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Database: UniProt
Entry: Q31YU3
LinkDB: Q31YU3
Original site: Q31YU3 
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   26-NOV-2014, entry version 71.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210};
DE            EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE            Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE            Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210};
GN   Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210};
GN   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   -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC       phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-
CC       phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and
CC       inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC       phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC       {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00210}.
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DR   EMBL; CP000036; ABB66765.1; -; Genomic_DNA.
DR   RefSeq; YP_408593.1; NC_007613.1.
DR   ProteinModelPortal; Q31YU3; -.
DR   SMR; Q31YU3; 1-427.
DR   STRING; 300268.SBO_2194; -.
DR   BindingDB; Q31YU3; -.
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   OrthoDB; EOG6Z6FZ4; -.
DR   BioCyc; SBOY300268:GJFL-2191-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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; SSF55205; 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.
FT   REGION       22     23       Shikimate-3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   REGION       94     97       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   REGION      169    171       Shikimate-3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   ACT_SITE    313    313       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   ACT_SITE    341    341       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING      27     27       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     124    124       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     197    197       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     336    336       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     340    340       Shikimate-3-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00210}.
FT   BINDING     344    344       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     386    386       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     411    411       Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00210}.
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
//
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