ID   PDXAL_PASMU             Reviewed;         337 AA.
AC   Q9CKG8;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Putative 4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000250|UniProtKB:P19624};
DE            EC=1.1.1.262 {ECO:0000250|UniProtKB:P19624};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000250|UniProtKB:P19624};
GN   OrderedLocusNames=PM1650;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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:0000250|UniProtKB:P19624}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC       Zn(2+), Mg(2+) or Co(2+). {ECO:0000250|UniProtKB:P19624};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC       {ECO:0000250|UniProtKB:P19624}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19624}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19624}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000250|UniProtKB:P19624}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000305}.
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DR   EMBL; AE004439; AAK03734.1; -; Genomic_DNA.
DR   RefSeq; WP_005718533.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKG8; -.
DR   SMR; Q9CKG8; -.
DR   STRING; 272843.PM1650; -.
DR   EnsemblBacteria; AAK03734; AAK03734; PM1650.
DR   GeneID; 77206571; -.
DR   KEGG; pmu:PM1650; -.
DR   HOGENOM; CLU_040168_0_1_6; -.
DR   OrthoDB; 9801783at2; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR005255; PdxA_fam.
DR   PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30004:SF3; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE 2-RELATED; 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..337
FT                   /note="Putative 4-hydroxythreonine-4-phosphate
FT                   dehydrogenase"
FT                   /id="PRO_0000188814"
FT   BINDING         172
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         216
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         271
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
SQ   SEQUENCE   337 AA;  37033 MW;  7D0955556B98D657 CRC64;
     MTKSTVALTL GDPAGIGPEL VAKLLAKQNI REKANIVLVA DKDELEKGME IAKAQFVYEE
     VSFHQLGQYE FKTGVPVLIS HKSSHPKPFE YGKVTEQSGV YILETLKVAL NLAKMGYVQA
     ICFAPLNKQA MHKGGLRYRD ELHWFAEQTD FNEFVCELNV VDDIWAARVT SHIPFKDIVP
     NLSIKGVFDC IHLLYRSLVQ AGVENPKIAV QALNPHGGEG GVFGDEEMTI IQPGMEQARK
     AGIDVYGPFP GDTTMREVER LKINGVVSMY HDQFSTALKI LGFERGVTVQ GGIPIPITTA
     NHGTAFDLHG KNIAIPTAFE AAFNIAVRMG QGVLNQK
//