ID   AROC_SYNS9              Reviewed;         364 AA.
AC   Q3AUR6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Syncc9902_2040;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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;
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}.
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DR   EMBL; CP000097; ABB26998.1; -; Genomic_DNA.
DR   RefSeq; WP_011360786.1; NC_007513.1.
DR   AlphaFoldDB; Q3AUR6; -.
DR   SMR; Q3AUR6; -.
DR   STRING; 316279.Syncc9902_2040; -.
DR   EnsemblBacteria; ABB26998; ABB26998; Syncc9902_2040.
DR   KEGG; sye:Syncc9902_2040; -.
DR   eggNOG; COG0082; Bacteria.
DR   HOGENOM; CLU_034547_0_1_3; -.
DR   OMA; MLSINAV; -.
DR   OrthoDB; 981870at2; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid 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; IPR035904; Chorismate_synth_AroC_sf.
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; FAD;
KW   Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT   CHAIN           1..364
FT                   /note="Chorismate synthase"
FT                   /id="PRO_0000256354"
FT   BINDING         47
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         125..127
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         288
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         303..307
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         329
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ   SEQUENCE   364 AA;  38550 MW;  00666D39430C8001 CRC64;
     MGSSFGDLFR ISTFGESHGG GVGVIVEGCP PRLELDLDEI QAELNRRKPG QSHITTPRKE
     ADQVEILSGL LDGKTTLGTP IAMLVRNKDQ RPGDYSDMAV AFRPSHADAT YQSKYGIQAR
     SGGGRASARE TIGRVAAGAI AKQLLRKAAG TEILAWVKQI HTIEAHGIDP STVSMNDIEA
     NIVRCPEASV ANQMIERIEA IGREGDSCGG VIECVVRQPA VGLGMPVFDK LEADLAKAVM
     SLPATKGFEI GSGFSGTLLK GSEHNDAFIP GDDGRLHTAT NNSGGIQGGI SNGEPIVIRV
     GFKPTATIRK EQQTIDSDGN ATTLAAKGRH DPCVLPRAVP MVEAMVALTL ADHLLRQQGQ
     CSLW