ID PDXA_GLUOX Reviewed; 334 AA. AC Q5FNS3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536}; DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536}; GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_00536}; GN OrderedLocusNames=GOX2240; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H; RX PubMed=15665824; DOI=10.1038/nbt1062; RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., RA Ehrenreich A., Gottschalk G., Deppenmeier U.; RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). 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:0000255|HAMAP-Rule:MF_00536}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00536}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00536}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00536}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00536}; CC Note=Binds 1 divalent metal cation per subunit. Can use ions such as CC Zn(2+), Mg(2+) or Co(2+). {ECO:0000255|HAMAP-Rule:MF_00536}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. CC {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- MISCELLANEOUS: The active site is located at the dimer interface. CC {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP- CC Rule:MF_00536}. 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; CP000009; AAW61974.1; -; Genomic_DNA. DR RefSeq; WP_011253744.1; NZ_LT900338.1. DR AlphaFoldDB; Q5FNS3; -. DR SMR; Q5FNS3; -. DR STRING; 290633.GOX2240; -. DR KEGG; gox:GOX2240; -. DR eggNOG; COG1995; Bacteria. DR HOGENOM; CLU_040168_1_0_5; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000006375; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR HAMAP; MF_00536; PdxA; 1. DR InterPro; IPR037510; PdxA. 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 Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase; KW Pyridoxine biosynthesis; Reference proteome; Zinc. FT CHAIN 1..334 FT /note="4-hydroxythreonine-4-phosphate dehydrogenase" FT /id="PRO_1000051502" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 133 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 163 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 208 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 263 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 289 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" SQ SEQUENCE 334 AA; 35719 MW; B15C1C5680145CB4 CRC64; MKRPPPLALT LGDPAGIGPQ LAAEAWRRLR HSGEGIFFWL GDPRLVERAV PVTCIATPEE AAAVFADSLP VLPVPCEVEV IPGQPDSRNA AATITSIRQA VEYALAGRAG GVVTNPIAKH VLAAAGFPYP GHTEFLAALC DMPGEEIMML ASPQLRVVPV TVHVSLRRAL ETLTTERIVQ VAEIANAALR RDFGIMSPRL AIAGLNPHAG EHGMMGDEEI TIVQPAIDRL RAQGIDCRGP MPPDTMFSDK ARPHYDVAIC MYHDQALIPL KTLDMEEGVN VTLGLPIIRT SPDHGTAFDI AGPVTETCRA DVSSLLAAIW LAGEMSAYRE GRGS //