PDXAL_PASMU
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 03-AUG-2022, entry version 115.
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; Proteobacteria; 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; 747.DR93_712; -.
DR EnsemblBacteria; AAK03734; AAK03734; PM1650.
DR KEGG; pmu:PM1650; -.
DR HOGENOM; CLU_040168_0_1_6; -.
DR OMA; CGREEID; -.
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 InterPro; IPR005255; PdxA_fam.
DR PANTHER; PTHR30004; PTHR30004; 1.
DR Pfam; PF04166; PdxA; 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
