ID   PDXA_CAMFF              Reviewed;         307 AA.
AC   A0RNS3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase;
DE            EC=1.1.1.262;
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase;
GN   Name=pdxA; OrderedLocusNames=CFF8240_0681;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
CC       (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
CC       (phosphohydroxy)butyric acid which spontaneously decarboxylates to
CC       form 3-amino-2-oxopropyl phosphate (AHAP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4-(phosphonooxy)-L-threonine + NAD(+) = (2S)-
CC       2-amino-3-oxo-4-phosphonooxybutanoate + NADH.
CC   -!- COFACTOR: Binds 1 divalent metal cation per subunit. Can use ions
CC       such as zinc, magnesium or cobalt (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the pdxA family.
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DR   EMBL; CP000487; ABK83061.1; -; Genomic_DNA.
DR   RefSeq; YP_891856.1; -.
DR   GeneID; 4538213; -.
DR   GenomeReviews; CP000487_GR; CFF8240_0681.
DR   KEGG; cff:CFF8240_0681; -.
DR   NMPDR; fig|360106.5.peg.644; -.
DR   TIGR; CFF8240_0681; -.
DR   OMA; A0RNS3; DKSINVS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenas...; IEA:HAMAP.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00536; -; 1.
DR   InterPro; IPR005255; PyrdxlP_synth_PdxA.
DR   Pfam; PF04166; PdxA; 1.
DR   TIGRFAMs; TIGR00557; pdxA; 1.
PE   3: Inferred from homology;
KW   Cobalt; Complete proteome; Cytoplasm; Magnesium; Metal-binding; NAD;
KW   NADP; Oxidoreductase; Pyridoxine biosynthesis; Zinc.
FT   CHAIN         1    307       4-hydroxythreonine-4-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_1000051492.
FT   METAL       150    150       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       189    189       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       246    246       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   BINDING     121    121       Substrate (By similarity).
FT   BINDING     122    122       Substrate (By similarity).
FT   BINDING     254    254       Substrate (By similarity).
FT   BINDING     263    263       Substrate (By similarity).
FT   BINDING     272    272       Substrate (By similarity).
SQ   SEQUENCE   307 AA;  33925 MW;  A3439845911CFA96 CRC64;
     MSLPKIAISV GDINGVGIEI ALKSHDEIKN ICSPIYFINN ELLNSAANIL KFTVPNDFEI
     FECGSSFNIK PGRVSKKSGK FSFVSFENAI LYTQNKRAQA LVTMPINKES WKKAGVPYVG
     HTDALGKYFG KNAIMMLGCE ELFVALYTDH LALKDVSAKI KAKNLALFLV DFYNSSKFEN
     IGVLGFNPHA SDNETIGGKE EKEIIKAIKS ANNRLKKEVF TGPLVPDAAF TKSSLKRCNR
     LVSMYHDVGL APLKALYFDK SINVSLNLPI VRTSVDHGTA FDIAYKGKAE TKSYIEAIKF
     AIKLCDY
//