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 24-JAN-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}; OrderedLocusNames=Minf_0184; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain OS V4)). OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales; OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023). 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., Koonin E.V., RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F., RA Feng L., Wang L., Alam M.; RT "Complete genome sequence of the extremely acidophilic methanotroph isolate RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum RT Verrucomicrobia."; RL Biol. Direct 3:26-26(2008). 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; 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 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; CP000975; ACD82244.1; -; Genomic_DNA. DR RefSeq; WP_012462526.1; NC_010794.1. DR AlphaFoldDB; B3DXL0; -. DR SMR; B3DXL0; -. DR STRING; 481448.Minf_0184; -. DR KEGG; min:Minf_0184; -. DR eggNOG; COG0082; Bacteria. DR HOGENOM; CLU_034547_0_1_0; -. DR OMA; MLSINAV; -. DR OrthoDB; 9771806at2; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000009149; Chromosome. 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..366 FT /note="Chorismate synthase" FT /id="PRO_1000115369" FT BINDING 47 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 124..126 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 286 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 301..305 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 327 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="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 //