ID PDXA_HELPH Reviewed; 307 AA.
AC Q1CR24;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02086};
DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_02086};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02086};
GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_02086}; OrderedLocusNames=HPAG1_1531;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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_02086}.
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_02086};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02086};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02086};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02086};
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_02086}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02086}.
CC -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC {ECO:0000255|HAMAP-Rule:MF_02086}.
CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP-
CC Rule:MF_02086}.
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DR EMBL; CP000241; ABF85598.1; -; Genomic_DNA.
DR RefSeq; WP_001074979.1; NC_008086.1.
DR AlphaFoldDB; Q1CR24; -.
DR SMR; Q1CR24; -.
DR KEGG; hpa:HPAG1_1531; -.
DR HOGENOM; CLU_040168_0_0_7; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000008835; 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 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_02086; PdxA_Epsilonprot; 1.
DR InterPro; IPR037539; PdxA_epsilonprot.
DR InterPro; IPR005255; PdxA_fam.
DR NCBIfam; TIGR00557; pdxA; 1.
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.
PE 3: Inferred from homology;
KW Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase;
KW Pyridoxine biosynthesis; Zinc.
FT CHAIN 1..307
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_1000051504"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 156
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_02086"
FT BINDING 195
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_02086"
FT BINDING 251
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_02086"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
SQ SEQUENCE 307 AA; 33780 MW; 8DCBBA3ABAE3B4A5 CRC64;
MAKKKIAISC GDIQGVGLEL ILKSHKEVSA FCEPLYLIDG ELLERANQLL HNAYETKTLN
TLAIHSPLPL LNSSTIGKVS AQSGAYSFES FKKACELADD KEVDGVCTLP INKLAWQQAQ
IPFVGHTDFL KQRYKDHQII MMLGCSKLFV GLFSDHVPLG AVSQLIQVKE LVKFLLAFQK
STQAKIVQVC GFNPHAGEEG LFGEEDEKIL KAIQKSNQTL GFECFLGPLP ADSAFAPNKR
KITPFYVSMS HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKANNKSYL
NAIKYLA
//
