ID PDXA_DESOH Reviewed; 338 AA. AC A8ZUN0; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 94. 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=Dole_0633; OS Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus OS oleovorans). OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales; OC Desulfosudaceae; Desulfosudis. OX NCBI_TaxID=96561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6200 / JCM 39069 / Hxd3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B., RA Richardson P.; RT "Complete sequence of Desulfococcus oleovorans Hxd3."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000859; ABW66443.1; -; Genomic_DNA. DR RefSeq; WP_012174062.1; NC_009943.1. DR AlphaFoldDB; A8ZUN0; -. DR SMR; A8ZUN0; -. DR STRING; 96561.Dole_0633; -. DR KEGG; dol:Dole_0633; -. DR eggNOG; COG1995; Bacteria. DR HOGENOM; CLU_040168_0_0_7; -. DR OrthoDB; 9801783at2; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000008561; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. 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..338 FT /note="4-hydroxythreonine-4-phosphate dehydrogenase" FT /id="PRO_1000211913" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 169 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 214 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 270 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 278 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 287 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 296 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" SQ SEQUENCE 338 AA; 35285 MW; 2F821914F8A5FDD8 CRC64; MNPRPLIGIT MGDPVGIGPE IILTALAGTS VYEKCRPLVI GDPGVLGQAM AVAGYAPVIH MTDTPETGVY RPGTISMFSP APPLSPVTWG EPTPETGGAM EAWITTAVDM AMAGAISAMV TCPINKEALK MAGSAFAGHT EMLAMRTGTN RYAMMLAGNR LRVVLVTIHT ALQNVPGLLS VDAIADTILL TVESLKQRFG MNAPRVAVAG LNPHAGEGGL FGDEEARLIT PAIEAARRKT EAAITGPWPP DTVFVKAAAG DFDAVVCMYH DQGLIPFKLL HFEDGVNTTL GLPIIRTSVD HGTAYDIAGT GRADCRSLTA AIDMAIDQAA CLGKRPAA //