ID PDXAL_RHIME Reviewed; 348 AA. AC Q92TP3; 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 4-hydroxythreonine-4-phosphate dehydrogenase 2 {ECO:0000250|UniProtKB:P19624}; DE EC=1.1.1.262 {ECO:0000250|UniProtKB:P19624}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase 2 {ECO:0000250|UniProtKB:P19624}; GN OrderedLocusNames=RB1464; ORFNames=SMb20772; 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(P)-dependent oxidation of 4-(phosphooxy)-L- CC threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which CC spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate CC (AHAP). {ECO:0000250|UniProtKB:P19624}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl CC phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58452; EC=1.1.1.262; CC Evidence={ECO:0000250|UniProtKB:P19624}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P19624}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P19624}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000250|UniProtKB:P19624}; CC Note=Binds 1 divalent metal cation per subunit. Can use ions such as CC Zn(2+), Mg(2+) or Co(2+). {ECO:0000250|UniProtKB:P19624}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. CC {ECO:0000250|UniProtKB:P19624}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19624}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19624}. CC -!- MISCELLANEOUS: The active site is located at the dimer interface. CC {ECO:0000250|UniProtKB:P19624}. CC -!- SIMILARITY: Belongs to the PdxA family. {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; CAC49864.1; -; Genomic_DNA. DR PIR; H96024; H96024. DR RefSeq; NP_438004.1; NC_003078.1. DR RefSeq; WP_010976261.1; NC_003078.1. DR AlphaFoldDB; Q92TP3; -. DR SMR; Q92TP3; -. DR EnsemblBacteria; CAC49864; CAC49864; SM_b20772. DR GeneID; 61601373; -. DR KEGG; sme:SM_b20772; -. DR PATRIC; fig|266834.11.peg.6391; -. DR eggNOG; COG1995; Bacteria. DR HOGENOM; CLU_040168_0_1_5; -. DR OrthoDB; 9801783at2; -. DR UniPathway; UPA00244; UER00312. DR PRO; PR:Q92TP3; -. DR Proteomes; UP000001976; Plasmid pSymB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR005255; PdxA_fam. DR PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR30004:SF3; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE 2-RELATED; 1. DR Pfam; PF04166; PdxA; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 3: Inferred from homology; KW Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase; KW Plasmid; Pyridoxine biosynthesis; Reference proteome; Zinc. FT CHAIN 1..348 FT /note="Putative 4-hydroxythreonine-4-phosphate FT dehydrogenase 2" FT /id="PRO_0000188823" FT BINDING 180 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 224 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 279 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" SQ SEQUENCE 348 AA; 36868 MW; 76F1B36A1AD334A2 CRC64; MTTSGADGTK ERRPVIALAM GDPAGISPEL TARLLALSDI RDAAHIIAIG DRRILDEGAR VAGVTLDLEA ASLDALDNAG TARHVFVDLA HLDPADVVRG EATLAGGTFA TRNFRTALEL AHAGKADAVC FTPFNKKAMR FAYPGYDDEI RFVADVLSFT GKVREFNVLE KVWNARVTSH IPLKDVASHL SVEAILAELK LTQACLKDAG YEEAKIAVAG LNPHAGDGGS FGMEEIDIIE PAVEKARALG FNVEGPFPAD TVFLRALKEG FNAVMTMYHD QGQIAMKIIG FDKGVTMMGG LPFPLCTPAH GTAYDIAGKG IADIGATREA ILLAARMAKK KRALSAAA //