ID A0A2M7SFQ4_9DELT Unreviewed; 345 AA. AC A0A2M7SFQ4; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 16-JAN-2019, entry version 6. DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956571}; DE EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956565}; 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; Proteobacteria; 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., RA Stieglmeier M., Klingl A., Woyke T., Ryan C.M., Banfield J.F.; RT "Depth-based differentiation of microbial function through sediment- RT hosted aquifers and enrichment of novel symbionts in the deep RT terrestrial subsurface."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4- CC (phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4- CC (phosphooxy)butyric acid which spontaneously decarboxylates to CC form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000256|HAMAP- CC Rule:MF_00536, ECO:0000256|SAAS:SAAS01062167}. 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, ECO:0000256|SAAS:SAAS01115138}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00536}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00536}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00536}; CC Note=Binds 1 divalent metal cation per subunit. Can use ions such CC as Zn(2+), Mg(2+) or Co(2+). {ECO:0000256|HAMAP-Rule:MF_00536}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4- CC phosphate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00536, CC ECO:0000256|SAAS:SAAS00956575}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536, CC ECO:0000256|SAAS:SAAS00956582}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536, CC ECO:0000256|SAAS:SAAS00956573}. 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, ECO:0000256|SAAS:SAAS00701249}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 HAMAP; MF_00536; PdxA; 1. DR InterPro; IPR037510; PdxA. DR InterPro; IPR005255; PdxA_fam. DR PANTHER; PTHR30004; PTHR30004; 1. DR Pfam; PF04166; PdxA; 1. DR TIGRFAMs; TIGR00557; pdxA; 1. PE 3: Inferred from homology; KW Cobalt {ECO:0000256|HAMAP-Rule:MF_00536}; KW Complete proteome {ECO:0000313|Proteomes:UP000231291}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00956585}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00536}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00701256}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00701266}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956572}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00701261}; KW Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00956552}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00536}. FT METAL 169 169 Divalent metal cation; shared with FT dimeric partner. {ECO:0000256|HAMAP-Rule: FT MF_00536}. FT METAL 214 214 Divalent metal cation; shared with FT dimeric partner. {ECO:0000256|HAMAP-Rule: FT MF_00536}. FT METAL 269 269 Divalent metal cation; shared with FT dimeric partner. {ECO:0000256|HAMAP-Rule: FT MF_00536}. FT BINDING 139 139 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00536}. FT BINDING 140 140 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00536}. FT BINDING 277 277 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00536}. FT BINDING 286 286 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00536}. FT BINDING 295 295 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //