ID PDXA_HELPG Reviewed; 307 AA. AC B5Z9L3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02086}; DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_02086}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02086}; GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_02086}; GN OrderedLocusNames=HPG27_1520; OS Helicobacter pylori (strain G27). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=563041; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G27; RX PubMed=18952803; DOI=10.1128/jb.01416-08; RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S., RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.; RT "The complete genome sequence of Helicobacter pylori strain G27."; RL J. Bacteriol. 191:447-448(2009). 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_02086}. 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_02086}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_02086}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_02086}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_02086}; 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_02086}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02086}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02086}. CC -!- MISCELLANEOUS: The active site is located at the dimer interface. CC {ECO:0000255|HAMAP-Rule:MF_02086}. CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP- CC Rule:MF_02086}. 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; CP001173; ACI28262.1; -; Genomic_DNA. DR RefSeq; WP_001074972.1; NC_011333.1. DR AlphaFoldDB; B5Z9L3; -. DR SMR; B5Z9L3; -. DR KEGG; hpg:HPG27_1520; -. DR HOGENOM; CLU_040168_0_0_7; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000001735; 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_02086; PdxA_Epsilonprot; 1. DR InterPro; IPR037539; PdxA_epsilonprot. 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; Zinc. FT CHAIN 1..307 FT /note="4-hydroxythreonine-4-phosphate dehydrogenase" FT /id="PRO_1000128252" FT BINDING 126 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086" FT BINDING 127 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086" FT BINDING 156 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_02086" FT BINDING 195 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_02086" FT BINDING 251 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_02086" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086" FT BINDING 268 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086" FT BINDING 277 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086" SQ SEQUENCE 307 AA; 33734 MW; 0A8730B63654DDB2 CRC64; MAKKKIAISC GDIQGVGLEL ILKSHKEVNA FCEPLYLIDG ELLERANQLL HNAYETKTLN TLAIHSPLPL LNSSTIGKVS AQSGAYSFES FKKACELADS KEVDGICTLP INKLAWQQAQ IPFVGHTDFL KQRYKDHQII MMLGCSKLFV GLFSDHVPLG AVSQLIQVKA LVKFLLAFQK STQAKIVQVC GFNPHAGEEG LFGKEDEKIL KAIQKSNQTL GFECFLGPLP ADSAFAPNKR QITPFYVSMS HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKANNKSYL NAIKYLA //