ID   PDXA_SULSY              Reviewed;         322 AA.
AC   B2V9E6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=SYO3AOP1_0946;
OS   Sulfurihydrogenibium sp. (strain YO3AOP1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX   NCBI_TaxID=436114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YO3AOP1;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001080; ACD66569.1; -; Genomic_DNA.
DR   RefSeq; WP_012459640.1; NC_010730.1.
DR   AlphaFoldDB; B2V9E6; -.
DR   SMR; B2V9E6; -.
DR   STRING; 436114.SYO3AOP1_0946; -.
DR   EnsemblBacteria; ACD66569; ACD66569; SYO3AOP1_0946.
DR   KEGG; sul:SYO3AOP1_0946; -.
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..322
FT                   /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT                   /id="PRO_1000146493"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         161
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         206
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         259
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         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
SQ   SEQUENCE   322 AA;  35609 MW;  B5AFA28A3EAECBEE CRC64;
     MVKLAITLGD PSGINSEILL KALNKLPKRN ISYVIYGSKK ALEKAKKLTG VDLNIKEIKS
     INDVVKSGIY LINLYDLDVE FGSSSKETGK ASVVYLENAV KDVLEKKADA LITLPISKQW
     IMESGFPYAG HTDYLAEVSG AKEYAMVLMC KKLKVALITT HIPLKDVPSQ ITKEKIISKV
     RLINREFKEK FGISKPKIAI LGLNPHASDN GNIGNEEQNI ILPAVKTLRE DGIEITDPLS
     PDTAFNRYKD FDIYVAMYHD QGLIPLKLLC FRKAVNITLG LPFIRTSPDH GTGYDIAGKN
     IADPSSTIEA VELAILLKRV RK