ID A0A2M7SFQ4_9DELT Unreviewed; 345 AA. AC A0A2M7SFQ4; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 03-MAY-2023, entry version 15. DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536}; DE EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536}; GN Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536, GN ECO:0000313|EMBL:PIZ18367.1}; GN ORFNames=COY50_15705 {ECO:0000313|EMBL:PIZ18367.1}; OS Deltaproteobacteria bacterium CG_4_10_14_0_8_um_filter_43_12. OC Bacteria; Pseudomonadota; Deltaproteobacteria. OX NCBI_TaxID=1973958 {ECO:0000313|EMBL:PIZ18367.1, ECO:0000313|Proteomes:UP000231291}; RN [1] {ECO:0000313|EMBL:PIZ18367.1, ECO:0000313|Proteomes:UP000231291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CG_4_10_14_0_8_um_filter_43_12 {ECO:0000313|EMBL:PIZ18367.1}; RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M., RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M., RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.; RT "Depth-based differentiation of microbial function through sediment-hosted RT aquifers and enrichment of novel symbionts in the deep terrestrial RT subsurface."; RL Submitted (SEP-2017) 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:0000256|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:0000256|HAMAP- CC Rule:MF_00536}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00536}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00536}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|HAMAP-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:0000256|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:0000256|HAMAP-Rule:MF_00536}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536}. CC -!- MISCELLANEOUS: The active site is located at the dimer interface. CC {ECO:0000256|HAMAP-Rule:MF_00536}. CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP- CC Rule:MF_00536}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PIZ18367.1}. 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; PFMT01000457; PIZ18367.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2M7SFQ4; -. DR EnsemblBacteria; PIZ18367; PIZ18367; COY50_15705. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000231291; Unassembled WGS sequence. 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 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. DR TIGRFAMs; TIGR00557; pdxA; 1. PE 3: Inferred from homology; KW Cobalt {ECO:0000256|HAMAP-Rule:MF_00536}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00536}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00536}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00536}; NAD {ECO:0000256|HAMAP-Rule:MF_00536}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00536}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00536}; Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00536}. FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00536" FT BINDING 269 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536" FT BINDING 277 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536" FT BINDING 286 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536" FT BINDING 295 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536" SQ SEQUENCE 345 AA; 37054 MW; 9F4FD063EB3CDBCE CRC64; MELPVIGITM GDPAGVGPEI IVKALSDPQI FKICRPLVLG DQGIIAKAAQ ILGLEIKVNV AKDIRSGRYE VGAINVLNLS NLDASAVAWG KPDERFGKAV VGYIKAGTKL ALEGETEAIT TAPINKEVIN RAGYAYAGHT ELFAELTHTK DYVMMLTGEK LRVALVTTHC RLKDVAALLN TQRIFTIIKV TNNSLKEYFA ISKPRIAVAS LNPHAGEGGM FGDEEDRIIA PAINRAKDAG IHAIGPLPSD TLFYYASRGD YDVVVCMYHD QGLIPLKLLS FQNAVNVTLG LPIIRTSVDH GTAYDIAGTG KANPESLKKA ITLAASMANK RRKLSKDMSG NLTLC //