ID   AROC_ANADE              Reviewed;         381 AA.
AC   Q2IMD4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 103.
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=Adeh_0186;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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}.
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DR   EMBL; CP000251; ABC79963.1; -; Genomic_DNA.
DR   RefSeq; WP_011419246.1; NC_007760.1.
DR   AlphaFoldDB; Q2IMD4; -.
DR   SMR; Q2IMD4; -.
DR   STRING; 290397.Adeh_0186; -.
DR   KEGG; ade:Adeh_0186; -.
DR   eggNOG; COG0082; Bacteria.
DR   HOGENOM; CLU_034547_2_0_7; -.
DR   OrthoDB; 9771806at2; -.
DR   UniPathway; UPA00053; UER00090.
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; 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..381
FT                   /note="Chorismate synthase"
FT                   /id="PRO_1000071965"
FT   BINDING         41
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         47
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         291
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         306..310
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         332
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ   SEQUENCE   381 AA;  40537 MW;  7D7718C9F77BC9A2 CRC64;
     MTLRYLTAGE SHGPALVAIA EGFPAGLPVD FEAVDRDLRR RQKGYGRGGR MKIETDAAQF
     LAGLRGGVTT GAPIALAVWN KDHENWKDLV SPYARGGRKF TQVRPGHADL AGALKYGLDD
     ARDVLERASA RSTAVIVALG ALAKALLSSQ GVEVCSRVVA IGPRDIRPDA PPTPAQRDAI
     EASDLHVDDE ALAAEWRALI DAEKARGGSI GGAFDVYATG LPIGLGSHVH PDRRLDARLA
     GALCGVQAIR AVEIGDGTQV GRPGYEFHDA IHHDPARGFW RETNRAGGLE GGMTDGMPLR
     VRAYMKPIPT MLHPLATVDL ATRAATQARY ERSDVCAVPA AAVVGEAVVA WELANALLEK
     FGGDTVEDVR RAVEAYAARI R
//