PDXA_HELAH
ID PDXA_HELAH Reviewed; 310 AA.
AC Q17ZN0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Hac_0032;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(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; AM260522; CAJ98896.1; -; Genomic_DNA.
DR RefSeq; WP_011577018.1; NC_008229.1.
DR AlphaFoldDB; Q17ZN0; -.
DR SMR; Q17ZN0; -.
DR STRING; 382638.Hac_0032; -.
DR PRIDE; Q17ZN0; -.
DR EnsemblBacteria; CAJ98896; CAJ98896; Hac_0032.
DR KEGG; hac:Hac_0032; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_0_7; -.
DR OMA; PINKLAW; -.
DR OrthoDB; 1414545at2; -.
DR BioCyc; HACI382638:HAC_RS00155-MON; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000000775; 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 HAMAP; MF_02086; PdxA_Epsilonprot; 1.
DR InterPro; IPR037539; PdxA_epsilonprot.
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; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase;
KW Pyridoxine biosynthesis; Zinc.
FT CHAIN 1..310
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_1000051503"
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 310 AA; 34293 MW; 3FBFB4E3817BF438 CRC64;
MVKKKIAISC GDIQGIGLEL ILKSHKEVSV LCEPLYLIHS ELLGRANQLL TNAYEVKPLN
AIAINSPLPS FNSSTIGKVS AQSGAYSFES FRKACELADD KEVDSICTMP INKLAWQQAQ
IPFVGHTDFL KQRYKEHQII MMLGCPKLFV GLFSDHVPLR AVSQLIQVKA LVQFLLAFQK
STQAQIIQVC GFNPHAGEEG LFGEEDEKIL KAIQESNQTL GFECFLGPLP ADSAFAPNKR
QITPFYVSMS HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKANNKSYL
NAIKYLSQRL
