ID T5CRI6_HELPX Unreviewed; 307 AA.
AC T5CRI6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02086};
DE EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_02086};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02086};
GN Name=pdxA {ECO:0000256|HAMAP-Rule:MF_02086,
GN ECO:0000313|EMBL:EQL57506.1};
GN ORFNames=N411_03855 {ECO:0000313|EMBL:EQL57506.1};
OS Helicobacter pylori FD535.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191464 {ECO:0000313|EMBL:EQL57506.1, ECO:0000313|Proteomes:UP000015966};
RN [1] {ECO:0000313|EMBL:EQL57506.1, ECO:0000313|Proteomes:UP000015966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD535 {ECO:0000313|EMBL:EQL57506.1,
RC ECO:0000313|Proteomes:UP000015966};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL57506.1, ECO:0000313|Proteomes:UP000015966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD535 {ECO:0000313|EMBL:EQL57506.1,
RC ECO:0000313|Proteomes:UP000015966};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(2013).
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_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:0000256|HAMAP-
CC Rule:MF_02086};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02086};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02086};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_02086}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02086}.
CC -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC {ECO:0000256|HAMAP-Rule:MF_02086}.
CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP-
CC Rule:MF_02086}.
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:EQL57506.1}.
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DR EMBL; AKHP02000017; EQL57506.1; -; Genomic_DNA.
DR RefSeq; WP_001075086.1; NZ_AKHP02000017.1.
DR AlphaFoldDB; T5CRI6; -.
DR PATRIC; fig|1191464.11.peg.1334; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000015966; 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_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 {ECO:0000256|HAMAP-Rule:MF_02086};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02086};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02086};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02086}; NAD {ECO:0000256|HAMAP-Rule:MF_02086};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_02086};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02086}; Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02086};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02086}.
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02086"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_02086"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02086"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02086"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02086"
SQ SEQUENCE 307 AA; 33622 MW; 708E92828B3B5857 CRC64;
MAKKKIAISC GDVQGVGLEL ILKSHKEVSA LCEPLYLIDG ELLERANQLL HNAYETKTLN
TLAINSPLPL LNSSTIGKVS AQSGAYSFES FKKACELADN KEVDGICTLP INKLAWQQAQ
IPFVGHTDFL KQRYKDHQII MMLGCSKLFV GLFSDHVPLG AVSQLIQVGA LVKFLLAFQK
STQAKIVQVC GFNPHAGEEG LFGEEDERIL KAIQKSNQTL GFECFLGPLP ADSAFAPNKR
KITPFYVSMS HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKADNKSYL
NAIKYLA
//
