ID A0A2N1JQB8_9BACI Unreviewed; 390 AA. AC A0A2N1JQB8; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 29-MAY-2024, entry version 18. DE RecName: Full=Chorismate synthase {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300}; DE Short=CS {ECO:0000256|HAMAP-Rule:MF_00300}; DE EC=4.2.3.5 {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000256|HAMAP-Rule:MF_00300}; GN Name=aroC {ECO:0000256|HAMAP-Rule:MF_00300}; GN ORFNames=CWE34_29585 {ECO:0000313|EMBL:PKJ52125.1}; OS Bacillus sp. SN10. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=2056493 {ECO:0000313|EMBL:PKJ52125.1, ECO:0000313|Proteomes:UP000233528}; RN [1] {ECO:0000313|EMBL:PKJ52125.1, ECO:0000313|Proteomes:UP000233528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN10 {ECO:0000313|EMBL:PKJ52125.1, RC ECO:0000313|Proteomes:UP000233528}; RA Nazipi S.; RT "Bacillus sp. isolated from nest material of social spiders."; RL Submitted (DEC-2017) 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:0000256|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:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}; CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 7/7. {ECO:0000256|ARBA:ARBA00005044, ECO:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00300}. CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC {ECO:0000256|ARBA:ARBA00008014, ECO:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PKJ52125.1}. 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; PJCU01000029; PKJ52125.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2N1JQB8; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000233528; Unassembled WGS sequence. 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: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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00300}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_00300}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00300}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00300}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00300}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00300}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00300}. FT BINDING 39 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300" FT BINDING 45 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300" FT BINDING 132..134 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300" FT BINDING 253..254 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300" FT BINDING 298 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300" FT BINDING 313..317 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300" FT BINDING 339 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00300" SQ SEQUENCE 390 AA; 42482 MW; B84ABCD0BFFCF55D CRC64; MRYITAGESH GPQLTVILEG VPAGLTLAAE HINKELLRRQ KGHGRGRRMQ IETDTVEIVS GVRHGMTLGS PITLIVKNDD FKHWTKVMGA EPISEKESKE MKRTITKPRP GHADLNGAIK YGHRDIRNVL ERSSARETTV RVAAGAVAKQ ILKELGVEIA GHVLEIGGVK AKHISNLSIE EIQTITENSP VRCLDKEVEQ EMMDAIDHAK SSGDSIGGIV EVIAEGMPIG VGSYVHYDRK LDAKLAGAIM SINAFKGAEI GVGFEAARQP GSKVHDEILW DEEQGYMRKT NNAGGFEGGM TTGMPIVVRG VMKPIPTLYK PLASVDIDTK EAFQASIERS DSCAVPAAGV VAESVVAWEL AHALVEQFGK DRMELIQQNI TQHNKYAKEF //