ID AROC_BRUC2 Reviewed; 364 AA. AC A9M8V2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300}; DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300}; DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300}; GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; GN OrderedLocusNames=BCAN_A0432; OS Brucella canis (strain ATCC 23365 / NCTC 10854). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=483179; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23365 / NCTC 10854; RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Bruce D., Detter C., Munk C., Brettin T.S.; RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and CC the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to CC yield chorismate, which is the branch point compound that serves as the CC starting substrate for the three terminal pathways of aromatic amino CC acid biosynthesis. This reaction introduces a second double bond into CC the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300}; CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00300}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000872; ABX61516.1; -; Genomic_DNA. DR RefSeq; WP_002963585.1; NC_010103.1. DR AlphaFoldDB; A9M8V2; -. DR SMR; A9M8V2; -. DR GeneID; 58776403; -. DR KEGG; bcs:BCAN_A0432; -. DR HOGENOM; CLU_034547_0_0_5; -. DR PhylomeDB; A9M8V2; -. DR UniPathway; UPA00053; UER00090. DR PRO; PR:A9M8V2; -. DR Proteomes; UP000001385; Chromosome I. DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd07304; Chorismate_synthase; 1. DR Gene3D; 3.60.150.10; Chorismate synthase AroC; 1. DR HAMAP; MF_00300; Chorismate_synth; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR035904; Chorismate_synth_AroC_sf. DR InterPro; IPR020541; Chorismate_synthase_CS. DR NCBIfam; TIGR00033; aroC; 1. DR PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1. DR PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR SUPFAM; SSF103263; Chorismate synthase, 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; FAD; KW Flavoprotein; FMN; Lyase; NADP. FT CHAIN 1..364 FT /note="Chorismate synthase" FT /id="PRO_1000078986" FT BINDING 48 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 131..133 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 243..244 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 288 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 303..307 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 329 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" 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 //