Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    199 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 270
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    271 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaepeteaicfFVQQFTDMEHNrvLEALLP---- 346
Cdd:pfam00975  79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    347 LKGLEERVAAAVDLIIKSHQGLDRQelsfaarsfyykLRAAEQYTPKAKYHGNVMLlraktggtygqdlgaDYNLSQVCD 426
Cdd:pfam00975 141 LSMLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTP 193

                         250
                  ....*....|....*....
gi 1245769    427 GKVSVHVIEGDHRTLLEGS 445
Cdd:pfam00975 194 GEFDVHVFDGDHFYLIEHL 212

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1245769      68 LAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 136
Cdd:smart00823   1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    199 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 270
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    271 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaepeteaicfFVQQFTDMEHNrvLEALLP---- 346
Cdd:pfam00975  79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    347 LKGLEERVAAAVDLIIKSHQGLDRQelsfaarsfyykLRAAEQYTPKAKYHGNVMLlraktggtygqdlgaDYNLSQVCD 426
Cdd:pfam00975 141 LSMLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTP 193

                         250
                  ....*....|....*....
gi 1245769    427 GKVSVHVIEGDHRTLLEGS 445
Cdd:pfam00975 194 GEFDVHVFDGDHFYLIEHL 212

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1245769    2 SGKRRHEGLPGLAVQWGAIGHVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMVLSSFVLA 69
Cdd:cd08954 382 SRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLVLSSFNFA 452

enterobactin non-ribosomal peptide synthetase EntF;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769     83 DLVEAVAHILGirdLAAVNLDSSLADLGLDSLMSVEVRQTLERELNlvlsvrevRQLTLRKLQELSSKADEASELAcptp 162
Cdd:PRK10252  982 IIAAAFSSLLG---CDVVDADADFFALGGHSLLAMKLAAQLSRQFA--------RQVTPGQVMVASTVAKLATLLD---- 1046

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    163 kEDGLAQQQTQLNLRSLLVNPEGPTLmrlnsvqsserplFLVHPIEGSTTVFHSLASRLS--IPTYGLQCTR---AAPL- 236
Cdd:PRK10252 1047 -AEEDESRRLGFGTILPLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSPRpdgPMQTa 1112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    237 DSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQqspAPTHNSLFLFDGSPtyvlAYTQSYRAKltPGC 316
Cdd:PRK10252 1113 TSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR---GEEVAFLGLLDTWP----PETQNWREK--EAN 1183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1245769    317 EAEPETEAicffvqqftDMEHNR-----VLEALLP---LKGLEERVAAAVDLIIKSHQ 366
Cdd:PRK10252 1184 GLDPEVLA---------EIDREReaflaAQQGSLStelFTTIEGNYADAVRLLTTAHS 1232

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1245769   84 LVEAVAHILGIrDLAAVNLDSSL-ADLGLDSLMSVEVRQTLERELNLVLSVREVRQL-TLRKL 144
Cdd:COG0236  10 LAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    199 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 270
Cdd:pfam00975   1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    271 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaepeteaicfFVQQFTDMEHNrvLEALLP---- 346
Cdd:pfam00975  79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    347 LKGLEERVAAAVDLIIKSHQGLDRQelsfaarsfyykLRAAEQYTPKAKYHGNVMLlraktggtygqdlgaDYNLSQVCD 426
Cdd:pfam00975 141 LSMLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTP 193

                         250
                  ....*....|....*....
gi 1245769    427 GKVSVHVIEGDHRTLLEGS 445
Cdd:pfam00975 194 GEFDVHVFDGDHFYLIEHL 212

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1245769    2 SGKRRHEGLPGLAVQWGAIGHVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMVLSSFVLA 69
Cdd:cd08954 382 SRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLVLSSFNFA 452

enterobactin non-ribosomal peptide synthetase EntF;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769     83 DLVEAVAHILGirdLAAVNLDSSLADLGLDSLMSVEVRQTLERELNlvlsvrevRQLTLRKLQELSSKADEASELAcptp 162
Cdd:PRK10252  982 IIAAAFSSLLG---CDVVDADADFFALGGHSLLAMKLAAQLSRQFA--------RQVTPGQVMVASTVAKLATLLD---- 1046

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    163 kEDGLAQQQTQLNLRSLLVNPEGPTLmrlnsvqsserplFLVHPIEGSTTVFHSLASRLS--IPTYGLQCTR---AAPL- 236
Cdd:PRK10252 1047 -AEEDESRRLGFGTILPLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSPRpdgPMQTa 1112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245769    237 DSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQqspAPTHNSLFLFDGSPtyvlAYTQSYRAKltPGC 316
Cdd:PRK10252 1113 TSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR---GEEVAFLGLLDTWP----PETQNWREK--EAN 1183

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1245769    317 EAEPETEAicffvqqftDMEHNR-----VLEALLP---LKGLEERVAAAVDLIIKSHQ 366
Cdd:PRK10252 1184 GLDPEVLA---------EIDREReaflaAQQGSLStelFTTIEGNYADAVRLLTTAHS 1232

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1245769   84 LVEAVAHILGIrDLAAVNLDSSL-ADLGLDSLMSVEVRQTLERELNLVLSVREVRQL-TLRKL 144
Cdd:COG0236  10 LAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 1245769    5 RRHEGLPGLAVQWGAIGHVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVL 63
Cdd:cd05274 311 RRRRGLPATSVQWGAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQA 369