PDXA_HYDS0
ID PDXA_HYDS0 Reviewed; 310 AA.
AC B4U950;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=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 Name=pdxA {ECO:0000250|UniProtKB:P19624}; OrderedLocusNames=HY04AAS1_0974;
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC unclassified Hydrogenobaculum.
OX NCBI_TaxID=380749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y04AAS1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Note=Binds 1 divalent metal cation per subunit.
CC {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; CP001130; ACG57661.1; -; Genomic_DNA.
DR RefSeq; WP_012514017.1; NC_011126.1.
DR AlphaFoldDB; B4U950; -.
DR SMR; B4U950; -.
DR STRING; 380749.HY04AAS1_0974; -.
DR EnsemblBacteria; ACG57661; ACG57661; HY04AAS1_0974.
DR KEGG; hya:HY04AAS1_0974; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_0_0; -.
DR OMA; TAQVVMM; -.
DR OrthoDB; 1414545at2; -.
DR UniPathway; UPA00244; UER00312.
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.
DR TIGRFAMs; TIGR00557; pdxA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; NADP; Oxidoreductase;
KW Pyridoxine biosynthesis.
FT CHAIN 1..310
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_1000146489"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 158
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 202
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 250
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 258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 310 AA; 34242 MW; 2C1FDF60B25CB139 CRC64;
MKIFGITMGD PAGIGPELIL KLQKDMEDEN AYVIYGEEYI LKHASSVLGQ NFYYEKVNSV
DDVKDKGIYL ISLSLKGALE PSPSSGKLAI AYLARATADA ISKKLNGILT MPINKYFAKA
SGFSFNGQTE YLAFADNKKD FAMMMYSDAI KVVLATIHIP LKDIANAINV ELIKQKIKLI
KDYIPKYFRF IPTIKVLGLN PHAGEGGLIG DEEAKIIIPA IRDEDVVGPI PPDTAFIDIK
KDDIFLCMYH DQGLIPFKML AFDKGSNVTI GLSFLRTSPD HGTAYDIAYK GLARVDSAGY
SLELLKRYGY
