ID AROC_ALKOO Reviewed; 384 AA. AC A8MH14; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 02-SEP-2026, entry version 82. 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=Clos_1357; OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OS OhILAs)). OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales; OC Natronincolaceae; Alkaliphilus. OX NCBI_TaxID=350688; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OhILAs; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.; RT "Complete genome of Alkaliphilus oremlandii OhILAs."; 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; CP000853; ABW18901.1; -; Genomic_DNA. DR RefSeq; WP_012159213.1; NC_009922.1. DR AlphaFoldDB; A8MH14; -. DR SMR; A8MH14; -. DR STRING; 350688.Clos_1357; -. DR KEGG; aoe:Clos_1357; -. DR eggNOG; COG0082; Bacteria. DR HOGENOM; CLU_034547_2_0_9; -. DR OrthoDB; 9771806at2; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000000269; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0010181; F:FMN binding; IEA:TreeGrafter. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd07304; Chorismate_synthase; 1. DR FunFam; 3.60.150.10:FF:000002; 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 NCBIfam; NF003793; PRK05382.1; 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD; KW Flavoprotein; FMN; Lyase; NADP; Reference proteome. FT CHAIN 1..384 FT /note="Chorismate synthase" FT /id="PRO_0000322385" FT BINDING 40 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 46 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 127..129 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 247..248 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 292 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 307..311 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" FT BINDING 333 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300" SQ SEQUENCE 384 AA; 42764 MW; 7B2C2736D2106F59 CRC64; MLRYLSAGES HGKGLIAIIE GLPSNIPMDI NRINADLGRR QQGFGRGNRM KIEKDRVEIL SGVRDGKTLG TPLTLMIENL DYKNWTSIMS VEKLEKQNII VEPRPGHGDL VGSLKYNHKD IRNVIERTSA RDTAIRTAIG AVVKQFLSIF DIEILSHVIS IGRAHYVPFV EDLFQYKSQI EASPVRCLNP TIEERMMGEI QRAKETGDSL GGVFEVIVRN VPIGIGSYAH FDRKLDGILA QGLMSLQAIK AVEIGNGIEG SSKMGSQFHD EIKYSEAKGY YHDTNRAGGI EAGVSNGEDI LIRGYMKPIP TLMKPLKTVD MGTKEVKEAI IERSDNCAVP SAAVVAEGIC AFAIAKEFLE KFRGDSIEEV EWNYERYMNY LRSR //