ID   AROA1_BURPS    STANDARD;      PRT;   451 AA.
AC   Q63X54;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   07-MAR-2006, entry version 15.
DE   3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19)
DE   (5-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; pseudomallei group.
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: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and PEP:
CC       step 6.
CC   -!- PATHWAY: Context: Aromatic amino acids biosynthesis.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
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DR   EMBL; BX571965; CAH34676.1; -; Genomic_DNA.
DR   GenomeReviews; BX571965_GR; BPSL0683.
DR   HAMAP; MF_00210; -; 1.
DR   InterPro; IPR001986; EPSP_synth.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   ProDom; PD001867; EPSP_synth; 1.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; FALSE_NEG.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Transferase.
FT   CHAIN         1    451       3-phosphoshikimate
FT                                1-carboxyvinyltransferase.
FT                                /FTId=PRO_0000088238.
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
//