ID PDXA2_RHIME Reviewed; 321 AA. AC Q92X16; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Putative D-threonate 4-phosphate dehydrogenase {ECO:0000250|UniProtKB:P58718}; DE EC=1.1.1.408 {ECO:0000250|UniProtKB:P58718}; GN Name=pdxA2 {ECO:0000312|EMBL:CAC48546.1}; OrderedLocusNames=RB0146; GN ORFNames=SMb20146; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymB (megaplasmid 2). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing RT endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation and subsequent CC decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone CC phosphate (DHAP). {ECO:0000250|UniProtKB:P58718}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-O-phospho-D-threonate + NAD(+) = CO2 + dihydroxyacetone CC phosphate + NADH; Xref=Rhea:RHEA:52396, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:136590; EC=1.1.1.408; CC Evidence={ECO:0000250|UniProtKB:P58718}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P19624}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000250|UniProtKB:P19624}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P58718}. CC -!- SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL591985; CAC48546.1; -; Genomic_DNA. DR PIR; B95860; B95860. DR RefSeq; NP_436686.1; NC_003078.1. DR RefSeq; WP_003532057.1; NC_003078.1. DR AlphaFoldDB; Q92X16; -. DR SMR; Q92X16; -. DR EnsemblBacteria; CAC48546; CAC48546; SM_b20146. DR GeneID; 61600161; -. DR KEGG; sme:SM_b20146; -. DR PATRIC; fig|266834.11.peg.5061; -. DR eggNOG; COG1995; Bacteria. DR HOGENOM; CLU_040168_0_1_5; -. DR OrthoDB; 9801783at2; -. DR PRO; PR:Q92X16; -. DR Proteomes; UP000001976; Plasmid pSymB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR005255; PdxA_fam. DR NCBIfam; TIGR00557; pdxA; 1. DR PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR30004:SF6; D-THREONATE 4-PHOSPHATE DEHYDROGENASE; 1. DR Pfam; PF04166; PdxA; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase; Plasmid; KW Reference proteome. FT CHAIN 1..321 FT /note="Putative D-threonate 4-phosphate dehydrogenase" FT /id="PRO_0000188822" FT BINDING 123 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 153 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 197 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 252 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 269 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" SQ SEQUENCE 321 AA; 33689 MW; F6C54F187F325110 CRC64; MSKIIGITMG DPCGVGPEIT VRSLAEMSAA DREATRIYGN LATLEAAREA LGLSVDLQPY VVDLTVEGAP LPWGSLSAVA GDAAFRFIER AVRDAEAGNI GCIVTAPINK EALNMAGHHY DGHTGMLRSL TGSSAAYMLL ASERLKVIHV STHVSLKEAI GRATTERVLA TIRAGNAHLK RIGYEHPRIA VAGINPHCGE NGLFGTEDDD QIGPAVAAAR EEGIDVQGPI SADTVFHRAY SGGFDLVVAQ YHDQGHIPIK LVAFDTAVNV SVDLPIDRTS VDHGTAFDIA GKGIANHGNL NSAIAYARKL VAGQASRKAA S //