ID AROC_COXBU Reviewed; 352 AA. AC Q83D67; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 102. 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=CBU_0874; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). 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; AE016828; AAO90406.1; -; Genomic_DNA. DR RefSeq; NP_819892.1; NC_002971.3. DR RefSeq; WP_005772323.1; NZ_CDBG01000001.1. DR AlphaFoldDB; Q83D67; -. DR SMR; Q83D67; -. DR STRING; 227377.CBU_0874; -. DR EnsemblBacteria; AAO90406; AAO90406; CBU_0874. DR GeneID; 1208767; -. DR KEGG; cbu:CBU_0874; -. DR PATRIC; fig|227377.7.peg.860; -. DR eggNOG; COG0082; Bacteria. DR HOGENOM; CLU_034547_0_2_6; -. DR OrthoDB; 9771806at2; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004107; F:chorismate synthase activity; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IBA:GO_Central. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central. DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central. 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; Reference proteome. FT CHAIN 1..352 FT /note="Chorismate synthase" FT /id="PRO_0000140580" FT BINDING 48 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 54 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 125..127 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 238..239 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 278 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 293..297 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 319 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" SQ SEQUENCE 352 AA; 37949 MW; 00744BEF3C1AA44B CRC64; MSGNSFGKLF TVTTAGESHG PALVAIVDGC PAGLSLTEAD IQPDIDRRKT GKSRFTSQRR ESDQVKILSG VFEGVTTGTP IALLIENADQ RPRDYSQIKD LFRPGHGDYT YFKKYGFRDY RGGGRASARE TVMRVAAGAI AKKYLREKVN LTIQGYTAAV GAIRAERIDL SAVEKNPFFF PDEVQIPHLE QLIMKLRRDG DSIGARLNVI AKGVPCGLGE PVFDKLDADI ASAMMGINAV KGVEIGDGFA VVEQKGSFHR DELSKKGFLS NHAGGTLAGI SSGQDILVSL AFKPASSIRI PGKTLDINGK AVEVVTTGRH DPCVGLRAVP IAEAMLALVL MDHYLRYKAQ RG //