ID   PDXA_ECOLI              Reviewed;         329 AA.
AC   P19624;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
DE            EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|PubMed:15026039};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
GN   Name=pdxA; OrderedLocusNames=b0052, JW0051;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2670894; DOI=10.1128/jb.171.9.4767-4777.1989;
RA   Roa B.B., Connolly D.M., Winkler M.E.;
RT   "Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 171:4767-4777(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA   Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the
RT   0-2.4 min region.";
RL   Nucleic Acids Res. 20:3305-3308(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX   DOI=10.1021/ja9742085;
RA   Cane D.E., Hsiung Y., Cornish J.A., Robinson J.K., Spenser I.D.;
RT   "Biosynthesis of vitamin B6: the oxidation of 4-hydroxy-L-threonine 4-
RT   phosphate by pdxA.";
RL   J. Am. Chem. Soc. 120:1936-1937(1998).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15026039; DOI=10.1016/j.bmcl.2004.01.065;
RA   Banks J., Cane D.E.;
RT   "Biosynthesis of vitamin B6: direct identification of the product of the
RT   PdxA-catalyzed oxidation of 4-hydroxy-L-threonine-4-phosphate using
RT   electrospray ionization mass spectrometry.";
RL   Bioorg. Med. Chem. Lett. 14:1633-1636(2004).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ZINC
RP   IONS, COFACTOR, AND SUBUNIT.
RX   PubMed=12896974; DOI=10.1074/jbc.m306344200;
RA   Sivaraman J., Li Y., Banks J., Cane D.E., Matte A., Cygler M.;
RT   "Crystal structure of Escherichia coli PdxA, an enzyme involved in the
RT   pyridoxal phosphate biosynthesis pathway.";
RL   J. Biol. Chem. 278:43682-43690(2003).
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_00536, ECO:0000269|PubMed:15026039,
CC       ECO:0000269|Ref.5}.
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_00536, ECO:0000269|PubMed:15026039};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00536, ECO:0000269|PubMed:12896974, ECO:0000269|Ref.5};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00536, ECO:0000269|PubMed:12896974, ECO:0000269|Ref.5};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00536, ECO:0000269|PubMed:12896974, ECO:0000269|Ref.5};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC       Zn(2+), Mg(2+) or Co(2+). {ECO:0000255|HAMAP-Rule:MF_00536,
CC       ECO:0000269|PubMed:12896974, ECO:0000269|Ref.5};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=85 uM for 4-(phosphooxy)-L-threonine (at 0.1 M Tris-HCl and pH
CC         7.5) {ECO:0000269|Ref.5};
CC         KM=113 uM for 4-(phosphooxy)-L-threonine (at 0.1 M phosphate buffer
CC         and pH 7.5) {ECO:0000269|Ref.5};
CC         Vmax=2.8 umol/min/mg enzyme with 4-(phosphooxy)-L-threonine as
CC         substrate (at 0.1 M Tris-HCl and pH 7.5) {ECO:0000269|Ref.5};
CC         Vmax=0.66 umol/min/mg enzyme with 4-(phosphooxy)-L-threonine as
CC         substrate (at 0.1 M phosphate buffer and pH 7.5) {ECO:0000269|Ref.5};
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_00536}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536,
CC       ECO:0000269|PubMed:12896974}.
CC   -!- INTERACTION:
CC       P19624; P19624: pdxA; NbExp=3; IntAct=EBI-1112869, EBI-1112869;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|PubMed:12896974}.
CC   -!- MISCELLANEOUS: According to PubMed:15026039, PdxA may catalyze both
CC       oxidation and decarboxylation reactions that directly lead to AHAP.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00536, ECO:0000305}.
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DR   EMBL; M68521; AAA24305.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73163.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96619.1; -; Genomic_DNA.
DR   PIR; JV0026; BVECXA.
DR   RefSeq; NP_414594.1; NC_000913.3.
DR   RefSeq; WP_000241277.1; NZ_STEB01000010.1.
DR   PDB; 1PS6; X-ray; 2.25 A; A/B=2-329.
DR   PDB; 1PS7; X-ray; 2.47 A; A/B/C/D=1-329.
DR   PDB; 1PTM; X-ray; 1.96 A; A/B=1-329.
DR   PDBsum; 1PS6; -.
DR   PDBsum; 1PS7; -.
DR   PDBsum; 1PTM; -.
DR   AlphaFoldDB; P19624; -.
DR   SMR; P19624; -.
DR   BioGRID; 4261013; 7.
DR   BioGRID; 849317; 5.
DR   DIP; DIP-10448N; -.
DR   IntAct; P19624; 5.
DR   STRING; 511145.b0052; -.
DR   DrugBank; DB02609; 4-Hydroxy-L-Threonine-5-Monophosphate.
DR   jPOST; P19624; -.
DR   PaxDb; 511145-b0052; -.
DR   EnsemblBacteria; AAC73163; AAC73163; b0052.
DR   GeneID; 944919; -.
DR   KEGG; ecj:JW0051; -.
DR   KEGG; eco:b0052; -.
DR   PATRIC; fig|1411691.4.peg.2231; -.
DR   EchoBASE; EB0685; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_1_0_6; -.
DR   InParanoid; P19624; -.
DR   OMA; FDIAYQN; -.
DR   OrthoDB; 9801783at2; -.
DR   PhylomeDB; P19624; -.
DR   BioCyc; EcoCyc:PDXA-MONOMER; -.
DR   BioCyc; MetaCyc:PDXA-MONOMER; -.
DR   BRENDA; 1.1.1.262; 2026.
DR   UniPathway; UPA00244; UER00312.
DR   EvolutionaryTrace; P19624; -.
DR   PRO; PR:P19624; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IMP:EcoCyc.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR037510; PdxA.
DR   InterPro; IPR005255; PdxA_fam.
DR   NCBIfam; TIGR00557; pdxA; 1.
DR   PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30004:SF5; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP;
KW   Oxidoreductase; Pyridoxine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..329
FT                   /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT                   /id="PRO_0000188804"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000269|PubMed:12896974"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000269|PubMed:12896974"
FT   BINDING         166
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_00536,
FT                   ECO:0000305|PubMed:12896974"
FT   BINDING         211
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_00536,
FT                   ECO:0000305|PubMed:12896974"
FT   BINDING         266
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_00536,
FT                   ECO:0000305|PubMed:12896974"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000269|PubMed:12896974"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000269|PubMed:12896974"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00536,
FT                   ECO:0000269|PubMed:12896974"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           18..25
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           40..49
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           93..109
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           123..128
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           136..143
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          150..157
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           178..194
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           210..216
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           221..224
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           226..235
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          239..244
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          259..265
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           266..274
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   STRAND          282..294
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   HELIX           301..303
FT                   /evidence="ECO:0007829|PDB:1PTM"
FT   TURN            304..306
FT                   /evidence="ECO:0007829|PDB:1PS7"
FT   HELIX           312..328
FT                   /evidence="ECO:0007829|PDB:1PTM"
SQ   SEQUENCE   329 AA;  35114 MW;  44E1FEE233C86233 CRC64;
     MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTNRAAML GLPLTLRPYS
     PNSPAQPQTA GTLTLLPVAL RAPVTAGQLA VENGHYVVET LARACDGCLN GEFAALITGP
     VHKGVINDAG IPFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR DIADAITPAL
     LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL NELRAQGMKL
     NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
     LELAGRGKAD VGSFITALNL AIKMIVNTQ
//