ID PDXA_SACD2 Reviewed; 335 AA. AC Q21MS9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 02-SEP-2026, entry version 102. 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=Sde_0738; OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Cellvibrionales; Cellvibrionaceae; Saccharophagus. OX NCBI_TaxID=203122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-40 / ATCC 43961 / DSM 17024; RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087; RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., RA Richardson P.M., Borovok I., Hutcheson S.; RT "Complete genome sequence of the complex carbohydrate-degrading marine RT bacterium, Saccharophagus degradans strain 2-40 T."; RL PLoS Genet. 4:E1000087-E1000087(2008). 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; CP000282; ABD80000.1; -; Genomic_DNA. DR RefSeq; WP_011467221.1; NC_007912.1. DR AlphaFoldDB; Q21MS9; -. DR SMR; Q21MS9; -. DR STRING; 203122.Sde_0738; -. DR GeneID; 98612423; -. DR KEGG; sde:Sde_0738; -. DR eggNOG; COG1995; Bacteria. DR HOGENOM; CLU_040168_2_0_6; -. DR OrthoDB; 9801783at2; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000001947; 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 5'-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..335 FT /note="4-hydroxythreonine-4-phosphate dehydrogenase" FT /id="PRO_1000051513" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 136 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 165 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 210 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 265 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 273 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 282 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" SQ SEQUENCE 335 AA; 35022 MW; 2C97F33B5DF966A5 CRC64; MSHPAIIALT PGEPAGIGPD LTVMAAQQAR DYPLVALCDP QLLKDRAKLL GLPLTVSTYI QGSAVTTSAQ HISVMPIPLG APCEAGTLDS TNAAYVIETL KQATEGCLSG EFAAVVTGPV QKSVINEAGI NFSGHTEYFA DNSNTPRVVM MLATEGLRVA LATTHLPLKD VSAAITTASL TETLNILLAD LQLKFGLSQP RVLVCGLNPH AGEGGHLGME EIDTIIPVLE QFRARGHNLV GPLPADTLFN PKYLSDADAV LAMYHDQGLP VLKYKGFGNA VNITLGLPFI RTSVDHGTAL DLAGTGKANI GSLQVALGYA QNLAMQQASI NEIAG //