ID AROA_SHIBS Reviewed; 427 AA.
AC Q31YU3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase;
DE EC=2.5.1.19;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase;
DE Short=EPSP synthase;
DE Short=EPSPS;
GN Name=aroA; OrderedLocusNames=SBO_2194;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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
CC phosphoenolpyruvate: step 6/7.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
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DR EMBL; CP000036; ABB66765.1; -; Genomic_DNA.
DR RefSeq; YP_408593.1; NC_007613.1.
DR HSSP; P0A6D3; 2AA9.
DR ProteinModelPortal; Q31YU3; -.
DR SMR; Q31YU3; 1-427.
DR STRING; 300268.SBO_2194; -.
DR PRIDE; Q31YU3; -.
DR EnsemblBacteria; ABB66765; ABB66765; SBO_2194.
DR GeneID; 3781177; -.
DR KEGG; sbo:SBO_2194; -.
DR PATRIC; 18683696; VBIShiBoy33460_2767.
DR eggNOG; COG0128; -.
DR HOGENOM; HOG000247372; -.
DR KO; K00800; -.
DR OMA; GADIEWG; -.
DR ProtClustDB; PRK02427; -.
DR BioCyc; SBOY300268:GJFL-2191-MONOMER; -.
DR UniPathway; UPA00053; UER00089.
DR BindingDB; Q31YU3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:HAMAP.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:HAMAP.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_00210; EPSP_synth; 1; -.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR Pfam; PF00275; EPSP_synthase; 1.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; RNA3'_cycl/enolpyr_transf_A/B; 1.
DR TIGRFAMs; TIGR01356; aroA; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Cytoplasm; Transferase.
FT CHAIN 1 427 3-phosphoshikimate 1-
FT carboxyvinyltransferase.
FT /FTId=PRO_1000012478.
SQ SEQUENCE 427 AA; 46096 MW; B1F55469EB4D9F97 CRC64;
MESLTLQPIA RVDGTINLPG SKSVSNRALL LAALAHGKTV LTNLLDSDDV RHMLNALTAL
GVSYTLSADR TRCEIIGNGG PLHAEGALEL FLGNAGTAMR PLAAALCLGS NDIVLTGEPR
MKERPIGHLV DALRLGGAKI TYLEQENYPP LRLQGGFTGG NVDVDGSVSS QFLTALLMTA
PLAPEDTVIR IKGDLVSKPY IDITLNLMKT FGVEIENQHY QQFVVKGGQS YQSPGTYLVE
GDASSASYFL AAAAIKGGTV KVTGIGRNSM QGDIRFADVL EKMGATICWG DDYISCTRGE
LNAIDMDMNH IPDAAMTIAT AALFAKGTTT LRNIYNWRVK ETDRLFAMAT ELRKVGAEVE
EGHDYIRITP PEKLNFAEIA TYNDHRMAMC FSLVALSDTP VTILDPKCTA KTFPDYFEQL
ARISQAA
//
