NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|83715985|ref|NP_001032900|]
View 

3-hydroxyacyl-CoA dehydrogenase type-2 isoform 2 [Homo sapiens]

Protein Classification

3-hydroxyacyl-CoA dehydrogenase( domain architecture ID 10143295)

3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in the beta-oxidation of fatty acids, the beta-oxidation of androgens and estrogens, as well as the oxidative conversion of bile acids

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 9-252 8.64e-154

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: 427.86  E-value: 8.64e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKkLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 169 SASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNG 239
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQgirvvtiapGLFDTPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIENPYLNG 239

                       250
                ....*....|...
gi 83715985 240 EVIRLDGAIRMQP 252
Cdd:cd05371 240 EVIRLDGAIRMPP 252
 
Name Accession Description Interval E-value
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 9-252 8.64e-154

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: 427.86  E-value: 8.64e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKkLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 169 SASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNG 239
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQgirvvtiapGLFDTPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIENPYLNG 239

                       250
                ....*....|...
gi 83715985 240 EVIRLDGAIRMQP 252
Cdd:cd05371 240 EVIRLDGAIRMPP 252
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 9-250 4.56e-60

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: 190.00  E-value: 4.56e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:COG1028   5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  86 DVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQ 165
Cdd:COG1028  85 DILVNNAGITPPGPL------EELTEEDWDRVLDVNLKGPFLLTRAALPHM----RERGG--GRIVNISSIAGLRGSPGQ 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 166 AAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLP--EKVCNFLASQVPFpSRLGDPAEYAHLVQAII-- 232
Cdd:COG1028 153 AAYAASKAAVVGLTRSLALELAPRgirvnavapGPIDTPMTRALLgaEEVREALAARIPL-GRLGTPEEVAAAVLFLAsd 231

                       250
                ....*....|....*...
gi 83715985 233 ENPFLNGEVIRLDGAIRM 250
Cdd:COG1028 232 AASYITGQVLAVDGGLTA 249
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-251 2.91e-52

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 169.99  E-value: 2.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGG----EAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaealVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQ 162
Cdd:PRK05557  82 GGVDILVNNAGIT------RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMK------QRSGRIINISSVVGLMGN 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAP--I-------GLFGTPLLTSLPEKVCNFLASQVPFPsRLGDPAEYAHLVQ--AI 231
Cdd:PRK05557 150 PGQANYAASKAGVIGFTKSLARELASrgItvnavapGFIETDMTDALPEDVKEAILAQIPLG-RLGQPEEIASAVAflAS 228

                        250       260
                 ....*....|....*....|
gi 83715985  232 IENPFLNGEVIRLDGAIRMQ 251
Cdd:PRK05557 229 DEAAYITGQTLHVNGGMVMG 248
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-204 7.77e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 154.31  E-value: 7.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCV---FAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGkalFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    89 VNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:pfam00106  82 VNNAGITGLGPFSEL------SDEDWERVIDVNLTGVFNLTRAVLPAM------IKGSGGRIVNISSVAGLVPYPGGSAY 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 83715985   169 SASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKV 204
Cdd:pfam00106 150 SASKAAVIGFTRSLALELAPHgirvnavapGGVDTDMTKELREDE 194
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 14-170 1.99e-12

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: 63.66  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985     14 VITGGASGLGLATAERLVGQGASAVLL----DLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLlsrsGPDAPGAAALLAELeaaGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985     87 VAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEmgqnEPDqggqrgVIINTASVAAFEGQVGQA 166
Cdd:smart00822  84 GVIHAAGVL------DDGVLASLTPERFAAVLAPKAAGAWNLHELTADL----PLD------FFVLFSSIAGVLGSPGQA 147


                   ....
gi 83715985    167 AYSA 170
Cdd:smart00822 148 NYAA 151
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 12-248 8.53e-06

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: 45.69  E-value: 8.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    12 VAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQA------KKLGNNCVFAPADVTsekDVQTALALAKG----- 80
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYR-VVLHYHRSAAAASTlaaelnARRPNSAVTCQADLS---NSATLFSRCEAiidac 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    81 --KFGRVDVAVNCAG----IAVASKTYNLKKGQTHTLE-DFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINT 153
Cdd:TIGR02685  79 frAFGRCDVLVNNASafypTPLLRGDAGEGVGDKKSLEvQVAELFGSNAIAPYFLIKAFAQRQAGTRAEQRSTNLSIVNL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   154 ASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGLF------GTPLL-TSLPEKVCNFLASQVPFPSRLGDPAEYAH 226
Cdd:TIGR02685 159 CDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRvngvapGLSLLpDAMPFEVQEDYRRKVPLGQREASAEQIAD 238

                         250       260
                  ....*....|....*....|....
gi 83715985   227 LVQAIIENP--FLNGEVIRLDGAI 248
Cdd:TIGR02685 239 VVIFLVSPKakYITGTCIKVDGGL 262
 
Name Accession Description Interval E-value
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 9-252 8.64e-154

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: 427.86  E-value: 8.64e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKkLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05371  80 VNCAGIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQAAY 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 169 SASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNG 239
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQgirvvtiapGLFDTPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIENPYLNG 239

                       250
                ....*....|...
gi 83715985 240 EVIRLDGAIRMQP 252
Cdd:cd05371 240 EVIRLDGAIRMPP 252
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 9-250 4.56e-60

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: 190.00  E-value: 4.56e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:COG1028   5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  86 DVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQ 165
Cdd:COG1028  85 DILVNNAGITPPGPL------EELTEEDWDRVLDVNLKGPFLLTRAALPHM----RERGG--GRIVNISSIAGLRGSPGQ 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 166 AAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLP--EKVCNFLASQVPFpSRLGDPAEYAHLVQAII-- 232
Cdd:COG1028 153 AAYAASKAAVVGLTRSLALELAPRgirvnavapGPIDTPMTRALLgaEEVREALAARIPL-GRLGTPEEVAAAVLFLAsd 231

                       250
                ....*....|....*...
gi 83715985 233 ENPFLNGEVIRLDGAIRM 250
Cdd:COG1028 232 AASYITGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 13-245 5.33e-54

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: 174.01  E-value: 5.33e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE--AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAelAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  91 CAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAYSA 170
Cdd:cd05233  81 NAGIARPGPLEEL------TDEDWDRVLDVNLTGVFLLTRAALPHM------KKQGGGRIVNISSVAGLRPLPGQAAYAA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 171 SKGGIVGMTLPIARDLAP---------IGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENP--FLNG 239
Cdd:cd05233 149 SKAALEGLTRSLALELAPygirvnavaPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEasYITG 228


                ....*.
gi 83715985 240 EVIRLD 245
Cdd:cd05233 229 QVIPVD 234
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-251 2.91e-52

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 169.99  E-value: 2.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGG----EAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaealVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQ 162
Cdd:PRK05557  82 GGVDILVNNAGIT------RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMK------QRSGRIINISSVVGLMGN 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAP--I-------GLFGTPLLTSLPEKVCNFLASQVPFPsRLGDPAEYAHLVQ--AI 231
Cdd:PRK05557 150 PGQANYAASKAGVIGFTKSLARELASrgItvnavapGFIETDMTDALPEDVKEAILAQIPLG-RLGQPEEIASAVAflAS 228

                        250       260
                 ....*....|....*....|
gi 83715985  232 IENPFLNGEVIRLDGAIRMQ 251
Cdd:PRK05557 229 DEAAYITGQTLHVNGGMVMG 248
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-250 5.52e-51

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 166.67  E-value: 5.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSG---GEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK08217   4 KDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKleeAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLKKGQTHT---LEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAfEGQ 162
Cdd:PRK08217  84 NGLINNAGILRDGLLVKAKDGKVTSkmsLEQFQSVIDVNLTGVFLCGREAAAKM-----IESGSKGVIINISSIAR-AGN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDL----------APiGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAII 232
Cdd:PRK08217 158 MGQTNYSASKAGVAAMTVTWAKELarygirvaaiAP-GVIETEMTAAMKPEALERLEKMIPV-GRLGEPEEIAHTVRFII 235

                        250
                 ....*....|....*...
gi 83715985  233 ENPFLNGEVIRLDGAIRM 250
Cdd:PRK08217 236 ENDYVTGRVLEIDGGLRL 253
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 12-246 9.30e-48

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: 158.09  E-value: 9.30e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA---QAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAEtveEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDIL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05333  82 VNNAGITRDNLLMRMSE------EDWDAVINVNLTGVFNVTQAVIRAMIKR------RSGRIINISSVVGLIGNPGQANY 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 169 SASKGGIVGMTLPIARDLAP--I-------GLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAIIENP--FL 237
Cdd:cd05333 150 AASKAGVIGFTKSLAKELASrgItvnavapGFIDTDMTDALPEKVKEKILKQIPL-GRLGTPEEVANAVAFLASDDasYI 228


                ....*....
gi 83715985 238 NGEVIRLDG 246
Cdd:cd05333 229 TGQVLHVNG 237
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
7-228 3.53e-47

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 156.86  E-value: 3.53e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAvasktynlKKGQTH--TLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEG 161
Cdd:PRK05653  82 ALDILVNNAGIT--------RDALLPrmSEEDWDRVIDVNLTGTFNVVRAALPPMIKA------RYGRIVNISSVSGVTG 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83715985  162 QVGQAAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCNFLASQVPfPSRLGDPAEYAHLV 228
Cdd:PRK05653 148 NPGQTNYSAAKAGVIGFTKALALELASRgitvnavapGFIDTDMTEGLPEEVKAEILKEIP-LGRLGQPEEVANAV 222
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-204 7.77e-47

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 154.31  E-value: 7.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCV---FAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGkalFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    89 VNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:pfam00106  82 VNNAGITGLGPFSEL------SDEDWERVIDVNLTGVFNLTRAVLPAM------IKGSGGRIVNISSVAGLVPYPGGSAY 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 83715985   169 SASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKV 204
Cdd:pfam00106 150 SASKAAVIGFTRSLALELAPHgirvnavapGGVDTDMTKELREDE 194
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 7-203 2.69e-45

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: 151.87  E-value: 2.69e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQA 166
Cdd:COG4221  82 VLVNNAGVALLGPLEEL------DPEDWDRMIDVNVKGVLYVTRAALPAMRAR------GSGHIVNISSIAGLRPYPGGA 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 83715985 167 AYSASKGGIVGMTLPIARDLAP---------IGLFGTPLLTSLPEK 203
Cdd:COG4221 150 VYAATKAAVRGLSESLRAELRPtgirvtviePGAVDTEFLDSVFDG 195
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 7-248 5.12e-45

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: 151.38  E-value: 5.12e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:cd05341  82 VLVNNAGILT------GGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPM----KEAGG--GSIINMSSIEGLVGDPALA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 167 AYSASKGGIVGMTLPIARDLAPI-----------GLFGTPLLTSLPEKVcnfLASQVPFPS---RLGDPAEYAHLVQAII 232
Cdd:cd05341 150 AYNASKGAVRGLTKSAALECATQgygirvnsvhpGYIYTPMTDELLIAQ---GEMGNYPNTpmgRAGEPDEIAYAVVYLA 226

                       250
                ....*....|....*...
gi 83715985 233 --ENPFLNGEVIRLDGAI 248
Cdd:cd05341 227 sdESSFVTGSELVVDGGY 244
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-246 1.05e-37

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 132.27  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVL-LDLPNSGGEAQAKKLGNN---CVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKEEggdAIAVKADVSSEEDVENLVEQIVEKFGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVG 164
Cdd:PRK05565  84 IDILVNNAGIS------NFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKR------KSGVIVNISSIWGLIGASC 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSLPEKVCNFLASQVPFPsRLGDPAEYAHLVQAII--E 233
Cdd:PRK05565 152 EVLYSASKGAVNAFTKALAKELAPSGIrvnavapgaIDTEMWSSFSEEDKEGLAEEIPLG-RLGKPEEIAKVVLFLAsdD 230

                        250
                 ....*....|...
gi 83715985  234 NPFLNGEVIRLDG 246
Cdd:PRK05565 231 ASYITGQIITVDG 243
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 10-247 1.30e-37

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: 132.13  E-value: 1.30e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:cd05345   5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  90 NCAGIavaskTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAYS 169
Cdd:cd05345  85 NNAGI-----THRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHM------EEQGGGVIINIASTAGLRPRPGLTWYN 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 170 ASKGGIVGMTLPIARDLAPIG---------LFGTPLLTSL-----PEKVCNFLASqVPFpSRLGDPAEYAH--LVQAIIE 233
Cdd:cd05345 154 ASKGWVVTATKAMAVELAPRNirvnclcpvAGETPLLSMFmgedtPENRAKFRAT-IPL-GRLSTPDDIANaaLYLASDE 231

                       250
                ....*....|....
gi 83715985 234 NPFLNGEVIRLDGA 247
Cdd:cd05345 232 ASFITGVALEVDGG 245
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-190 4.27e-37

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 130.76  E-value: 4.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  84 RVDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGgqRGVIINTASVAAFEGQV 163
Cdd:COG0300  82 PIDVLVNNAGVGGGGPF------EELDLEDLRRVFEVNVFGPVRLTRALLPLMRA----RG--RGRIVNVSSVAGLRGLP 149

                       170       180
                ....*....|....*....|....*..
gi 83715985 164 GQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:COG0300 150 GMAAYAASKAALEGFSESLRAELAPTG 176
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-248 5.12e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 131.01  E-value: 5.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    5 CRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNncVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK06057   2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGG--LFVPTDVTDEDAVNALFDTAAETYGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYNLKKGqthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTAS-VAAFEGQV 163
Cdd:PRK06057  80 VDIAFNNAGISPPEDDSILNTG----LDAWQRVQDVNLTSVYLCCKAALPHMVRQ------GKGSIINTASfVAVMGSAT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  164 GQAAYSASKGGIVGMT----LPIARD------LAPiGLFGTPLLTSL----PEKVCNFLAsQVPFpSRLGDPAEYAHLVQ 229
Cdd:PRK06057 150 SQISYTASKGGVLAMSrelgVQFARQgirvnaLCP-GPVNTPLLQELfakdPERAARRLV-HVPM-GRFAEPEEIAAAVA 226

                        250       260
                 ....*....|....*....|.
gi 83715985  230 --AIIENPFLNGEVIRLDGAI 248
Cdd:PRK06057 227 flASDDASFITASTFLVDGGI 247
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 12-246 5.28e-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: 130.50  E-value: 5.28e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA---QAKKLGNNCVFAPADVTSeKDVQTALAL-AKGKFGRVDV 87
Cdd:cd05323   2 VAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAaelQAINPKVKATFVQCDVTS-WEQLAAAFKkAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAVASKTYNLKKGQthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05323  81 LINNAGILDEKSYLFAGKLP----PPWEKTIDVNLTGVINTTYLALHYMDKN---KGGKGGVIVNIGSVAGLYPAPQFPV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 168 YSASKGGIVGMTlpiaRDLAPI--------------GLFGTPLLTSLPEKVCNFLASQvPFPSrlgdPAEYAHLVQAIIE 233
Cdd:cd05323 154 YSASKHGVVGFT----RSLADLleyktgvrvnaicpGFTNTPLLPDLVAKEAEMLPSA-PTQS----PEVVAKAIVYLIE 224

                       250
                ....*....|...
gi 83715985 234 NPFLNGEVIRLDG 246
Cdd:cd05323 225 DDEKNGAIWIVDG 237
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 10-191 1.20e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 129.78  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:PRK06841  15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   90 NCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQAAYS 169
Cdd:PRK06841  95 NSAGVAL------LAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIA----AGG--GKIVNLASQAGVVALERHVAYC 162

                        170       180
                 ....*....|....*....|..
gi 83715985  170 ASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK06841 163 ASKAGVVGMTKVLALEWGPYGI 184
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
12-250 1.22e-36

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 129.50  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSggeAQAKKLGNNCVF-------APADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK12824   4 IALVTGAKRGIGSAIARELLNDGYRVIATYFSGN---DCAKDWFEEYGFtedqvrlKELDVTDTEECAEALAEIEEEEGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIavaSKTYNLKKgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGQRgvIINTASVAAFEGQVG 164
Cdd:PRK12824  81 VDILVNNAGI---TRDSVFKR---MSHQEWNDVINTNLNSVFNVTQPLFAAMCE----QGYGR--IINISSVNGLKGQFG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAIIENP 235
Cdd:PRK12824 149 QTNYSAAKAGMIGFTKALASEGARYGItvnciapgyIATPMVEQMGPEVLQSIVNQIPM-KRLGTPEEIAAAVAFLVSEA 227

                        250
                 ....*....|....*..
gi 83715985  236 --FLNGEVIRLDGAIRM 250
Cdd:PRK12824 228 agFITGETISINGGLYM 244
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 12-250 8.50e-36

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: 127.88  E-value: 8.50e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNsggEAQAKKL-------GNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNL---EEAAKSTiqeiseaGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAFEGQVG 164
Cdd:cd05366  81 FDVMVNNAGIAPITPL------LTITEEDLKKVYAVNVFGVLFGIQAAARQF-----KKLGHGGKIINASSIAGVQGFPN 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 165 QAAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCN-----------FLASQVPFpSRLGDPAEY 224
Cdd:cd05366 150 LGAYSASKFAVRGLTQTAAQELAPKgitvnayapGIVKTEMWDYIDEEVGEiagkpegegfaEFSSSIPL-GRLSEPEDV 228

                       250       260
                ....*....|....*....|....*...
gi 83715985 225 AHLVQ--AIIENPFLNGEVIRLDGAIRM 250
Cdd:cd05366 229 AGLVSflASEDSDYITGQTILVDGGMVY 256
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 20-246 9.39e-36

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: 127.16  E-value: 9.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    20 SGLGLATAERLVGQGASAVLLDLPNSGG---EAQAKKLGnnCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAv 96
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAkrvEELAEELG--AAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    97 asktyNLKKGQTH--TLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQVGQAAYSASKGG 174
Cdd:pfam13561  83 -----PKLKGPFLdtSREDFDRALDVNLYSLFLLAKAALPLMKEG--------GSIVNLSSIGAERVVPNYNAYGAAKAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   175 IVGMTLPIARDLAP--I-------GLFGTPLLTSLP--EKVCNFLASQVPFPsRLGDPAEYAHLVQAII--ENPFLNGEV 241
Cdd:pfam13561 150 LEALTRYLAVELGPrgIrvnaispGPIKTLAASGIPgfDELLAAAEARAPLG-RLGTPEEVANAAAFLAsdLASYITGQV 228


                  ....*
gi 83715985   242 IRLDG 246
Cdd:pfam13561 229 LYVDG 233
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-190 6.61e-35

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 124.98  E-value: 6.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKK----LGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEaveaLGRRAQAVQADVTDKAALEAAVAAAVERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQ 162
Cdd:PRK12825  83 GRIDILVNNAGIFEDKPLADM------SDDEWDEVIDVNLSGVFHLLRAVVPPMRK----QRG--GRIVNISSVAGLPGW 150

                        170       180
                 ....*....|....*....|....*...
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK12825 151 PGRSNYAAAKAGLVGLTKALARELAEYG 178
FabG-like PRK07231
SDR family oxidoreductase;
10-248 3.75e-34

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 123.40  E-value: 3.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN--NCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAggRAIAVAADVSDEADVEAAVAAALERFGSVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIavasktyNLKKGQTH--TLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQ 165
Cdd:PRK07231  85 LVNNAGT-------THRNGPLLdvDEAEFDRIFAVNVKSPYLWTQAAVPAM----RGEGG--GAIVNVASTAGLRPRPGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSL-----PEKVCNFLASqvpFPS-RLGDPAEYAHLVQ- 229
Cdd:PRK07231 152 GWYNASKGAVITLTKALAAELGPDkirvnavapVVVETGLLEAFmgeptPENRAKFLAT---IPLgRLGTPEDIANAALf 228

                        250       260
                 ....*....|....*....|
gi 83715985  230 -AIIENPFLNGEVIRLDGAI 248
Cdd:PRK07231 229 lASDEASWITGVTLVVDGGR 248
PRK12826 PRK12826
SDR family oxidoreductase;
6-228 3.18e-33

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 120.79  E-value: 3.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVeaaGGKARARQVDVRDRAALKAAVAAGVEDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFE-G 161
Cdd:PRK12826  82 GRLDILVANAGIF------PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPAL------IRAGGGRIVLTSSVAGPRvG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83715985  162 QVGQAAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCN-FLASQVPFPsRLGDPAEYAHLV 228
Cdd:PRK12826 150 YPGLAHYAASKAGLVGFTRALALELAARnitvnsvhpGGVDTPMAGNLGDAQWAeAIAAAIPLG-RLGEPEDIAAAV 225
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 7-190 3.63e-32

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 118.58  E-value: 3.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQakklgnNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK06171   6 NLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQHE------NYQFVPTDVSSAEEVNHTVAEIIEKFGRID 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYNLK--KGQTHTLE-DFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQV 163
Cdd:PRK06171  80 GLVNNAGINIPRLLVDEKdpAGKYELNEaAFDKMFNINQKGVFLMSQAVARQMVKQ------HDGVIVNMSSEAGLEGSE 153

                        170       180
                 ....*....|....*....|....*..
gi 83715985  164 GQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK06171 154 GQSCYAATKAALNSFTRSWAKELGKHN 180
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 9-252 2.05e-31

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: 116.33  E-value: 2.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGAsAVLLDLpNSGGEA------QAKKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGA-NVVVNY-RSKEDAaeevveEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  83 GRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggQRGVIINTASVAAFEGQ 162
Cdd:cd05358  80 GTLDILVNNAGLQGDASSHEM------TLEDWNKVIDVNLTGQFLCAREAIKRFRKSK-----IKGKIINMSSVHEKIPW 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 163 VGQAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPL---LTSLPEKVCNFLaSQVPFPsRLGDPAEYAHLVQA 230
Cdd:cd05358 149 PGHVNYAASKGGVKMMTKTLAQEYAPKGIrvnaiapgaINTPInaeAWDDPEQRADLL-SLIPMG-RIGEPEEIAAAAAW 226

                       250       260
                ....*....|....*....|....
gi 83715985 231 II--ENPFLNGEVIRLDGAIRMQP 252
Cdd:cd05358 227 LAsdEASYVTGTTLFVDGGMTLYP 250
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 9-191 3.21e-31

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: 115.63  E-value: 3.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCV-FAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05326   3 DGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDIsFVHCDVTVEADVRAAVDTAVARFGRLDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAVASKTYNLKkgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05326  83 MFNNAGVLGAPCYSILE----TSLEEFERVLDVNVYGAFLGTKHAARVM------IPAKKGSIVSVASVAGVVGGLGPHA 152

                       170       180
                ....*....|....*....|....
gi 83715985 168 YSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd05326 153 YTASKHAVLGLTRSAATELGEHGI 176
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-248 4.11e-31

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: 115.15  E-value: 4.11e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAK---KLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQlieKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  84 RVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGgqRGVIINTASVAAFEGQV 163
Cdd:cd05347  82 KIDILVNNAGII------RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIK----QG--HGKIINICSLLSELGGP 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 164 GQAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPL---LTSLPEKVcNFLASQVPFpSRLGDPAEyahLVQAI 231
Cdd:cd05347 150 PVPAYAASKGGVAGLTKALATEWARHGIqvnaiapgyFATEMteaVVADPEFN-DDILKRIPA-GRWGQPED---LVGAA 224

                       250       260
                ....*....|....*....|..
gi 83715985 232 I-----ENPFLNGEVIRLDGAI 248
Cdd:cd05347 225 VflasdASDYVNGQIIFVDGGW 246
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 12-177 5.05e-31

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: 115.03  E-value: 5.05e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05339  81 INNAGVV------SGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLER------NHGHIVTIASVAGLISPAGLADY 148


                ....*....
gi 83715985 169 SASKGGIVG 177
Cdd:cd05339 149 CASKAAAVG 157
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
10-190 7.19e-31

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 120.34  E-value: 7.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAP--ADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALGvaCDVTDEAAVQAAFEEAALAFGGVDI 501

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqRGVIINTASVAAFEGQVGQAA 167
Cdd:PRK08324 502 VVSNAGIAISGPI------EETSDEDWRRSFDVNATGHFLVAREAVRIM----KAQGL-GGSIVFIASKNAVNPGPNFGA 570

                        170       180
                 ....*....|....*....|...
gi 83715985  168 YSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK08324 571 YGAAKAAELHLVRQLALELGPDG 593
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 6-191 7.98e-31

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 114.72  E-value: 7.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGiavaskTYnLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnepdQGGqrGVIINTASVAAFEGQVGQ 165
Cdd:PRK08265  82 DILVNLAC------TY-LDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLA-----RGG--GAIVNFTSISAKFAQTGR 147

                        170       180
                 ....*....|....*....|....*.
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK08265 148 WLYPASKAAIRQLTRSMAMDLAPDGI 173
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 7-251 1.78e-30

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 113.53  E-value: 1.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK12939   4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaaGGRAHAIAADLADPASVQRFFDAAAAALG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQV 163
Cdd:PRK12939  84 GLDGLVNNAGIT------NSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRD------SGRGRIVNLASDTALWGAP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  164 GQAAYSASKGGIVGMTLPIARDL----------APiGLFGTPLLTSLP-EKVCNFLASQVPFPsRLGDPAEYAHLVQAII 232
Cdd:PRK12939 152 KLGAYVASKGAVIGMTRSLARELggrgitvnaiAP-GLTATEATAYVPaDERHAYYLKGRALE-RLQVPDDVAGAVLFLL 229

                        250       260
                 ....*....|....*....|.
gi 83715985  233 --ENPFLNGEVIRLDGAIRMQ 251
Cdd:PRK12939 230 sdAARFVTGQLLPVNGGFVMN 250
PRK06138 PRK06138
SDR family oxidoreductase;
9-246 5.42e-30

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 112.55  E-value: 5.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL--GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK06138   4 AGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIaaGGRAFARQGDVGSAEAVEALVDFVAARWGRLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK06138  84 VLVNNAGFGCGGTV------VTTDEADWDAVMRVNVGGVFLWAKYAIPIMQR----QGG--GSIVNTASQLALAGGRGRA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  167 AYSASKGGIVGMTLPIARD----------LAPiGLFGTPLLTSL------PEKVCNFLASQVPFpSRLGDPAEYAH--LV 228
Cdd:PRK06138 152 AYVASKGAIASLTRAMALDhatdgirvnaVAP-GTIDTPYFRRIfarhadPEALREALRARHPM-NRFGTAEEVAQaaLF 229

                        250
                 ....*....|....*...
gi 83715985  229 QAIIENPFLNGEVIRLDG 246
Cdd:PRK06138 230 LASDESSFATGTTLVVDG 247
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 10-191 5.67e-30

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: 111.96  E-value: 5.67e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL-------GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIeaeanasGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  83 GRVDVAVNCAGIAVAsktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPdqggqrGVIINTASVAAFEGQ 162
Cdd:cd08939  81 GPPDLVVNCAGISIP------GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRP------GHIVFVSSQAALVGI 148

                       170       180
                ....*....|....*....|....*....
gi 83715985 163 VGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd08939 149 YGYSAYCPSKFALRGLAESLRQELKPYNI 177
PRK06484 PRK06484
short chain dehydrogenase; Validated
 12-246 1.70e-29

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 115.72  E-value: 1.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNC 91
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNN 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   92 AGIAVAsktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:PRK06484 351 AGIAEV-----FKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG--------GVIVNLGSIASLLALPPRNAYCAS 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  172 KGGIVGMTLPIARDLAPIGL---------FGTP---LLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVqAIIENP---F 236
Cdd:PRK06484 418 KAAVTMLSRSLACEWAPAGIrvntvapgyIETPavlALKASGRADFDSIRRRIPL-GRLGDPEEVAEAI-AFLASPaasY 495

                        250
                 ....*....|
gi 83715985  237 LNGEVIRLDG 246
Cdd:PRK06484 496 VNGATLTVDG 505
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-179 3.83e-29

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 109.78  E-value: 3.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAeevEAYGVKVVIATADVSDYEEVTAAIEQLKNELG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQV 163
Cdd:PRK07666  84 SIDILINNAGISKFGKFLEL------DPAEWEKIIQVNLMGVYYATRAVLPSMIER------QSGDIINISSTAGQKGAA 151

                        170
                 ....*....|....*.
gi 83715985  164 GQAAYSASKGGIVGMT 179
Cdd:PRK07666 152 VTSAYSASKFGVLGLT 167
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 12-246 4.93e-29

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: 109.92  E-value: 4.93e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL-----GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05330   5 VVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapDAEVLLIKADVSDEAQVEAYVDATVEQFGRID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIavaSKTYNLKkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:cd05330  85 GFFNNAGI---EGKQNLT--EDFGADEFDKVVSINLRGVFYGLEKVLKVMRE----QGS--GMIVNTASVGGIRGVGNQS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 167 AYSASKGGIVGMTLPIARD----------LAPiGLFGTPLLTSL--------PEKVCNFLASQVPFpSRLGDPAEYAHLV 228
Cdd:cd05330 154 GYAAAKHGVVGLTRNSAVEygqygirinaIAP-GAILTPMVEGSlkqlgpenPEEAGEEFVSVNPM-KRFGEPEEVAAVV 231

                       250       260
                ....*....|....*....|
gi 83715985 229 QAII--ENPFLNGEVIRLDG 246
Cdd:cd05330 232 AFLLsdDAGYVNAAVVPIDG 251
PRK06398 PRK06398
aldose dehydrogenase; Validated
 6-249 6.20e-29

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 109.92  E-value: 6.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLpNSGGEAQAKklgnncvFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK06398   2 LGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDI-KEPSYNDVD-------YFKVDVSNKEQVIKGIDYVISKYGRI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQ 165
Cdd:PRK06398  74 DILVNNAGIESYGAIHAVE------EDEWDRIINVNVNGIFLMSKYTIPYMLK----QDK--GVIINIASVQSFAVTRNA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPI--------GLFGTPLLT--------SLPEKV---CNFLASQVPFpSRLGDPAEYAH 226
Cdd:PRK06398 142 AAYVTSKHAVLGLTRSIAVDYAPTircvavcpGSIRTPLLEwaaelevgKDPEHVerkIREWGEMHPM-KRVGKPEEVAY 220

                        250       260
                 ....*....|....*....|....*
gi 83715985  227 LVQ--AIIENPFLNGEVIRLDGAIR 249
Cdd:PRK06398 221 VVAflASDLASFITGECVTVDGGLR 245
PRK06114 PRK06114
SDR family oxidoreductase;
7-191 6.20e-29

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 109.87  E-value: 6.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA----KKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETaehiEAAGRRAIQIAADVTSKADLRAAVARTEAEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQ 162
Cdd:PRK06114  85 GALTLAVNAAGIA------NANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLEN------GGGSIVNIASMSGIIVN 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 83715985  163 VG--QAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK06114 153 RGllQAHYNASKAGVIHLSKSLAMEWVGRGI 183
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 6-190 6.52e-29

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 109.76  E-value: 6.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDL-PNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK12829   7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVsEAALAATAARLPGAKVTATVADVADPAQVERVFDTAVERFGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQVG 164
Cdd:PRK12829  87 LDVLVNNAGIAGPTGGI-----DEITPEQWEQTLAVNLNGQFYFARAAVPLLKAS-----GHGGVIIALSSVAGRLGYPG 156

                        170       180
                 ....*....|....*....|....*.
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK12829 157 RTPYAASKWAVVGLVKSLAIELGPLG 182
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 8-190 7.02e-29

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 109.59  E-value: 7.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaGGKAIGVAMDVTDEEAINAGIDYAVETFGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVG 164
Cdd:PRK12429  82 VDILVNNAGIQHVAPIEDFP------TEKWKKMIAIMLDGAFLTTKAALPIMKA----QGG--GRIINMASVHGLVGSAG 149

                        170       180
                 ....*....|....*....|....*.
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK12429 150 KAAYVSAKHGLIGLTKVVALEGATHG 175
PRK07063 PRK07063
SDR family oxidoreductase;
9-247 2.85e-28

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 108.21  E-value: 2.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL-----GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK07063   6 AGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardvaGARVLAVPADVTDAASVAAAVAAAEEAFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGgqRGVIINTASVAAFEGQV 163
Cdd:PRK07063  86 PLDVLVNNAGINVFADPLAM------TDEDWRRCFAVDLDGAWNGCRAVLPGM----VERG--RGSIVNIASTHAFKIIP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  164 GQAAYSASKGGIVGMT--LPI---ARD-----LAPiGLFGTPLLTSL------PEKVCNFLASQVPfPSRLGDPAE--YA 225
Cdd:PRK07063 154 GCFPYPVAKHGLLGLTraLGIeyaARNvrvnaIAP-GYIETQLTEDWwnaqpdPAAARAETLALQP-MKRIGRPEEvaMT 231

                        250       260
                 ....*....|....*....|..
gi 83715985  226 HLVQAIIENPFLNGEVIRLDGA 247
Cdd:PRK07063 232 AVFLASDEAPFINATCITIDGG 253
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 9-225 4.30e-28

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: 107.76  E-value: 4.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQ-----AKKLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd05355  25 KGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEetkklIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFG 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  84 RVDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQV 163
Cdd:cd05355 105 KLDILVNNAAYQHPQESI-----EDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG--------SSIINTTSVTAYKGSP 171

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83715985 164 GQAAYSASKGGIVGMTLPIARDLAP--I-------GLFGTPLLTS--LPEKVCNFlASQVPfPSRLGDPAEYA 225
Cdd:cd05355 172 HLLDYAATKGAIVAFTRGLSLQLAEkgIrvnavapGPIWTPLIPSsfPEEKVSEF-GSQVP-MGRAGQPAEVA 242
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 12-242 5.57e-28

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: 106.93  E-value: 5.57e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQG----ASA-VLLDLPNSGGE--AQAKKLgnncvfaPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGyrviATArNPDKLESLGELlnDNLEVL-------ELDVTDEESIKAAVKEVIERFGR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVG 164
Cdd:cd05374  75 IDVLVNNAGYGLFGPLEET------SIEEVRELFEVNVFGPLRVTRAFLPLMRK----QGS--GRIVNVSSVAGLVPTPF 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 165 QAAYSASKGGIVGMTLPIARDLAPIGLfgtplltslpeKVC---------NFLASQVPFPSRLGDPAEYAHLVQAIIENP 235
Cdd:cd05374 143 LGPYCASKAALEALSESLRLELAPFGI-----------KVTiiepgpvrtGFADNAAGSALEDPEISPYAPERKEIKENA 211


                ....*..
gi 83715985 236 FLNGEVI 242
Cdd:cd05374 212 AGVGSNP 218
PRK06484 PRK06484
short chain dehydrogenase; Validated
 6-228 1.34e-27

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 110.32  E-value: 1.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK06484   1 SKAQSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLKKgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAFEGQVGQ 165
Cdd:PRK06484  81 DVLVNNAGVTDPTMTATLDT----TLEEFARLQAINLTGAYLVAREALRLM-----IEQGHGAAIVNVASGAGLVALPKR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSLpEKVCNF----LASQVPFpSRLGDPAEYAHLV 228
Cdd:PRK06484 152 TAYSASKAAVISLTRSLACEWAAKGIrvnavlpgyVRTQMVAEL-ERAGKLdpsaVRSRIPL-GRLGRPEEIAEAV 225
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 7-223 4.17e-27

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: 104.72  E-value: 4.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELakkyGVKTKAYKCDVSSQESVEKTFKQIQKDF 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  83 GRVDVAVNCAGIAVAsktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAafeGQ 162
Cdd:cd05352  85 GKIDILIANAGITVH------KPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQ------GKGSLIITASMS---GT 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83715985 163 VG-----QAAYSASKGGIVGMTLPIARDLA----------PiGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAE 223
Cdd:cd05352 150 IVnrpqpQAAYNASKAAVIHLAKSLAVEWAkyfirvnsisP-GYIDTDLTDFVDKELRKKWESYIPL-KRIALPEE 223
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-246 4.23e-27

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 104.80  E-value: 4.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL-------GNNCVFAPADVTSEKDVQTALALAK 79
Cdd:PRK12827   3 SLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVaagieaaGGKALGLAFDVRDFAATRAALDAGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   80 GKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAF 159
Cdd:PRK12827  83 EEFGRLDILVNNAGIATDAAFAEL------SIEEWDDVIDVNLDGFFNVTQAALPPM-----IRARRGGRIVNIASVAGV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  160 EGQVGQAAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPekVCNFLASQVPFpSRLGDPAEYAHLVQA 230
Cdd:PRK12827 152 RGNRGQVNYAASKAGLIGLTKTLANELAPRgitvnavapGAINTPMADNAA--PTEHLLNPVPV-QRLGEPDEVAALVAF 228

                        250
                 ....*....|....*...
gi 83715985  231 II--ENPFLNGEVIRLDG 246
Cdd:PRK12827 229 LVsdAASYVTGQVIPVDG 246
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 7-187 5.68e-27

(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: 104.33  E-value: 5.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDL-------PNSGGEAQA-----KKLGNNCVFAPADVT-SEKDVQT 73
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsGKSSSAADKvvdeiKAAGGKAVANYDSVEdGEKIVKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  74 ALAlakgKFGRVDVAVNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINT 153
Cdd:cd05353  82 AID----AFGRVDILVNNAGILRDRSFAKMSE------EDWDLVMRVHLKGSFKVTRAAWPYMRKQ------KFGRIINT 145

                       170       180       190
                ....*....|....*....|....*....|....
gi 83715985 154 ASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLA 187
Cdd:cd05353 146 SSAAGLYGNFGQANYSAAKLGLLGLSNTLAIEGA 179
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
9-191 7.32e-27

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 104.34  E-value: 7.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK07067   5 QGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIavasktYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:PRK07067  85 FNNAAL------FDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHM-----VEQGRGGKIINMASQAGRRGEALVSHY 153

                        170       180
                 ....*....|....*....|...
gi 83715985  169 SASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK07067 154 CATKAAVISYTQSAALALIRHGI 176
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 8-246 1.09e-26

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: 103.72  E-value: 1.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQAA 167
Cdd:cd08944  81 LVNNAGAMHLTPAI-----IDTDLAVWDQTMAINLRGTFLCCRHAAPRMIA----RGG--GSIVNLSSIAGQSGDPGYGA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 168 YSASKGGIVGMTLPIARD----------LAPiGLFGTPLLTS-LPE-----KVCNFLASQVPFPSRLGDPAEYAHLVQAI 231
Cdd:cd08944 150 YGASKAAIRNLTRTLAAElrhagircnaLAP-GLIDTPLLLAkLAGfegalGPGGFHLLIHQLQGRLGRPEDVAAAVVFL 228

                       250
                ....*....|....*..
gi 83715985 232 I--ENPFLNGEVIRLDG 246
Cdd:cd08944 229 LsdDASFITGQVLCVDG 245
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
12-250 1.38e-26

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 103.55  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA----QAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK12938   5 IAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVkwleDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIavaSKTYNLKKgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnepDQGGQRgvIINTASVAAFEGQVGQAA 167
Cdd:PRK12938  85 LVNNAGI---TRDVVFRK---MTREDWTAVIDTNLTSLFNVTKQVIDGMV----ERGWGR--IINISSVNGQKGQFGQTN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  168 YSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQ--AIIENPF 236
Cdd:PRK12938 153 YSTAKAGIHGFTMSLAQEVATKGVtvntvspgyIGTDMVKAIRPDVLEKIVATIPV-RRLGSPDEIGSIVAwlASEESGF 231

                        250
                 ....*....|....
gi 83715985  237 LNGEVIRLDGAIRM 250
Cdd:PRK12938 232 STGADFSLNGGLHM 245
PRK08589 PRK08589
SDR family oxidoreductase;
12-248 1.95e-26

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 103.70  E-value: 1.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLpNSGGEAQAKKLGNNCVFAPA---DVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK08589   8 VAVITGASTGIGQASAIALAQEGAYVLAVDI-AEAVSETVDKIKSNGGKAKAyhvDISDEQQVKDFASEIKEQFGRVDVL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAVASktynlkkGQTHT--LEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGQrgvIINTASVAAFEGQVGQA 166
Cdd:PRK08589  87 FNNAGVDNAA-------GRIHEypVDVFDKIMAVDMRGTFLMTKMLLPLM----MEQGGS---IINTSSFSGQAADLYRS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  167 AYSASKGGIVGMTLPIARD----------LAPiGLFGTPLL-----TSLPEKVCNFLASQ--VPFPSRLGDPAEYAHLVQ 229
Cdd:PRK08589 153 GYNAAKGAVINFTKSIAIEygrdgiranaIAP-GTIETPLVdkltgTSEDEAGKTFRENQkwMTPLGRLGKPEEVAKLVV 231

                        250       260
                 ....*....|....*....|.
gi 83715985  230 --AIIENPFLNGEVIRLDGAI 248
Cdd:PRK08589 232 flASDDSSFITGETIRIDGGV 252
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 9-213 2.05e-26

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 103.19  E-value: 2.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN-----NCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAeygegMAYGFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQV 163
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQ------LGDFDRSLQVNLVGYFLCAREFSRLMIRD-----GIQGRIIQINSKSGKVGSK 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83715985  164 GQAAYSASKGGIVGMTLPIARDLAPIG----------LFGTPLLTSL-----------PEKVCNFLASQVP 213
Cdd:PRK12384 150 HNSGYSAAKFGGVGLTQSLALDLAEYGitvhslmlgnLLKSPMFQSLlpqyakklgikPDEVEQYYIDKVP 220
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 12-248 4.74e-26

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 101.74  E-value: 4.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGAsAVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK12937   7 VAIVTGASRGIGAAIARRLAADGF-AVAVNYAGSAAAADElvaeiEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIavasktYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK12937  86 VLVNNAGV------MPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG--------GRIINLSTSVIALPLPGYG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIGLFGT-----PLLTSLP-----EKVCNFLASQVPFpSRLGDPAEYAHLVQ--AIIEN 234
Cdd:PRK12937 152 PYAASKAAVEGLVHVLANELRGRGITVNavapgPVATELFfngksAEQIDQLAGLAPL-ERLGTPEEIAAAVAflAGPDG 230

                        250
                 ....*....|....
gi 83715985  235 PFLNGEVIRLDGAI 248
Cdd:PRK12937 231 AWVNGQVLRVNGGF 244
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 9-246 8.31e-26

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: 101.20  E-value: 8.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGAS-VVVNYASSKAAAEEvvaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  84 RVDVAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQV 163
Cdd:cd05362  81 GVDILVNNAGVML------KKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG--------GRIINISSSLTAAYTP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 164 GQAAYSASKGGIVGMTLPIARDL----------APiGLFGTPL-LTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAII 232
Cdd:cd05362 147 NYGAYAGSKAAVEAFTRVLAKELggrgitvnavAP-GPVDTDMfYAGKTEEAVEGYAKMSPL-GRLGEPEDIAPVVAFLA 224

                       250
                ....*....|....*.
gi 83715985 233 --ENPFLNGEVIRLDG 246
Cdd:cd05362 225 spDGRWVNGQVIRANG 240
PRK07326 PRK07326
SDR family oxidoreductase;
7-191 9.12e-26

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 100.86  E-value: 9.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN--NCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNkgNVLGLAADVRDEADVQRAVDAIVAAFGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqrGVIINTASVA---AFEg 161
Cdd:PRK07326  83 LDVLIANAGVGH------FAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-------GYIINISSLAgtnFFA- 148

                        170       180       190
                 ....*....|....*....|....*....|
gi 83715985  162 qvGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK07326 149 --GGAAYNASKFGLVGFSEAAMLDLRQYGI 176
PRK07831 PRK07831
SDR family oxidoreductase;
9-190 1.76e-25

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 100.88  E-value: 1.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGA-SGLGLATAERLVGQGASAVLLDL-PNSGGEAQ---AKKLGNNCVFA-PADVTSEKDVQTALALAKGKF 82
Cdd:PRK07831  16 AGKVVLVTAAAgTGIGSATARRALEEGARVVISDIhERRLGETAdelAAELGLGRVEAvVCDVTSEAQVDALIDAAVERL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAvasktynlkkGQTH----TLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAA 158
Cdd:PRK07831  96 GRLDVLVNNAGLG----------GQTPvvdmTDDEWSRVLDVTLTGTFRATRAALRYMRAR-----GHGGVIVNNASVLG 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 83715985  159 FEGQVGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK07831 161 WRAQHGQAHYAAAKAGVMALTRCSALEAAEYG 192
PRK07069 PRK07069
short chain dehydrogenase; Validated
 13-248 2.03e-25

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 100.17  E-value: 2.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   13 AVITGGASGLGLATAERLVGQGASAVLLDLPN-SGGEAQAKKLGNNC----VFA-PADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDaAGLDAFAAEINAAHgegvAFAaVQDVTDEAQWQALLAQAADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPdqggqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK07069  82 VLVNNAGVGSFGAI------EQIELDEWRRVMAINVESIFLGCKHALPYLRASQP------ASIVNISSVAAFKAEPDYT 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIGL-----------FGTPLLTSL-----PEKVCNFLASQVPFpSRLGDPAEYAHLV-- 228
Cdd:PRK07069 150 AYNASKAAVASLTKSIALDCARRGLdvrcnsihptfIRTGIVDPIfqrlgEEEATRKLARGVPL-GRLGEPDDVAHAVly 228

                        250       260
                 ....*....|....*....|
gi 83715985  229 QAIIENPFLNGEVIRLDGAI 248
Cdd:PRK07069 229 LASDESRFVTGAELVIDGGI 248
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 12-191 3.16e-25

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: 99.38  E-value: 3.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELArevRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05360  82 VNNAGVAVFGRF------EDVTPEEFRRVFDVNYLGHVYGTLAALPHLRR------RGGGALINVGSLLGYRSAPLQAAY 149

                       170       180
                ....*....|....*....|....*..
gi 83715985 169 SASKGGIVGMT----LPIARDLAPIGL 191
Cdd:cd05360 150 SASKHAVRGFTeslrAELAHDGAPISV 176
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 10-248 3.34e-25

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: 99.58  E-value: 3.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  90 NCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqRGVIINTASVAAFEGQVGQAAYS 169
Cdd:cd09761  81 NNAARG------SKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKN-------KGRIINIASTRAFQSEPDSEAYA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 170 ASKGGIVGMTLPIARDLAPIGLF-----GTPLLTSLPEKVCNFLA----SQVPfPSRLGDPAEYAHLVQAIIENP--FLN 238
Cdd:cd09761 148 ASKGGLVALTHALAMSLGPDIRVncispGWINTTEQQEFTAAPLTqedhAQHP-AGRVGTPKDIANLVLFLCQQDagFIT 226

                       250
                ....*....|
gi 83715985 239 GEVIRLDGAI 248
Cdd:cd09761 227 GETFIVDGGM 236
PRK06172 PRK06172
SDR family oxidoreductase;
9-246 6.15e-25

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 99.06  E-value: 6.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE---AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK06172   6 SGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEetvALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTynLKKGqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQ 165
Cdd:PRK06172  86 DYAFNNAGIEIEQGR--LAEG---SEAEFDAIMGVNVKGVWLCMKYQIPLMLA----QGG--GAIVNTASVAGLGAAPKM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSLPE---KVCNFLASQVPFpSRLGDPAEYAHLVQAIIE 233
Cdd:PRK06172 155 SIYAASKHAVIGLTKSAAIEYAKKGIrvnavcpavIDTDMFRRAYEadpRKAEFAAAMHPV-GRIGKVEEVASAVLYLCS 233

                        250
                 ....*....|....*
gi 83715985  234 N--PFLNGEVIRLDG 246
Cdd:PRK06172 234 DgaSFTTGHALMVDG 248
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 12-250 8.11e-25

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: 98.68  E-value: 8.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNS-GGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTeSAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  91 CAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYSA 170
Cdd:cd05349  82 NALIDFPFDPDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKER------GSGRVINIGTNLFQNPVVPYHDYTT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 171 SKGGIVGMTLPIARDLAPIG----------LFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQ--AIIENPFLN 238
Cdd:cd05349 156 AKAALLGFTRNMAKELGPYGitvnmvsgglLKVTDASAATPKEVFDAIAQTTPL-GKVTTPQDIADAVLffASPWARAVT 234

                       250
                ....*....|..
gi 83715985 239 GEVIRLDGAIRM 250
Cdd:cd05349 235 GQNLVVDGGLVM 246
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 6-190 9.34e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 99.24  E-value: 9.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGnNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG-LVVGGPLDVTDPASFAAFLDAVEADLGPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLKKGQTHtledfqRVLDVNLMGTFNVIRLVAGEMgqnePDQGgqRGVIINTASVAAFEGQVGQ 165
Cdd:PRK07825  80 DVLVNNAGVMPVGPFLDEPDAVTR------RILDVNVYGVILGSKLAAPRM----VPRG--RGHVVNVASLAGKIPVPGM 147

                        170       180
                 ....*....|....*....|....*
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK07825 148 ATYCASKHAVVGFTDAARLELRGTG 172
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 9-248 9.74e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 98.87  E-value: 9.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLL-----DLPnsggEAQA--KKLGNNCVFAPADVTSEKDVQTALALAKGK 81
Cdd:PRK08213  11 SGKTALVTGGSRGLGLQIAEALGEAGARVVLSarkaeELE----EAAAhlEALGIDALWIAADVADEADIERLAEETLER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   82 FGRVDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepDQGGqrGVIINTASVAAFEG 161
Cdd:PRK08213  87 FGHVDILVNNAGATWGAPA------EDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMI---PRGY--GRIINVASVAGLGG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  162 ----QVGQAAYSASKGGIVGMTlpiaRDLA--------------PiGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAE 223
Cdd:PRK08213 156 nppeVMDTIAYNTSKGAVINFT----RALAaewgphgirvnaiaP-GFFPTKMTRGTLERLGEDLLAHTPL-GRLGDDED 229

                        250       260
                 ....*....|....*....|....*..
gi 83715985  224 Y--AHLVQAIIENPFLNGEVIRLDGAI 248
Cdd:PRK08213 230 LkgAALLLASDASKHITGQILAVDGGV 256
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 10-248 1.50e-24

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: 98.11  E-value: 1.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQA 166
Cdd:cd05344  81 ILVNNAGGPPPGPFAEL------TDEDWLEAFDLKLLSVIRIVRAVLPGMKER------GWGRIVNISSLTVKEPEPNLV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 167 AYSASKGGIVGMTLPIARDLAP---------IGLFGTPLLTSL-----------PEKVCNFLASQVPFpSRLGDPAEYAH 226
Cdd:cd05344 149 LSNVARAGLIGLVKTLSRELAPdgvtvnsvlPGYIDTERVRRLlearaekegisVEEAEKEVASQIPL-GRVGKPEELAA 227

                       250       260
                ....*....|....*....|....*
gi 83715985 227 LVqAIIENP---FLNGEVIRLDGAI 248
Cdd:cd05344 228 LI-AFLASEkasYITGQAILVDGGL 251
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-191 2.16e-24

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 98.70  E-value: 2.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLD----LPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGk 81
Cdd:PRK07792   8 TDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDvasaLDASDVLDEIRAAGAKAVAVAGDISQRATADELVATAVG- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   82 FGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQ-RGVIINTASVAAFE 160
Cdd:PRK07792  87 LGGLDIVVNNAGITRDRMLFNM------SDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKAAGGPvYGRIVNTSSEAGLV 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 83715985  161 GQVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK07792 161 GPVGQANYGAAKAGITALTLSAARALGRYGV 191
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
12-191 2.22e-24

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 97.87  E-value: 2.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK08643   4 VALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLskdGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNVV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIrlvagEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:PRK08643  84 VNNAGVAPTTPI------ETITEEQFDKVYNINVGGVIWGI-----QAAQEAFKKLGHGGKIINATSQAGVVGNPELAVY 152

                        170       180
                 ....*....|....*....|...
gi 83715985  169 SASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK08643 153 SSTKFAVRGLTQTAARDLASEGI 175
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 9-191 3.23e-24

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: 97.52  E-value: 3.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLpnsGGEAQAKKL--------GNNCVFAPADVTSEKDVQTALALAKG 80
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGF---GDAAEIEAVraglaakhGVKVLYHGADLSKPAAIEDMVAYAQR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  81 KFGRVDVAVNCAGIA-VASKTynlkkgqTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAF 159
Cdd:cd08940  78 QFGGVDILVNNAGIQhVAPIE-------DFPTEKWDAIIALNLSAVFHTTRLALPHMKKQ------GWGRIINIASVHGL 144

                       170       180       190
                ....*....|....*....|....*....|..
gi 83715985 160 EGQVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd08940 145 VASANKSAYVAAKHGVVGLTKVVALETAGTGV 176
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-247 3.26e-24

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: 97.53  E-value: 3.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalGGRAIALAADVLDRASLERAREEIVAQFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  84 RVDVAVNCAG-----IAVASKTYNLKKGQTH---TLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTAS 155
Cdd:cd08935  82 TVDILINGAGgnhpdATTDPEHYEPETEQNFfdlDEEGWEFVFDLNLNGSFLPSQVFGKDM------LEQKGGSIINISS 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 156 VAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSL-------PEKVCNFLASQVPFpSRLG 219
Cdd:cd08935 156 MNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVrvnaiapgfFVTPQNRKLlinpdgsYTDRSNKILGRTPM-GRFG 234

                       250       260       270
                ....*....|....*....|....*....|.
gi 83715985 220 DPAEYAHLVQAIIENP---FLNGEVIRLDGA 247
Cdd:cd08935 235 KPEELLGALLFLASEKassFVTGVVIPVDGG 265
PLN02253 PLN02253
xanthoxin dehydrogenase
 5-191 3.84e-24

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 97.59  E-value: 3.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    5 CRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN--NCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PLN02253  13 SQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGepNVCFFHCDVTVEDDVSRAVDFTVDKF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAvASKTYNLKKgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQ 162
Cdd:PLN02253  93 GTLDIMVNNAGLT-GPPCPDIRN---VELSEFEKVFDVNVKGVFLGMKHAARIMIPL------KKGSIVSLCSVASAIGG 162

                        170       180
                 ....*....|....*....|....*....
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PLN02253 163 LGPHAYTGSKHAVLGLTRSVAAELGKHGI 191
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 6-191 4.71e-24

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 97.10  E-value: 4.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA----KKLGNNCVFAPADVTSEKDVQTALALAKGK 81
Cdd:PRK08936   3 SDLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVaeeiKKAGGEAIAVKGDVTVESDVVNLIQTAVKE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   82 FGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEG 161
Cdd:PRK08936  83 FGTLDVMINNAGIENAVPSHEM------SLEDWNKVINTNLTGAFLGSREAIKYFVEH-----DIKGNIINMSSVHEQIP 151

                        170       180       190
                 ....*....|....*....|....*....|
gi 83715985  162 QVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK08936 152 WPLFVHYAASKGGVKLMTETLAMEYAPKGI 181
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-246 6.80e-24

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 95.80  E-value: 6.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLpnsggeAQAKKLGNNCVFAPADVTSEkdvqtaLALAKGKFGRVDVAVNC 91
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQGAQVYGVDK------QDKPDLSGNFHFLQLDLSDD------LEPLFDWVPSVDILCNT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   92 AGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:PRK06550  75 AGILDDYKPL-----LDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER------KSGIIINMCSIASFVAGGGGAAYTAS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  172 KGGIVGMTLPIARDLAPIGL--FG-------TPLLTS--LPEKVCNFLASQVPFpSRLGDPAEYAHLV------QAiien 234
Cdd:PRK06550 144 KHALAGFTKQLALDYAKDGIqvFGiapgavkTPMTAAdfEPGGLADWVARETPI-KRWAEPEEVAELTlflasgKA---- 218

                        250
                 ....*....|..
gi 83715985  235 PFLNGEVIRLDG 246
Cdd:PRK06550 219 DYMQGTIVPIDG 230
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 12-250 9.96e-24

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: 95.99  E-value: 9.96e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPN----SGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDddqaTEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAVASKTYNLKKgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05337  83 LVNNAGIAVRPRGDLLDL----TEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFDGPHRSIIFVTSINAYLVSPNRGE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 168 YSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCNFLAS-QVPFPsRLGDPAEYAHLVQAIIEN--P 235
Cdd:cd05337 159 YCISKAGLSMATRLLAYRLADEgiavheirpGLIHTDMTAPVKEKYDELIAAgLVPIR-RWGQPEDIAKAVRTLASGllP 237

                       250
                ....*....|....*
gi 83715985 236 FLNGEVIRLDGAIRM 250
Cdd:cd05337 238 YSTGQPINIDGGLSM 252
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 7-187 1.11e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 96.12  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEInkaGGKAIGVAMDVTNEDAVNAGIDKVAERFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAVASKTYNlkkgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepDQGgqrGVIINTASVAAFEGQV 163
Cdd:PRK13394  84 SVDILVSNAGIQIVNPIEN------YSFADWKKMQAIHVDGAFLTTKAALKHMYKD--DRG---GVVIYMGSVHSHEASP 152

                        170       180
                 ....*....|....*....|....
gi 83715985  164 GQAAYSASKGGIVGMTLPIARDLA 187
Cdd:PRK13394 153 LKSAYVTAKHGLLGLARVLAKEGA 176
PRK07774 PRK07774
SDR family oxidoreductase;
9-186 1.26e-23

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 95.58  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK07774   5 DDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadGGTAIAVQVDVSDPDSAKAMADATVSAFGGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFegqVGQ 165
Cdd:PRK07774  85 DYLVNNAAIYGGMKLDLL---ITVPWDYYKKFMSVNLDGALVCTRAVYKHMAK----RGG--GAIVNQSSTAAW---LYS 152

                        170       180
                 ....*....|....*....|.
gi 83715985  166 AAYSASKGGIVGMTLPIARDL 186
Cdd:PRK07774 153 NFYGLAKVGLNGLTQQLAREL 173
PRK07832 PRK07832
SDR family oxidoreductase;
13-191 2.12e-23

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 95.49  E-value: 2.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE---AQAKKLGNNCVFAPA-DVTsekDVQTALALAK---GKFGRV 85
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAqtvADARALGGTVPEHRAlDIS---DYDAVAAFAAdihAAHGSM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLkkgqTHtlEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAFEGQVGQ 165
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRL----TH--EQWRRMVDVNLMGPIHVIETFVPPM-----VAAGRGGHLVNVSSAAGLVALPWH 148

                        170       180
                 ....*....|....*....|....*.
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK07832 149 AAYSASKFGLRGLSEVLRFDLARHGI 174
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
10-246 2.34e-23

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 95.25  E-value: 2.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAqAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKL-ADELcgrGHRCTAVVADVRDPASVAAAIKRAKEKEGRID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYNLkkgqTHTLEDFQrvLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAA-FEGQVGQ 165
Cdd:PRK08226  85 ILVNNAGVCRLGSFLDM----SDEDRDFH--IDINIKGVWNVTKAVLPEMIAR------KDGRIVMMSSVTGdMVADPGE 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAP---------IGLFGTPLLTSL--------PEKVCNFLASQVPFpSRLGDPAEYAHLV 228
Cdd:PRK08226 153 TAYALTKAAIVGLTKSLAVEYAQsgirvnaicPGYVRTPMAESIarqsnpedPESVLTEMAKAIPL-RRLADPLEVGELA 231

                        250       260
                 ....*....|....*....|
gi 83715985  229 Q--AIIENPFLNGEVIRLDG 246
Cdd:PRK08226 232 AflASDESSYLTGTQNVIDG 251
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 9-190 2.80e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 94.64  E-value: 2.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVL-------LDlpnsGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGK 81
Cdd:PRK07890   4 KGKVVVVSGVGPGLGRTLAVRAARAGADVVLaartaerLD----EVAAEIDDLGRRALAVPTDITDEDQCANLVALALER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   82 FGRVDVAVNcagiaVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqggQRGVIINTASVAAFEG 161
Cdd:PRK07890  80 FGRVDALVN-----NAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAE-------SGGSIVMINSMVLRHS 147

                        170       180
                 ....*....|....*....|....*....
gi 83715985  162 QVGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK07890 148 QPKYGAYKMAKGALLAASQSLATELGPQG 176
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 6-175 2.96e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 95.42  E-value: 2.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVF--APADVTSEKDVQTALALAKGKFG 83
Cdd:PRK05872   5 TSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVltVVADVTDLAAMQAAAEEAVERFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnePDQGGQRGVIINTASVAAFEGQV 163
Cdd:PRK05872  85 GIDVVVANAGIASGGSV------AQVDPDAFRRVIDVNLLGVFHTVRATL-------PALIERRGYVLQVSSLAAFAAAP 151

                        170
                 ....*....|..
gi 83715985  164 GQAAYSASKGGI 175
Cdd:PRK05872 152 GMAAYCASKAGV 163
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 12-179 3.14e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 96.14  E-value: 3.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLL------------DLPNSGGEAqakklgnncVFAPADVTSEKDVQTALALAK 79
Cdd:PRK07109  10 VVVITGASAGVGRATARAFARRGAKVVLLargeeglealaaEIRAAGGEA---------LAVVADVADAEAVQAAADRAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   80 GKFGRVDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAF 159
Cdd:PRK07109  81 EELGPIDTWVNNAMVTVFGPF------EDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRD------RGAIIQVGSALAY 148

                        170       180
                 ....*....|....*....|
gi 83715985  160 EGQVGQAAYSASKGGIVGMT 179
Cdd:PRK07109 149 RSIPLQSAYCAAKHAIRGFT 168
PRK05650 PRK05650
SDR family oxidoreductase;
14-200 5.25e-23

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 94.34  E-value: 5.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   14 VITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLreaGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   91 CAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQAAYSA 170
Cdd:PRK05650  84 NAGVASGGFFEEL------SLEDWDWQIAINLMGVVKGCKAFLPLFKR----QKS--GRIVNIASMAGLMQGPAMSSYNV 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 83715985  171 SKGGIVGMTLPIARDLAPIGL---------FGTPLLTSL 200
Cdd:PRK05650 152 AKAGVVALSETLLVELADDEIgvhvvcpsfFQTNLLDSF 190
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 7-250 5.32e-23

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 93.92  E-value: 5.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVL-LDLPNSGGEAQAKKLGNN---CVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGKEghdVYAVQADVSKVEDANRLVEEAVNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIavaSKTYNLKKGQThtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAFEGQ 162
Cdd:PRK12935  83 GKVDILVNNAGI---TRDRTFKKLNR---EDWERVIDVNLSSVFNTTSAVLPYITEAE------EGRIISISSIIGQAGG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCNFLASQVPfPSRLGDPAEYAH-LVQAII 232
Cdd:PRK12935 151 FGQTNYSAAKAGMLGFTKSLALELAKTnvtvnaicpGFIDTEMVAEVPEEVRQKIVAKIP-KKRFGQADEIAKgVVYLCR 229

                        250
                 ....*....|....*...
gi 83715985  233 ENPFLNGEVIRLDGAIRM 250
Cdd:PRK12935 230 DGAYITGQQLNINGGLYM 247
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-188 9.82e-23

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 93.26  E-value: 9.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA--KKLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDETRRliEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGgqRGVIINTASVAAFEGQVG 164
Cdd:PRK06935  92 IDILVNNAGTIRRAPLLEYKD------EDWNAVMDINLNSVYHLSQAVAKVMAK----QG--SGKIINIASMLSFQGGKF 159

                        170       180
                 ....*....|....*....|....
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAP 188
Cdd:PRK06935 160 VPAYTASKHGVAGLTKAFANELAA 183
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 9-191 1.56e-22

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: 92.98  E-value: 1.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA--KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd08937   3 EGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAeiLAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQvgQA 166
Cdd:cd08937  83 VLINNVGGTIWAKPY-----EHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLER------QQGVIVNVSSIATRGIY--RI 149

                       170       180
                ....*....|....*....|....*
gi 83715985 167 AYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd08937 150 PYSAAKGGVNALTASLAFEHARDGI 174
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 9-247 1.73e-22

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: 92.65  E-value: 1.73e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLL--DLPNSggEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05369   2 KGKVAFITGGGTGIGKAIAKAFAELGASVAIAgrKPEVL--EAAAEEIssatGGRAHPIQCDVRDPEAVEAAVDETLKEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  83 GRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAgemgqNEPDQGGQRGVIINTASVAAFEGQ 162
Cdd:cd05369  80 GKIDILINNAAGNFLAPAESL------SPNGFKTVIDIDLNGTFNTTKAVG-----KRLIEAKHGGSILNISATYAYTGS 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 163 VGQAAYSASKGGIVGMTLPIARDLAPIGL----------FGTPLLTSL--PEKVCNFLASQVPFpSRLGDPAEYAHLVqA 230
Cdd:cd05369 149 PFQVHSAAAKAGVDALTRSLAVEWGPYGIrvnaiapgpiPTTEGMERLapSGKSEKKMIERVPL-GRLGTPEEIANLA-L 226

                       250       260
                ....*....|....*....|
gi 83715985 231 IIENP---FLNGEVIRLDGA 247
Cdd:cd05369 227 FLLSDaasYINGTTLVVDGG 246
PRK07074 PRK07074
SDR family oxidoreductase;
12-191 3.29e-22

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 91.75  E-value: 3.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPA-DVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:PRK07074   4 TALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVPVAcDLTDAASLAAALANAAAERGPVDVLVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   91 CAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASV---AAFegqvGQAA 167
Cdd:PRK07074  84 NAGAARAASL------HDTTPASWRADNALNLEAAYLCVEAVLEGMLKR------SRGAVVNIGSVngmAAL----GHPA 147

                        170       180
                 ....*....|....*....|....
gi 83715985  168 YSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK07074 148 YSAAKAGLIHYTKLLAVEYGRFGI 171
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 9-190 4.27e-22

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 91.48  E-value: 4.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDL---PNSGGEAQAKKLgnncvfapaDVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK08220   7 SGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQaflTQEDYPFATFVL---------DVSDAAAVAQVCQRLLAETGPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIavasktynLKKGQTHTL--EDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQV 163
Cdd:PRK08220  78 DVLVNAAGI--------LRMGATDSLsdEDWQQTFAVNAGGAFNLFRAVMPQFRRQ------RSGAIVTVGSNAAHVPRI 143

                        170       180
                 ....*....|....*....|....*..
gi 83715985  164 GQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK08220 144 GMAAYGASKAALTSLAKCVGLELAPYG 170
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 9-246 5.69e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 92.02  E-value: 5.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK06701  45 KGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRvekeGVKCLLIPGDVSDEAFCKDAVEETVRELGR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQVG 164
Cdd:PRK06701 125 LDILVNNAAFQYPQQSL-----EDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG--------SAIINTGSITGYEGNET 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLL--TSLPEKVCNFlASQVPFpSRLGDPAEY--AHLVQAI 231
Cdd:PRK06701 192 LIDYSATKGAIHAFTRSLAQSLVQKGIrvnavapgpIWTPLIpsDFDEEKVSQF-GSNTPM-QRPGQPEELapAYVFLAS 269

                        250
                 ....*....|....*
gi 83715985  232 IENPFLNGEVIRLDG 246
Cdd:PRK06701 270 PDSSYITGQMLHVNG 284
PRK06181 PRK06181
SDR family oxidoreductase;
12-177 6.19e-22

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 91.19  E-value: 6.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK06181   3 VVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELadhGGEALVVPTDVSDAEACERLIEAAVARFGGIDIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAVASKTynlkkGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqRGVIINTASVAAFEGQVGQAAY 168
Cdd:PRK06181  83 VNNAGITMWSRF-----DELTDLSVFERVMRVNYLGAVYCTHAALPHLKAS-------RGQIVVVSSLAGLTGVPTRSGY 150


                 ....*....
gi 83715985  169 SASKGGIVG 177
Cdd:PRK06181 151 AASKHALHG 159
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 12-191 6.68e-22

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: 91.06  E-value: 6.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd08945   5 VALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGiavasktyNLKKGQTHTLED--FQRVLDVNLMGTFNVIR--LVAGEMGQNEpdqggqRGVIINTASVAAFEGQVG 164
Cdd:cd08945  85 VNNAG--------RSGGGATAELADelWLDVVETNLTGVFRVTKevLKAGGMLERG------TGRIINIASTGGKQGVVH 150

                       170       180
                ....*....|....*....|....*..
gi 83715985 165 QAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd08945 151 AAPYSASKHGVVGFTKALGLELARTGI 177
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 8-191 6.72e-22

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: 91.14  E-value: 6.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIavasktYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnepdQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05363  81 LVNNAAL------FDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMI-----AQGRGGKIINMASQAGRRGEALVGV 149

                       170       180
                ....*....|....*....|....
gi 83715985 168 YSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd05363 150 YCATKAAVISLTQSAGLNLIRHGI 173
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-251 7.22e-22

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 90.79  E-value: 7.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK12745   4 VALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATqqelRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIAVASKTYNLKKgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:PRK12745  84 LVNNAGVGVKVRGDLLDL----TPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEELPHRSIVFVSSVNAIMVSPNRGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  168 YSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSLPEKVCNFLASQ-VPFPsRLGDPAEYAHLVQAIIEN--P 235
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEgigvyevrpGLIKTDMTAPVTAKYDALIAKGlVPMP-RWGEPEDVARAVAALASGdlP 238

                        250
                 ....*....|....*.
gi 83715985  236 FLNGEVIRLDGAIRMQ 251
Cdd:PRK12745 239 YSTGQAIHVDGGLSIP 254
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 9-246 7.65e-22

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: 90.61  E-value: 7.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLpnSGGEAQAKKLGNNCVFAPADVTSEKDVQTALAlakgKFGRVDVA 88
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDI--NEEKLKELERGPGITTRVLDVTDKEQVAALAK----EEGRIDVL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAA-FEGQVGQAA 167
Cdd:cd05368  75 FNCAGFVHHGSILDCED------DDWDFAMNLNVRSMYLMIKAVLPKMLA----RKD--GSIINMSSVASsIKGVPNRFV 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 168 YSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSL------PEKVCNFLASQVPFpSRLGDPAEYAHLVQ--A 230
Cdd:cd05368 143 YSTTKAAVIGLTKSVAADFAQQGIrcnaicpgtVDTPSLEERiqaqpdPEEALKAFAARQPL-GRLATPEEVAALAVylA 221

                       250
                ....*....|....*.
gi 83715985 231 IIENPFLNGEVIRLDG 246
Cdd:cd05368 222 SDESAYVTGTAVVIDG 237
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 10-174 7.69e-22

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: 90.91  E-value: 7.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE--AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEkvAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd08943  81 VVSNAGIATSSPIAET------SLEDWNRSMDINLTGHFLVSREAFRIMKSQ-----GIGGNIVFNASKNAVAPGPNAAA 149


                ....*..
gi 83715985 168 YSASKGG 174
Cdd:cd08943 150 YSAAKAA 156
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 13-191 1.10e-21

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: 90.22  E-value: 1.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDLPnsggEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCA 92
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLP----FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  93 GIavasktynLKKGQTHTL--EDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQAAYSA 170
Cdd:cd05331  77 GV--------LRPGATDPLstEDWEQTFAVNVTGVFNLLQAVAPHM----KDRRT--GAIVTVASNAAHVPRISMAAYGA 142

                       170       180
                ....*....|....*....|.
gi 83715985 171 SKGGIVGMTLPIARDLAPIGL 191
Cdd:cd05331 143 SKAALASLSKCLGLELAPYGV 163
PRK08267 PRK08267
SDR family oxidoreductase;
15-204 1.19e-21

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 90.38  E-value: 1.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   15 ITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN-NCVFAPADVTSEKDVQTALA-LAKGKFGRVDVAVNCA 92
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAgNAWTGALDVTDRAAWDAALAdFAAATGGRLDVLFNNA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   93 GIavasktynLKKG--QTHTLEDFQRVLDVNLMGTFNVI-------RLVAGemgqnepdqggqrGVIINTASVAAFEGQV 163
Cdd:PRK08267  86 GI--------LRGGpfEDIPLEAHDRVIDINVKGVLNGAhaalpylKATPG-------------ARVINTSSASAIYGQP 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 83715985  164 GQAAYSASKGGIVGMT--LPI--------ARDLAPiGLFGTPLLTSLPEKV 204
Cdd:PRK08267 145 GLAVYSATKFAVRGLTeaLDLewrrhgirVADVMP-LFVDTAMLDGTSNEV 194
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-191 1.22e-21

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: 90.67  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   1 MAAACRsVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN----CVFAPADVTSEKDVQTALA 76
Cdd:cd08933   1 MASGLR-YADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAgpgsCKFVPCDVTKEEDIKTLIS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  77 LAKGKFGRVDVAVNCAGIAVASKTYNlkkgqTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqRGVIINTASV 156
Cdd:cd08933  80 VTVERFGRIDCLVNNAGWHPPHQTTD-----ETSAQEFRDLLNLNLISYFLASKYALPHLRKS-------QGNIINLSSL 147

                       170       180       190
                ....*....|....*....|....*....|....*
gi 83715985 157 AAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd08933 148 VGSIGQKQAAPYVATKGAITAMTKALAVDESRYGV 182
PRK05717 PRK05717
SDR family oxidoreductase;
10-188 1.95e-21

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 89.95  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   90 NCAGIAvasKTYNLKKgQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnePDQGGQRGVIINTASVAAFEGQVGQAAYS 169
Cdd:PRK05717  90 CNAAIA---DPHNTTL-ESLSLAHWNRVLAVNLTGPMLLAKHCA-------PYLRAHNGAIVNLASTRARQSEPDTEAYA 158

                        170
                 ....*....|....*....
gi 83715985  170 ASKGGIVGMTLPIARDLAP 188
Cdd:PRK05717 159 ASKGGLLALTHALAISLGP 177
PRK08628 PRK08628
SDR family oxidoreductase;
9-190 2.10e-21

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 89.63  E-value: 2.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE--AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK08628   6 KDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEfaEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIavasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVagemgqnEPDQGGQRGVIINTASVAAFEGQVGQA 166
Cdd:PRK08628  86 GLVNNAGV-------NDGVGLEAGREAFVASLERNLIHYYVMAHYC-------LPHLKASRGAIVNISSKTALTGQGGTS 151

                        170       180
                 ....*....|....*....|....
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK08628 152 GYAAAKGAQLALTREWAVALAKDG 175
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 7-191 2.27e-21

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 89.47  E-value: 2.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNS-GGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAApLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFGRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqGGQRgvIINTASVAAFEGQVGQ 165
Cdd:PRK12828  84 DALVNIAGAFVWGTIADG------DADTWDRMYGVNVKTTLNASKAALPALTAS----GGGR--IVNIGAGAALKAGPGM 151

                        170       180
                 ....*....|....*....|....*.
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK12828 152 GAYAAAKAGVARLTEALAAELLDRGI 177
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 7-191 2.88e-21

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 89.96  E-value: 2.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK08277   7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIkaaGGEALAVKADVLDKESLEQARQQILEDFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAG------IAVASKTYNLKKGQTH---TLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTA 154
Cdd:PRK08277  87 PCDILINGAGgnhpkaTTDNEFHELIEPTKTFfdlDEEGFEFVFDLNLLGTLLPTQVFAKDM------VGRKGGNIINIS 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 83715985  155 SVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK08277 161 SMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGI 197
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 10-179 3.42e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 89.29  E-value: 3.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSG-GEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEkGEAQAaelEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEM-GQNEPdqggqrGVIINTASVAAFEGQVG 164
Cdd:PRK06198  86 DALVNAAGLTDRGTILDT------SPELFDRHFAVNVRAPFFLMQEAIKLMrRRKAE------GTIVNIGSMSAHGGQPF 153

                        170
                 ....*....|....*
gi 83715985  165 QAAYSASKGGIVGMT 179
Cdd:PRK06198 154 LAAYCASKGALATLT 168
PRK06194 PRK06194
hypothetical protein; Provisional
 9-190 4.00e-21

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 89.69  E-value: 4.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLD-LPNSGGEAQA--KKLGNNCVFAPADVTSEKDVQtALALA-KGKFGR 84
Cdd:PRK06194   5 AGKVAVITGAASGFGLAFARIGAALGMKLVLADvQQDALDRAVAelRAQGAEVLGVRTDVSDAAQVE-ALADAaLERFGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYNlkkgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEM-GQNEPDQGgQRGVIINTASVAAFEGQV 163
Cdd:PRK06194  84 VHLLFNNAGVGAGGLVWE------NSLADWEWVLGVNLWGVIHGVRAFTPLMlAAAEKDPA-YEGHIVNTASMAGLLAPP 156

                        170       180
                 ....*....|....*....|....*..
gi 83715985  164 GQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK06194 157 AMGIYNVSKHAVVSLTETLYQDLSLVT 183
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 9-188 5.34e-21

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: 88.56  E-value: 5.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05348   3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAvaskTYNLKKGQT--HTLED-FQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqrGVIINTASVAAFEGQVGQ 165
Cdd:cd05348  83 IGNAGIW----DYSTSLVDIpeEKLDEaFDELFHINVKGYILGAKAALPALYATE-------GSVIFTVSNAGFYPGGGG 151

                       170       180
                ....*....|....*....|...
gi 83715985 166 AAYSASKGGIVGMTLPIARDLAP 188
Cdd:cd05348 152 PLYTASKHAVVGLVKQLAYELAP 174
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 9-188 5.68e-21

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 88.86  E-value: 5.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK06200   5 HGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAvaskTYNLKkgqthtLED---------FQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqRGVIINTASVAAF 159
Cdd:PRK06200  85 VGNAGIW----DYNTS------LVDipaetldtaFDEIFNVNVKGYLLGAKAALPALKAS-------GGSMIFTLSNSSF 147

                        170       180
                 ....*....|....*....|....*....
gi 83715985  160 EGQVGQAAYSASKGGIVGMTLPIARDLAP 188
Cdd:PRK06200 148 YPGGGGPLYTASKHAVVGLVRQLAYELAP 176
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-248 6.49e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 88.58  E-value: 6.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPN---SGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQelvDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIavasktynLKKGQTH--TLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQrGVIINTASVAAFEG 161
Cdd:PRK07097  87 VIDILVNNAGI--------IKRIPMLemSAEDFRQVIDIDLNAPFIVSKAVIPSMIKK-----GH-GKIINICSMMSELG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  162 QVGQAAYSASKGGIVGMTLPIARDLA----------PiGLFGTPLLTSLPEKVC--------NFLASQVPfPSRLGDPAE 223
Cdd:PRK07097 153 RETVSAYAAAKGGLKMLTKNIASEYGeaniqcngigP-GYIATPQTAPLRELQAdgsrhpfdQFIIAKTP-AARWGDPED 230

                        250       260
                 ....*....|....*....|....*..
gi 83715985  224 YA--HLVQAIIENPFLNGEVIRLDGAI 248
Cdd:PRK07097 231 LAgpAVFLASDASNFVNGHILYVDGGI 257
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 9-187 1.48e-20

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 87.52  E-value: 1.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAK----KLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADeinaEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFnvirLVAGEMGQNEPDQGGQRGVI-INTASvaafeGQV 163
Cdd:cd05322  81 VDLLVYSAGIAKSAKITDFE------LGDFDRSLQVNLVGYF----LCAREFSKLMIRDGIQGRIIqINSKS-----GKV 145

                       170       180
                ....*....|....*....|....*..
gi 83715985 164 G---QAAYSASKGGIVGMTLPIARDLA 187
Cdd:cd05322 146 GskhNSGYSAAKFGGVGLTQSLALDLA 172
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 12-191 1.61e-20

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: 87.24  E-value: 1.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAaaiQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05365  81 VNNAGGGGPK-----PFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKA------GGGAILNISSMSSENKNVRIAAY 149

                       170       180
                ....*....|....*....|...
gi 83715985 169 SASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd05365 150 GSSKAAVNHMTRNLAFDLGPKGI 172
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 9-246 3.62e-20

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: 86.23  E-value: 3.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELtnlyKNRVIALELDITSKESIKELIESYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAV---ASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASV----- 156
Cdd:cd08930  81 IDILINNAYPSPkvwGSRFEEF------PYEQWNEVLNVNLGGAFLCSQAFIKLFKKQ------GKGSIINIASIygvia 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 157 AAFE-----GQVGQAAYSASKGGIVGMTLPIARDLAPIG-----LFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAH 226
Cdd:cd08930 149 PDFRiyentQMYSPVEYSVIKAGIIHLTKYLAKYYADTGirvnaISPGGILNNQPSEFLEKYTKKCPL-KRMLNPEDLRG 227

                       250       260
                ....*....|....*....|....*
gi 83715985 227 lvqAII-----ENPFLNGEVIRLDG 246
Cdd:cd08930 228 ---AIIfllsdASSYVTGQNLVIDG 249
PRK12743 PRK12743
SDR family oxidoreductase;
12-191 5.54e-20

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 85.86  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGAS-AVLLDLPNSGGEAQAKK---LGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK12743   4 VAIVTASDSGIGKACALLLAQQGFDiGITWHSDEEGAKETAEEvrsHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRIDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepDQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:PRK12743  84 LVNNAGAMTKAPFLDM------DFDEWRKIFTVDVDGAFLCSQIAARHM-----VKQGQGGRIINITSVHEHTPLPGASA 152

                        170       180
                 ....*....|....*....|....
gi 83715985  168 YSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK12743 153 YTAAKHALGGLTKAMALELVEHGI 176
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 7-191 8.19e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 85.15  E-value: 8.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGnnCVFAPADVTSEkdvqTALALAKGKFGRVD 86
Cdd:PRK07060   6 DFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETG--CEPLRLDVGDD----AAIRAALAAAGAFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqGGQRGVIINTASVAAFEGQVGQA 166
Cdd:PRK07060  80 GLVNCAGIAS------LESALDMTAEGFDRVMAVNARGAALVARHVARAMIA-----AGRGGSIVNVSSQAALVGLPDHL 148

                        170       180
                 ....*....|....*....|....*
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK07060 149 AYCASKAALDAITRVLCVELGPHGI 173
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 13-191 8.32e-20

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: 84.87  E-value: 8.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCA 92
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  93 GIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnEPDQGGQRGVIINTASVAAFEGQVGQAAYSASK 172
Cdd:cd08929  83 GVGV------MKPVEELTPEEWRLVLDTNLTGAFYCIHKAA------PALLRRGGGTIVNVGSLAGKNAFKGGAAYNASK 150

                       170
                ....*....|....*....
gi 83715985 173 GGIVGMTLPIARDLAPIGL 191
Cdd:cd08929 151 FGLLGLSEAAMLDLREANI 169
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 10-191 1.48e-19

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 84.90  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA---KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGiAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqGGqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK06113  91 ILVNNAG-GGGPKPFDMP------MADFRRAYELNVFSFFHLSQLVAPEMEKN----GG--GVILTITSMAAENKNINMT 157

                        170       180
                 ....*....|....*....|....*
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK06113 158 SYASSKAAASHLVRNMAFDLGEKNI 182
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 12-172 2.93e-19

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 86.51  E-value: 2.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN-----CVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:COG3347 427 VALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGygadaVDATDVDVTAEAAVAAAFGFAGLDIGGSD 506

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGQRGVIINTASVAAFEGQVGQA 166
Cdd:COG3347 507 IGVANAGIASSSPE------EETRLSFWLNNFAHLSTGQFLVARAAFQGTGG----QGLGGSSVFAVSKNAAAAAYGAAA 576


                ....*.
gi 83715985 167 AYSASK 172
Cdd:COG3347 577 AATAKA 582
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-245 4.92e-19

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 83.23  E-value: 4.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQ-----AKKLGNNCVFAPADVTSEKDVQTALALAKGK 81
Cdd:PRK06077   3 SLKDKVVVVTGSGRGIGRAIAVRLAKEGSL-VVVNAKKRAEEMNetlkmVKENGGEGIGVLADVSTREGCETLAKATIDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   82 FGRVDVAVNCAGIAVASKTYNLkkgqthtlED--FQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAF 159
Cdd:PRK06077  82 YGVADILVNNAGLGLFSPFLNV--------DDklIDKHISTDFKSVIYCSQELAKEMREG--------GAIVNIASVAGI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  160 EGQVGQAAYSASKGGIVGMTLPIARDLAP--------IGLFGTPLLTSLPeKVCNF----LASQVPFPSRLGDPAEYAHL 227
Cdd:PRK06077 146 RPAYGLSIYGAMKAAVINLTKYLALELAPkirvnaiaPGFVKTKLGESLF-KVLGMsekeFAEKFTLMGKILDPEEVAEF 224

                        250
                 ....*....|....*...
gi 83715985  228 VQAIIENPFLNGEVIRLD 245
Cdd:PRK06077 225 VAAILKIESITGQVFVLD 242
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-191 8.41e-19

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 82.52  E-value: 8.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLdlpNSGGEAQAKKLGNNCVFA-PADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK06463   6 KGKVALITGGTRGIGRAIAEAFLREGAKVAVL---YNSAENEAKELREKGVFTiKCDVGNRDQVKKSKEVVEKEFGRVDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIavasktYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAfegqVGQAA 167
Cdd:PRK06463  83 LVNNAGI------MYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSK------NGAIVNIASNAG----IGTAA 146

                        170       180
                 ....*....|....*....|....*....
gi 83715985  168 -----YSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK06463 147 egttfYAITKAGIIILTRRLAFELGKYGI 175
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-228 1.62e-18

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 82.06  E-value: 1.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQ--AKKLGNNCVFAPADVTSEKDVQTALALAKGKFGR-VDVA 88
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGAR-VVVNYHQSEDAAEalADELGDRAIALQADVTDREQVQAMFATATEHFGKpITTV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:PRK08642  86 VNNALADFSFDGDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGM------REQGFGRIINIGTNLFQNPVVPYHDY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  169 SASKGGIVGMTLPIARDLAPIG----------LFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLV 228
Cdd:PRK08642 160 TTAKAALLGLTRNLAAELGPYGitvnmvsgglLRTTDASAATPDEVFDLIAATTPL-RKVTTPQEFADAV 228
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 9-191 1.81e-18

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: 81.69  E-value: 1.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL------GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd05364   2 SGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSClqagvsEKKILLVVADLTEEEGQDRIISTTLAKF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  83 GRVDVAVNCAGIAVASktynlkKGQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnePDQGGQRGVIINTASVAAFEGQ 162
Cdd:cd05364  82 GRLDILVNNAGILAKG------GGEDQDIEEYDKVMNLNLRAVIYLTKLAV-------PHLIKTKGEIVNVSSVAGGRSF 148

                       170       180
                ....*....|....*....|....*....
gi 83715985 163 VGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd05364 149 PGVLYYCISKAALDQFTRCTALELAPKGV 177
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 12-247 2.24e-18

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: 81.17  E-value: 2.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGAsAVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAAEGY-RVVVHYNRSEAEAQRlkdelNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVASKTynlkkGQThTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnepdqGGQRGVIINTASVAAFEGQVGQA 166
Cdd:cd05357  81 VLVNNASAFYPTPL-----GQG-SEDAWAELFGINLKAPYLLIQAFARRLA------GSRNGSIINIIDAMTDRPLTGYF 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 167 AYSASKGGIVGMTLPIARDLAP------IGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQAIIENPFLNGE 240
Cdd:cd05357 149 AYCMSKAALEGLTRSAALELAPnirvngIAPGLILLPEDMDAEYRENALRKVPL-KRRPSAEEIADAVIFLLDSNYITGQ 227


                ....*..
gi 83715985 241 VIRLDGA 247
Cdd:cd05357 228 IIKVDGG 234
PRK05855 PRK05855
SDR family oxidoreductase;
6-172 3.95e-18

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 83.11  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPA---DVTSEKDVQTALALAKGKF 82
Cdd:PRK05855 311 GPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAyrvDVSDADAMEAFAEWVRAEH 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAVAsktynlkkGQ--THTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFE 160
Cdd:PRK05855 391 GVPDIVVNNAGIGMA--------GGflDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVER-----GTGGHIVNVASAAAYA 457

                        170
                 ....*....|..
gi 83715985  161 GQVGQAAYSASK 172
Cdd:PRK05855 458 PSRSLPAYATSK 469
PRK07454 PRK07454
SDR family oxidoreductase;
13-179 7.82e-18

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 79.62  E-value: 7.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   13 AVITGGASGLGLATAERLVGQGASAVLL-----DLPNSGGEAQAKklGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLALVarsqdALEALAAELRST--GVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIAvasKTYNLkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAA 167
Cdd:PRK07454  87 LINNAGMA---YTGPL---LEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRAR------GGGLIINVSSIAARNAFPQWGA 154

                        170
                 ....*....|..
gi 83715985  168 YSASKGGIVGMT 179
Cdd:PRK07454 155 YCVSKAALAAFT 166
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 10-190 9.31e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 80.49  E-value: 9.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDL-------PNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALAL 77
Cdd:PRK07791   6 GRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsASGGSAAQAvvdeiVAAGGEAVANGDDIADWDGAANLVDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   78 AKGKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLvAGEMGQNEPDQGGQR-GVIINTASV 156
Cdd:PRK07791  86 AVETFGGLDVLVNNAGILRDRMIANM------SEEEWDAVIAVHLKGHFATLRH-AAAYWRAESKAGRAVdARIINTSSG 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 83715985  157 AAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK07791 159 AGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYG 192
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-246 1.24e-17

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: 79.41  E-value: 1.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKF- 82
Cdd:cd05329   3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWrekGFKVEGSVCDVSSRSERQELMDTVASHFg 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  83 GRVDVAVNCAGIAVAsktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQ 162
Cdd:cd05329  83 GKLNILVNNAGTNIR------KEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAS------GNGNIVFISSVAGVIAV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 163 VGQAAYSASKGGIVGMTLPIARD----------LAPiGLFGTPLLTSL---PEKVCNFLaSQVPFpSRLGDPAEYAHLVq 229
Cdd:cd05329 151 PSGAPYGATKGALNQLTRSLACEwakdnirvnaVAP-WVIATPLVEPViqqKENLDKVI-ERTPL-KRFGEPEEVAALV- 226

                       250       260
                ....*....|....*....|
gi 83715985 230 AIIENP---FLNGEVIRLDG 246
Cdd:cd05329 227 AFLCMPaasYITGQIIAVDG 246
PRK07035 PRK07035
SDR family oxidoreductase;
7-246 2.76e-17

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 78.52  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL----GNNCVFApADVTSEKDVQTALALAKGKF 82
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIvaagGKAEALA-CHIGEMEQIDALFAHIRERH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAgiavASKTYnlkkgQTHTLED----FQRVLDVNLMGTFNVIRLVAGEMGqnepDQGGqrGVIINTASVAA 158
Cdd:PRK07035  84 GRLDILVNNA----AANPY-----FGHILDTdlgaFQKTVDVNIRGYFFMSVEAGKLMK----EQGG--GSIVNVASVNG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  159 FEGQVGQAAYSASKGGIVGMTLPIARDLAPIGLFGTPLLTSLP-----------EKVCNFLASQVPFpSRLGDPAEYAHL 227
Cdd:PRK07035 149 VSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTdtkfasalfknDAILKQALAHIPL-RRHAEPSEMAGA 227

                        250       260
                 ....*....|....*....|.
gi 83715985  228 VQAIIEN--PFLNGEVIRLDG 246
Cdd:PRK07035 228 VLYLASDasSYTTGECLNVDG 248
PRK06128 PRK06128
SDR family oxidoreductase;
10-246 2.77e-17

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 79.13  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEvvqliQAEGRKAVALPGDLKDEAFCRQLVERAVKELGG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQVG 164
Cdd:PRK06128 135 LDILVNIAGKQTAVKDI-----ADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG--------ASIINTGSIQSYQPSPT 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTS---LPEKVCNFlASQVPFpSRLGDPAEYA--HLVQA 230
Cdd:PRK06128 202 LLDYASTKAAIVAFTKALAKQVAEKGIrvnavapgpVWTPLQPSggqPPEKIPDF-GSETPM-KRPGQPVEMAplYVLLA 279

                        250
                 ....*....|....*.
gi 83715985  231 IIENPFLNGEVIRLDG 246
Cdd:PRK06128 280 SQESSYVTGEVFGVTG 295
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 10-250 2.87e-17

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 78.42  E-value: 2.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:PRK12936   6 GRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   90 NCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYS 169
Cdd:PRK12936  86 NNAGITKDGLFVRMSD------EDWDSVLEVNLTATFRLTRELTHPMMRR------RYGRIINITSVVGVTGNPGQANYC 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  170 ASKGGIVGMTLPIARDLA---------PIGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAEYAHLVQ--AIIENPFLN 238
Cdd:PRK12936 154 ASKAGMIGFSKSLAQEIAtrnvtvncvAPGFIESAMTGKLNDKQKEAIMGAIPM-KRMGTGAEVASAVAylASSEAAYVT 232

                        250
                 ....*....|..
gi 83715985  239 GEVIRLDGAIRM 250
Cdd:PRK12936 233 GQTIHVNGGMAM 244
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 10-179 3.81e-17

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: 77.96  E-value: 3.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:cd08934   3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDEQQVDAAVERTVEALGRLD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQA 166
Cdd:cd08934  83 ILVNNAGIML------LGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLR------NKGTIVNISSVAGRVAVRNSA 150

                       170
                ....*....|...
gi 83715985 167 AYSASKGGIVGMT 179
Cdd:cd08934 151 VYNATKFGVNAFS 163
PRK06947 PRK06947
SDR family oxidoreductase;
12-191 5.08e-17

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 77.54  E-value: 5.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAeRLVGQGASAVLLdlpNSGGEAQAKKL---------GNNCVFApADVTSEKDVQTALALAKGKF 82
Cdd:PRK06947   4 VVLITGASRGIGRATA-VLAAARGWSVGI---NYARDAAAAEEtadavraagGRACVVA-GDVANEADVIAMFDAVQSAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepDQGGQRGVIINTASVAAFEGQ 162
Cdd:PRK06947  79 GRLDALVNNAGIVAPSMPL-----ADMDAARLRRMFDTNVLGAYLCAREAARRLST---DRGGRGGAIVNVSSIASRLGS 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 83715985  163 VGQ-AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK06947 151 PNEyVDYAGSKGAVDTLTLGLAKELGPHGV 180
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 12-183 8.15e-17

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 76.94  E-value: 8.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL----GNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARSEEPLQELKEelrpGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAvasktYNLKKGQTHTLEDFQRVLDVNLmgtFNVIRLVAGEMgqNEPDQGGQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05367  81 LINNAGSL-----GPVSKIEFIDLDELQKYFDLNL---TSPVCLTSTLL--RAFKKRGLKKTVVNVSSGAAVNPFKGWGL 150

                       170
                ....*....|....*.
gi 83715985 168 YSASKGGIVGMTLPIA 183
Cdd:cd05367 151 YCSSKAARDMFFRVLA 166
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 12-187 1.17e-16

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: 76.12  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSG-GEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLAKSGPGTVILTARDVErGQAAVEKLraeGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAvasktYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRlvagEMgqNEPDQGGQRGVIINTASVAAfegqVGQAA 167
Cdd:cd05324  82 LVNNAGIA-----FKGFDDSTPTREQARETMKTNFFGTVDVTQ----AL--LPLLKKSPAGRIVNVSSGLG----SLTSA 146

                       170       180
                ....*....|....*....|
gi 83715985 168 YSASKGGIVGMTLPIARDLA 187
Cdd:cd05324 147 YGVSKAALNALTRILAKELK 166
PRK06124 PRK06124
SDR family oxidoreductase;
7-246 1.29e-16

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 76.68  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASaVLL-------------DLPNSGGEAQAkklgnncvfAPADVTSEKDVQT 73
Cdd:PRK06124   8 SLAGQVALVTGSARGLGFEIARALAGAGAH-VLVngrnaatleaavaALRAAGGAAEA---------LAFDIADEEAVAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   74 ALALAKGKFGRVDVAVNCAGiavaskTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGQRgvIINT 153
Cdd:PRK06124  78 AFARIDAEHGRLDILVNNVG------ARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKR----QGYGR--IIAI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  154 ASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSLP--EKVCNFLASQVPFpSRLGDPA 222
Cdd:PRK06124 146 TSIAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGItsnaiapgyFATETNAAMAadPAVGPWLAQRTPL-GRWGRPE 224

                        250       260
                 ....*....|....*....|....*.
gi 83715985  223 EYAH--LVQAIIENPFLNGEVIRLDG 246
Cdd:PRK06124 225 EIAGaaVFLASPAASYVNGHVLAVDG 250
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 1-248 2.12e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 75.96  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    1 MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLldlpN-------SGGEAQAKKLGNNCVFAPADVTSEKDVQT 73
Cdd:PRK07523   1 MSLNLFDLTGRRALVTGSSQGIGYALAEGLAQAGAEVIL----NgrdpaklAAAAESLKGQGLSAHALAFDVTDHDAVRA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   74 ALALAKGKFGRVDVAVNCAGIAVASKtynlkkgqthtLEDF-----QRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRG 148
Cdd:PRK07523  77 AIDAFEAEIGPIDILVNNAGMQFRTP-----------LEDFpadafERLLRTNISSVFYVGQAVARHM------IARGAG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  149 VIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSL--PEKVCNFLASQVPfPSR 217
Cdd:PRK07523 140 KIINIASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLqcnaiapgyFDTPLNAALvaDPEFSAWLEKRTP-AGR 218

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 83715985  218 LGDPAEyahLVQAII-----ENPFLNGEVIRLDGAI 248
Cdd:PRK07523 219 WGKVEE---LVGACVflasdASSFVNGHVLYVDGGI 251
PRK07856 PRK07856
SDR family oxidoreductase;
9-188 2.54e-16

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 75.74  E-value: 2.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLdlpnsGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVVC-----GRRAPETVDGRPAEFHAADVRDPDQVAALVDAIVERHGRLDVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAG------IAVASKTYnlkkgqthtledFQRVLDVNLMGTFNVIRLVAGEMgQNEPDqggqRGVIINTASVAAFEGQ 162
Cdd:PRK07856  80 VNNAGgspyalAAEASPRF------------HEKIVELNLLAPLLVAQAANAVM-QQQPG----GGSIVNIGSVSGRRPS 142

                        170       180
                 ....*....|....*....|....*.
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAP 188
Cdd:PRK07856 143 PGTAAYGAAKAGLLNLTRSLAVEWAP 168
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 15-179 3.90e-16

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: 74.80  E-value: 3.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  15 ITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLG-NNCVFAPADVTSEKDVQTALA-LAKGKFGRVDVAVNCA 92
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGaENVVAGALDVTDRAAWAAALAdFAAATGGRLDALFNNA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  93 GIavasktynLKKGQTHT--LEDFQRVLDVNLMGTFNVIRlVAGEMGQNEPdqGGQrgvIINTASVAAFEGQVGQAAYSA 170
Cdd:cd08931  85 GV--------GRGGPFEDvpLAAHDRMVDINVKGVLNGAY-AALPYLKATP--GAR---VINTASSSAIYGQPDLAVYSA 150


                ....*....
gi 83715985 171 SKGGIVGMT 179
Cdd:cd08931 151 TKFAVRGLT 159
PRK06949 PRK06949
SDR family oxidoreductase;
10-183 4.49e-16

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 75.18  E-value: 4.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVL------------LDLPNSGGEAQAKKLgnncvfapaDVTSEKDVQTALAL 77
Cdd:PRK06949   9 GKVALVTGASSGLGARFAQVLAQAGAKVVLasrrverlkelrAEIEAEGGAAHVVSL---------DVTDYQSIKAAVAH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   78 AKGKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEM---GQNEPDQGGQrGVIINTA 154
Cdd:PRK06949  80 AETEAGTIDILVNNSGVSTTQKLVDV------TPADFDFVFDTNTRGAFFVAQEVAKRMiarAKGAGNTKPG-GRIINIA 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 83715985  155 SVAAFE--GQVGqaAYSASKGGIVGMTLPIA 183
Cdd:PRK06949 153 SVAGLRvlPQIG--LYCMSKAAVVHMTRAMA 181
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 13-188 7.60e-16

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: 74.62  E-value: 7.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN----CVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKfpvkVLPLQLDVSDRESIEAALENLPEEFRDIDIL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVAsktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05346  83 VNNAGLALG-----LDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARN------QGHIINLGSIAGRYPYAGGNVY 151

                       170       180
                ....*....|....*....|
gi 83715985 169 SASKGGIVGMTLPIARDLAP 188
Cdd:cd05346 152 CATKAAVRQFSLNLRKDLIG 171
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 12-242 7.98e-16

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: 73.94  E-value: 7.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFaPADVTSEKDVQTALALAKGKFGRVDVAVNC 91
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGDVEAV-PYDARDPEDARALVDALRDRFGRIDVLVHN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  92 AGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:cd08932  81 AGIGRPTTLREG------SDAELEAHFSINVIAPAELTRALLPAL------REAGSGRVVFLNSLSGKRVLAGNAGYSAS 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 172 KGGIVGMTLPIARDLAPIGL---------FGTPLLTSLPEkvcnflaSQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVI 242
Cdd:cd08932 149 KFALRALAHALRQEGWDHGVrvsavcpgfVDTPMAQGLTL-------VGAFPPEEMIQPKDIANLVRMVIELPENITSVA 221
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 15-175 1.24e-15

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: 73.66  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  15 ITGGASGLGLATAERLVGQGA-------SAVLLDlpnsggeaQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:COG3967  10 ITGGTSGIGLALAKRLHARGNtviitgrREEKLE--------EAAAANPGLHTIVLDVADPASIAALAEQVTAEFPDLNV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIavaSKTYNLKKGQTHtLEDFQRVLDVNLMGTfnvIRLVAG--EMGQNEPDqggqrGVIINTASVAAFEGQVGQ 165
Cdd:COG3967  82 LINNAGI---MRAEDLLDEAED-LADAEREITTNLLGP---IRLTAAflPHLKAQPE-----AAIVNVSSGLAFVPLAVT 149

                       170
                ....*....|
gi 83715985 166 AAYSASKGGI 175
Cdd:COG3967 150 PTYSATKAAL 159
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 9-190 1.40e-15

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 73.83  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE--AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEvaAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAfeGQVGQA 166
Cdd:PRK12823  87 VLINNVGGTIWAKPF-----EEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQ------GGGAIVNVSSIAT--RGINRV 153

                        170       180
                 ....*....|....*....|....
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK12823 154 PYSAAKGGVNALTASLAFEYAEHG 177
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 12-179 1.48e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 74.17  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVlldlpnSGGEAQAKKLGNNCV-FAPADVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLARAGYRVF------GTSRNPARAAPIPGVeLLELDVTDDASVQAAVDEVIARAGRIDVLVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   91 CAGIAVASKTYNLKKGQThtledfQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGQRgvIINTASVAAFEGQVGQAAYSA 170
Cdd:PRK06179  80 NAGVGLAGAAEESSIAQA------QALFDTNVFGILRMTRAVLPHMRA----QGSGR--IINISSVLGFLPAPYMALYAA 147


                 ....*....
gi 83715985  171 SKGGIVGMT 179
Cdd:PRK06179 148 SKHAVEGYS 156
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 9-191 1.73e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 73.43  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVL-------LD-----LPNSGGEAqakklgnncVFAPADVTSEKDVQTALA 76
Cdd:PRK07478   5 NGKVAIITGASSGIGRAAAKLFAREGAKVVVgarrqaeLDqlvaeIRAEGGEA---------VALAGDVRDEAYAKALVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   77 LAKGKFGRVDVAVNCAGIavaskTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTAS- 155
Cdd:PRK07478  76 LAVERFGGLDIAFNNAGT-----LGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLA----RGG--GSLIFTSTf 144

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 83715985  156 VAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK07478 145 VGHTAGFPGMAAYAASKAGLIGLTQVLAAEYGAQGI 180
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 12-170 3.44e-15

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: 74.33  E-value: 3.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLL---------DLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:cd08953 207 VYLVTGGAGGIGRALARALARRYGARLVLlgrsplppeEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERY 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  83 GRVDVAVNCAGIaVASKTYNLKkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEmgqnEPDQggqrgvIINTASVAAFEGQ 162
Cdd:cd08953 287 GAIDGVIHAAGV-LRDALLAQK-----TAEDFEAVLAPKVDGLLNLAQALADE----PLDF------FVLFSSVSAFFGG 350


                ....*...
gi 83715985 163 VGQAAYSA 170
Cdd:cd08953 351 AGQADYAA 358
PRK07201 PRK07201
SDR family oxidoreductase;
8-235 3.55e-15

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 74.60  E-value: 3.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLL-----DLPNSGGEAQAKKlGNNCVFaPADVTSEKDVQTALALAKGKF 82
Cdd:PRK07201 369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVarngeALDELVAEIRAKG-GTAHAY-TCDLTDSAAVDHTVKDILAEH 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAVASKTYNlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQ 162
Cdd:PRK07201 447 GHVDYLVNNAGRSIRRSVEN----STDRFHDYERTMAVNYFGAVRLILGLLPHMRER------RFGHVVNVSSIGVQTNA 516

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAPIG---------LFGTPLLTslPEKVCNflasQVPFPSrlgdPAEYAHLV-QAII 232
Cdd:PRK07201 517 PRFSAYVASKAALDAFSDVAASETLSDGitfttihmpLVRTPMIA--PTKRYN----NVPTIS----PEEAADMVvRAIV 586


                 ...
gi 83715985  233 ENP 235
Cdd:PRK07201 587 EKP 589
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-190 4.55e-15

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 74.10  E-value: 4.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQ--AKKLGNNCVfaPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK08261 206 RPLAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGEALAavANRVGGTAL--ALDITAPDAPARIAEHLAERHG 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAVASKTYNLKKGQthtledFQRVLDVNLMGTFNVIR--LVAGEMGQNepdqggqrGVIINTASVAAFEG 161
Cdd:PRK08261 284 GLDIVVHNAGITRDKTLANMDEAR------WDSVLAVNLLAPLRITEalLAAGALGDG--------GRIVGVSSISGIAG 349

                        170       180
                 ....*....|....*....|....*....
gi 83715985  162 QVGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK08261 350 NRGQTNYAASKAGVIGLVQALAPLLAERG 378
PRK06139 PRK06139
SDR family oxidoreductase;
6-188 4.57e-15

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 73.22  E-value: 4.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLldlPNSGGEA------QAKKLGNNCVFAPADVTSEKDVQtALALAK 79
Cdd:PRK06139   3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVL---AARDEEAlqavaeECRALGAEVLVVPTDVTDADQVK-ALATQA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   80 GKF-GRVDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqneP---DQGgqRGVIINTAS 155
Cdd:PRK06139  79 ASFgGRIDVWVNNVGVGAVGRF------EETPIEAHEQVIQTNLIGYMRDAHAAL-------PifkKQG--HGIFINMIS 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 83715985  156 VAAFEGQVGQAAYSASKGGIVGMTLPIARDLAP 188
Cdd:PRK06139 144 LGGFAAQPYAAAYSASKFGLRGFSEALRGELAD 176
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 7-249 4.58e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 72.48  E-value: 4.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK08085   6 SLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLrqeGIKAHAAPFNVTHKQEVEAAIEHIEKDIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAGIAvasktynlkkgQTHTL-----EDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAA 158
Cdd:PRK08085  86 PIDVLINNAGIQ-----------RRHPFtefpeQEWNDVIAVNQTAVFLVSQAVARYMVKR------QAGKIINICSMQS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  159 FEGQVGQAAYSASKGGIV----GMTLPIAR------DLAPiGLFGTPLLTSLPE--KVCNFLASQVPfPSRLGDPAEyah 226
Cdd:PRK08085 149 ELGRDTITPYAASKGAVKmltrGMCVELARhniqvnGIAP-GYFKTEMTKALVEdeAFTAWLCKRTP-AARWGDPQE--- 223

                        250       260
                 ....*....|....*....|....*...
gi 83715985  227 LVQAII-----ENPFLNGEVIRLDGAIR 249
Cdd:PRK08085 224 LIGAAVflsskASDFVNGHLLFVDGGML 251
PRK06123 PRK06123
SDR family oxidoreductase;
12-191 5.45e-15

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 72.12  E-value: 5.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAeRLVGQGASAVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK06123   4 VMIITGASRGIGAATA-LLAAERGYAVCLNYLRNRDAAEAvvqaiRRQGGEALAVAADVADEADVLRLFEAVDRELGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnePDQGGQRGVIINTASVAAFEGQVGQ- 165
Cdd:PRK06123  83 ALVNNAGILEAQ-----MRLEQMDAARLTRIFATNVVGSFLCAREAVKRMS---TRHGGRGGAIVNVSSMAARLGSPGEy 154

                        170       180
                 ....*....|....*....|....*.
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK06123 155 IDYAASKGAIDTMTIGLAKEVAAEGI 180
PRK07024 PRK07024
SDR family oxidoreductase;
11-176 6.03e-15

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 72.27  E-value: 6.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   11 LVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFA--PADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK07024   3 LKVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSvyAADVRDADALAAAAADFIAAHGLPDVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAVASKTynlkkGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:PRK07024  83 IANAGISVGTLT-----EEREDLAVFREVMDTNYFGMVATFQPFIAPM------RAARRGTLVGIASVAGVRGLPGAGAY 151


                 ....*...
gi 83715985  169 SASKGGIV 176
Cdd:PRK07024 152 SASKAAAI 159
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 10-191 6.03e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 72.30  E-value: 6.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLraeGFDVHGVMCDVRHREEVTHLADEAFRLLGHVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYNLkkgqTHtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQVGQA 166
Cdd:PRK05876  86 VVFSNAGIVVGGPIVEM----TH--DDWRWVIDVDLWGSIHTVEAFLPRLLEQ-----GTGGHVVFTASFAGLVPNAGLG 154

                        170       180
                 ....*....|....*....|....*
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK05876 155 AYGVAKYGVVGLAETLAREVTADGI 179
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 12-246 9.94e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 71.25  E-value: 9.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVLldlpnSG--GEA--QAKK----LGNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK07677   3 VVIITGGSSGMGKAMAKRFAEEGANVVI-----TGrtKEKleEAKLeieqFPGQVLTVQMDVRNPEDVQKMVEQIDEKFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   84 RVDVAVNCAG---IAVASKTynlkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFE 160
Cdd:PRK07677  78 RIDALINNAAgnfICPAEDL---------SVNGWNSVIDIVLNGTFYCSQAVGKYWIEK-----GIKGNIINMVATYAWD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  161 GQVGQAAYSASKGGIVGMTlpiaRDLA-----------------PIGLFGTPLLTSLPEKVCNFLASQVPFpSRLGDPAE 223
Cdd:PRK07677 144 AGPGVIHSAAAKAGVLAMT----RTLAvewgrkygirvnaiapgPIERTGGADKLWESEEAAKRTIQSVPL-GRLGTPEE 218

                        250       260
                 ....*....|....*....|....*
gi 83715985  224 YAHLVQAII--ENPFLNGEVIRLDG 246
Cdd:PRK07677 219 IAGLAYFLLsdEAAYINGTCITMDG 243
PRK09242 PRK09242
SDR family oxidoreductase;
7-246 1.58e-14

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 70.93  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLL-----DLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGK 81
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVardadALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   82 FGRVDVAVNCAGIAVAsktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAFEG 161
Cdd:PRK09242  86 WDGLHILVNNAGGNIR------KAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHA------SSAIVNIGSVSGLTH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  162 QVGQAAYSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSL---PEKVCNFLaSQVPFpSRLGDPAEYAHLVQ 229
Cdd:PRK09242 154 VRSGAPYGMTKAALLQMTRNLAVEWAEDGIrvnavapwyIRTPLTSGPlsdPDYYEQVI-ERTPM-RRVGEPEEVAAAVA 231

                        250
                 ....*....|....*....
gi 83715985  230 --AIIENPFLNGEVIRLDG 246
Cdd:PRK09242 232 flCMPAASYITGQCIAVDG 250
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 10-235 1.76e-14

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: 70.50  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLL-------------DLPNSGGEA--QAKKLGNNCVFAPADVTSEKDVQTA 74
Cdd:cd05338   3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAaktasegdngsakSLPGTIEETaeEIEAAGGQALPIVVDVRDEDQVRAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  75 LALAKGKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTA 154
Cdd:cd05338  83 VEATVDQFGRLDILVNNAGAIWLSLVEDT------PAKRFDLMQRVNLRGTYLLSQAALPHMVKA------GQGHILNIS 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 155 SVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGLFGTPL--LTSLPEKVCNFLASQVpFPSRLGDPAEYAHLVQAII 232
Cdd:cd05338 151 PPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLwpSTAIETPAATELSGGS-DPARARSPEILSDAVLAIL 229


                ...
gi 83715985 233 ENP 235
Cdd:cd05338 230 SRP 232
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 13-191 2.31e-14

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: 70.02  E-value: 2.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN---NCVFAPADVTSE-KDVQTALAlAKGKFGRVDVA 88
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGAshsRLHILELDVTDEiAESAEAVA-ERLGDAGLDVL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASKTynlkkGQTHTLEDFQRVLDVNLMGTFNVIRLVAgEMGQNepdqgGQRGVIINTASVAA---FEGQVGQ 165
Cdd:cd05325  80 INNAGILHSYGP-----ASEVDSEDLLEVFQVNVLGPLLLTQAFL-PLLLK-----GARAKIINISSRVGsigDNTSGGW 148

                       170       180
                ....*....|....*....|....*.
gi 83715985 166 AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd05325 149 YSYRASKAALNMLTKSLAVELKRDGI 174
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 13-190 3.76e-14

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: 69.67  E-value: 3.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDL---PNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARrtdRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  90 NCAGIavaSKTYNLKKGQthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGgqRGVIINTASVAAFEGQVGQAAYS 169
Cdd:cd05350  81 INAGV---GKGTSLGDLS---FKAFRETIDTNLLGAAAILEAALPQFRA----KG--RGHLVLISSVAALRGLPGAAAYS 148

                       170       180
                ....*....|....*....|.
gi 83715985 170 ASKGGIVGMTLPIARDLAPIG 190
Cdd:cd05350 149 ASKAALSSLAESLRYDVKKRG 169
PRK09072 PRK09072
SDR family oxidoreductase;
14-190 4.87e-14

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 69.59  E-value: 4.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   14 VITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFApADVTSEKDVQTALALAKgKFGRVDVAVN 90
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLpypGRHRWVV-ADLTSEAGREAVLARAR-EMGGINVLIN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   91 CAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYSA 170
Cdd:PRK09072  87 NAGVNHFALL------EDQDPEAIERLLALNLTAPMQLTRALLPLLRAQ------PSAMVVNVGSTFGSIGYPGYASYCA 154

                        170       180
                 ....*....|....*....|
gi 83715985  171 SKGGIVGMTLPIARDLAPIG 190
Cdd:PRK09072 155 SKFALRGFSEALRRELADTG 174
PRK06500 PRK06500
SDR family oxidoreductase;
9-246 5.60e-14

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 69.21  E-value: 5.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDvQTALALA-KGKFGRVDV 87
Cdd:PRK06500   5 QGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAA-QKALAQAlAEAFGRLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnePDQGGQRGVIINTaSVAAFEGQVGQAA 167
Cdd:PRK06500  84 VFINAGVAK------FAPLEDWDEAMFDRSFNTNVKGPYFLIQALL-------PLLANPASIVLNG-SINAHIGMPNSSV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  168 YSASKGGIVGMTLPIARDLAPIGL---------FGTPLLTSLP------EKVCNFLASQVPFpSRLGDPAEYAHLVQ--A 230
Cdd:PRK06500 150 YAASKAALLSLAKTLSGELLPRGIrvnavspgpVQTPLYGKLGlpeatlDAVAAQIQALVPL-GRFGTPEEIAKAVLylA 228

                        250
                 ....*....|....*.
gi 83715985  231 IIENPFLNGEVIRLDG 246
Cdd:PRK06500 229 SDESAFIVGSEIIVDG 244
PRK09135 PRK09135
pteridine reductase; Provisional
 12-246 5.88e-14

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 69.19  E-value: 5.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAK------GKFGRV 85
Cdd:PRK09135   8 VALITGGARRIGAAIARTLHAAGYR-VAIHYHRSAAEADALAAELNALRPGSAAALQADLLDPDALPElvaacvAAFGRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAgiavaSKTYNLKKGQTHTlEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqggQRGVIINTASVAAFEGQVGQ 165
Cdd:PRK09135  87 DALVNNA-----SSFYPTPLGSITE-AQWDDLFASNLKAPFFLSQAAAPQLRK-------QRGAIVNITDIHAERPLKGY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPI----GLFGTPLLtsLPEKVCNF-------LASQVPFpSRLGDPAEYAHLVQ-AIIE 233
Cdd:PRK09135 154 PVYCAAKAALEMLTRSLALELAPEvrvnAVAPGAIL--WPEDGNSFdeearqaILARTPL-KRIGTPEDIAEAVRfLLAD 230

                        250
                 ....*....|...
gi 83715985  234 NPFLNGEVIRLDG 246
Cdd:PRK09135 231 ASFITGQILAVDG 243
PRK09186 PRK09186
flagellin modification protein A; Provisional
 7-179 6.14e-14

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 69.25  E-value: 6.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN------CVFApADVTSEKDVQTALALAKG 80
Cdd:PRK09186   1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEfkskklSLVE-LDITDQESLEEFLSKSAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   81 KFGRVDVAVNCAgiAVASKTYNlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTAS---VA 157
Cdd:PRK09186  80 KYGKIDGAVNCA--YPRNKDYG-KKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKK----QGG--GNLVNISSiygVV 150

                        170       180
                 ....*....|....*....|....*....
gi 83715985  158 A--FEGQVGQA-----AYSASKGGIVGMT 179
Cdd:PRK09186 151 ApkFEIYEGTSmtspvEYAAIKAGIIHLT 179
PRK12744 PRK12744
SDR family oxidoreductase;
7-172 9.65e-14

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 68.61  E-value: 9.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA-------KKLGNNCVFAPADVTSEKDVQTALALAK 79
Cdd:PRK12744   5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAeetvaavKAAGAKAVAFQADLTTAAAVEKLFDDAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   80 GKFGRVDVAVNCAGIAvasktynLKKGQTHTLE-DFQRVLDVNLMGTFNVIRlvagEMGQNEPDQGgqRGVIINTASVAA 158
Cdd:PRK12744  85 AAFGRPDIAINTVGKV-------LKKPIVEISEaEYDEMFAVNSKSAFFFIK----EAGRHLNDNG--KIVTLVTSLLGA 151

                        170
                 ....*....|....
gi 83715985  159 FEGqvGQAAYSASK 172
Cdd:PRK12744 152 FTP--FYSAYAGSK 163
PRK05867 PRK05867
SDR family oxidoreductase;
8-247 9.70e-14

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 68.91  E-value: 9.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIgtsGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFnvirLVAGEMGQNEPDQgGQRGVIINTASVAAFEGQVG 164
Cdd:PRK05867  87 IDIAVCNAGIITVTPMLDMP------LEEFQRLQNTNVTGVF----LTAQAAAKAMVKQ-GQGGVIINTASMSGHIINVP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  165 Q--AAYSASKGGIVGMTLPIARDLAP---------IGLFGTPLLTSLPEKVCNFlASQVPFpSRLGDPAEYA--HLVQAI 231
Cdd:PRK05867 156 QqvSHYCASKAAVIHLTKAMAVELAPhkirvnsvsPGYILTELVEPYTEYQPLW-EPKIPL-GRLGRPEELAglYLYLAS 233

                        250
                 ....*....|....*.
gi 83715985  232 IENPFLNGEVIRLDGA 247
Cdd:PRK05867 234 EASSYMTGSDIVIDGG 249
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 13-175 1.03e-13

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: 68.10  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLldlpnsGGE-----AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05370   8 VLITGGTSGIGLALARKFLEAGNTVII------TGRreerlAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIavaSKTYNLKKGQTHtLEDFQRVLDVNLMGTFNVIR-LVAGEMGQNEpdqggqrGVIINTASVAAFEGQVGQA 166
Cdd:cd05370  82 LINNAGI---QRPIDLRDPASD-LDKADTEIDTNLIGPIRLIKaFLPHLKKQPE-------ATIVNVSSGLAFVPMAANP 150


                ....*....
gi 83715985 167 AYSASKGGI 175
Cdd:cd05370 151 VYCATKAAL 159
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 12-191 1.05e-13

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: 68.18  E-value: 1.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA----QAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAllvdIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAA 167
Cdd:cd05373  81 LVYNAGANVWFPILET------TPRVFEKVWEMAAFGGFLAAREAAKRMLAR------GRGTIIFTGATASLRGRAGFAA 148

                       170       180
                ....*....|....*....|....
gi 83715985 168 YSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd05373 149 FAGAKFALRALAQSMARELGPKGI 172
PRK07062 PRK07062
SDR family oxidoreductase;
8-190 1.23e-13

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 68.53  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQGASAVL-------LD-----LPNSGGEAQakklgnncVFA-PADVTSEKDVQTA 74
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAIcgrdeerLAsaearLREKFPGAR--------LLAaRCDVLDEADVAAF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   75 LALAKGKFGRVDVAVNCAGiavasktynlkKGQTHTLEDFQRV-----LDVNLmgtFNVIRLVAGEMGQNEpdqGGQRGV 149
Cdd:PRK07062  78 AAAVEARFGGVDMLVNNAG-----------QGRVSTFADTTDDawrdeLELKY---FSVINPTRAFLPLLR---ASAAAS 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 83715985  150 IINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK07062 141 IVCVNSLLALQPEPHMVATSAARAGLLNLVKSLATELAPKG 181
PRK08264 PRK08264
SDR family oxidoreductase;
7-190 2.10e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 67.61  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSggeAQAKKLGNNCVFAPADVTSEKDVQTALALAkgkfGRVD 86
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAAKVYAAARDP---ESVTDLGPRVVPLQLDVTDPASVAAAAEAA----SDVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqGGqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK08264  76 ILVNNAGIFRTGSLL-----LEGDEDALRAEMETNYFGPLAMARAFAPVLAAN----GG--GAIVNVLSVLSWVNFPNLG 144

                        170       180
                 ....*....|....*....|....
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK08264 145 TYSASKAAAWSLTQALRAELAPQG 168
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-191 4.36e-13

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 66.82  E-value: 4.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDL--PNSGGEaQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK08993   7 SLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIvePTETIE-QVTALGRRFLSLTADLRKIDGIPALLERAVAEFGH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQVG 164
Cdd:PRK08993  86 IDILVNNAGLIRREDAIEFSE------KDWDDVMNLNIKSVFFMSQAAAKHFIAQ-----GNGGKIINIASMLSFQGGIR 154

                        170       180
                 ....*....|....*....|....*..
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK08993 155 VPSYTASKSGVMGVTRLMANEWAKHNI 181
PRK06914 PRK06914
SDR family oxidoreductase;
12-238 7.67e-13

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 66.59  E-value: 7.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQG--ASAVLLDLPNSGG-EAQAKKLG--NNCVFAPADVTSEKDVQTALALAKgKFGRVD 86
Cdd:PRK06914   5 IAIVTGASSGFGLLTTLELAKKGylVIATMRNPEKQENlLSQATQLNlqQNIKVQQLDVTDQNSIHNFQLVLK-EIGRID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAafeGQVGQA 166
Cdd:PRK06914  84 LLVNNAGYANGGFVEEI------PVEEYRKQFETNVFGAISVTQAVLPYMRKQ------KSGKIINISSIS---GRVGFP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  167 AYS---ASKGGIVGMT-------LPIARDLAPI--GLFGTPLLTSLPEKVCNFLASQVPFPSRL--------------GD 220
Cdd:PRK06914 149 GLSpyvSSKYALEGFSeslrlelKPFGIDVALIepGSYNTNIWEVGKQLAENQSETTSPYKEYMkkiqkhinsgsdtfGN 228

                        250
                 ....*....|....*...
gi 83715985  221 PAEYAHLVQAIIENPFLN 238
Cdd:PRK06914 229 PIDVANLIVEIAESKRPK 246
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 14-246 7.79e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 66.36  E-value: 7.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   14 VITGGASGLGLATAERLVGQGASAVLL-----DLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVgrnpdKLAAAAEEIEALKGAGAVRYEPADVTDEDQVARAVDAATAWHGRLHGV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGiavASKTYNlkkGQTHT-LEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFEGQVGQAA 167
Cdd:PRK05875  91 VHCAG---GSETIG---PITQIdSDAWRRTVDLNVNGTMYVLKHAARELVR------GGGGSFVGISSIAASNTHRWFGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  168 YSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSL---PEKVCNFLASqVPFPsRLGDPAEYAHLVQAIIEN- 234
Cdd:PRK05875 159 YGVTKSAVDHLMKLAADELGPSwvrvnsirpGLIRTDLVAPItesPELSADYRAC-TPLP-RVGEVEDVANLAMFLLSDa 236

                        250
                 ....*....|...
gi 83715985  235 -PFLNGEVIRLDG 246
Cdd:PRK05875 237 aSWITGQVINVDG 249
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 12-204 1.15e-12

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: 65.56  E-value: 1.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGAS-----AVLLDLPNSGG--EAQAKKLGNNCVFAPADVTSEKDVQTALALAKGkfGR 84
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASDPSKrfkvyATMRDLKKKGRlwEAAGALAGGTLETLQLDVCDSKSVAAAVERVTE--RH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVG 164
Cdd:cd09806  80 VDVLVCNAGVGL------LGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRR------GSGRILVTSSVGGLQGLPF 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 83715985 165 QAAYSASKGGIVGMTLPIARDLAPIGLFGT-----PLLTSLPEKV 204
Cdd:cd09806 148 NDVYCASKFALEGLCESLAVQLLPFNVHLSliecgPVHTAFMEKV 192
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 14-170 1.51e-12

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: 64.12  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    14 VITGGASGLGLATAERLVGQGASAVLL----DLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARHLVLlsrsAAPRPDAQALIAELearGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    87 VAVNCAGIavasktynLKKG--QTHTLEDFQRVLDVNLMGTFNVIRLVAGEmgqnEPDQggqrgvIINTASVAAFEGQVG 164
Cdd:pfam08659  84 GVIHAAGV--------LRDAllENMTDEDWRRVLAPKVTGTWNLHEATPDE----PLDF------FVLFSSIAGLLGSPG 145


                  ....*.
gi 83715985   165 QAAYSA 170
Cdd:pfam08659 146 QANYAA 151
PRK09730 PRK09730
SDR family oxidoreductase;
12-191 1.58e-12

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 65.26  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQG-------------ASAVLLDLPNSGGEAQAKKlgnncvfapADVTSEKDVQTALALA 78
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGytvavnyqqnlhaAQEVVNLITQAGGKAFVLQ---------ADISDENQVVAMFTAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   79 KGKFGRVDVAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdQGGQRGVIINTASVAA 158
Cdd:PRK09730  74 DQHDEPLAALVNNAGILFTQCTV-----ENLTAERINRVLSTNVTGYFLCCREAVKRMALK---HGGSGGAIVNVSSAAS 145

                        170       180       190
                 ....*....|....*....|....*....|....
gi 83715985  159 FEGQVGQ-AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK09730 146 RLGAPGEyVDYAASKGAIDTLTTGLSLEVAAQGI 179
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 14-170 1.99e-12

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: 63.66  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985     14 VITGGASGLGLATAERLVGQGASAVLL----DLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARRLVLlsrsGPDAPGAAALLAELeaaGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985     87 VAVNCAGIAvasktyNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEmgqnEPDqggqrgVIINTASVAAFEGQVGQA 166
Cdd:smart00822  84 GVIHAAGVL------DDGVLASLTPERFAAVLAPKAAGAWNLHELTADL----PLD------FFVLFSSIAGVLGSPGQA 147


                   ....
gi 83715985    167 AYSA 170
Cdd:smart00822 148 NYAA 151
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
10-187 2.05e-12

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 64.93  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDL-PNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK12481   8 GKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVaEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQVGQAAY 168
Cdd:PRK12481  88 INNAGIIRRQDLLEFGN------KDWDDVININQKTVFFLSQAVAKQFVKQ-----GNGGKIINIASMLSFQGGIRVPSY 156

                        170
                 ....*....|....*....
gi 83715985  169 SASKGGIVGMTLPIARDLA 187
Cdd:PRK12481 157 TASKSAVMGLTRALATELS 175
PRK07577 PRK07577
SDR family oxidoreductase;
13-246 2.76e-12

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 64.36  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   13 AVITGGASGLGLATAERLVGQGASAVLL------DLPnsgGEAQAkklgnnCVFAPADvtsekdvQTALALAK-GKFGRV 85
Cdd:PRK07577   6 VLVTGATKGIGLALSLRLANLGHQVIGIarsaidDFP---GELFA------CDLADIE-------QTAATLAQiNEIHPV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggqRGVIINTASVAAFeGQVGQ 165
Cdd:PRK07577  70 DAIVNNVGIALPQPLGKID------LAALQDVYDLNVRAAVQVTQAFLEGMKLRE------QGRIVNICSRAIF-GALDR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGLFGT-----PLLTSL--------PEKVCNFLASqVPFpSRLGDPAEYAHLVQAII 232
Cdd:PRK07577 137 TSYSAAKSALVGCTRTWALELAEYGITVNavapgPIETELfrqtrpvgSEEEKRVLAS-IPM-RRLGTPEEVAAAIAFLL 214

                        250
                 ....*....|....*.
gi 83715985  233 EN--PFLNGEVIRLDG 246
Cdd:PRK07577 215 SDdaGFITGQVLGVDG 230
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 13-246 3.73e-12

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: 63.91  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGG----EAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAaaevAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAAFEGQVGQAAY 168
Cdd:cd05359  81 VSNAAAGA------FRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLM----RERGG--GRIVAISSLGSIRALPNYLAV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 169 SASKGGIVGMTLPIARDLAP---------IGLFGTPLLTSLP--EKVCNFLASQVPFPsRLGDPAEYAHLVQ--AIIENP 235
Cdd:cd05359 149 GTAKAALEALVRYLAVELGPrgirvnavsPGVIDTDALAHFPnrEDLLEAAAANTPAG-RVGTPQDVADAVGflCSDAAR 227

                       250
                ....*....|.
gi 83715985 236 FLNGEVIRLDG 246
Cdd:cd05359 228 MITGQTLVVDG 238
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 15-194 4.00e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 64.55  E-value: 4.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   15 ITGGASGLGLATAERLVGQGASAV--------LLDLPN-SGGEAQAKKLgnncvfapaDVTSEKDVQTALALAKGKFGRV 85
Cdd:PRK06180   9 ITGVSSGFGRALAQAALAAGHRVVgtvrseaaRADFEAlHPDRALARLL---------DVTDFDAIDAVVADAEATFGPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKtynLKKGqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQ 165
Cdd:PRK06180  80 DVLVNNAGYGHEGA---IEES---PLAEMRRQFEVNVFGAVAMTKAVLPGMRAR------RRGHIVNITSMGGLITMPGI 147

                        170       180
                 ....*....|....*....|....*....
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGLFGT 194
Cdd:PRK06180 148 GYYCGSKFALEGISESLAKEVAPFGIHVT 176
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 8-192 4.62e-12

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: 63.58  E-value: 4.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQ-AKKLGNNCVFAPADVTSEKDVQTALALAKgkfgRVD 86
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGSAAHlVAKYGDKVVPLRLDVTDPESIKAAAAQAK----DVD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  87 VAVNCAGIAVASKTYnlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQA 166
Cdd:cd05354  77 VVINNAGVLKPATLL-----EEGALEALKQEMDVNVFGLLRLAQAFAPVLKAN------GGGAIVNLNSVASLKNFPAMG 145

                       170       180
                ....*....|....*....|....*.
gi 83715985 167 AYSASKGGIVGMTLPIARDLAPIGLF 192
Cdd:cd05354 146 TYSASKSAAYSLTQGLRAELAAQGTL 171
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 9-179 6.01e-12

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: 63.69  E-value: 6.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA---QAKKLGNNCVFA-PADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05343   5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEAlaaECQSAGYPTLFPyQCDLSNEEQILSMFSAIRTQHQG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAVASKtynLKKGQThtlEDFQRVLDVNLMGTFNVIRLVAGEMGqnepDQGGQRGVIINTASVAAFEGQVG 164
Cdd:cd05343  85 VDVCINNAGLARPEP---LLSGKT---EGWKEMFDVNVLALSICTREAYQSMK----ERNVDDGHIININSMSGHRVPPV 154

                       170
                ....*....|....*..
gi 83715985 165 QAA--YSASKGGIVGMT 179
Cdd:cd05343 155 SVFhfYAATKHAVTALT 171
PRK06482 PRK06482
SDR family oxidoreductase;
15-191 6.54e-12

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 63.98  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   15 ITGGASGLGLATAERLVGQG-ASAVLLDLPNSGGEAQAKKlGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAG 93
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGdRVAATVRRPDALDDLKARY-GDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVSNAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   94 iavasktYNLkKGQTHTLEDFQ--RVLDVNLMGTFNVIRLVAGEMGQnepdQGGQRGVIINTasvaafegQVGQAA---- 167
Cdd:PRK06482  86 -------YGL-FGAAEELSDAQirRQIDTNLIGSIQVIRAALPHLRR----QGGGRIVQVSS--------EGGQIAypgf 145

                        170       180
                 ....*....|....*....|....*.
gi 83715985  168 --YSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK06482 146 slYHATKWGIEGFVEAVAQEVAPFGI 171
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 8-172 9.46e-12

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: 62.99  E-value: 9.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   8 VKGLVAVITGGASGLGLATAERLVGQGASAVLldlpnSG--GEA------QAKKLGNNCVFA-PADVTSEKDVQTALALA 78
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVL-----SArrEERleevksECLELGAPSPHVvPLDMSDLEDAEQVVEEA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  79 KGKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAA 158
Cdd:cd05332  76 LKLFGGLDILINNAGISMRSLFHDT------SIDVDRKIMEVNYFGPVALTKAALPHLIER------SQGSIVVVSSIAG 143

                       170
                ....*....|....
gi 83715985 159 FEGQVGQAAYSASK 172
Cdd:cd05332 144 KIGVPFRTAYAASK 157
PRK07814 PRK07814
SDR family oxidoreductase;
10-252 1.02e-11

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 63.26  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE---AQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDevaEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYNlkkgqtHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepDQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK07814  90 IVVNNVGGTMPNPLLS------TSTKDLADAFTFNVATAHALTVAAVPLMLE---HSGG--GSVINISSTMGRLAGRGFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPI----GLFGTPLLTSLPEKVC------NFLASQVPFpSRLGDPAEYAH--LVQAIIEN 234
Cdd:PRK07814 159 AYGTAKAALAHYTRLAALDLCPRirvnAIAPGSILTSALEVVAandelrAPMEKATPL-RRLGDPEDIAAaaVYLASPAG 237

                        250
                 ....*....|....*...
gi 83715985  235 PFLNGEVIRLDGAIRMQP 252
Cdd:PRK07814 238 SYLTGKTLEVDGGLTFPN 255
PRK07985 PRK07985
SDR family oxidoreductase;
8-241 1.02e-11

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 63.48  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQ-AKKL----GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAQdVKKIieecGRKAVLLPGDLSDEKFARSLVHEAHKAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   83 GRVDVAVNCAGIAVA-SKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIR-----LVAGemgqnepdqggqrGVIINTASV 156
Cdd:PRK07985 127 GGLDIMALVAGKQVAiPDIADL------TSEQFQKTFAINVFALFWLTQeaiplLPKG-------------ASIITTSSI 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  157 AAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGLFGT-----PLLTSL------PEKVCNFLASQVPFpSRLGDPAEYA 225
Cdd:PRK07985 188 QAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNivapgPIWTALqisggqTQDKIPQFGQQTPM-KRAGQPAELA 266

                        250
                 ....*....|....*...
gi 83715985  226 --HLVQAIIENPFLNGEV 241
Cdd:PRK07985 267 pvYVYLASQESSYVTAEV 284
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 10-246 1.66e-11

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: 62.56  E-value: 1.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVL-----LDLPNSGGEAQAKKL---GNNCvfapaDVTSEKDVQTALALAKGK 81
Cdd:cd08936  10 NKVALVTASTDGIGLAIARRLAQDGAHVVVssrkqQNVDRAVATLQGEGLsvtGTVC-----HVGKAEDRERLVATAVNL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  82 FGRVDVAVNCAgiAVASKTYNLKKGqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEG 161
Cdd:cd08936  85 HGGVDILVSNA--AVNPFFGNILDS---TEEVWDKILDVNVKATALMTKAVVPEMEK----RGG--GSVVIVSSVAAFHP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 162 QVGQAAYSASKGGIVGMTLPIARDLAPI---------GLFGTPLLTSL--PEKVCNFLASQVPFpSRLGDPAEYAHLVQA 230
Cdd:cd08936 154 FPGLGPYNVSKTALLGLTKNLAPELAPRnirvnclapGLIKTSFSSALwmDKAVEESMKETLRI-RRLGQPEDCAGIVSF 232

                       250
                ....*....|....*...
gi 83715985 231 II--ENPFLNGEVIRLDG 246
Cdd:cd08936 233 LCseDASYITGETVVVGG 250
PRK07775 PRK07775
SDR family oxidoreductase;
13-178 1.87e-11

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 62.46  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   13 AVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIradGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   90 NCAGiavasKTYNLKKGQTHTlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYS 169
Cdd:PRK07775  93 SGAG-----DTYFGKLHEIST-EQFESQVQIHLVGANRLATAVLPGMIER------RRGDLIFVGSDVALRQRPHMGAYG 160


                 ....*....
gi 83715985  170 ASKGGIVGM 178
Cdd:PRK07775 161 AAKAGLEAM 169
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 7-187 7.06e-11

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: 60.57  E-value: 7.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN--NCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd08942   3 SVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAygECIAIPADLSSEEGIEALVARVAERSDR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAVASktynlkkgqthTLEDF-----QRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRgvIINTASVAAF 159
Cdd:cd08942  83 LDVLVNNAGATWGA-----------PLEAFpesgwDKVMDINVKSVFFLTQALLPLLRAAATAENPAR--VINIGSIAGI 149

                       170       180
                ....*....|....*....|....*....
gi 83715985 160 EGQVGQA-AYSASKGGIVGMTLPIARDLA 187
Cdd:cd08942 150 VVSGLENySYGASKAAVHQLTRKLAKELA 178
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 12-183 1.27e-10

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: 59.26  E-value: 1.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLpnsggeAQAKKLGNNCVFAPADVTSEKdVQTALALAKGKFGRVDVAVNC 91
Cdd:cd05334   3 VVLVYGGRGALGSAVVQAFKSRGWWVASIDL------AENEEADASIIVLDSDSFTEQ-AKQVVASVARLSGKVDALICV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  92 AGIAVASKTynlkkGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:cd05334  76 AGGWAGGSA-----KSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSG--------GLLVLTGAKAALEPTPGMIGYGAA 142

                       170
                ....*....|..
gi 83715985 172 KGGIVGMTLPIA 183
Cdd:cd05334 143 KAAVHQLTQSLA 154
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 7-188 1.36e-10

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: 59.79  E-value: 1.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLdlpnSGGEAQAKKLGNNCV-FAP--ADVTSEKDVQTALalakGKFG 83
Cdd:cd05351   4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAV----SRTQADLDSLVRECPgIEPvcVDLSDWDATEEAL----GSVG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  84 RVDVAVNCAGIAVasktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqgGQRGVIINTASVAAFEGQV 163
Cdd:cd05351  76 PVDLLVNNAAVAI------LQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIAR-----GVPGSIVNVSSQASQRALT 144

                       170       180
                ....*....|....*....|....*
gi 83715985 164 GQAAYSASKGGIVGMTLPIARDLAP 188
Cdd:cd05351 145 NHTVYCSTKAALDMLTKVMALELGP 169
PRK06182 PRK06182
short chain dehydrogenase; Validated
 12-190 1.49e-10

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 59.97  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQG----ASAVLLDLPNSggeaqAKKLGNNCVfaPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQGytvyGAARRVDKMED-----LASLGVHPL--SLDVTDEASIKAAVDTIIAEEGRIDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAA 167
Cdd:PRK06182  78 LVNNAGYGSYGAIEDV------PIDEARRQFEVNLFGAARLTQLVLPHMRAQ------RSGRIINISSMGGKIYTPLGAW 145

                        170       180
                 ....*....|....*....|...
gi 83715985  168 YSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK06182 146 YHATKFALEGFSDALRLEVAPFG 168
PRK07041 PRK07041
SDR family oxidoreductase;
14-246 2.41e-10

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 58.90  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   14 VITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN--CVFAPADVTSEKDVQTALALAkgkfGRVD-VAVN 90
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGapVRTAALDITDEAAVDAFFAEA----GPFDhVVIT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   91 CAGIAVASKtynlkkgQTHTLEDFQRVLDVNLMGTFNVIRlvAGEMGQNepdqggqrGVIINTASVAAFEGQVGQAAYSA 170
Cdd:PRK07041  77 AADTPGGPV-------RALPLAAAQAAMDSKFWGAYRVAR--AARIAPG--------GSLTFVSGFAAVRPSASGVLQGA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  171 SKGGIVGMTLPIARDLAPI-------GLFGTPLLTSLPE--KVCNFLASQVPFPS-RLGDPAEYAHLVQAIIENPFLNGE 240
Cdd:PRK07041 140 INAALEALARGLALELAPVrvntvspGLVDTPLWSKLAGdaREAMFAAAAERLPArRVGQPEDVANAILFLAANGFTTGS 219


                 ....*.
gi 83715985  241 VIRLDG 246
Cdd:PRK07041 220 TVLVDG 225
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
14-172 7.06e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 58.07  E-value: 7.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  14 VITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGnnCVFAPADVTSEKDVQTALAlakgkfgRVDVAVNCAG 93
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPG--VEFVRGDLRDPEALAAALA-------GVDAVVHLAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  94 IAvasktynlkkgqTHTLEDFQRVLDVNLMGTFNVIRLVAgemgqnepDQGGQRgvIINTASVAAFEGQVG--------- 164
Cdd:COG0451  74 PA------------GVGEEDPDETLEVNVEGTLNLLEAAR--------AAGVKR--FVYASSSSVYGDGEGpidedtplr 131


                ....*....
gi 83715985 165 -QAAYSASK 172
Cdd:COG0451 132 pVSPYGASK 140
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 2-170 7.12e-10

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 58.55  E-value: 7.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   2 AAACRSVKGLVaVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL------GNNCVFAPADVTSEKDVQTAL 75
Cdd:cd05274 143 AAAPGGLDGTY-LITGGLGGLGLLVARWLAARGARHLVLLSRRGPAPRAAARAallragGARVSVVRCDVTDPAALAALL 221

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  76 AlAKGKFGRVDVAVNCAGIAVASktynlkKGQTHTLEDFQRVLDVNLMGTFNVIRLVagemgqnePDQGGQRGVIinTAS 155
Cdd:cd05274 222 A-ELAAGGPLAGVIHAAGVLRDA------LLAELTPAAFAAVLAAKVAGALNLHELT--------PDLPLDFFVL--FSS 284

                       170
                ....*....|....*
gi 83715985 156 VAAFEGQVGQAAYSA 170
Cdd:cd05274 285 VAALLGGAGQAAYAA 299
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 10-172 7.25e-10

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: 57.61  E-value: 7.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNN-----CVFApADVTSEKDVQTAL-ALAKGKfg 83
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKygvetKTIA-ADFSAGDDIYERIeKELEGL-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  84 RVDVAVNCAGIavaSKTYNLKKGQThTLEDFQRVLDVNLMGTFNVIRLVAGEMgqnepdQGGQRGVIINTASVAAFEGQV 163
Cdd:cd05356  78 DIGILVNNVGI---SHSIPEYFLET-PEDELQDIINVNVMATLKMTRLILPGM------VKRKKGAIVNISSFAGLIPTP 147


                ....*....
gi 83715985 164 GQAAYSASK 172
Cdd:cd05356 148 LLATYSASK 156
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 15-190 1.48e-09

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: 56.90  E-value: 1.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  15 ITGGASGLGLATAERLVGQGAS--AVLLDLPNSGgeaqAKKLGNNCV----FAPADVTSEKDVQTALALAKGKFGRVDV- 87
Cdd:cd09805   5 ITGCDSGFGNLLAKKLDSLGFTvlAGCLTKNGPG----AKELRRVCSdrlrTLQLDVTKPEQIKRAAQWVKEHVGEKGLw 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 -AVNCAGIAVasktyNLKKGQTHTLEDFQRVLDVNLMGTFNV-------IRlvagemgqnepdqgGQRGVIINTASVAAF 159
Cdd:cd09805  81 gLVNNAGILG-----FGGDEELLPMDDYRKCMEVNLFGTVEVtkaflplLR--------------RAKGRVVNVSSMGGR 141

                       170       180       190
                ....*....|....*....|....*....|.
gi 83715985 160 EGQVGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:cd09805 142 VPFPAGGAYCASKAAVEAFSDSLRRELQPWG 172
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 15-190 1.61e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 56.97  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   15 ITGGASGLGLATAERLVGQGASAV--------LLDLpnsggeaqAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK08263   8 ITGASRGFGRAWTEAALERGDRVVatardtatLADL--------AEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK08263  80 IVVNNAGYGLFGMIEEV------TESEARAQIDTNFFGALWVTQAVLPYLRE----QRS--GHIIQISSIGGISAFPMSG 147

                        170       180
                 ....*....|....*....|....
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK08263 148 IYHASKWALEGMSEALAQEVAEFG 171
PRK05866 PRK05866
SDR family oxidoreductase;
8-172 2.00e-09

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 56.67  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLL------------DLPNSGGEAQAkklgnncvfAPADVTSEKDVQTAL 75
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVarredlldavadRITRAGGDAMA---------VPCDLSDLDAVDALV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   76 ALAKGKFGRVDVAVNCAGIAVASKTYNlkkgqthTLE---DFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIIN 152
Cdd:PRK05866 109 ADVEKRIGGVDILINNAGRSIRRPLAE-------SLDrwhDVERTMVLNYYAPLRLIRGLAPGMLER------GDGHIIN 175

                        170       180
                 ....*....|....*....|.
gi 83715985  153 TASVAAFEGQVGQ-AAYSASK 172
Cdd:PRK05866 176 VATWGVLSEASPLfSVYNASK 196
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 11-186 2.36e-09

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 56.30  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   11 LVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVN 90
Cdd:PRK10538   1 MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   91 CAGIAVAsktynLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQAAYSA 170
Cdd:PRK10538  81 NAGLALG-----LEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVER------NHGHIINIGSTAGSWPYAGGNVYGA 149

                        170
                 ....*....|....*.
gi 83715985  171 SKGGIVGMTLPIARDL 186
Cdd:PRK10538 150 TKAFVRQFSLNLRTDL 165
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 9-190 5.61e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 55.30  E-value: 5.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVlldlpnSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK06523   8 AGKRALVTGGTKGIGAATVARLLEAGARVV------TTARSRPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 VNCAGIAVASktynlkKGQTHTL--EDFQRVLDVNLMGTFNVIRLVAGEMgqnePDQGGqrGVIINTASVAA----FEgq 162
Cdd:PRK06523  82 VHVLGGSSAP------AGGFAALtdEEWQDELNLNLLAAVRLDRALLPGM----IARGS--GVIIHVTSIQRrlplPE-- 147

                        170       180
                 ....*....|....*....|....*...
gi 83715985  163 vGQAAYSASKGGIVGMTLPIARDLAPIG 190
Cdd:PRK06523 148 -STTAYAAAKAALSTYSKSLSKEVAPKG 174
PRK06720 PRK06720
hypothetical protein; Provisional
 10-94 1.50e-08

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 52.67  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKK---LGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK06720  16 GKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEitnLGGEALFVSYDMEKQGDWQRVISITLNAFSRID 95


                 ....*...
gi 83715985   87 VAVNCAGI 94
Cdd:PRK06720  96 MLFQNAGL 103
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 10-157 2.60e-08

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: 53.38  E-value: 2.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLL--DlPNSGGEAQA---KKLGNNCVFA-PADVTSEKDVQTALALAKGKFG 83
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIAcrN-EEKGEEAAAeikKETGNAKVEViQLDLSSLASVRQFAEEFLARFP 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83715985  84 RVDVAVNCAGIAVASKTYnlkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPdqggqrGVIINTASVA 157
Cdd:cd05327  80 RLDILINNAGIMAPPRRL--------TKDGFELQFAVNYLGHFLLTNLLLPVLKASAP------SRIVNVSSIA 139
PRK08278 PRK08278
SDR family oxidoreductase;
7-126 2.89e-08

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 52.98  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLL--------DLPNS-----------GGEAQAKKLgnncvfapaDVTS 67
Cdd:PRK08278   3 SLSGKTLFITGASRGIGLAIALRAARDGANIVIAaktaephpKLPGTihtaaeeieaaGGQALPLVG---------DVRD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 83715985   68 EKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTF 126
Cdd:PRK08278  74 EDQVAAAVAKAVERFGGIDICVNNASAINLTGTEDT------PMKRFDLMQQINVRGTF 126
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 14-248 3.73e-08

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: 52.50  E-value: 3.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  14 VITGGASGLGLATAERLVGQGASAVLLDLpnsgGEAqakklgnncvFAPADVTSEKDVQTALALAKGKFGRV-DVAVNCA 92
Cdd:cd05328   3 VITGAASGIGAATAELLEDAGHTVIGIDL----REA----------DVIADLSTPEGRAAAIADVLARCSGVlDGLVNCA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  93 GIAVASKTYNlkkgqthtledfqrVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIINTASVAAFE------------ 160
Cdd:cd05328  69 GVGGTTVAGL--------------VLKVNYFGLRALMEALLPRLRK------GHGPAAVVVSSIAGAGwaqdklelakal 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 161 ---------------GQVGQAAYSASKGGIVGMTLPIARD-----------LAPiGLFGTPLLTSLpEKVCNFLASQVPF 214
Cdd:cd05328 129 aagtearavalaehaGQPGYLAYAGSKEALTVWTRRRAATwlygagvrvntVAP-GPVETPILQAF-LQDPRGGESVDAF 206

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 83715985 215 PSRLGDPAEYAHLVQAII-----ENPFLNGEVIRLDGAI 248
Cdd:cd05328 207 VTPMGRRAEPDEIAPVIAflasdAASWINGANLFVDGGL 245
PRK12742 PRK12742
SDR family oxidoreductase;
9-191 4.73e-08

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 52.07  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVL-LDLPNSGGEAQAKKLGNNCVFApaDVTSEKDVQTALAlakgKFGRVDV 87
Cdd:PRK12742   5 TGKKVLVLGGSRGIGAAIVRRFVTDGANVRFtYAGSKDAAERLAQETGATAVQT--DSADRDAVIDVVR----KSGALDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   88 AVNCAGIAVAsktynlkkGQTHTL--EDFQRVLDVNLMGTFNVirlvAGEMGQNEPDQGgqRGVIIntASVAAFEGQV-G 164
Cdd:PRK12742  79 LVVNAGIAVF--------GDALELdaDDIDRLFKINIHAPYHA----SVEAARQMPEGG--RIIII--GSVNGDRMPVaG 142

                        170       180
                 ....*....|....*....|....*..
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK12742 143 MAAYAASKSALQGMARGLARDFGPRGI 169
PRK08219 PRK08219
SDR family oxidoreductase;
12-179 6.20e-08

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 51.86  E-value: 6.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERL-------VGQGASAVLLDLPNSGGEAQAkklgnncvfAPADVTSEKDVQTALAlakgKFGR 84
Cdd:PRK08219   5 TALITGASRGIGAAIARELapthtllLGGRPAERLDELAAELPGATP---------FPVDLTDPEAIAAAVE----QLGR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAgemgqnePDQGGQRG--VIINtaSVAAFEGQ 162
Cdd:PRK08219  72 LDVLVHNAGVADLGPVAES------TVDEWRATLEVNVVAPAELTRLLL-------PALRAAHGhvVFIN--SGAGLRAN 136

                        170
                 ....*....|....*..
gi 83715985  163 VGQAAYSASKGGIVGMT 179
Cdd:PRK08219 137 PGWGSYAASKFALRALA 153
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-246 9.17e-08

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 51.71  E-value: 9.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGG--ASGLGLATAERLVGQGASAVL---------LDLPNSGGEA-----QAKKLGNNCVFAPADVTSEKD 70
Cdd:PRK12859   3 QLKNKVAVVTGVsrLDGIGAAICKELAEAGADIFFtywtaydkeMPWGVDQDEQiqlqeELLKNGVKVSSMELDLTQNDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   71 VQTALALAKGKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFnvirLVAGEMGQN-EPDQGGQrgv 149
Cdd:PRK12859  83 PKELLNKVTEQLGYPHILVNNAAYSTNNDFSNL------TAEELDKHYMVNVRATT----LLSSQFARGfDKKSGGR--- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  150 IINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGLFGT---PLLTS---LPEKVCNFLASQVPFpSRLGDPAE 223
Cdd:PRK12859 150 IINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNainPGPTDtgwMTEEIKQGLLPMFPF-GRIGEPKD 228

                        250       260
                 ....*....|....*....|....*
gi 83715985  224 YAHLVQAII--ENPFLNGEVIRLDG 246
Cdd:PRK12859 229 AARLIKFLAseEAEWITGQIIHSEG 253
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 9-94 9.53e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 51.95  E-value: 9.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL-----GNNCVFAPADVTSEKDVQTALALAKGKFG 83
Cdd:PRK06197  15 SGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItaatpGADVTLQELDLTSLASVRAAADALRAAYP 94

                         90
                 ....*....|.
gi 83715985   84 RVDVAVNCAGI 94
Cdd:PRK06197  95 RIDLLINNAGV 105
PRK12746 PRK12746
SDR family oxidoreductase;
6-191 1.46e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 51.19  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    6 RSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGE----AQAKKLGNNCVFAPADVTSEKDVQTALALAKGK 81
Cdd:PRK12746   2 KNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAAdetiREIESNGGKAFLIEADLNSIDGVKKLVEQLKNE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   82 F------GRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRlvagemgQNEPDQGGQrGVIINTAS 155
Cdd:PRK12746  82 LqirvgtSEIDILVNNAGIGTQGTIENT------TEEIFDEIMAVNIKAPFFLIQ-------QTLPLLRAE-GRVINISS 147

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 83715985  156 VAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK12746 148 AEVRLGFTGSIAYGLSKGALNTMTLPLAKHLGERGI 183
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
12-191 2.06e-07

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 50.49  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK08063   6 VALVTGSSRGIGKAIALRLAEEGYD-IAVNYARSRKAAEEtaeeiEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGIAVASKTYNLKkgQTHtledFQRVLDVNLMGtfnvIRLVAGEMGQNEPDQGGqrGVIINTASVAAFEGQVGQA 166
Cdd:PRK08063  85 VFVNNAASGVLRPAMELE--ESH----WDWTMNINAKA----LLFCAQEAAKLMEKVGG--GKIISLSSLGSIRYLENYT 152

                        170       180
                 ....*....|....*....|....*
gi 83715985  167 AYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK08063 153 TVGVSKAALEALTRYLAVELAPKGI 177
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 10-186 1.30e-06

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: 48.23  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQA----KKLGNNCVFA-PADVTSEKDVQTALALAKGKFGR 84
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAaeirRDTLNHEVIVrHLDLASLKSIRAFAAEFLAEEDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  85 VDVAVNCAGIAVASKtynlkkgqTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQggqrgvIINTASVAAFEGQVG 164
Cdd:cd09807  81 LDVLINNAGVMRCPY--------SKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSR------IVNVSSLAHKAGKIN 146

                       170       180       190
                ....*....|....*....|....*....|....
gi 83715985 165 ------------QAAYSASKGGIVGMTLPIARDL 186
Cdd:cd09807 147 fddlnseksyntGFAYCQSKLANVLFTRELARRL 180
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 10-175 1.56e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 48.03  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK07576   9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLqqaGPEGLGVSADVRDYAAVEAAFAQIADEFGPID 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVN-CAGIAVASKTYNLKKGqthtledFQRVLDVNLMGTFNVIRLVAGEMgqNEPDqggqrGVIINTASVAAFEGQVGQ 165
Cdd:PRK07576  89 VLVSgAAGNFPAPAAGMSANG-------FKTVVDIDLLGTFNVLKAAYPLL--RRPG-----ASIIQISAPQAFVPMPMQ 154

                        170
                 ....*....|
gi 83715985  166 AAYSASKGGI 175
Cdd:PRK07576 155 AHVCAAKAGV 164
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-249 7.26e-06

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 45.84  E-value: 7.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGA--SGLGLATAERLVGQGASAVL-------LDLPNSGGEAQA-------KKLGNNCVFAPADVTSEKDVQT 73
Cdd:PRK12748   5 KKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydKTMPWGMHDKEPvllkeeiESYGVRCEHMEIDLSQPYAPNR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   74 ALALAKGKFGRVDVAVNCAGIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGqnepdqGGQRGVIINT 153
Cdd:PRK12748  85 VFYAVSERLGDPSILINNAAYSTHTRLEEL------TAEQLDKHYAVNVRATMLLSSAFAKQYD------GKAGGRIINL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  154 ASvaafeGQ-----VGQAAYSASKGGIVGMTLPIARDLAPIGLF------GTPLLTSLPEKVCNFLASQVPFpSRLGDPA 222
Cdd:PRK12748 153 TS-----GQslgpmPDELAYAATKGAIEAFTKSLAPELAEKGITvnavnpGPTDTGWITEELKHHLVPKFPQ-GRVGEPV 226

                        250       260
                 ....*....|....*....|....*....
gi 83715985  223 EYAHLVQAII--ENPFLNGEVIRLDGAIR 249
Cdd:PRK12748 227 DAARLIAFLVseEAKWITGQVIHSEGGFS 255
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 12-248 8.53e-06

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: 45.69  E-value: 8.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    12 VAVITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQA------KKLGNNCVFAPADVTsekDVQTALALAKG----- 80
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYR-VVLHYHRSAAAASTlaaelnARRPNSAVTCQADLS---NSATLFSRCEAiidac 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    81 --KFGRVDVAVNCAG----IAVASKTYNLKKGQTHTLE-DFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINT 153
Cdd:TIGR02685  79 frAFGRCDVLVNNASafypTPLLRGDAGEGVGDKKSLEvQVAELFGSNAIAPYFLIKAFAQRQAGTRAEQRSTNLSIVNL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   154 ASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGLF------GTPLL-TSLPEKVCNFLASQVPFPSRLGDPAEYAH 226
Cdd:TIGR02685 159 CDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRvngvapGLSLLpDAMPFEVQEDYRRKVPLGQREASAEQIAD 238

                         250       260
                  ....*....|....*....|....
gi 83715985   227 LVQAIIENP--FLNGEVIRLDGAI 248
Cdd:TIGR02685 239 VVIFLVSPKakYITGTCIKVDGGL 262
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 8-191 1.55e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 45.07  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQG-------------ASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTA 74
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGalvaihygnrkeeAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   75 LALAKGKFgrvDVAVNCAGIAVASKTynlkkgQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPdqggqrgvIINTA 154
Cdd:PRK12747  82 NRTGSTKF---DILINNAGIGPGAFI------EETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR--------IINIS 144

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 83715985  155 SVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK12747 145 SAATRISLPDFIAYSMTKGAINTMTFTLAKQLGARGI 181
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 8-178 2.10e-05

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: 44.49  E-value: 2.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   8 VKGLVAVITGGASGLGLATAERLVGQGASAVLL-----------DLPNSGGEAQAKKLgnncVFAPADVTSEKDVQTALA 76
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLgrneeklrqvaDHINEEGGRQPQWF----ILDLLTCTSENCQQLAQR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  77 LAKgKFGRVDVAVNCAGIavaskTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPdqggqrGVIINTASV 156
Cdd:cd05340  78 IAV-NYPRLDGVLHNAGL-----LGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDA------GSLVFTSSS 145

                       170       180
                ....*....|....*....|..
gi 83715985 157 AAFEGQVGQAAYSASKGGIVGM 178
Cdd:cd05340 146 VGRQGRANWGAYAVSKFATEGL 167
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
13-175 2.44e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 44.29  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   13 AVITGGASGLGLATAERLVGQGASAVLLD-LPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALalaKGKFGRVDVA--- 88
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISrTENKELTKLAEQYNSNLTFHSLDLQDVHELETNF---NEILSSIQEDnvs 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   89 ----VNCAGIaVASktynLKKGQTHTLEDFQRVLDVNLMGTfnVIrLVAGEMGQNEPDQGGQRgvIINTASVAAFEGQVG 164
Cdd:PRK06924  81 sihlINNAGM-VAP----IKPIEKAESEELITNVHLNLLAP--MI-LTSTFMKHTKDWKVDKR--VINISSGAAKNPYFG 150

                        170
                 ....*....|.
gi 83715985  165 QAAYSASKGGI 175
Cdd:PRK06924 151 WSAYCSSKAGL 161
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 9-191 2.73e-05

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: 44.36  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGAS------AVLLDLPNSGGEAQAKklGNNCVFAPADVTSEKDVQTALA-LAKGK 81
Cdd:cd09763   2 SGKIALVTGASRGIGRGIALQLGEAGATvyitgrTILPQLPGTAEEIEAR--GGKCIPVRCDHSDDDEVEALFErVAREQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  82 FGRVDVAVNCAGIAV-ASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFE 160
Cdd:cd09763  80 QGRLDILVNNAYAAVqLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKA------GKGLIVIISSTGGLE 153

                       170       180       190
                ....*....|....*....|....*....|.
gi 83715985 161 GQVgQAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:cd09763 154 YLF-NVAYGVGKAAIDRMAADMAHELKPHGV 183
PRK07806 PRK07806
SDR family oxidoreductase;
10-93 3.59e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 43.94  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVlldLPNSGGEAQAKKL-------GNNCVFAPADVTSEKDVQTALALAKGKF 82
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVV---VNYRQKAPRANKVvaeieaaGGRASAVGADLTDEESVAALMDTAREEF 82

                         90
                 ....*....|..
gi 83715985   83 GRVDVAV-NCAG 93
Cdd:PRK07806  83 GGLDALVlNASG 94
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 13-245 4.38e-05

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: 42.95  E-value: 4.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVlldlpnsggeaqakKLGNNCVFAPADVTSEKDVQTALAlakgKFGRVDVAVNCA 92
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVI--------------TAGRSSGDYQVDITDEASIKALFE----KVGHFDAIVSTA 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  93 GIAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqrGVIINTASVAAFEGQVGQAAYSASK 172
Cdd:cd11731  63 GDAEFAPLAEL------TDADFQRGLNSKLLGQINLVRHGLPYLNDG--------GSITLTSGILAQRPIPGGAAAATVN 128

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83715985 173 GGIVGMTLPIARDLAP---IGLFGTPLLTSLPEKVCNFLASQVPFPSrlgdpAEYAHLVQAIIENPFlNGEVIRLD 245
Cdd:cd11731 129 GALEGFVRAAAIELPRgirINAVSPGVVEESLEAYGDFFPGFEPVPA-----EDVAKAYVRSVEGAF-TGQVLHVD 198
PRK05693 PRK05693
SDR family oxidoreductase;
12-191 9.78e-05

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 42.47  E-value: 9.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGASAVlldlpnsggeAQAKKLGNNCVFAPADVTSEK-DVQTALALAK------GKFGR 84
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVW----------ATARKAEDVEALAAAGFTAVQlDVNDGAALARlaeeleAEHGG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 VDVAVNCAGIAVASKtynLKKGQThtlEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggqRGVIINTASVAAFEGQVG 164
Cdd:PRK05693  73 LDVLINNAGYGAMGP---LLDGGV---EAMRRQFETNVFAVVGVTRALFPLLRRS-------RGLVVNIGSVSGVLVTPF 139

                        170       180
                 ....*....|....*....|....*..
gi 83715985  165 QAAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK05693 140 AGAYCASKAAVHALSDALRLELAPFGV 166
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 13-211 1.05e-04

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 42.50  E-value: 1.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGASAVLLDLPN-SGGEAQAKKLG---NNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGEWHVVMACRDfLKAEQAAQEVGmpkDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDAL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  89 VNCAGIAVASktynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQggQRGVII-----NTASVAafeGQV 163
Cdd:cd09810  84 VCNAAVYLPT-----AKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENAS--PRIVIVgsithNPNTLA---GNV 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 83715985 164 GQAAYSASKGGIVGmTLPIARDLAPIGLFgTPLLTSLPEKVCNFLASQ 211
Cdd:cd09810 154 PPRATLGDLEGLAG-GLKGFNSMIDGGEF-EGAKAYKDSKVCNMLTTY 199
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 9-100 1.20e-04

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 42.53  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASgLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPadvtSEKDVQTAL-ALAKGKFgrVDV 87
Cdd:cd08233 172 PGDTALVLGAGP-IGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVLDP----TEVDVVAEVrKLTGGGG--VDV 244

                        90
                ....*....|...
gi 83715985  88 AVNCAGIAVASKT 100
Cdd:cd08233 245 SFDCAGVQATLDT 257
PRK09134 PRK09134
SDR family oxidoreductase;
12-246 1.35e-04

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 42.22  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   12 VAVITGGASGLGLATAERLVGQGaSAVLLDLPNSGGEAQA-----KKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVD 86
Cdd:PRK09134  11 AALVTGAARRIGRAIALDLAAHG-FDVAVHYNRSRDEAEAlaaeiRALGRRAVALQADLADEAEVRALVARASAALGPIT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   87 VAVNCAGI----AVASKTYnlkkgqthtlEDFQRVLDVNLMGTFnvirLVAGEMGQNEPDqgGQRGVIINTASVAAFEGQ 162
Cdd:PRK09134  90 LLVNNASLfeydSAASFTR----------ASWDRHMATNLRAPF----VLAQAFARALPA--DARGLVVNMIDQRVWNLN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  163 VGQAAYSASKGGIVGMTLPIARDLAP----IGLFGTPLLTSLPEKVCNFLASQVPFPSRLG-DPAEYAHLVQAIIENPFL 237
Cdd:PRK09134 154 PDFLSYTLSKAALWTATRTLAQALAPrirvNAIGPGPTLPSGRQSPEDFARQHAATPLGRGsTPEEIAAAVRYLLDAPSV 233


                 ....*....
gi 83715985  238 NGEVIRLDG 246
Cdd:PRK09134 234 TGQMIAVDG 242
PRK06196 PRK06196
oxidoreductase; Provisional
 9-94 2.03e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 41.98  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    9 KGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLgNNCVFAPADVTSEKDVQTALALAKGKFGRVDVA 88
Cdd:PRK06196  25 SGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI-DGVEVVMLDLADLESVRAFAERFLDSGRRIDIL 103


                 ....*.
gi 83715985   89 VNCAGI 94
Cdd:PRK06196 104 INNAGV 109
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 9-92 3.17e-04

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: 40.89  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   9 KGLVAVITGGASGLGLATAERLVGQGASAVLL--------DLPNSGGEAQA--KKLGNNCVFAPADVTSEKDVQTALALA 78
Cdd:cd09762   2 AGKTLFITGASRGIGKAIALKAARDGANVVIAaktaephpKLPGTIYTAAEeiEAAGGKALPCIVDIRDEDQVRAAVEKA 81

                        90
                ....*....|....
gi 83715985  79 KGKFGRVDVAVNCA 92
Cdd:cd09762  82 VEKFGGIDILVNNA 95
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 10-132 9.99e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 39.50  E-value: 9.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGN-----NCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEewhkaRVEAMTLDLASLRSVQRFAEAFKAKNSP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 83715985  85 VDVAVNCAgiAVASKTYNLkkgqthTLEDFQRVLDVNLMGTFNVIRLV 132
Cdd:cd09809  81 LHVLVCNA--AVFALPWTL------TEDGLETTFQVNHLGHFYLVQLL 120
PRK09291 PRK09291
SDR family oxidoreductase;
15-191 1.11e-03

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 39.21  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   15 ITGGASGLGLATAERLVGQGASAVlldlpnSGGE---------AQAKKLGNNCVFAPADVTSEKDVQTALALakgkfgRV 85
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGHNVI------AGVQiapqvtalrAEAARRGLALRVEKLDLTDAIDRAQAAEW------DV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   86 DVAVNCAGIAVASKTYNLKkgqthtLEDFQRVLDVNLMGTFNVIRLVAGEMGQNepdqggQRGVIINTASVAAFEGQVGQ 165
Cdd:PRK09291  75 DVLLNNAGIGEAGAVVDIP------VELVRELFETNVFGPLELTQGFVRKMVAR------GKGKVVFTSSMAGLITGPFT 142

                        170       180
                 ....*....|....*....|....*.
gi 83715985  166 AAYSASKGGIVGMTLPIARDLAPIGL 191
Cdd:PRK09291 143 GAYCASKHALEAIAEAMHAELKPFGI 168
PRK08862 PRK08862
SDR family oxidoreductase;
8-242 1.15e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 39.32  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    8 VKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEA---QAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:PRK08862   3 IKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDtyeQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   85 V-DVAVNCagiAVASKTYNLKKGQthTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEpdqggQRGVIINTASVAAFEGQV 163
Cdd:PRK08862  83 ApDVLVNN---WTSSPLPSLFDEQ--PSESFIQQLSSLASTLFTYGQVAAERMRKRN-----KKGVIVNVISHDDHQDLT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  164 GqaaYSASKGGIVGMTLPIARDLAPIGL-FG--TPLLTSLPEKVCNFLASQVpfPSRLGDPAEYahlvqaIIENPFLNGE 240
Cdd:PRK08862 153 G---VESSNALVSGFTHSWAKELTPFNIrVGgvVPSIFSANGELDAVHWAEI--QDELIRNTEY------IVANEYFSGR 221


                 ..
gi 83715985  241 VI 242
Cdd:PRK08862 222 VV 223
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 14-170 1.22e-03

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: 39.58  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  14 VITGGASGLGLATAERLVGQGA-SAVLL--DLPNSGGEAQAKKL---GNNCVFAPADVTSEKDVQTALALAKGKFGRVDV 87
Cdd:cd08955 153 LITGGLGGLGLLVAEWLVERGArHLVLTgrRAPSAAARQAIAALeeaGAEVVVLAADVSDRDALAAALAQIRASLPPLRG 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  88 AVNCAGIavasktynLKKG--QTHTLEDFQRVLDVNLMGTFNVIRLVagemgQNEP-DQggqrgvIINTASVAAFEGQVG 164
Cdd:cd08955 233 VIHAAGV--------LDDGvlANQDWERFRKVLAPKVQGAWNLHQLT-----QDLPlDF------FVLFSSVASLLGSPG 293


                ....*.
gi 83715985 165 QAAYSA 170
Cdd:cd08955 294 QANYAA 299
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 13-175 1.43e-03

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: 38.66  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  13 AVITGGASGLGLATAERLVGQGaSAVLLDLPNSGGEAQ-AKKLGNNCVfaPADVTSEKDVQtalALAKGkFGRVDVAVNC 91
Cdd:cd11730   1 ALILGATGGIGRALARALAGRG-WRLLLSGRDAGALAGlAAEVGALAR--PADVAAELEVW---ALAQE-LGPLDLLVYA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  92 AGIAVASKTYNLKKgqthtlEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdqgGQRGVIIntasvAAFEGQV---GQAAY 168
Cdd:cd11730  74 AGAILGKPLARTKP------AAWRRILDANLTGAALVLKHALALLAA------GARLVFL-----GAYPELVmlpGLSAY 136


                ....*..
gi 83715985 169 SASKGGI 175
Cdd:cd11730 137 AAAKAAL 143
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 15-94 2.24e-03

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 38.63  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  15 ITGGASGLGLATAERLVGQGASaVLLDLPNSGGEAQAKKLGNNCVFAP-ADVTSEKDVQtALALAKGKFGRVDVAVNCAG 93
Cdd:cd08951  12 ITGSSDGLGLAAARTLLHQGHE-VVLHARSQKRAADAKAACPGAAGVLiGDLSSLAETR-KLADQVNAIGRFDAVIHNAG 89


                .
gi 83715985  94 I 94
Cdd:cd08951  90 I 90
PLN00015 PLN00015
protochlorophyllide reductase
 14-163 2.39e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 38.53  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985   14 VITGGASGLGLATAERLVGQGASAVLLDLPN-SGGEAQAKKLG---NNCVFAPADVTSEKDVQTALALAKGKFGRVDVAV 89
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACRDfLKAERAAKSAGmpkDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDVLV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 83715985   90 NCAgiAVASKTynlKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnePDQGGQRGVII-----NTASVAafeGQV 163
Cdd:PLN00015  81 CNA--AVYLPT---AKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKK--SDYPSKRLIIVgsitgNTNTLA---GNV 149
PRK08703 PRK08703
SDR family oxidoreductase;
7-130 4.36e-03

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 37.60  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985    7 SVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKL---GNNCVFA-PADV--TSEKDV-QTALALAK 79
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIveaGHPEPFAiRFDLmsAEEKEFeQFAATIAE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 83715985   80 GKFGRVDVAVNCAGiavasKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIR 130
Cdd:PRK08703  83 ATQGKLDGIVHCAG-----YFYALSPLDFQTVAEWVNQYRINTVAPMGLTR 128
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 10-120 6.38e-03

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: 37.18  E-value: 6.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  10 GLVAVITGGAS--GLGLATAERLVGQGASAVLLDLPNSG-GEAQ--AKKLGNNCVFAPADVTSEKDVQTALALAKGKFGR 84
Cdd:cd05372   1 GKRILITGIANdrSIAWGIAKALHEAGAELAFTYQPEALrKRVEklAERLGESALVLPCDVSNDEEIKELFAEVKKDWGK 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 83715985  85 VDVAVNCagIAVASKTYnlKKGQTH--TLEDFQRVLDV 120
Cdd:cd05372  81 LDGLVHS--IAFAPKVQ--LKGPFLdtSRKGFLKALDI 114
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 12-246 8.55e-03

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: 36.79  E-value: 8.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  12 VAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPadvTSEKDVQTALALAKGKFGRVDVAVNC 91
Cdd:cd05361   3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQAFESENPGTKA---LSEQKPEELVDAVLQAGGAIDVLVSN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985  92 AGIAVASKTYNlkkgqTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQnepdQGGqrGVIINTASVAAFEGQVGQAAYSAS 171
Cdd:cd05361  80 DYIPRPMNPID-----GTSEADIRQAFEALSIFPFALLQAAIAQMKK----AGG--GSIIFITSAVPKKPLAYNSLYGPA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83715985 172 KGGIVGMTLPIARDLAPIGL---------------FGTPLLTSLPEKVCNFLaSQVPFpSRLGDPAEYAHLVqAIIENP- 235
Cdd:cd05361 149 RAAAVALAESLAKELSRDNIlvyaigpnffnsptyFPTSDWENNPELRERVK-RDVPL-GRLGRPDEMGALV-AFLASRr 225

                       250
                ....*....|...
gi 83715985 236 --FLNGEVIRLDG 246
Cdd:cd05361 226 adPITGQFFAFAG 238
PRK05854 PRK05854
SDR family oxidoreductase;
10-39 9.63e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 36.58  E-value: 9.63e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 83715985   10 GLVAVITGGASGLGLATAERLVGQGASAVL 39
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVIL 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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