ID   PDXA_CAMJE              Reviewed;         364 AA.
AC   Q9PN58; Q0P917;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=Cj1239;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
RN   [2] {ECO:0007744|PDB:3TSN}
RP   X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) IN COMPLEX WITH NICKEL.
RA   Osipiuk J., Gu M., Kwon K., Anderson W.F., Joachimiak A.;
RT   "4-hydroxythreonine-4-phosphate dehydrogenase from Campylobacter jejuni.";
RL   Submitted (SEP-2011) to the PDB data bank.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02086};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02086};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-
CC         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; AL111168; CAL35354.1; -; Genomic_DNA.
DR   PIR; A81331; A81331.
DR   RefSeq; WP_002853162.1; NZ_SZUC01000001.1.
DR   RefSeq; YP_002344630.1; NC_002163.1.
DR   PDB; 3TSN; X-ray; 2.63 A; A/B/C/D=1-364.
DR   PDBsum; 3TSN; -.
DR   AlphaFoldDB; Q9PN58; -.
DR   SMR; Q9PN58; -.
DR   IntAct; Q9PN58; 2.
DR   STRING; 192222.Cj1239; -.
DR   PaxDb; 192222-Cj1239; -.
DR   EnsemblBacteria; CAL35354; CAL35354; Cj1239.
DR   GeneID; 905530; -.
DR   KEGG; cje:Cj1239; -.
DR   PATRIC; fig|192222.6.peg.1221; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_0_0_7; -.
DR   OrthoDB; 9801783at2; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000000799; 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   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_02086; PdxA_Epsilonprot; 1.
DR   InterPro; IPR037539; PdxA_epsilonprot.
DR   InterPro; IPR005255; PdxA_fam.
DR   PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30004:SF6; D-THREONATE 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..364
FT                   /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT                   /id="PRO_0000188802"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT   BINDING         177
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                   ECO:0000305|Ref.2"
FT   BINDING         216
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                   ECO:0000305|Ref.2"
FT   BINDING         301
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                   ECO:0000305|Ref.2"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   TURN            11..14
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           38..48
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          54..62
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          67..73
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          75..84
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           103..121
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           135..140
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           148..156
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          169..175
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           183..186
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           189..203
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          206..211
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           215..218
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   TURN            219..222
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           226..244
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           248..254
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           258..266
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           281..284
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           287..292
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           301..311
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   TURN            313..315
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          317..325
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:3TSN"
FT   HELIX           348..359
FT                   /evidence="ECO:0007829|PDB:3TSN"
SQ   SEQUENCE   364 AA;  41387 MW;  DDD26465821FFC3E CRC64;
     MKKLAISIGD INSIGLEILV RSHEELSKIC TPFYFIHESL LNKALKLLNL KLFNAKIVAF
     KDDKDYEFNF IKKENSLEIY SFCLPLGFKV DENFEIQAGE IDAKSGLYGF LSFKAASYFV
     YEKHAHALLT LPIHKKAWED AGLKYKGHTD ALRDFFKKNA IMMLGCKELF VGLFSEHIPL
     AKVSKKITFK NLSIFLKDFY KETHFKKMGL LGFNPHAGDY GVIGGEEEKI MEKAIAFVNA
     FLHSKKDEKF FKKALKDENL QKELLLNFKG KGVYLPYPLV ADTAFTKTGL KNCNRLVAMY
     HDLALAPLKA LYFDKSINVS LNLPIIRVSV DHGTAFDKAY KNAKINTKSY FEAAKFAINL
     HSKA
//