ID PDXA_METCA Reviewed; 330 AA. AC Q3V8A3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 96. 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=MCA0603; OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylococcus. OX NCBI_TaxID=243233; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath; RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303; RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J., RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.; RT "Genomic insights into methanotrophy: the complete genome sequence of RT Methylococcus capsulatus (Bath)."; RL PLoS Biol. 2:1616-1628(2004). 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; AE017282; AAU93126.1; -; Genomic_DNA. DR RefSeq; WP_010959948.1; NC_002977.6. DR AlphaFoldDB; Q3V8A3; -. DR SMR; Q3V8A3; -. DR STRING; 243233.MCA0603; -. DR KEGG; mca:MCA0603; -. DR eggNOG; COG1995; Bacteria. DR HOGENOM; CLU_040168_1_0_6; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000006821; 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:SF5; 4-HYDROXYTHREONINE-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..330 FT /note="4-hydroxythreonine-4-phosphate dehydrogenase" FT /id="PRO_1000081868" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 135 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 330 AA; 34736 MW; 76C8BA8F1A44BD44 CRC64; MPPRLLLTSG EPAGIGPDLC VLLSRRPFPC GITVLGDPDL LESRARLLGV PIELRRVVSG DVVPPHEPGV LHVLPTRRQP GTAPGKLDPA NAAYVLETIA DGARACLAGH YDALVTAPVQ KSVINEAGIA FTGHTEFIAG ITGGSPVMML AAEGFRVALA TTHLPLAEVS RAITVERLTG VLGVLHEDLV RRFGFSRPRI LVCGLNPHAG EGGHLGGEEI TVIEPVLARL RQDGMDLTGP LPADTLFLPH NLDRADAVLA MYHDQGLPVL KYAGFSRAVN ITLGLPIIRT SVDHGTALDR AGTGQIDTGS LEEAVRVAME MATGRPAESP //