESVEALAEALLSEYPN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRD-NLLMRMKDEEWNDI-IETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:cd05370   79 LDILINNAGIQRPiDLRDPASDLDKADTeIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILA 202
Cdd:cd05370  159 LHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRK 203
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
6-205 1.03e-29

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: 111.99  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAI------SDYLgangKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAKelrrvcSDRL----RTLQLDVTKPEQIKRAAQWVKEHVGE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDI--LVNNAGIT---RDNLLMRMKDeeWNDIIETNLSSVFRLSKAvMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAA 154
Cdd:cd09805   77 KGLwgLVNNAGILgfgGDEELLPMDD--YRKCMEVNLFGTVEVTKA-FLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCAS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTR--ALSDDQRAGILAQVP 205
Cdd:cd09805  154 KAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGnsELWEKQAKKLWERLP 206
PRK08264 PRK08264
SDR family oxidoreductase;
1-192 1.92e-29

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 110.36  E-value: 1.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGA-KVIGTATSENGAqaisDYLGANGKGLMLNVTDPASIESVLEKIraefGE 79
Cdd:PRK08264   2 MDIKGKVVLVTGANRGIGRAFVEQLLARGAaKVYAAARDPESV----TDLGPRVVPLQLDVTDPASVAAAAEAA----SD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEE-WNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK08264  74 VTILVNNAGIFRTGSLLLEGDEDaLRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAA 153
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTRAL 192
Cdd:PRK08264 154 WSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGL 187
PRK05717 PRK05717
SDR family oxidoreductase;
5-241 2.78e-29

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 110.36  E-value: 2.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGIT--RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMrAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:PRK05717  90 CNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCA-PYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLALT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRgITVNVVAPGFIET-DMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:PRK05717 169 HALAISLGPE-IRVNAVSPGWIDArDPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVVDGGM 247
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
10-186 2.81e-29

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: 109.78  E-value: 2.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  10 VTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNN 86
Cdd:cd05360    5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVrelGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  87 AGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLA 166
Cdd:cd05360   85 AGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLR 164
                        170       180
                 ....*....|....*....|..
gi 446931279 167 REVASRG--ITVNVVAPGFIET 186
Cdd:cd05360  165 AELAHDGapISVTLVQPTAMNT 186
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
3-244 4.28e-29

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: 109.73  E-value: 4.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGA--SRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFG 78
Cdd:COG0623    3 LKGKRGLITGVanDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEELGSALVLpcDVTDDEQIDALFDEIKEKWG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILV-------NNAG------ITRDNLLMRMkdeewnDIietnlsSVFRLsKAVMRA---MMKKRhGRIIT---IGSV 139
Cdd:COG0623   83 KLDFLVhsiafapKEELggrfldTSREGFLLAM------DI------SAYSL-VALAKAaepLMNEG-GSIVTltyLGAE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 140 V-----GTMGnggqanyaAAKAGLIGFSKSLAREVASRGITVNVVAPGFIetdMTRALS-----DDQRAGILAQVPAGRL 209
Cdd:COG0623  149 RvvpnyNVMG--------VAKAALEASVRYLAADLGPKGIRVNAISAGPI---KTLAASgipgfDKLLDYAEERAPLGRN 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446931279 210 GGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV 244
Cdd:COG0623  218 VTIEEVGNAAAFLLSDLASGITGEIIYVDGGYHIM 252
PRK06482 PRK06482
SDR family oxidoreductase;
9-209 5.81e-29

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 110.20  E-value: 5.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSengAQAISDYLGANGKGL---MLNVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRR---PDALDDLKARYGDRLwvlQLDVTDSAAVRAVVDRAFAALGRIDVVVS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:PRK06482  83 NAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAV 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446931279 166 AREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRL 209
Cdd:PRK06482 163 AQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDAYDDTPVGDL 206
PRK05855 PRK05855
SDR family oxidoreductase;
3-203 6.46e-29

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 113.92  E-value: 6.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQA---ISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK05855 313 FSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERtaeLIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGV 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKK-RHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK05855 393 PDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSLPAYATSKAAV 472
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDMTR-----ALSDDQRAGILAQ 203
Cdd:PRK05855 473 LMLSECLRAELAAAGIGVTAICPGFVDTNIVAttrfaGADAEDEARRRGR 522
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
7-244 9.04e-29

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: 109.25  E-value: 9.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    7 IALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKG--------LMLNVTDPASIESVLEKIRAEF 77
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVvLHYHRSAAAASTLAAELNARRPNsavtcqadLSNSATLFSRCEAIIDACFRAF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   78 GEVDILVNNAGITRDNLLMRMKDEEWN-----------DIIETNLSSVFRLSKAVMRAMMKKR---HGRIITIGSVVGTM 143
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLRGDAGEGVgdkkslevqvaELFGSNAIAPYFLIKAFAQRQAGTRaeqRSTNLSIVNLCDAM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  144 GNG---GQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGF--IETDMTRALSDDQRAgilaQVPAG-RLGGAQEIAN 217
Cdd:TIGR02685 163 TDQpllGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLslLPDAMPFEVQEDYRR----KVPLGqREASAEQIAD 238
                         250       260
                  ....*....|....*....|....*..
gi 446931279  218 AVAFLASDEAAYITGETLHVNGGMYMV 244
Cdd:TIGR02685 239 VVIFLVSPKAKYITGTCIKVDGGLSLT 265
PRK08339 PRK08339
short chain dehydrogenase; Provisional
1-240 9.12e-29

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 109.17  E-value: 9.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG----AQAISDYLGANGKGLMLNVTDPASIESVLEKIRaE 76
Cdd:PRK08339   4 IDLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENlkkaREKIKSESNVDVSYIVADLTKREDLERTVKELK-N 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK08339  83 IGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDD--QRAGILAQ---------VPAGRLGGAQEIANAVAFLASD 225
Cdd:PRK08339 163 SMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDraKREGKSVEealqeyakpIPLGRLGEPEEIGYLVAFLASD 242
                        250
                 ....*....|....*
gi 446931279 226 EAAYITGETLHVNGG 240
Cdd:PRK08339 243 LGSYINGAMIPVDGG 257
PRK07775 PRK07775
SDR family oxidoreductase;
8-224 2.08e-28

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 108.69  E-value: 2.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK---GLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGeavAFPLDVTDPDSVKSFVAQAEEALGEIEVLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKS 164
Cdd:PRK07775  93 SGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTN 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446931279 165 LAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILA------QVPAGRLGGAQEIANAVAFLAS 224
Cdd:PRK07775 173 LQMELEGTGVRASIVHPGPTLTGMGWSLPAEVIGPMLEdwakwgQARHDYFLRASDLARAITFVAE 238
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
4-241 2.18e-28

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 108.12  E-value: 2.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:PRK06200   5 HGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITrdNLLMRMKDEEWNDI-------IETNLSSVFRLSKAVMRAmMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK06200  85 VGNAGIW--DYNTSLVDIPAETLdtafdeiFNVNVKGYLLGAKAALPA-LKASGGSMIFTLSNSSFYPGGGGPLYTASKH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRgITVNVVAPGFIETDM---------TRALSD-DQRAGILAQV-PAGRLGGAQEIANAVAFLASD 225
Cdd:PRK06200 162 AVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLrgpaslgqgETSISDsPGLADMIAAItPLQFAPQPEDHTGPYVLLASR 240
                        250
                 ....*....|....*..
gi 446931279 226 E-AAYITGETLHVNGGM 241
Cdd:PRK06200 241 RnSRALTGVVINADGGL 257
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
3-189 3.12e-28

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: 107.11  E-value: 3.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGA-KVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRaefgEVD 81
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAK----DVD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDII-ETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:cd05354   77 VVINNAGVLKPATLLEEGALEALKQEmDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYS 156
                        170       180
                 ....*....|....*....|....*....
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMT 189
Cdd:cd05354  157 LTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
4-241 4.18e-28

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: 107.44  E-value: 4.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:cd05348    3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGI-----TRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIgSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05348   83 IGNAGIwdystSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTV-SNAGFYPGGGGPLYTASKHAV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRgITVNVVAPGFIETDMTRALS-------------DDQRAGILaqvPAGRLGGAQEIANAVAFLAS- 224
Cdd:cd05348  162 VGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASlgqgetsistpplDDMLKSIL---PLGFAPEPEDYTGAYVFLASr 237
                        250
                 ....*....|....*..
gi 446931279 225 DEAAYITGETLHVNGGM 241
Cdd:cd05348  238 GDNRPATGTVINYDGGM 254
PRK07985 PRK07985
SDR family oxidoreductase;
3-243 6.61e-28

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 107.77  E-value: 6.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGT--ATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEF 77
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylPVEEEDAQDVKKIIEECGRKAVLlpgDLSDEKFARSLVHEAHKAL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGI-TRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK07985 127 GGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSPHLLDYAATKA 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIET--DMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGET 234
Cdd:PRK07985 205 AILNYSRGLAKQVAEKGIRVNIVAPGPIWTalQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYVTAEV 284

                 ....*....
gi 446931279 235 LHVNGGMYM 243
Cdd:PRK07985 285 HGVCGGEHL 293
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
7-243 2.76e-27

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: 104.97  E-value: 2.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPAS-IESVLEkiraEFGEVDILVN 85
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQAFESENPGTKALSEQKPEElVDAVLQ----AGGAIDVLVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRD-NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKS 164
Cdd:cd05361   79 NDYIPRPmNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAES 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 165 LAREVASRGITVNVVAPGFIETDMTRALSD-----DQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNG 239
Cdd:cd05361  159 LAKELSRDNILVYAIGPNFFNSPTYFPTSDwennpELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAFAG 238

                 ....
gi 446931279 240 GMYM 243
Cdd:cd05361  239 GYLP 242
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
7-199 3.03e-27

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 104.84  E-value: 3.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNN 86
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  87 AGITrdnLLM----RMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:PRK10538  82 AGLA---LGLepahKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRGITVNVVAPGFI---ETDMTRALSDDQRAG 199
Cdd:PRK10538 159 LNLRTDLHGTAVRVTDIEPGLVggtEFSNVRFKGDDGKAE 198
PRK08219 PRK08219
SDR family oxidoreductase;
6-221 5.79e-27

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 103.47  E-value: 5.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAngKGLMLNVTDPASIESVLEKIraefGEVDILVN 85
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPTHTLLLGGRPAERLDELAAELPGA--TPFPVDLTDPEAIAAAVEQL----GRLDVLVH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAmMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:PRK08219  78 NAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPA-LRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALADAL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446931279 166 AREVASRgITVNVVAPGFIETDMTRALsddqRAGILAQVPAGRLGGAQEIANAVAF 221
Cdd:PRK08219 157 REEEPGN-VRVTSVHPGRTDTDMQRGL----VAQEGGEYDPERYLRPETVAKAVRF 207
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
6-206 6.47e-27

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: 104.08  E-value: 6.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLA---ARGAKVIGT----ATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAefG 78
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLAsdpSKRFKVYATmrdlKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTE--R 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd09806   79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFAL 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETD-MTRALSDDQRAGILAQVPA 206
Cdd:cd09806  159 EGLCESLAVQLLPFNVHLSLIECGPVHTAfMEKVLGSPEEVLDRTADDI 207
PRK12747 PRK12747
short chain dehydrogenase; Provisional
3-240 1.01e-26

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 103.62  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVI---GTATSE----------NGAQAISdyLGANGKGLMLNVTDPASIESV 69
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAihyGNRKEEaeetvyeiqsNGGSAFS--IGANLESLHGVEALYSSLDNE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  70 LEKiRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQA 149
Cdd:PRK12747  80 LQN-RTGSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 150 NYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAG--RLGGAQEIANAVAFLASDEA 227
Cdd:PRK12747 157 AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAfnRLGEVEDIADTAAFLASPDS 236
                        250
                 ....*....|...
gi 446931279 228 AYITGETLHVNGG 240
Cdd:PRK12747 237 RWVTGQLIDVSGG 249
PRK07201 PRK07201
SDR family oxidoreductase;
4-220 1.17e-26

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 107.73  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK07201 370 VGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGgtaHAYTCDLTDSAAVDHTVKDILAEHGHV 449
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAG--ITR--DNLLMRMKDEEwnDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVvgtmgnGGQAN------ 150
Cdd:PRK07201 450 DYLVNNAGrsIRRsvENSTDRFHDYE--RTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSI------GVQTNaprfsa 521
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 151 YAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDM---------TRALSDDQRAGILAQV----P---AGRLGGAQE 214
Cdd:PRK07201 522 YVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMiaptkrynnVPTISPEEAADMVVRAivekPkriDTPLGTFAE 601

                 ....*.
gi 446931279 215 IANAVA 220
Cdd:PRK07201 602 VGHALA 607
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
9-241 1.56e-26

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: 102.96  E-value: 1.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAisdylgangkglmlNVTDPASIESVLEKIRAEFGEV-DILVNNA 87
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLREADVIA--------------DLSTPEGRAAAIADVLARCSGVlDGLVNCA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 GITRDNLLmrmkdeewNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNG--------------------- 146
Cdd:cd05328   69 GVGGTTVA--------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQdklelakalaagtearavala 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 147 ------GQANYAAAKAGLIGFSKSLAREVAS-RGITVNVVAPGFIETDMTRALSDDQRAGILAQV---PAGRLGGAQEIA 216
Cdd:cd05328  141 ehagqpGYLAYAGSKEALTVWTRRRAATWLYgAGVRVNTVAPGPVETPILQAFLQDPRGGESVDAfvtPMGRRAEPDEIA 220
                        250       260
                 ....*....|....*....|....*
gi 446931279 217 NAVAFLASDEAAYITGETLHVNGGM 241
Cdd:cd05328  221 PVIAFLASDAASWINGANLFVDGGL 245
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
9-233 1.78e-26

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 102.75  E-value: 1.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARG--AKVIGTATSENGAQAISDYLGANGK--GLMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:cd05367    3 ILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELRPGLRvtTVKADLSDAAGVEQLLEAIRKLDGERDLLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDnlLMRMKD---EEWNDIIETNLSSVFRLSKAVMRAMMKKR-HGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:cd05367   83 NNAGSLGP--VSKIEFidlDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446931279 161 FSKSLAREvaSRGITVNVVAPGFIETDMTRAL----SDDQRAGILAQVPA-GRLGGAQEIANAVAFLAsDEAAYITGE 233
Cdd:cd05367  161 FFRVLAAE--EPDVRVLSYAPGVVDTDMQREIretsADPETRSRFRSLKEkGELLDPEQSAEKLANLL-EKDKFESGA 235
PRK05693 PRK05693
SDR family oxidoreductase;
6-205 2.58e-26

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 102.95  E-value: 2.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISdylGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALA---AAGFTAVQLDVNDGAALARLAEELEAEHGGLDVLIN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRhGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSL 165
Cdd:PRK05693  79 NAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSR-GLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDAL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446931279 166 AREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVP 205
Cdd:PRK05693 158 RLELAPFGVQVMEVQPGAIASQFASNASREAEQLLAEQSP 197
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
5-235 8.80e-26

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: 101.37  E-value: 8.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTA-TSENGAQAISDYLGAN-GKGLMLNV--TDPASIESVLEKIRAEF-GE 79
Cdd:cd09763    3 GKIALVTGASRGIGRGIALQLGEAGATVYITGrTILPQLPGTAEEIEARgGKCIPVRCdhSDDDEVEALFERVAREQqGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNA-------GITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQAnYA 152
Cdd:cd09763   83 LDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVA-YG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 153 AAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVP-AGRLGGAQE-IANAVAFLASD-EAAY 229
Cdd:cd09763  162 VGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKERdAFLNGETTEySGRCVVALAADpDLME 241

                 ....*.
gi 446931279 230 ITGETL 235
Cdd:cd09763  242 LSGRVL 247
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
7-190 9.80e-26

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: 100.53  E-value: 9.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISD----YLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVdiirDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALA 160
                        170       180
                 ....*....|....*....|....*....
gi 446931279 163 KSLAREVASRGITV-NVVAPGFIETDMTR 190
Cdd:cd05373  161 QSMARELGPKGIHVaHVIIDGGIDTDFIR 189
PRK09186 PRK09186
flagellin modification protein A; Provisional
4-240 1.14e-25

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 100.83  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG-----LMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkklslVELDITDQESLEEFLSKSAEKYG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIET---NLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMG------NGGQ- 148
Cdd:PRK09186  83 KIDGAVNCAYPRNKDYGKKFFDVSLDDFNENlslHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVApkfeiyEGTSm 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 149 ---ANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIetdmtralSDDQRAGILAQVP-----AGRLgGAQEIANAVA 220
Cdd:PRK09186 163 tspVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGI--------LDNQPEAFLNAYKkccngKGML-DPDDICGTLV 233
                        250       260
                 ....*....|....*....|
gi 446931279 221 FLASDEAAYITGETLHVNGG 240
Cdd:PRK09186 234 FLLSDQSKYITGQNIIVDDG 253
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
5-235 1.36e-25

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: 100.34  E-value: 1.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG----LMLNVTDPAS--IESVLEKIRAEFG 78
Cdd:cd05340    4 DRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRqpqwFILDLLTCTSenCQQLAQRIAVNYP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLM-RMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:cd05340   84 RLDGVLHNAGLLGDVCPLsEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFA 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446931279 158 LIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILaQVPAgrlggaqEIANAVAFLASDEAAYITGETL 235
Cdd:cd05340  164 TEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKL-KTPA-------DIMPLYLWLMGDDSRRKTGMTF 233
PRK09134 PRK09134
SDR family oxidoreductase;
6-244 2.58e-25

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 100.00  E-value: 2.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANG-KGLML--NVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVaVHYNRSRDEAEALAAEIRALGrRAVALqaDLADEAEVRALVARASAALGPIT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIIT-IGSVVGTMgNGGQANYAAAKAGLIG 160
Cdd:PRK09134  90 LLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNmIDQRVWNL-NPDFLSYTLSKAALWT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRgITVNVVAPG--FIETDMTRALSDDQRAGilaqVPAGRLGGAQEIANAVAFLAsdEAAYITGETLHVN 238
Cdd:PRK09134 169 ATRTLAQALAPR-IRVNAIGPGptLPSGRQSPEDFARQHAA----TPLGRGSTPEEIAAAVRYLL--DAPSVTGQMIAVD 241

                 ....*.
gi 446931279 239 GGMYMV 244
Cdd:PRK09134 242 GGQHLA 247
PRK12744 PRK12744
SDR family oxidoreductase;
4-240 3.60e-25

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 99.43  E-value: 3.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIG-----TATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAE 76
Cdd:PRK12744   7 KGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynsAASKADAEETVAAVKAAGAKAVAFqaDLTTAAAVEKLFDDAKAA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIgsVVGTMG--NGGQANYAAA 154
Cdd:PRK12744  87 FGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTL--VTSLLGafTPFYSAYAGS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIET------DMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDeAA 228
Cdd:PRK12744 163 KAPVEHFTRAASKEFGARGISVTAVGPGPMDTpffypqEGAEAVAYHKTAAALSPFSKTGLTDIEDIVPFIRFLVTD-GW 241
                        250
                 ....*....|..
gi 446931279 229 YITGETLHVNGG 240
Cdd:PRK12744 242 WITGQTILINGG 253
PRK07832 PRK07832
SDR family oxidoreductase;
6-190 1.47e-24

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 98.19  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM----LNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPehraLDISDYDAVAAFAADIHAAHGSMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGR-IITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRGGhLVNVSSAAGLVALPWHAAYSASKFGLRG 160
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTR 190
Cdd:PRK07832 161 LSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK07109 PRK07109
short chain dehydrogenase; Provisional
1-186 1.67e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 96.53  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG-AQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEF 77
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGlEALAAEIRAAGGEALAVvaDVADAEAVQAAADRAEEEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK07109  84 GPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHA 163
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446931279 158 LIGFSKSLAREVASRG--ITVNVVAPGFIET 186
Cdd:PRK07109 164 IRGFTDSLRCELLHDGspVSVTMVQPPAVNT 194
PRK07024 PRK07024
SDR family oxidoreductase;
10-190 2.80e-23

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 94.61  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  10 VTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM--LNVTDPASIESVLEKIRAEFGEVDILVNNA 87
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSVyaADVRDADALAAAAADFIAAHGLPDVVIANA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 GITRDNLLMRMKD-EEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLA 166
Cdd:PRK07024  87 GISVGTLTEEREDlAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLR 166
                        170       180
                 ....*....|....*....|....
gi 446931279 167 REVASRGITVNVVAPGFIETDMTR 190
Cdd:PRK07024 167 VELRPAGVRVVTIAPGYIRTPMTA 190
PRK07041 PRK07041
SDR family oxidoreductase;
9-240 7.67e-23

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 92.79  E-value: 7.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGL--MLNVTDPASIESVLekirAEFGEVDILVNN 86
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVRtaALDITDEAAVDAFF----AEAGPFDHVVIT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  87 AGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVmrammkkrhgRIITIGSVVGTMG------NGGQANYAAAKAGLIG 160
Cdd:PRK07041  77 AADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----------RIAPGGSLTFVSGfaavrpSASGVLQGAINAALEA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASrgITVNVVAPGFIETDMTRALSDDQRAGILAQ----VPAGRLGGAQEIANAVAFLASDeaAYITGETLH 236
Cdd:PRK07041 147 LARGLALELAP--VRVNTVSPGLVDTPLWSKLAGDAREAMFAAaaerLPARRVGQPEDVANAILFLAAN--GFTTGSTVL 222

                 ....
gi 446931279 237 VNGG 240
Cdd:PRK07041 223 VDGG 226
PRK05866 PRK05866
SDR family oxidoreductase;
5-199 7.72e-23

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 94.04  E-value: 7.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK05866  40 GKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGgdaMAVPCDLSDLDAVDALVADVEKRIGGVD 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAG--ITR---DNLlmrmkdEEWNDIIET---NLSSVFRLSKAVMRAMMKKRHGRIITigsvVGTMGNGGQAN--- 150
Cdd:PRK05866 120 ILINNAGrsIRRplaESL------DRWHDVERTmvlNYYAPLRLIRGLAPGMLERGDGHIIN----VATWGVLSEASplf 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 151 --YAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDM---TR------ALSDDQRAG 199
Cdd:PRK05866 190 svYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMiapTKaydglpALTADEAAE 249
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
5-241 1.67e-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: 92.26  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGAS--RGIGRAIAETLAARGAKVIGTATSE---NGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd05372    1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQPEalrKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILV------NNAGITRDnlLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAA 153
Cdd:cd05372   81 LDGLVhsiafaPKVQLKGP--FLDTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYLGSERVVPGYNVMGV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIetdMTRALS-----DDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAA 228
Cdd:cd05372  157 AKAALESSVRYLAYELGRKGIRVNAISAGPI---KTLAASgitgfDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDLSS 233
                        250
                 ....*....|...
gi 446931279 229 YITGETLHVNGGM 241
Cdd:cd05372  234 GITGEIIYVDGGY 246
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-240 8.49e-22

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 90.21  E-value: 8.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFG 78
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYVvgDVSSTESARNVIEKAAKVLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKdeEWNDIIETNLSSVFRLSKAVMRAMmkkRHGRIITIGSVVGTMGNGG--QANYAAAKA 156
Cdd:PRK05786  81 AIDGLVVTVGGYVEDTVEEFS--GLEEMLTNHIKIPLYAVNASLRFL---KEGSSIVLVSSMSGIYKASpdQLSYAVAKA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMT--------RALSDDqragilaQVPagrlggAQEIANAVAFLASDEAA 228
Cdd:PRK05786 156 GLAKAVEILASELLGRGIRVNGIAPTTISGDFEpernwkklRKLGDD-------MAP------PEDFAKVIIWLLTDEAD 222
                        250
                 ....*....|..
gi 446931279 229 YITGETLHVNGG 240
Cdd:PRK05786 223 WVDGVVIPVDGG 234
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
4-191 8.83e-22

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 90.32  E-value: 8.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKG------LMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK08945  11 KDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPqpaiipLDLLTATPQNYQQLADTIEEQF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEE-WNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:PRK08945  91 GRLDGVLHNAGLLGELGPMEQQDPEvWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVSKF 170
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMtRA 191
Cdd:PRK08945 171 ATEGMMQVLADEYQGTNLRVNCINPGGTRTAM-RA 204
PRK08267 PRK08267
SDR family oxidoreductase;
9-219 9.15e-22

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 90.38  E-value: 9.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGA-NGKGLMLNVTDPASIESVLekirAEF-----GEVDI 82
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAgNAWTGALDVTDRAAWDAAL----ADFaaatgGRLDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFS 162
Cdd:PRK08267  81 LFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 163 KSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAqvpagRLG---GAQEIANAV 219
Cdd:PRK08267 161 EALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTK-----RLGvrlTPEDVAEAV 215
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
10-244 9.16e-22

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: 89.82  E-value: 9.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  10 VTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGA-NGKGLMLNVTDPASIESVLEKI-RAEFGEVDILVNNA 87
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAeNVVAGALDVTDRAAWAAALADFaAATGGRLDALFNNA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 GITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAR 167
Cdd:cd08931   85 GVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDV 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446931279 168 EVASRGITVNVVAPGFIETDMtralsddqragilaqVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV 244
Cdd:cd08931  165 EWARHGIRVADVWPWFVDTPI---------------LTKGETGAAPKKGLGRVLPVSDVAKVVWAAAHGVPKLHYTV 226
PRK05876 PRK05876
short chain dehydrogenase; Provisional
3-188 1.46e-21

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 90.40  E-value: 1.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANG---KGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGfdvHGVMCDVRHREEVTHLADEAFRLLGH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLMRMKDEEWNDIIETNL-SSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK05876  84 VDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLwGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGV 163
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRGITVNVVAPGFIETDM 188
Cdd:PRK05876 164 VGLAETLAREVTADGIGVSVLCPMVVETNL 193
PRK08278 PRK08278
SDR family oxidoreductase;
1-235 6.12e-20

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 85.73  E-value: 6.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTA-----------TSENGAQAISDylgANGKGL--MLNVTDPASIE 67
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAktaephpklpgTIHTAAEEIEA---AGGQALplVGDVRDEDQVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  68 SVLEKIRAEFGEVDILVNNAGITR----DNLLMRMKDeEWNDIietNLSSVFRLSKAVMRAMMKKRHGRIITIGSVV--G 141
Cdd:PRK08278  79 AAVAKAVERFGGIDICVNNASAINltgtEDTPMKRFD-LMQQI---NVRGTFLVSQACLPHLKKSENPHILTLSPPLnlD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 142 TMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAP-GFIETDMTRALsddqrAGILAQVPAGRlggAQEI-ANAV 219
Cdd:PRK08278 155 PKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrTTIATAAVRNL-----LGGDEAMRRSR---TPEImADAA 226
                        250
                 ....*....|....*.
gi 446931279 220 AFLASDEAAYITGETL 235
Cdd:PRK08278 227 YEILSRPAREFTGNFL 242
PRK05875 PRK05875
short chain dehydrogenase; Provisional
1-240 2.08e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 84.47  E-value: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML-----NVTDPASIESVLEKIRA 75
Cdd:PRK05875   3 LSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAGAVryepaDVTDEDQVARAVDAATA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  76 EFGEVDILVNNAGITRD-NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAA 154
Cdd:PRK05875  83 WHGRLHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYITG 232
Cdd:PRK05875 163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPElsADYRACTPLPRVGEVEDVANLAMFLLSDAASWITG 242

                 ....*...
gi 446931279 233 ETLHVNGG 240
Cdd:PRK05875 243 QVINVDGG 250
PRK09291 PRK09291
SDR family oxidoreductase;
5-186 2.13e-19

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 84.28  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGL---MLNVTDPASIEsvlekiRAEFGEVD 81
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALrveKLDLTDAIDRA------QAAEWDVD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK09291  76 VLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAI 155
                        170       180
                 ....*....|....*....|....*
gi 446931279 162 SKSLAREVASRGITVNVVAPGFIET 186
Cdd:PRK09291 156 AEAMHAELKPFGIQVATVNPGPYLT 180
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
9-240 3.06e-19

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 83.44  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGkgLMLNVTDPASIESVLEKIRAEFGEVDILVNNA- 87
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAGAQC--IQADFSTNAGIMAFIDELKQHTDGLRAIIHNAs 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 -------GITRDNLLMRMkdeewndiIETNLSSVFRLSKAVMRAMMKKRHGR--IITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:PRK06483  84 dwlaekpGAPLADVLARM--------MQIHVNAPYLLNLALEDLLRGHGHAAsdIIHITDYVVEKGSDKHIAYAASKAAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLAREVASRgITVNVVAPGFI---ETDmtralSDDQRAGILAQVPAGRLGGAQEIANAVAFLAsdEAAYITGETL 235
Cdd:PRK06483 156 DNMTLSFAAKLAPE-VKVNSIAPALIlfnEGD-----DAAYRQKALAKSLLKIEPGEEEIIDLVDYLL--TSCYVTGRSL 227

                 ....*
gi 446931279 236 HVNGG 240
Cdd:PRK06483 228 PVDGG 232
PRK06139 PRK06139
SDR family oxidoreductase;
1-186 4.21e-19

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 84.39  E-value: 4.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDY---LGANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK06139   3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEEcraLGAEVLVVPTDVTDADQVKALATQAASFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK06139  83 GRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFG 162
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 158 LIGFSKSLAREVAS-RGITVNVVAPGFIET 186
Cdd:PRK06139 163 LRGFSEALRGELADhPDIHVCDVYPAFMDT 192
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
9-167 7.91e-19

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: 84.73  E-value: 7.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAAR-GAKVI------GTATSENGAQAIsDYLGANGKGLM---LNVTDPASIESVLEKIRAEFG 78
Cdd:cd08953  209 LVTGGAGGIGRALARALARRyGARLVllgrspLPPEEEWKAQTL-AALEALGARVLyisADVTDAAAVRRLLEKVRERYG 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVmramMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd08953  288 AIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL----ADEPLDFFVLFSSVSAFFGGAGQADYAAANAFL 363

                 ....*....
gi 446931279 159 IGFSKSLAR 167
Cdd:cd08953  364 DAFAAYLRQ 372
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
3-232 1.19e-18

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 84.58  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQA-----ISDYLGANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:COG3347  423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAaaaelGGGYGADAVDATDVDVTAEAAVAAAFGFAGLDI 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMK-KRHGRIITIGSVVGTMGNGGQANYAAAKA 156
Cdd:COG3347  503 GGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGqGLGGSSVFAVSKNAAAAAYGAAAAATAKA 582
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 157 GLIGFSKSLAREVASRGITVNVVAPGFIETDMtRALSDDQRAGILAQVPAGRLGG---------------AQEIANAVAF 221
Cdd:COG3347  583 AAQHLLRALAAEGGANGINANRVNPDAVLDGS-AIWASAARAERAAAYGIGNLLLeevyrkrvalavlvlAEDIAEAAAF 661
                        250
                 ....*....|.
gi 446931279 222 LASDEAAYITG 232
Cdd:COG3347  662 FASDGGNKATG 672
PRK08251 PRK08251
SDR family oxidoreductase;
9-189 5.05e-18

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 80.36  E-value: 5.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM-----LNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYPGIKvavaaLDVNDHDQVFEVFAEFRDELGGLDRV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMG-NGGQANYAAAKAGLIGFS 162
Cdd:PRK08251  86 IVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGlPGVKAAYAASKAGVASLG 165
                        170       180
                 ....*....|....*....|....*..
gi 446931279 163 KSLAREVASRGITVNVVAPGFIETDMT 189
Cdd:PRK08251 166 EGLRAELAKTPIKVSTIEPGYIRSEMN 192
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
5-239 9.89e-18

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: 78.91  E-value: 9.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGkglmlnvTDPASIESVLEKIRAEFGEVDILV 84
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSD-------SFTEQAKQVVASVARLSGKVDALI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAG------ITRDNLLmrmkdEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVGTMGNGGQANYAAAKAGL 158
Cdd:cd05334   74 CVAGgwaggsAKSKSFV-----KNWDLMWKQNLWTSFIASHLATKHL--LSGGLLVLTGAKAALEPTPGMIGYGAAKAAV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 159 IGFSKSLARE--VASRGITVNVVAPGFIETDMTRALSDDqrAGILAQVPagrlggAQEIANAVAFLASDEAAYITGETLH 236
Cdd:cd05334  147 HQLTQSLAAEnsGLPAGSTANAILPVTLDTPANRKAMPD--ADFSSWTP------LEFIAELILFWASGAARPKSGSLIP 218

                 ...
gi 446931279 237 VNG 239
Cdd:cd05334  219 VVT 221
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
9-185 9.97e-18

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: 77.91  E-value: 9.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279     9 LVTGASRGIGRAIAETLAARGAK---VIG-TATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEFGEVD 81
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlvLLSrSGPDAPGAAALLAELEAAGARVTVvacDVADRDALAAVLAAIPAVEGPLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    82 ILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKkrhgRIITIGSVVGTMGNGGQANYAAAKAgligF 161
Cdd:smart00822  84 GVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLD----FFVLFSSIAGVLGSPGQANYAAANA----F 155
                          170       180
                   ....*....|....*....|....
gi 446931279   162 SKSLAREVASRGITVNVVAPGFIE 185
Cdd:smart00822 156 LDALAEYRRARGLPALSIAWGAWA 179
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
8-237 1.90e-17

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: 77.62  E-value: 1.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIgTATSENGAQAIsdylgangkglmlNVTDPASIESVLEKIraefGEVDILVNNA 87
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVI-TAGRSSGDYQV-------------DITDEASIKALFEKV----GHFDAIVSTA 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 GITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKrhGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAR 167
Cdd:cd11731   63 GDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDG--GSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAI 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 168 EVaSRGITVNVVAPGFIETDMTRALSDdqragilaqVPAGRLGGAQEIANAVAFLASDEaayITGETLHV 237
Cdd:cd11731  141 EL-PRGIRINAVSPGVVEESLEAYGDF---------FPGFEPVPAEDVAKAYVRSVEGA---FTGQVLHV 197
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
9-180 2.07e-17

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: 77.22  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    9 LVTGASRGIGRAIAETLAARGAKVIG----TATSENGAQAISDYL---GANGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARHLVllsrSAAPRPDAQALIAELearGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   82 ILVNNAGITRDNLLMRMKDEEWndiiETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAgligF 161
Cdd:pfam08659  84 GVIHAAGVLRDALLENMTDEDW----RRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANA----F 155
                         170
                  ....*....|....*....
gi 446931279  162 SKSLAREVASRGITVNVVA 180
Cdd:pfam08659 156 LDALAEYRRSQGLPATSIN 174
PRK08177 PRK08177
SDR family oxidoreductase;
6-188 2.32e-17

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 78.15  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAngKGLMLNVTDPASIESVLEKIRAEfgEVDILVN 85
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGV--HIEKLDMNDPASLDQLLQRLQGQ--RFDLLFV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGIT--RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMrAMMKKRHGRIITIGSVVG--TMGNGGQ-ANYAAAKAGLIG 160
Cdd:PRK08177  78 NAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLL-GQVRPGQGVLAFMSSQLGsvELPDGGEmPLYKASKAALNS 156
                        170       180
                 ....*....|....*....|....*...
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDM 188
Cdd:PRK08177 157 MTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK08303 PRK08303
short chain dehydrogenase; Provisional
1-188 3.20e-17

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 78.89  E-value: 3.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQaiSDY-------------LGANGKGLMLNV--TDPAS 65
Cdd:PRK08303   4 KPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTRARR--SEYdrpetieetaelvTAAGGRGIAVQVdhLVPEQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  66 IESVLEKIRAEFGEVDILVNNagITRDNLLMrmkdeEWNDII-ETNLSSVFRL-----------SKAVMRAMMKKRHGRI 133
Cdd:PRK08303  82 VRALVERIDREQGRLDILVND--IWGGEKLF-----EWGKPVwEHSLDKGLRMlrlaidthlitSHFALPLLIRRPGGLV 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446931279 134 ITIGSvvgtmgngGQANYAA-----------AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDM 188
Cdd:PRK08303 155 VEITD--------GTAEYNAthyrlsvfydlAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEM 212
PRK08017 PRK08017
SDR family oxidoreductase;
6-197 3.44e-17

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 78.20  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDyLGAngKGLMLNVTDPASIE-SVLEKIRAEFGEVDILV 84
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNS-LGF--TGILLDLDDPESVErAADEVIALTDNRLYGLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKS 164
Cdd:PRK08017  80 NNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSDA 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 165 LAREVASRGITVNVVAPGFIETDMTRALSDDQR 197
Cdd:PRK08017 160 LRMELRHSGIKVSLIEPGPIRTRFTDNVNQTQS 192
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
8-213 3.45e-17

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: 77.18  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAngkglMLNVTDPASiESVLEKIRAEFGEVDILVNNA 87
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA-----LARPADVAA-ELEVWALAQELGPLDLLVYAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 GITRDNLLMRMKDEEWNDIIETNLSSVFRLSKavMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAR 167
Cdd:cd11730   75 GAILGKPLARTKPAAWRRILDANLTGAALVLK--HALALLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARK 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446931279 168 EVasRGITVNVVAPGFIETDMTR--------ALSDDQRAgilAQVPAGRLGGAQ 213
Cdd:cd11730  153 EV--RGLRLTLVRPPAVDTGLWAppgrlpkgALSPEDVA---AAILEAHQGEPQ 201
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 4.30e-17

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 77.67  E-value: 4.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGAS--RGIGRAIAETLAARGAKVIGTATSENGA---QAISDYLGAngKGLM-LNVTDPASIESVLEKIR 74
Cdd:PRK07533   6 LPLAGKRGLVVGIAneQSIAWGCARAFRALGAELAVTYLNDKARpyvEPLAEELDA--PIFLpLDVREPGQLEAVFARIA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  75 AEFGEVDILVNN-AGITRDNLLMRMKD---EEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIIT---IGS--VV---GT 142
Cdd:PRK07533  84 EEWGRLDFLLHSiAFAPKEDLHGRVVDcsrEGFALAMDVSCHSFIRMARLAEPLM--TNGGSLLTmsyYGAekVVenyNL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 143 MGnggqanyaAAKAGLIGFSKSLAREVASRGITVNVVAPGFIetdMTRALS-----DDQRAGILAQVPAGRLGGAQEIAN 217
Cdd:PRK07533 162 MG--------PVKAALESSVRYLAAELGPKGIRVHAISPGPL---KTRAASgiddfDALLEDAAERAPLRRLVDIDDVGA 230
                        250       260
                 ....*....|....*....|....*..
gi 446931279 218 AVAFLASDEAAYITGETLHVNGGMYMV 244
Cdd:PRK07533 231 VAAFLASDAARRLTGNTLYIDGGYHIV 257
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
5-190 5.29e-17

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: 77.89  E-value: 5.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVI----GTATSENGAQAI-SDYLGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVImacrDMAKCEEAAAEIrRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRdnlLMRMKDEewnDIIETNLS----SVFRLSKAVMRAMMKKRHGRIITIGSVVGTMG----------- 144
Cdd:cd09807   81 LDVLINNAGVMR---CPYSKTE---DGFEMQFGvnhlGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGkinfddlnsek 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446931279 145 --NGGQAnYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTR 190
Cdd:cd09807  155 syNTGFA-YCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGR 201
PRK08340 PRK08340
SDR family oxidoreductase;
9-241 5.33e-17

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 77.54  E-value: 5.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK--GLMLNVTDPASIESVLEKIRAEFGEVDILVNN 86
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEvyAVKADLSDKDDLKNLVKEAWELLGGIDALVWN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  87 AGITRDNLLMrMKDEEWNDIIETNL----SSVFRLSKAVMRAMMKKRHGRIITIGS--VVGTMGNGGQANyaAAKAGLIG 160
Cdd:PRK08340  84 AGNVRCEPCM-LHEAGYSDWLEAALlhlvAPGYLTTLLIQAWLEKKMKGVLVYLSSvsVKEPMPPLVLAD--VTRAGLVQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTR------------ALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAA 228
Cdd:PRK08340 161 LAKGVSRTYGGKGIRAYTVLLGSFDTPGARenlariaeergvSFEETWEREVLERTPLKRTGRWEELGSLIAFLLSENAE 240
                        250
                 ....*....|...
gi 446931279 229 YITGETLHVNGGM 241
Cdd:PRK08340 241 YMLGSTIVFDGAM 253
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
6-188 1.14e-16

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 76.65  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGA-QAISDYLGANGKGLMLNVTDPASIESVLEKI--RAEFGEVD- 81
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKElTKLAEQYNSNLTFHSLDLQDVHELETNFNEIlsSIQEDNVSs 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 -ILVNNAGI-TRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRaMMKKRHG--RIITIGSVVGTMGNGGQANYAAAKAG 157
Cdd:PRK06924  82 iHLINNAGMvAPIKPIEKAESEELITNVHLNLLAPMILTSTFMK-HTKDWKVdkRVINISSGAAKNPYFGWSAYCSSKAG 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 158 LIGFSKSLAREVASRGITVNVVA--PGFIETDM 188
Cdd:PRK06924 161 LDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNM 193
PLN02780 PLN02780
ketoreductase/ oxidoreductase
5-189 2.95e-16

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 76.44  E-value: 2.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAN-GKGLMLNVTDPAS--IESVLEKIR--AEFGE 79
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKySKTQIKTVVVDFSgdIDEGVKRIKetIEGLD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRD--NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTM--GNGGQANYAAAK 155
Cdd:PLN02780 133 VGVLINNVGVSYPyaRFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVipSDPLYAVYAATK 212
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446931279 156 AGLIGFSKSLAREVASRGITVNVVAPGFIETDMT 189
Cdd:PLN02780 213 AYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMA 246
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
9-206 3.15e-16

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: 76.65  E-value: 3.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIgTATSENG-------AQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGeVD 81
Cdd:cd05274  154 LITGGLGGLGLLVARWLAARGARHL-VLLSRRGpapraaaRAALLRAGGARVSVVRCDVTDPAALAALLAELAAGGP-LA 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRDNLLMRMKDEEWNDiietnlssVFRlSKAV----MRAMMKKRHGRIITI-GSVVGTMGNGGQANYAAAKA 156
Cdd:cd05274  232 GVIHAAGVLRDALLAELTPAAFAA--------VLA-AKVAgalnLHELTPDLPLDFFVLfSSVAALLGGAGQAAYAAANA 302
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446931279 157 gligFSKSLAREVASRGITVNVVAPGFIETDM----TRALSDDQRAGILAQVPA 206
Cdd:cd05274  303 ----FLDALAAQRRRRGLPATSVQWGAWAGGGmaaaAALRARLARSGLGPLAPA 352
PRK05993 PRK05993
SDR family oxidoreductase;
9-189 1.94e-15

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 73.52  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAisdyLGANG-KGLMLNVTDPASIESVLEKIRAEF-GEVDILVNN 86
Cdd:PRK05993   8 LITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA----LEAEGlEAFQLDYAEPESIAALVAQVLELSgGRLDALFNN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  87 AGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLA 166
Cdd:PRK05993  84 GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFAIEGLSLTLR 163
                        170       180
                 ....*....|....*....|...
gi 446931279 167 REVASRGITVNVVAPGFIETDMT 189
Cdd:PRK05993 164 MELQGSGIHVSLIEPGPIETRFR 186
PRK06194 PRK06194
hypothetical protein; Provisional
2-191 2.53e-15

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 73.51  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGK---GLMLNVTDPASIESVLEKIRAEFG 78
Cdd:PRK06194   3 DFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAevlGVRTDVSDAAQVEALADAALERFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  79 EVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVF---RLSKAVMRAMMKKR---HGRIITIGSVVGTMGNGGQANYA 152
Cdd:PRK06194  83 AVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIhgvRAFTPLMLAAAEKDpayEGHIVNTASMAGLLAPPAMGIYN 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446931279 153 AAKAGLIGFSKSLAREVASRG--ITVNVVAPGFIETDMTRA 191
Cdd:PRK06194 163 VSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQS 203
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
4-244 7.42e-15

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 71.51  E-value: 7.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTG--ASRGIGRAIAETLAARGAKVIGTATSENG--AQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK07889   6 EGKRILVTGviTDSSIAFHVARVAQEQGAEVVLTGFGRALrlTERIAKRLPEPAPVLELDVTNEEHLASLADRVREHVDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGIT-RDNLLMRMKDEEWNDI---IETNLSSVFRLSKAVMRAMMKKrhgriitiGSVVGTMGNGGQA----NY 151
Cdd:PRK07889  86 LDGVVHSIGFApQSALGGNFLDAPWEDVataLHVSAYSLKSLAKALLPLMNEG--------GSIVGLDFDATVAwpayDW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 152 A-AAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSD--------DQRAgilaqvPAG-RLGGAQEIANAVAF 221
Cdd:PRK07889 158 MgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAIPGfelleegwDERA------PLGwDVKDPTPVARAVVA 231
                        250       260
                 ....*....|....*....|...
gi 446931279 222 LASDEAAYITGETLHVNGGMYMV 244
Cdd:PRK07889 232 LLSDWFPATTGEIVHVDGGAHAM 254
PRK07023 PRK07023
SDR family oxidoreductase;
7-196 3.75e-14

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 69.66  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRGIGRAIAETLAARGAKVIGTATSENgaQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVD----I 82
Cdd:PRK07023   3 RAIVTGHSRGLGAALAEQLLQPGIAVLGVARSRH--PSLAAAAGERLAEVELDLSDAAAAAAWLAGDLLAAFVDGasrvL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRD-NLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGF 161
Cdd:PRK07023  81 LINNAGTVEPiGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALDHH 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446931279 162 SKSLAREvASRGITVNVVAPGFIETDM---TRALSDDQ 196
Cdd:PRK07023 161 ARAVALD-ANRALRIVSLAPGVVDTGMqatIRATDEER 197
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
1-240 4.01e-14

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 69.74  E-value: 4.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGAS--RGIGRAIAETLAARGAKVIGT------ATSENGAQAISDYLgANGKGLMLNVTDPASIESVLEK 72
Cdd:PRK07370   2 LDLTGKKALVTGIAnnRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVRELTEPL-NPSLFLPCDVQDDAQIEETFET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  73 IRAEFGEVDILVNN-AGITRDNLLMRMKD---EEWNDIIETNLSSVFRLSKAVMRAMMKKrhGRIITIGSVVGTMGNGGQ 148
Cdd:PRK07370  81 IKQKWGKLDILVHClAFAGKEELIGDFSAtsrEGFARALEISAYSLAPLCKAAKPLMSEG--GSIVTLTYLGGVRAIPNY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 149 ANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIetdmtRALSDDQRAGILAQV-------PAGRLGGAQEIANAVAF 221
Cdd:PRK07370 159 NVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPI-----RTLASSAVGGILDMIhhveekaPLRRTVTQTEVGNTAAF 233
                        250
                 ....*....|....*....
gi 446931279 222 LASDEAAYITGETLHVNGG 240
Cdd:PRK07370 234 LLSDLASGITGQTIYVDAG 252
PRK07102 PRK07102
SDR family oxidoreductase;
9-192 9.03e-14

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 68.41  E-value: 9.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLM----LNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:PRK07102   5 LIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVstheLDILDTASHAAFLDSLPALPDIVLIAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 ----NNAGITRDNLLMRMkdeewndIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIG 160
Cdd:PRK07102  85 gtlgDQAACEADPALALR-------EFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTA 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446931279 161 FSKSLAREVASRGITVNVVAPGFIETDMTRAL 192
Cdd:PRK07102 158 FLSGLRNRLFKSGVHVLTVKPGFVRTPMTAGL 189
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 9.31e-14

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 68.60  E-value: 9.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGAS--RGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGA--NGKGLMLN--VTDPASIESVLEKIR 74
Cdd:PRK08594   3 LSLEGKTYVVMGVAnkRSIAWGIARSLHNAGAKLVFTYAGERLEKEVRELADTleGQESLLLPcdVTSDEEITACFETIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  75 AEFGEVDILVNN-------------AGITRDNLLMRmkdeewNDIIETNLSSVFRLSKAVMRAMmkkrhgriitiGSVVG 141
Cdd:PRK08594  83 EEVGVIHGVAHCiafankedlrgefLETSRDGFLLA------QNISAYSLTAVAREAKKLMTEG-----------GSIVT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 142 TMGNGGQ---ANY---AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSD--DQRAGILAQVPAGRLGGAQ 213
Cdd:PRK08594 146 LTYLGGErvvQNYnvmGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLSAKGVGGfnSILKEIEERAPLRRTTTQE 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446931279 214 EIANAVAFLASDEAAYITGETLHVNGGMYMV 244
Cdd:PRK08594 226 EVGDTAAFLFSDLSRGVTGENIHVDSGYHII 256
PRK06197 PRK06197
short chain dehydrogenase; Provisional
5-206 1.97e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 68.13  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKG---LM-LNVTDPASIESVLEKIRAEFGE 79
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVvLAVRNLDKGKAAAARITAATPGAdvtLQeLDLTSLASVRAAADALRAAYPR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGI-------TRDNLLMRMKdeewndiieTNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMG-------- 144
Cdd:PRK06197  96 IDLLINNAGVmytpkqtTADGFELQFG---------TNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHRIRaaihfddl 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446931279 145 ------NGGQAnYAAAKAGLIGFSKSLAREVASRGITVNVVA--PGFIETDMTRALSDDQR------AGILAQVPA 206
Cdd:PRK06197 167 qwerryNRVAA-YGQSKLANLLFTYELQRRLAAAGATTIAVAahPGVSNTELARNLPRALRpvatvlAPLLAQSPE 241
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
3-181 4.66e-13

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: 66.31  E-value: 4.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASRGIGRAIAETLAARGAK-VIGTATSE----------NGAQAISDylgANGKGL--MLNVTDPASIESV 69
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANvVIAAKTAEphpklpgtiyTAAEEIEA---AGGKALpcIVDIRDEDQVRAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  70 LEKIRAEFGEVDILVNNAGIT--RDNLLMRMKdeEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVG--TMGN 145
Cdd:cd09762   78 VEKAVEKFGGIDILVNNASAIslTGTLDTPMK--RYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNlnPKWF 155
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446931279 146 GGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAP 181
Cdd:cd09762  156 KNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06940 PRK06940
short chain dehydrogenase; Provisional
6-240 1.35e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 65.43  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASrGIGRAIAETLAArGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIR--AEFGEVDIL 83
Cdd:PRK06940   3 EVVVVIGAG-GIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAAtaQTLGPVTGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITR-----------DNLLMRMKDEEWNDIIETNLSSVF----------RLSKAVMRAMMKKRHGRIITIGSV-VG 141
Cdd:PRK06940  81 VHTAGVSPsqaspeailkvDLYGTALVLEEFGKVIAPGGAGVViasqsghrlpALTAEQERALATTPTEELLSLPFLqPD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 142 TMGNGGQAnYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMT-RALSDDQRAGI---LAQVPAGRLGGAQEIAN 217
Cdd:PRK06940 161 AIEDSLHA-YQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAqDELNGPRGDGYrnmFAKSPAGRPGTPDEIAA 239
                        250       260
                 ....*....|....*....|...
gi 446931279 218 AVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK06940 240 LAEFLMGPRGSFITGSDFLVDGG 262
PRK07806 PRK07806
SDR family oxidoreductase;
5-87 1.58e-12

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 65.13  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVI-----GTATSENGAQAISDylgANGKGLML--NVTDPASIESVLEKIRAEF 77
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVvnyrqKAPRANKVVAEIEA---AGGRASAVgaDLTDEESVAALMDTAREEF 82
                         90
                 ....*....|
gi 446931279  78 GEVDILVNNA 87
Cdd:PRK07806  83 GGLDALVLNA 92
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
7-209 2.25e-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: 64.93  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    7 IALVTGASRGIGRAIAETLAAR----GAKVIGTATSENGAQAISDYLGANGKGLMLnVTDPASIE----------SVLEK 72
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERSGLRV-VRVSLDLGaeagleqllkALREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   73 IRAEFGEVDILVNNAGITRDnlLMRMKDE-----EWNDIIETNLSSVFRLSKAVMRAmMKKRHG---RIITIGSVVGTMG 144
Cdd:TIGR01500  81 PRPKGLQRLLLINNAGTLGD--VSKGFVDlsdstQVQNYWALNLTSMLCLTSSVLKA-FKDSPGlnrTVVNISSLCAIQP 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  145 NGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMT-----RALSDDQRAGILAQVPAGRL 209
Cdd:TIGR01500 158 FKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQqqvreESVDPDMRKGLQELKAKGKL 227
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
1-240 9.92e-12

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 63.22  E-value: 9.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGAS--RGIGRAIAETLAARGAKVIGTATSE---NGAQAISDYLGANgKGLMLNVTDPASIESVLEKIRA 75
Cdd:PRK08415   1 MIMKGKKGLIVGVAnnKSIAYGIAKACFEQGAELAFTYLNEalkKRVEPIAQELGSD-YVYELDVSKPEHFKSLAESLKK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  76 EFGEVDILVNNAGITR----DNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIITIgSVVGtmGNGGQANY 151
Cdd:PRK08415  80 DLGKIDFIVHSVAFAPkealEGSFLETSKEAFNIAMEISVYSLIELTRALLPLL--NDGASVLTL-SYLG--GVKYVPHY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 152 ---AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRagIL----AQVPAGRLGGAQEIANAVAFLAS 224
Cdd:PRK08415 155 nvmGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKTLAASGIGDFRM--ILkwneINAPLKKNVSIEEVGNSGMYLLS 232
                        250
                 ....*....|....*.
gi 446931279 225 DEAAYITGETLHVNGG 240
Cdd:PRK08415 233 DLSSGVTGEIHYVDAG 248
PRK05884 PRK05884
SDR family oxidoreductase;
9-240 1.00e-10

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 59.82  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGkgLMLNVTDPASIESVLEKIRAEfgeVDILVNNAG 88
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDA--IVCDNTDPASLEEARGLFPHH---LDTIVNVPA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  89 IT---RDNLLMRMKD--EEWNDIIETNLSSVFRLSKAVMRAMmkKRHGRIItigSVVGTMGNGGQANyAAAKAGLIGFSK 163
Cdd:PRK05884  79 PSwdaGDPRTYSLADtaNAWRNALDATVLSAVLTVQSVGDHL--RSGGSII---SVVPENPPAGSAE-AAIKAALSNWTA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446931279 164 SLAREVASRGITVNVVAPGfietdmtraLSDDQRAGILAQVPAGRlggAQEIANAVAFLASDEAAYITGETLHVNGG 240
Cdd:PRK05884 153 GQAAVFGTRGITINAVACG---------RSVQPGYDGLSRTPPPV---AAEIARLALFLTTPAARHITGQTLHVSHG 217
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
22-241 1.34e-10

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 59.63  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  22 AETLAARGAKVIGTATSENGAqAISDYLGANgkglmlnVTDPASIESVLEKIRaefGEVDILVNNAGI--TRDNLLmrmk 99
Cdd:PRK12428   2 ARLLRFLGARVIGVDRREPGM-TLDGFIQAD-------LGDPASIDAAVAALP---GRIDALFNIAGVpgTAPVEL---- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 100 deewndIIETNLSSVFRLSKAVMRAMmkKRHGRIITIGSVVG-----------------TMGNGGQ----------ANYA 152
Cdd:PRK12428  67 ------VARVNFLGLRHLTEALLPRM--APGGAIVNVASLAGaewpqrlelhkalaataSFDEGAAwlaahpvalaTGYQ 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 153 AAKAGLIGFSKSLARE-VASRGITVNVVAPGFIET---DMTRALSDDQRAGILAQvPAGRLGGAQEIANAVAFLASDEAA 228
Cdd:PRK12428 139 LSKEALILWTMRQAQPwFGARGIRVNCVAPGPVFTpilGDFRSMLGQERVDSDAK-RMGRPATADEQAAVLVFLCSDAAR 217
                        250
                 ....*....|...
gi 446931279 229 YITGETLHVNGGM 241
Cdd:PRK12428 218 WINGVNLPVDGGL 230
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-139 1.55e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.99  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAngKGLMLNVTDPASIESVLEKiraefgeVDILVNNAG 88
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGV--EFVRGDLRDPEALAAALAG-------VDAVVHLAA 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446931279  89 ITRDNLlmrmkdEEWNDIIETNLssvfRLSKAVMRAMMKKRHGRIITIGSV 139
Cdd:COG0451   74 PAGVGE------EDPDETLEVNV----EGTLNLLEAARAAGVKRFVYASSS 114
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
4-244 1.78e-10

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 59.35  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGAS--RGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVD 81
Cdd:PRK06079   6 SGKKIVVMGVAnkRSIAWGCAQAIKDQGATVIYTYQNDRMKKSLQKLVDEEDLLVECDVASDESIERAFATIKERVGKID 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  82 ILVNNAGITRdnllmrmKDEEWNDIIETNLSSvFRLSK--------AVMRA---MMKKRhGRIIT---IGSV-----VGT 142
Cdd:PRK06079  86 GIVHAIAYAK-------KEELGGNVTDTSRDG-YALAQdisaysliAVAKYarpLLNPG-ASIVTltyFGSEraipnYNV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 143 MGnggqanyaAAKAGLIGFSKSLAREVASRGITVNVVAPGFIET-------------DMTRALSDDQRAGILaqvpagrl 209
Cdd:PRK06079 157 MG--------IAKAALESSVRYLARDLGKKGIRVNAISAGAVKTlavtgikghkdllKESDSRTVDGVGVTI-------- 220
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446931279 210 ggaQEIANAVAFLASDEAAYITGETLHVNGGMYMV 244
Cdd:PRK06079 221 ---EEVGNTAAFLLSDLSTGVTGDIIYVDKGVHLI 252
PRK06196 PRK06196
oxidoreductase; Provisional
5-198 2.07e-10

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 59.70  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISdyLGANGKGL-MLNVTDPASIESVLEKIRAEFGEVDIL 83
Cdd:PRK06196  26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREAL--AGIDGVEVvMLDLADLESVRAFAERFLDSGRRIDIL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRdNLLMRMKDeEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGS------------VVGTMGNGGQANY 151
Cdd:PRK06196 104 INNAGVMA-CPETRVGD-GWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSaghrrspirwddPHFTRGYDKWLAY 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446931279 152 AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSD-DQRA 198
Cdd:PRK06196 182 GQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQRHLPReEQVA 229
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
5-244 2.28e-10

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 59.38  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGAS--RGIGRAIAETLAARGAKVIGTATSENGAQAIsDYLGANGKGLML---NVTDPASIESVLEKIRAEFGE 79
Cdd:PRK08159  10 GKRGLILGVAnnRSIAWGIAKACRAAGAELAFTYQGDALKKRV-EPLAAELGAFVAghcDVTDEASIDAVFETLEKKWGK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGIT-RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRA-MMKKRHGRIITIgSVVGT---------MGnggq 148
Cdd:PRK08159  89 LDFVVHAIGFSdKDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAeKLMTDGGSILTL-TYYGAekvmphynvMG---- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 149 anyaAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRagILA----QVPAGRLGGAQEIANAVAFLAS 224
Cdd:PRK08159 164 ----VAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGDFRY--ILKwneyNAPLRRTVTIEEVGDSALYLLS 237
                        250       260
                 ....*....|....*....|
gi 446931279 225 DEAAYITGETLHVNGGMYMV 244
Cdd:PRK08159 238 DLSRGVTGEVHHVDSGYHVV 257
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
1-240 2.80e-10

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 58.83  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNF-EGKIALVTG--ASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRA 75
Cdd:PRK08690   1 MGFlQGKKILITGmiSERSIAYGIAKACREQGAELAFTYVVDKLEERVRKMAAELDSELVFrcDVASDDEINQVFADLGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  76 EFGEVDILVNNAGIT-----RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVmRAMMKKRHGRIITIgSVVGTMGNGGQAN 150
Cdd:PRK08690  81 HWDGLDGLVHSIGFApkealSGDFLDSISREAFNTAHEISAYSLPALAKAA-RPMMRGRNSAIVAL-SYLGAVRAIPNYN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 151 YAA-AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEA 227
Cdd:PRK08690 159 VMGmAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKllGHVAAHNPLRRNVTIEEVGNTAAFLLSDLS 238
                        250
                 ....*....|...
gi 446931279 228 AYITGETLHVNGG 240
Cdd:PRK08690 239 SGITGEITYVDGG 251
PRK06953 PRK06953
SDR family oxidoreductase;
6-188 3.78e-10

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 58.16  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAIsDYLGAngKGLMLNVTDPASIESVLEKIRAEFGEVDILVN 85
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAAL-QALGA--EALALDVADPASVAGLAWKLDGEALDAAVYVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVmrAMMKKRHGRIITI-----GSVVGTMGNGGQAnYAAAKAGLIG 160
Cdd:PRK06953  79 GVYGPRTEGVEPITREDFDAVMHTNVLGPMQLLPIL--LPLVEAAGGVLAVlssrmGSIGDATGTTGWL-YRASKAALND 155
                        170       180
                 ....*....|....*....|....*...
gi 446931279 161 FSKSLAREvaSRGITVNVVAPGFIETDM 188
Cdd:PRK06953 156 ALRAASLQ--ARHATCIALHPGWVRTDM 181
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
4-240 4.70e-10

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 58.22  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGAS--RGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGE 79
Cdd:PRK06505   6 QGKRGLIMGVAndHSIAWGIAKQLAAQGAELAFTYQGEALGKRVKPLAESLGSDFVLpcDVEDIASVDAVFEALEKKWGK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGITRDNLLM-RMKDEEWNDIIETNLSSVFRLSKAVMRAmmkkrhGRIITIGSVVGTMGNGGQA----NY--- 151
Cdd:PRK06505  86 LDFVVHAIGFSDKNELKgRYADTTRENFSRTMVISCFSFTEIAKRA------AKLMPDGGSMLTLTYGGSTrvmpNYnvm 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 152 AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSdDQRAGILAQ---VPAGRLGGAQEIANAVAFLASDEAA 228
Cdd:PRK06505 160 GVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGIG-DARAIFSYQqrnSPLRRTVTIDEVGGSALYLLSDLSS 238
                        250
                 ....*....|..
gi 446931279 229 YITGETLHVNGG 240
Cdd:PRK06505 239 GVTGEIHFVDSG 250
PRK08703 PRK08703
SDR family oxidoreductase;
5-182 6.94e-10

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 57.63  E-value: 6.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKglmlnvTDPASI------------ESVLEK 72
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGH------PEPFAIrfdlmsaeekefEQFAAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  73 IRAEF-GEVDILVNNAG-ITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQAN 150
Cdd:PRK08703  80 IAEATqGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGG 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 151 YAAAKAGLIGFSKSLAREVASRG-ITVNVVAPG 182
Cdd:PRK08703 160 FGASKAALNYLCKVAADEWERFGnLRANVLVPG 192
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
9-204 7.28e-10

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: 57.50  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAeFGEVDILVNNAG 88
Cdd:cd08951   11 FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHNAG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  89 ITRDNlLMRMKDEEWNDIIETNLssvfrLSKAVMRAMMkKRHGRIITIGSvvgTMGNGGQANYAA------AKAGLIGFS 162
Cdd:cd08951   90 ILSGP-NRKTPDTGIPAMVAVNV-----LAPYVLTALI-RRPKRLIYLSS---GMHRGGNASLDDidwfnrGENDSPAYS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446931279 163 KS------LAREVASR--GITVNVVAPGFIETDMTRA-LSDDQRAGILAQV 204
Cdd:cd08951  160 DSklhvltLAAAVARRwkDVSSNAVHPGWVPTKMGGAgAPDDLEQGHLTQV 210
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
3-240 1.55e-09

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 56.55  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   3 FEGKIALVTGASR--GIGRAIAETLAARGAKVIGTATS---ENGAQAISDYLGANGKGlMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK06603   6 LQGKKGLITGIANnmSISWAIAQLAKKHGAELWFTYQSevlEKRVKPLAEEIGCNFVS-ELDVTNPKSISNLFDDIKEKW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEVDILVNNAGITRDNLLM-RMKD---EEWNDIIETNLSSVFRLSKAVMRAMMKKrhgriitiGSVVGTMGNGGQA---N 150
Cdd:PRK06603  85 GSFDFLLHGMAFADKNELKgRYVDtslENFHNSLHISCYSLLELSRSAEALMHDG--------GSIVTLTYYGAEKvipN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 151 Y---AAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSD--DQRAGILAQVPAGRLGGAQEIANAVAFLASD 225
Cdd:PRK06603 157 YnvmGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGDfsTMLKSHAATAPLKRNTTQEDVGGAAVYLFSE 236
                        250
                 ....*....|....*
gi 446931279 226 EAAYITGETLHVNGG 240
Cdd:PRK06603 237 LSKGVTGEIHYVDCG 251
PRK06720 PRK06720
hypothetical protein; Provisional
1-149 1.98e-09

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 54.98  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDY---LGANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK06720  12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEitnLGGEALFVSYDMEKQGDWQRVISITLNAF 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446931279  78 GEVDILVNNAGITR-DNLLMRMKDEEWNDIIetnLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQA 149
Cdd:PRK06720  92 SRIDMLFQNAGLYKiDSIFSRQQENDSNVLC---INDVWIEIKQLTSSFMKQQEEVVLSDLPIFGIIGTKGQS 161
PRK08862 PRK08862
SDR family oxidoreductase;
1-181 4.66e-09

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 55.12  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQA---ISDYLGANGKGLMLNVTDPASIESVLEKIRAEF 77
Cdd:PRK08862   1 MDIKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDtyeQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  78 GEV-DILVNN-AGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAV---MRAMMKKrhGRIITIGS------VVGTMGng 146
Cdd:PRK08862  81 NRApDVLVNNwTSSPLPSLFDEQPSESFIQQLSSLASTLFTYGQVAaerMRKRNKK--GVIVNVIShddhqdLTGVES-- 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446931279 147 gqanyaaAKAGLIGFSKSLAREVASRGITVNVVAP 181
Cdd:PRK08862 157 -------SNALVSGFTHSWAKELTPFNIRVGGVVP 184
PRK06101 PRK06101
SDR family oxidoreductase;
9-189 4.92e-09

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 54.88  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYlGANGKGLMLNVTDPASIESVLEKIRAE-----FGEVDIL 83
Cdd:PRK06101   5 LITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTQ-SANIFTLAFDVTDHPGTKAALSQLPFIpelwiFNAGDCE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  84 VNNAGITRDNLLMRmkdeewndIIETNLSSVFRLSKAVmRAMMKKRHgRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:PRK06101  84 YMDDGKVDATLMAR--------VFNVNVLGVANCIEGI-QPHLSCGH-RVVIVGSIASELALPRAEAYGASKAAVAYFAR 153
                        170       180
                 ....*....|....*....|....*.
gi 446931279 164 SLAREVASRGITVNVVAPGFIETDMT 189
Cdd:PRK06101 154 TLQLDLRPKGIEVVTVFPGFVATPLT 179
PRK07578 PRK07578
short chain dehydrogenase; Provisional
6-237 6.82e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 54.05  E-value: 6.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIaLVTGASRGIGRAIAETLAARgAKVIGTatsengaqaisdylGANGKGLMLNVTDPASIESVLEKIraefGEVDILVN 85
Cdd:PRK07578   2 KI-LVIGASGTIGRAVVAELSKR-HEVITA--------------GRSSGDVQVDITDPASIRALFEKV----GKVDAVVS 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  86 NAGITRDNLLMRMKDEEWNDIIETNLSSVFRLskaVMRAMMKKRHGRIITIGSvvGTMG----NGGqANYAAAKAGLIGF 161
Cdd:PRK07578  62 AAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNL---VLIGQHYLNDGGSFTLTS--GILSdepiPGG-ASAATVNGALEGF 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446931279 162 SKSLAREvASRGITVNVVAPGFIETDMtRALSDDQRAGILaqVPAGRLggaqeianAVAFLASDEAAyITGETLHV 237
Cdd:PRK07578 136 VKAAALE-LPRGIRINVVSPTVLTESL-EKYGPFFPGFEP--VPAARV--------ALAYVRSVEGA-QTGEVYKV 198
PRK05854 PRK05854
SDR family oxidoreductase;
5-89 7.49e-09

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 55.07  E-value: 7.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSE-NGAQAISDYLGAN-GKGLMLNVTDPASIESVL---EKIRAEFGE 79
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRaKGEAAVAAIRTAVpDAKLSLRALDLSSLASVAalgEQLRAEGRP 93
                         90
                 ....*....|
gi 446931279  80 VDILVNNAGI 89
Cdd:PRK05854  94 IHLLINNAGV 103
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
9-162 1.02e-08

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


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 54.98  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAK---VIG-TATSENGAQAISDYLGANGKGLMLN--VTDPASIESVLEKIRAEFGEVDI 82
Cdd:cd08955  153 LITGGLGGLGLLVAEWLVERGARhlvLTGrRAPSAAARQAIAALEEAGAEVVVLAadVSDRDALAAALAQIRASLPPLRG 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  83 LVNNAGITRDNLLMRMKDEewndiietnlssvfRLSKaVMRAmmkKRHG----RIITIG----------SVVGTMGNGGQ 148
Cdd:cd08955  233 VIHAAGVLDDGVLANQDWE--------------RFRK-VLAP---KVQGawnlHQLTQDlpldffvlfsSVASLLGSPGQ 294
                        170
                 ....*....|....
gi 446931279 149 ANYAAAKAGLIGFS 162
Cdd:cd08955  295 ANYAAANAFLDALA 308
PRK12367 PRK12367
short chain dehydrogenase; Provisional
2-117 1.11e-08

short chain dehydrogenase; Provisional


Pssm-ID: 237079  Cd Length: 245  Bit Score: 53.86  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   2 NFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYlGANgKGLMLNVTDPASIESVLEKIraefgevD 81
Cdd:PRK12367  11 TWQGKRIGITGASGALGKALTKAFRAKGAKVIGLTHSKINNSESNDE-SPN-EWIKWECGKEESLDKQLASL-------D 81
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446931279  82 ILVNNAGItrdNLLMRMKDEEWNDIIETNLSSVFRL 117
Cdd:PRK12367  82 VLILNHGI---NPGGRQDPENINKALEINALSSWRL 114
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
7-189 1.68e-08

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 53.56  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   7 IALVTGASRgIGRAIAETLAARG-AKVIGTAT--SENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEfGEV 80
Cdd:PRK07904  11 ILLLGGTSE-IGLAICERYLKNApARVVLAALpdDPRRDAAVAQMKAAGASSVEVidfDALDTDSHPKVIDAAFAG-GDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNllmrmkDEEWND------IIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAA 154
Cdd:PRK07904  89 DVAIVAFGLLGDA------EELWQNqrkavqIAEINYTAAVSVGVLLGEKMRAQGFGQIIAMSSVAGERVRRSNFVYGST 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446931279 155 KAGLIGFSKSLAREVASRGITVNVVAPGFIETDMT 189
Cdd:PRK07904 163 KAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMS 197
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
5-190 1.82e-08

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: 53.76  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVI-GTATSENGAQAISDYLG----ANGKGLMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVIlACRNMSRASAAVSRILEewhkARVEAMTLDLASLRSVQRFAEAFKAKNSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  80 VDILVNNAGI-------TRDNLLMRMKDEEWNDIIETN-LSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMG----NGG 147
Cdd:cd09809   81 LHVLVCNAAVfalpwtlTEDGLETTFQVNHLGHFYLVQlLEDVLRRSAPARVIVVSSESHRFTDLPDSCGNLDfsllSPP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446931279 148 QANYAA------AKAGLIGFSKSLAREVASRGITVNVVAPG-FIETDMTR 190
Cdd:cd09809  161 KKKYWSmlaynrAKLCNILFSNELHRRLSPRGITSNSLHPGnMMYSSIHR 210
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
1-244 1.89e-08

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 53.67  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNF-EGKIALVTG--ASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRA 75
Cdd:PRK06997   1 MGFlAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVGDRFKDRITEFAAEFGSDLVFpcDVASDEQIDALFASLGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  76 EFGEVDILVNNAGIT-----RDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKrhGRIITIgSVVG--------- 141
Cdd:PRK06997  81 HWDGLDGLVHSIGFApreaiAGDFLDGLSRENFRIAHDISAYSFPALAKAALPMLSDD--ASLLTL-SYLGaervvpnyn 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 142 TMGnggqanyaAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRagILAQV----PAGRLGGAQEIAN 217
Cdd:PRK06997 158 TMG--------LAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLAASGIKDFGK--ILDFVesnaPLRRNVTIEEVGN 227
                        250       260
                 ....*....|....*....|....*..
gi 446931279 218 AVAFLASDEAAYITGETLHVNGGMYMV 244
Cdd:PRK06997 228 VAAFLLSDLASGVTGEITHVDSGFNAV 254
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
5-138 3.20e-08

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: 52.98  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKV-IGTATSENGAQAISDYLGANGKG----LMLNVTDPASIESVLEKIRAEFGE 79
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVhMVCRNQTRAEEARKEIETESGNQniflHIVDMSDPKQVWEFVEEFKEEGKK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446931279  80 VDILVNNAGItrdnllMRMKDEEWNDIIETNLSS----VFRLSKAVMRAMMKKRHGRIITIGS 138
Cdd:cd09808   81 LHVLINNAGC------MVNKRELTEDGLEKNFATntlgTYILTTHLIPVLEKEEDPRVITVSS 137
PRK07984 PRK07984
enoyl-ACP reductase FabI;
5-240 3.64e-08

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 52.60  E-value: 3.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTG--ASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML--NVTDPASIESVLEKIRAEFGEV 80
Cdd:PRK07984   6 GKRILVTGvaSKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLpcDVAEDASIDAMFAELGKVWPKF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLmrmkDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQ----ANY---AA 153
Cdd:PRK07984  86 DGFVHSIGFAPGDQL----DGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAeraiPNYnvmGL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 154 AKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQR--AGILAQVPAGRLGGAQEIANAVAFLASDEAAYIT 231
Cdd:PRK07984 162 AKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKmlAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS 241

                 ....*....
gi 446931279 232 GETLHVNGG 240
Cdd:PRK07984 242 GEVVHVDGG 250
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
1-241 6.16e-08

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 52.13  E-value: 6.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGAS--RGIGRAIAETLAARGAKV-IGTATS---------ENGAQAISDYLgANGKGLMLNVTDPA---- 64
Cdd:PRK06300   4 IDLTGKIAFIAGIGddQGYGWGIAKALAEAGATIlVGTWVPiykifsqslELGKFDASRKL-SNGSLLTFAKIYPMdasf 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  65 ----------------------SIESVLEKIRAEFGEVDILVNNagitrdnllMRMKDEEWNDIIETN----LSSVFRLS 118
Cdd:PRK06300  83 dtpedvpeeirenkrykdlsgyTISEVAEQVKKDFGHIDILVHS---------LANSPEISKPLLETSrkgyLAALSTSS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 119 KAVMRamMKKRHGRIITIGSVVGTM----------GNGGQANyaAAKAGLIGFSKSLAREVASR-GITVNVVAPGFIETD 187
Cdd:PRK06300 154 YSFVS--LLSHFGPIMNPGGSTISLtylasmravpGYGGGMS--SAKAALESDTKVLAWEAGRRwGIRVNTISAGPLASR 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446931279 188 MTRALS--DDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGM 241
Cdd:PRK06300 230 AGKAIGfiERMVDYYQDWAPLPEPMEAEQVGAAAAFLVSPLASAITGETLYVDHGA 285
PRK05599 PRK05599
SDR family oxidoreductase;
9-193 1.34e-06

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 47.96  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAArGAKVIGTATSENGAQAISDYLGANGKG----LMLNVTDPASIESVLEKIRAEFGEVDILV 84
Cdd:PRK05599   4 LILGGTSDIAGEIATLLCH-GEDVVLAARRPEAAQGLASDLRQRGATsvhvLSFDAQDLDTHRELVKQTQELAGEISLAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRH-GRIITIGSVVGTMGNGGQANYAAAKAGLIGFSK 163
Cdd:PRK05599  83 VAFGILGDQERAETDEAHAVEIATVDYTAQVSMLTVLADELRAQTApAAIVAFSSIAGWRARRANYVYGSTKAGLDAFCQ 162
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 164 SLAREVASRGITVNVVAPGFIETDMTRALS 193
Cdd:PRK05599 163 GLADSLHGSHVRLIIARPGFVIGSMTTGMK 192
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
6-167 1.40e-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: 48.28  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAARGA--KVIGTATSENGAQAISDYLGANGKGLMLNVtDPASIESV---LEKIRAEFGEV 80
Cdd:cd09810    2 GTVVITGASSGLGLAAAKALARRGEwhVVMACRDFLKAEQAAQEVGMPKDSYSVLHC-DLASLDSVrqfVDNFRRTGRPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGI--TRDNLLMRmKDEEWNDIIETNLSSVFRLSKAVMRAMMKK--RHGRIITIGSVVG-TMGNGGQANYAAAK 155
Cdd:cd09810   81 DALVCNAAVylPTAKEPRF-TADGFELTVGVNHLGHFLLTNLLLEDLQRSenASPRIVIVGSITHnPNTLAGNVPPRATL 159
                        170
                 ....*....|..
gi 446931279 156 AGLIGFSKSLAR 167
Cdd:cd09810  160 GDLEGLAGGLKG 171
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
1-117 5.73e-06

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 46.61  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKiraefgeV 80
Cdd:PRK07424 174 LSLKGKTVAVTGASGTLGQALLKELHQQGAKVVALTSNSDKITLEINGEDLPVKTLHWQVGQEAALAELLEK-------V 246
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446931279  81 DILVNNAGItrdNLLMRMKDEEWNDIIETNLSSVFRL 117
Cdd:PRK07424 247 DILIINHGI---NVHGERTPEAINKSYEVNTFSAWRL 280
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
9-91 3.55e-05

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


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 43.77  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSengaqaisdylgaNGKGLMLNVTDPASIESVLEKIRAefgevDILVNNAG 88
Cdd:cd05254    3 LITGATGMLGRALVRLLKERGYEVIGTGRS-------------RASLFKLDLTDPDAVEEAIRDYKP-----DVIINCAA 64

                 ...
gi 446931279  89 ITR 91
Cdd:cd05254   65 YTR 67
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
8-193 3.82e-05

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 43.44  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279    8 ALVTGASRGIGRAIAETLAARGAKVIGTAtseNGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRaefgeVDILVNNA 87
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLD---RLTSASNTARLADLRFVEGDLTDRDALEKLLADVR-----PDAVIHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   88 GIT--RDNLlmrmkdEEWNDIIETNlssvFRLSKAVMRAMMKKRHGRIITIGS--VVGTMGNGGQAN------------Y 151
Cdd:pfam01370  73 AVGgvGASI------EDPEDFIEAN----VLGTLNLLEAARKAGVKRFLFASSseVYGDGAEIPQEEttltgplapnspY 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446931279  152 AAAKAGLIGFSKSLAREVASRGITV---NVVAPGFIETDMTRALS 193
Cdd:pfam01370 143 AAAKLAGEWLVLAYAAAYGLRAVILrlfNVYGPGDNEGFVSRVIP 187
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
4-48 3.91e-05

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 43.87  E-value: 3.91e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDY 48
Cdd:PRK13771 162 KGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSKY 206
PRK09009 PRK09009
SDR family oxidoreductase;
9-209 7.88e-05

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 42.74  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAAR--GAKVIGTATSEngaqaISDYLGANGKGLMLNVTDPASIESVLEkiraEFGEVDILVNN 86
Cdd:PRK09009   4 LIVGGSGGIGKAMVKQLLERypDATVHATYRHH-----KPDFQHDNVQWHALDVTDEAEIKQLSE----QFTQLDWLINC 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  87 AGI--TRDN----LLMRMKDEEWNDIIETN-LSSVFrLSKAVMRAMMKKRHGRIITIGSVVGTMGN---GGQANYAAAKA 156
Cdd:PRK09009  75 VGMlhTQDKgpekSLQALDADFFLQNITLNtLPSLL-LAKHFTPKLKQSESAKFAVISAKVGSISDnrlGGWYSYRASKA 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446931279 157 GLIGFSKSLARE--VASRGITVNVVAPGFIETdmtrALSddqrAGILAQVPAGRL 209
Cdd:PRK09009 154 ALNMFLKTLSIEwqRSLKHGVVLALHPGTTDT----ALS----KPFQQNVPKGKL 200
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
5-142 8.14e-05

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 42.96  E-value: 8.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISdylgANGKGLMLNVTDpasiESVLEKIRAefgevdiLV 84
Cdd:cd08253  145 GETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAELVR----QAGADAVFNYRA----EDLADRILA-------AT 209
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446931279  85 NNAGITRdnllmrmkdeewndIIETNLSSVFRLSKAVMRammkkRHGRIITIGSVVGT 142
Cdd:cd08253  210 AGQGVDV--------------IIEVLANVNLAKDLDVLA-----PGGRIVVYGSGGLR 248
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
8-180 1.34e-04

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: 42.54  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAK----VIGTATSENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEfGEV 80
Cdd:cd08952  233 VLVTGGTGALGAHVARWLARRGAEhlvlTSRRGPDAPGAAELVAELTALGARVTVaacDVADRDALAALLAALPAG-HPL 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  81 DILVNNAGITRDNLLMRMKDEEWNDiietnlssvfrlskaVMRAmmKKRHGRI-------------ITIGSVVGTMGNGG 147
Cdd:cd08952  312 TAVVHAAGVLDDGPLDDLTPERLAE---------------VLRA--KVAGARHldeltrdrdldafVLFSSIAGVWGSGG 374
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446931279 148 QANYAAAKAGLigfsKSLAREVASRGITVNVVA 180
Cdd:cd08952  375 QGAYAAANAYL----DALAERRRARGLPATSVA 403
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
5-166 1.52e-04

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) 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-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); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP 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 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: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 42.44  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENG-----AQAISDYLGANGKG--LMLNVTDPASIESVLEKIRAE- 76
Cdd:cd08954  218 GKSYLITGGSGGLGLEILKWLVKRGAVENIIILSRSGmkwelELLIREWKSQNIKFhfVSVDVSDVSSLEKAINLILNAp 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  77 -FGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHgrIITIGSVVGTMGNGGQANYAAAK 155
Cdd:cd08954  298 kIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDY--FVLFSSVSSIRGSAGQCNYVCAN 375
                        170
                 ....*....|.
gi 446931279 156 AGLIGFSKSLA 166
Cdd:cd08954  376 SVLDSLSRYRK 386
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
138-198 2.01e-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: 41.87  E-value: 2.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446931279 138 SVVGTMGNGGQANYAAAKAgligFSKSLAREVASRGITVNVVAPGFIE--TDMTRALSDDQRA 198
Cdd:cd08956  329 SAAGVLGSPGQANYAAANA----FLDALAQHRRARGLPATSLAWGLWAqaSGMTAHLSDADLA 387
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
8-184 2.03e-04

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


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 41.89  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSEngaqaiSDYLGANGKGLML---NVTDPASIESVLEKiraefgeVDILV 84
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSG------SDAVLLDGLPVEVvegDLTDAASLAAAMKG-------CDRVF 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  85 NNAGITRDNLlmrmKDeeWNDIIETNLSSVFRLSKAVMRAMMKkrhgRIITIGSV-VGTMGNGGQANYAAAKAGLIGF-- 161
Cdd:cd05228   68 HLAAFTSLWA----KD--RKELYRTNVEGTRNVLDAALEAGVR----RVVHTSSIaALGGPPDGRIDETTPWNERPFPnd 137
                        170       180       190
                 ....*....|....*....|....*....|
gi 446931279 162 ---SKSLA----REVASRGITVNVVAPGFI 184
Cdd:cd05228  138 yyrSKLLAelevLEAAAEGLDVVIVNPSAV 167
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
8-192 3.72e-04

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


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 40.08  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGlmlNVTDPASIESVLEkiraefgEVDILVNNA 87
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVVEG---DLRDLDSLSDAVQ-------GVDVVIHLA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  88 GITRDNllmrmkdeewNDIIETNLSSVFRLSKAVmrammkKRHG--RIITIGSVVGTMGNGGQANYAAAKAgLIGFSKSL 165
Cdd:cd05226   71 GAPRDT----------RDFCEVDVEGTRNVLEAA------KEAGvkHFIFISSLGAYGDLHEETEPSPSSP-YLAVKAKT 133
                        170       180
                 ....*....|....*....|....*..
gi 446931279 166 AREVASRGITVNVVAPGFIETDMTRAL 192
Cdd:cd05226  134 EAVLREASLPYTIVRPGVIYGDLARAI 160
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
129-237 3.78e-04

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 40.98  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 129 RHGRIITIGSVVGTMGNGGQAnyaAAKAGLIGFSKSLAREVaSRGITVN--VVAPgfietdmtralsddqragilaqvpa 206
Cdd:PRK08261 115 PCGRVVVLGRPPEAAADPAAA---AAQRALEGFTRSLGKEL-RRGATAQlvYVAP------------------------- 165
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446931279 207 grlGGAQEIANAVAFLASDEAAYITGETLHV 237
Cdd:PRK08261 166 ---GAEAGLESTLRFFLSPRSAYVSGQVVRV 193
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
144-241 3.89e-04

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 40.91  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279 144 GNGGqaNYAAAKAGLIGFSKSLAREVASR-GITVNVVAPGFIETDMTRALS--DDQRAGILAQVPAGRLGGAQEIANAVA 220
Cdd:PLN02730 188 GYGG--GMSSAKAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKAIGfiDDMIEYSYANAPLQKELTADEVGNAAA 265
                         90       100
                 ....*....|....*....|.
gi 446931279 221 FLASDEAAYITGETLHVNGGM 241
Cdd:PLN02730 266 FLASPLASAITGATIYVDNGL 286
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
5-51 6.59e-04

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 40.27  E-value: 6.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446931279   5 GKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDyLGA 51
Cdd:cd08268  145 GDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLA-LGA 190
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
8-77 6.63e-04

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. 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: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 40.27  E-value: 6.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTAT-SENGAQAISDYLGANGKGLML---NVTDPASIESVLEKIRAEF 77
Cdd:cd05260    2 ALITGITGQDGSYLAEFLLEKGYEVHGIVRrSSSFNTDRIDHLYINKDRITLhygDLTDSSSLRRAIEKVRPDE 75
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
3-39 7.11e-04

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs; KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif 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: 187653 [Multi-domain]  Cd Length: 259  Bit Score: 39.87  E-value: 7.11e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446931279   3 FEGKIALVTGASRG-IGRAIAETLAARGAKVIGTATSE 39
Cdd:cd08950    5 FAGKVALVTGAGPGsIGAEVVAGLLAGGATVIVTTSRF 42
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
9-229 1.35e-03

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 38.67  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAIsdyLGANGKGLMLNVTDPASIESVLEkiraefgEVDILVNNAG 88
Cdd:COG0702    3 LVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAAL---AAAGVEVVQGDLDDPESLAAALA-------GVDAVFLLVP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  89 ITRDNLLMRMKdeewndiietnlssvfRLSKAVMRAMMKKRHGRIITIgSVVGTmGNGGQANYAAAKAGligfsksLARE 168
Cdd:COG0702   73 SGPGGDFAVDV----------------EGARNLADAAKAAGVKRIVYL-SALGA-DRDSPSPYLRAKAA-------VEEA 127
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446931279 169 VASRGITVNVVAPGFIETDMTRALSDDQRAGILAqVPAGRLG----GAQEIANAVAFLASDEAAY 229
Cdd:COG0702  128 LRASGLPYTILRPGWFMGNLLGFFERLRERGVLP-LPAGDGRvqpiAVRDVAEAAAAALTDPGHA 191
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
6-138 1.64e-03

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 38.30  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVtGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGAngkgLMLNVTDPASIESVLEkiraefgEVDILVN 85
Cdd:COG2910    1 KIAVI-GATGRVGSLIVREALARGHEVTALVRNPEKLPDEHPGLTV----VVGDVLDPAAVAEALA-------GADAVVS 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446931279  86 NAGITRDNLLMRMKDeewndiietnlssvfrLSKAVMRAMmkKRHG--RIITIGS 138
Cdd:COG2910   69 ALGAGGGNPTTVLSD----------------GARALIDAM--KAAGvkRLIVVGG 105
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
4-48 2.35e-03

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 38.31  E-value: 2.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSEN-------GAQAISDY 48
Cdd:cd05289  144 AGQTVLIHGAAGGVGSFAVQLAKARGARVIATASAANadflrslGADEVIDY 195
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
6-89 3.02e-03

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 38.14  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   6 KIALVTGASRGIGRAIAETLAA-----RGAKVIGTATS----ENGAQAISDYLGANGKG---LMLNVTDPASIESVLEKI 73
Cdd:cd08941    2 KVVLVTGANSGLGLAICERLLAeddenPELTLILACRNlqraEAACRALLASHPDARVVfdyVLVDLSNMVSVFAAAKEL 81
                         90
                 ....*....|....*.
gi 446931279  74 RAEFGEVDILVNNAGI 89
Cdd:cd08941   82 KKRYPRLDYLYLNAGI 97
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
10-179 3.76e-03

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 37.71  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  10 VTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDylgANGKGLMLNVTDPASiesvlekIRAEFGEVDIlVNNAGI 89
Cdd:cd05262    5 VTGATGFIGSAVVRELVAAGHEVVGLARSDAGAAKLEA---AGAQVHRGDLEDLDI-------LRKAAAEADA-VIHLAF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  90 TRDnllmrmkdeewndiiETNLSSVFRLSKAVMRAMMK--KRHGRIITIGSVVGTMGNGG------QANYAAAKAGLIGF 161
Cdd:cd05262   74 THD---------------FDNFAQACEVDRRAIEALGEalRGTGKPLIYTSGIWLLGPTGgqeedeEAPDDPPTPAARAV 138
                        170
                 ....*....|....*...
gi 446931279 162 SKSLAREVASRGITVNVV 179
Cdd:cd05262  139 SEAAALELAERGVRASVV 156
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
8-93 4.39e-03

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


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 37.61  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   8 ALVTGASRGIGRAIAETLAARGAKVIGTATSEngAQAISDYLGANGKGLMLNVTDPAsiesVLEKIRAEFGEVDILVNNA 87
Cdd:cd05271    3 VTVFGATGFIGRYVVNRLAKRGSQVIVPYRCE--AYARRLLVMGDLGQVLFVEFDLR----DDESIRKALEGSDVVINLV 76

                 ....*.
gi 446931279  88 GITRDN 93
Cdd:cd05271   77 GRLYET 82
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
4-85 5.46e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625 [Multi-domain]  Cd Length: 313  Bit Score: 37.50  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASrGIGRAIAETLAARGAKVIGTATSENGAQAISDYlgangkglmlnVTDPASIESVLekiraefGEVDIL 83
Cdd:cd05300  133 AGKTVLIVGLG-DIGREIARRAKAFGMRVIGVRRSGRPAPPVVDE-----------VYTPDELDELL-------PEADYV 193

                 ..
gi 446931279  84 VN 85
Cdd:cd05300  194 VN 195
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
4-51 6.65e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 37.05  E-value: 6.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDyLGA 51
Cdd:COG0604  139 PGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA-LGA 185
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
9-74 6.81e-03

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


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 36.86  E-value: 6.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLML------NVTDPASIESVLEKIR 74
Cdd:cd05227    3 LVTGATGFIASHIVEQLLKAGYKVRGTVRSLSKSAKLKALLKAAGYNDRLefvivdDLTAPNAWDEALKGVD 74
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
9-182 6.95e-03

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


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 36.44  E-value: 6.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279   9 LVTGASRGIGRAIAETLAARGAKVigTATSENGAQAiSDYLGANGKGLMLNVTDPASIESVLEKIraefgevDILVNNAG 88
Cdd:cd05243    3 LVVGATGKVGRHVVRELLDRGYQV--RALVRDPSQA-EKLEAAGAEVVVGDLTDAESLAAALEGI-------DAVISAAG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446931279  89 ITRDNLLMRMK-DEEWNdiietnlssvfrlsKAVMRAMMKKRHGRIItigsVVGTMGNGgqaNYAAAKAGLIGFS--KSL 165
Cdd:cd05243   73 SGGKGGPRTEAvDYDGN--------------INLIDAAKKAGVKRFV----LVSSIGAD---KPSHPLEALGPYLdaKRK 131
                        170
                 ....*....|....*...
gi 446931279 166 A-REVASRGITVNVVAPG 182
Cdd:cd05243  132 AeDYLRASGLDYTIVRPG 149
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
4-43 8.71e-03

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 36.65  E-value: 8.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446931279   4 EGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQ 43
Cdd:cd05286  136 PGDTVLVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKAE 175
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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