ID AROC_BRUSU Reviewed; 364 AA. AC P63608; Q8G299; Q8YFL4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 03-NOV-2009, entry version 29. DE RecName: Full=Chorismate synthase; DE EC=4.2.3.5; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase; GN Name=aroC; OrderedLocusNames=BR0428; OS Brucella suis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=29461; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330 / Biovar 1; RX MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., RA Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., RA Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., RA Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between RT animal and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). CC -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = CC chorismate + phosphate. CC -!- COFACTOR: Reduced flavin (By similarity). CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 7/7. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014291; AAN29371.1; -; Genomic_DNA. DR RefSeq; NP_697456.1; -. DR GeneID; 1166089; -. DR GenomeReviews; AE014291_GR; BR0428. DR KEGG; bms:BR0428; -. DR TIGR; BR0428; -. DR HOGENOM; P63608; -. DR OMA; SRFTTQR; -. DR BioCyc; BSUI204722:BR_0428-MON; -. DR BRENDA; 4.2.3.5; 281610. DR GO; GO:0004107; F:chorismate synthase activity; IEA:HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic pro...; IEA:HAMAP. DR HAMAP; MF_00300; -; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR020541; Chorismate_synthase_CS. DR PANTHER; PTHR21085; Chorismate_synth; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR ProDom; PD002941; Chorismate_synth; 1. DR TIGRFAMs; TIGR00033; aroC; 1. DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1. DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1. DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase. FT CHAIN 1 364 Chorismate synthase. FT /FTId=PRO_0000140562. SQ SEQUENCE 364 AA; 38988 MW; 95F83B4FD5230C0E CRC64; MSHNSFGHLF RVTTWGESHG LALGCVVDGC PPGITFTEAE IQSFLDKRKP GQSKYTTQRR EPDQVRVLSG VLLGEDGVTM TTTGTPISMM IENTDQRSKD YGEIARQYRP GHADYAYDVK YGIRDYRGGG RSSARETAAR VAAGAIARKV VPGLEVRGAL VSIGAHDIDR SRWNWAEVDN NPFFTPDAGS VEVFADYLDG IRKNGSSVGA IIEIVAEGVP AGIGAPIYGK LDQDIASYLM SINAVKGVEI GNGFEAARLT GEENADEMRM GNDGKPIFLS NHAGGVLGGI ATGAPVVARF AVKPTSSILT PRRSIDKDGN EVDVMTRGRH DPCVGIRAVP IGEAMVACAI ADHYLRHRGQ TGRV //