ID AROC_METI4 Reviewed; 366 AA. AC B3DXL0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 15-FEB-2017, entry version 50. 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=Minf_0184; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum OS (strain V4)). OC Bacteria; Verrucomicrobia; unclassified Verrucomicrobia; OC Methylacidiphilales; Methylacidiphilaceae; Methylacidiphilum. OX NCBI_TaxID=481448; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate V4; RX PubMed=18593465; DOI=10.1186/1745-6150-3-26; RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., RA Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., RA Dunfield P.F., Feng L., Wang L., Alam M.; RT "Complete genome sequence of the extremely acidophilic methanotroph RT isolate V4, Methylacidiphilum infernorum, a representative of the RT bacterial phylum Verrucomicrobia."; RL Biol. Direct 3:26-26(2008). CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate CC and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate CC (EPSP) to yield chorismate, which is the branch point compound CC that serves as the starting substrate for the three terminal CC pathways of aromatic amino acid biosynthesis. This reaction CC introduces a second double bond into the aromatic ring system. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = CC chorismate + phosphate. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 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; CP000975; ACD82244.1; -; Genomic_DNA. DR RefSeq; WP_012462526.1; NC_010794.1. DR ProteinModelPortal; B3DXL0; -. DR STRING; 481448.Minf_0184; -. DR EnsemblBacteria; ACD82244; ACD82244; Minf_0184. DR KEGG; min:Minf_0184; -. DR PATRIC; 22489363; VBIMetInf111569_0192. DR eggNOG; ENOG4105D10; Bacteria. DR eggNOG; COG0082; LUCA. DR HOGENOM; HOG000060335; -. DR KO; K01736; -. DR OMA; MLSINAV; -. DR OrthoDB; POG0935000V; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000009149; Chromosome. DR GO; GO:0004107; F:chorismate synthase 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 CDD; cd07304; Chorismate_synthase; 1. DR Gene3D; 3.60.150.10; -; 1. DR HAMAP; MF_00300; Chorismate_synth; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR020541; Chorismate_synthase_CS. DR PANTHER; PTHR21085; PTHR21085; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR SUPFAM; SSF103263; SSF103263; 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; FAD; Flavoprotein; FMN; Lyase; NADP; KW Reference proteome. FT CHAIN 1 366 Chorismate synthase. FT /FTId=PRO_1000115369. FT NP_BIND 124 126 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 301 305 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 47 47 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 286 286 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 327 327 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. SQ SEQUENCE 366 AA; 40267 MW; F6177B82EB3FA3DB CRC64; MPNTFGHLFR ITTWGESHGK GVGVVIDGCP PRIPLSEEDI QKELDRRRPG QSKITTQRKE RDIAAILSGT FNGMTLGTPI MIWVKNEDAR PEAYAEMEKI YRPSHADFTY QAKYGIRNWQ GGGRSSARET IGRVAGGAVG GKVLQFLYPE IEVIAWVSEV HGLKSLCDPN TVTREDVESN ILRWPNAENL GEALKEIERA QKEGDTVGGI VECIVRGMPV GLGEPVFDKL EADLAKAMLS LPASKGFEIG SGFRGALMRG SEHNDPFYME GNKVRTKTNW SGGVQGGISN GENLYFRVAF KPVATIAQEQ QTVSVDGEEV ILRARGRHDP CVLPRAVPIV EAMTKLVLVD HALRQKAIEL TPRSFS //