ID   AROA1_BURPS    STANDARD;      PRT;   451 AA.
AC   Q63X54;
DT   01-FEB-2005 (Rel. 46, Created)
DT   01-FEB-2005 (Rel. 46, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-
DE   enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS).
GN   Name=aroA; OrderedLocusNames=BPSL0683;
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=28450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC   -!- PATHWAY: Aromatic amino acids biosynthesis; shikimate pathway;
CC       sixth step.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable).
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; BX571965; CAH34676.1; -.
DR   HAMAP; MF_00210; -; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; FALSE_NEG.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
KW   Aromatic amino acid biosynthesis; Complete proteome; Transferase.
SQ   SEQUENCE   451 AA;  48627 MW;  E1B61DE73CCC5233 CRC64;
     MTTSDRLQPS FVEVKNTSTL SGTIDLPASK SSSTRALLTA ALTPGISTIR NVATGFNSNA
     MKHNCERLGA SFSSEGDTTV VKGVDVMHVD REIVFDPGNS GVVLRLLMGV AGYLPDTRFV
     TQYRYSLGVR SQAEMVAALR RLNVECEAVG PEARLPISMR STRALGKHTE VSCKKSSQFL
     SGLLYLGAIG ERDLEIDVVD HITAPSMVHT TINNLAHAGV AVEYDAAFRR FFVPGRDRFK
     PSEFTVGADP ASTAAILALC GSLASDVTLN GFFEEELGSG AVIRYLTDTG TLIDELPGNR
     IRIRGGASIR AQDFDGSLAP DAVPALAGRA AFAEGTSTFY NIEHIRYKES DRISDFRREL
     DKLGVRSEEK LDQLIIHGNP RSYRGGAVVD GHYDHGLIMA LTTIGLHCEH PVLIKEPHHV
     GQTYPDYFAD IGSIGANVDG LIYPNVAAAR A
//