ID   PDXA_NEIMB              Reviewed;         329 AA.
AC   Q9K1F9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   16-JUN-2009, entry version 47.
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=NMB0195;
OS   Neisseria meningitidis serogroup B.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58 / Serogroup B;
RX   MEDLINE=20175755; PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA   Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA   Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA   Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA   Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA   Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA   Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA   Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA   Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF40652.1; ALT_INIT; Genomic_DNA.
DR   PIR; H81227; H81227.
DR   RefSeq; NP_273253.1; -.
DR   GeneID; 902303; -.
DR   GenomeReviews; AE002098_GR; NMB0195.
DR   KEGG; nme:NMB0195; -.
DR   NMPDR; fig|122586.1.peg.187; -.
DR   TIGR; NMB0195; -.
DR   HOGENOM; Q9K1F9; -.
DR   BioCyc; NMEN122586:NMB_0195-MON; -.
DR   BRENDA; 1.1.1.262; 293828.
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    329       4-hydroxythreonine-4-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_0000188812.
FT   METAL       166    166       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       211    211       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       266    266       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     274    274       Substrate (By similarity).
FT   BINDING     283    283       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
SQ   SEQUENCE   329 AA;  34505 MW;  0126A0A7D7B16DDC CRC64;
     MKQPVFAVTS GEPAGIGPDI CLDLAFARLP CRCAVLGDKN LLRARAEALG KSVVLRDFDP
     ESGGAAYGEL EVLHIPAVEA VEAGKLNPAN AAYVLQLLDT ALAGISDGIF DGIVTAPLHK
     GIINDARAST GFFSGHTEYL AEKSGTGQVV MMLAGKGLRV ALVTTHLPLK DVAAAITQPL
     IESVARILHH DLKHKFGIKN PKILVAGLNP HAGEGGHLGH EETDTIIPAL ENLRREGINL
     AGPYPADTLF QPFMLEGADA VLAMYHDQGL PVLKYHSFGQ GVNITLGLPF IRTSVDHGTA
     LDLAATGRAD SGSLITAVET AVEMARGSL
//