dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170988132  21 LACLLQRTSPA-----------CSWFDFAQAIFQQAVRAVIVQHPPRLVPIATEAYPSPARRPAWSVLDCNDFAKRFGIA 89
Cdd:TIGR01214 193 IAALLQRLARArgvyhlansgqVSWYEFAQAIFEEAGADGLLLHPQEVKPISSKEYPRPARRPAYSVLDNTKLVKTLGLP 272

                          90
                  ....*....|....*
gi 1170988132  90 PCPWLPDLEVVIDAP 104
Cdd:TIGR01214 273 LPHWREALRRYLQEA 287

dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170988132  21 LACLLQRTSPA-----------CSWFDFAQAIFQQAVRAVIVQHPPRLVPIATEAYPSPARRPAWSVLDCNDFAKRFGIA 89
Cdd:TIGR01214 193 IAALLQRLARArgvyhlansgqVSWYEFAQAIFEEAGADGLLLHPQEVKPISSKEYPRPARRPAYSVLDNTKLVKTLGLP 272

                          90
                  ....*....|....*
gi 1170988132  90 PCPWLPDLEVVIDAP 104
Cdd:TIGR01214 273 LPHWREALRRYLQEA 287

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1170988132  29 SPACSWFDFAQAIFQQAvravivQHPPRLVPIATEAYPSPARRPAWSVLDCNDFAKRFGIAPCPW 93
Cdd:COG1091   209 SGETSWYEFARAIAELA------GLDALVEPITTAEYPTPAKRPANSVLDNSKLEATLGIKPPDW 267

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1170988132  31 ACSWFDFAQAIFQQAVRAVIvqhppRLVPIATEAYPSPARRPAWSVLDCNDFAKRFGIAPCPW 93
Cdd:cd05254   218 PISKYEFAKLIADALGLPDV-----EIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDW 275

dTDP-4-dehydrorhamnose reductase; This enzyme catalyzes the last of 4 steps in making dTDP-rhamnose, a precursor of LPS core antigen, O-antigen, etc. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170988132  21 LACLLQRTSPA-----------CSWFDFAQAIFQQAVRAVIVQHPPRLVPIATEAYPSPARRPAWSVLDCNDFAKRFGIA 89
Cdd:TIGR01214 193 IAALLQRLARArgvyhlansgqVSWYEFAQAIFEEAGADGLLLHPQEVKPISSKEYPRPARRPAYSVLDNTKLVKTLGLP 272

                          90
                  ....*....|....*
gi 1170988132  90 PCPWLPDLEVVIDAP 104
Cdd:TIGR01214 273 LPHWREALRRYLQEA 287

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1170988132  29 SPACSWFDFAQAIFQQAvravivQHPPRLVPIATEAYPSPARRPAWSVLDCNDFAKRFGIAPCPW 93
Cdd:COG1091   209 SGETSWYEFARAIAELA------GLDALVEPITTAEYPTPAKRPANSVLDNSKLEATLGIKPPDW 267

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1170988132  31 ACSWFDFAQAIFQQAVRAVIvqhppRLVPIATEAYPSPARRPAWSVLDCNDFAKRFGIAPCPW 93
Cdd:cd05254   218 PISKYEFAKLIADALGLPDV-----EIKPITSSEYPLPARRPANSSLDCSKLEELGGIKPPDW 275