ID   PDXA_AQUAE              Reviewed;         320 AA.
AC   O67019;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=aq_852;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06973.1; -; Genomic_DNA.
DR   PIR; H70373; H70373.
DR   RefSeq; NP_213580.1; NC_000918.1.
DR   RefSeq; WP_010880518.1; NC_000918.1.
DR   AlphaFoldDB; O67019; -.
DR   SMR; O67019; -.
DR   STRING; 224324.aq_852; -.
DR   EnsemblBacteria; AAC06973; AAC06973; aq_852.
DR   KEGG; aae:aq_852; -.
DR   PATRIC; fig|224324.8.peg.667; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_0_0_0; -.
DR   InParanoid; O67019; -.
DR   OMA; TAQVVMM; -.
DR   OrthoDB; 1414545at2; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000000798; Chromosome.
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; Reference proteome.
FT   CHAIN           1..320
FT                   /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT                   /id="PRO_0000188796"
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         205
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="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         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
SQ   SEQUENCE   320 AA;  35914 MW;  9A31DCECB3EA0AE0 CRC64;
     MNKKIGITLG DPAGIGPELI LKISKHFKEK FTYVIYGEEK TLLEASKLTG IKLNYKKIEK
     VEEAKERGVY LIDLNVLKVP VVEPSVSSGK AAVAYLARAV ADAIRGNIHG ILTMPINKFW
     AKKAGFQYEG QTEFLAKASG TKDYAMMMYS EKLKVVLLTT HIPLKDVPNY VKKEEILKKV
     RLIRKEFLEK FKFEPLIKVL GLNPHAGEMG ELGREEIEEI IPAVEEAKKE GIKVVGPLVP
     DVAFINPSEE DVFLCMYHDQ GLIPFKMLAF DEGVNFTLGL PFIRTSPDHG TAYDIAWKNK
     ARESSSLHAL RLIEDLLDKI