ID   AROC_METAR              Reviewed;         372 AA.
AC   Q0W6Q8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=UNCMA_22500;
GN   ORFNames=RCIX509;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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   -!- SIMILARITY: Belongs to the chorismate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00300}.
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DR   EMBL; AM114193; CAJ35935.1; -; Genomic_DNA.
DR   RefSeq; WP_012036570.1; NC_009464.1.
DR   AlphaFoldDB; Q0W6Q8; -.
DR   SMR; Q0W6Q8; -.
DR   STRING; 351160.RCIX509; -.
DR   EnsemblBacteria; CAJ35935; CAJ35935; RCIX509.
DR   GeneID; 5144742; -.
DR   KEGG; rci:RCIX509; -.
DR   PATRIC; fig|351160.9.peg.2302; -.
DR   eggNOG; arCOG04133; Archaea.
DR   OMA; MLSINAV; -.
DR   OrthoDB; 50229at2157; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000000663; 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..372
FT                   /note="Chorismate synthase"
FT                   /id="PRO_1000022569"
FT   BINDING         48
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         285
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         300..304
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   372 AA;  38671 MW;  38B782CFA5D0E9A2 CRC64;
     MTGNTFGNAF RITTFGESHG PGLGVVIDGC PAGLPLTEAD VQAELDKRKP GQSEVTTQRK
     EADMVEILSG VFEGLTTGTP IAMLVRNADA RSAAYENIRN IARPGHADFG YMEKYGMRDY
     RGGGRSSGRE TLSRVAGGAV AKKLLSLYGV EVHAHTVAIG NVRAKPATIE EIKANVWKNP
     VRCADLSAAD AMLREVSAAR EASDSVGGIV EIVATGVPAG VGTPAFDKLD ACLAYALMGI
     GGVKAVEIGA GIASAGMRGS EMNDEFCTED GKVRTKTNRC GGILGGISTG MPIVCRAAIK
     PTPSISRPQR TVNLETGAET IIEITGRHDP SIVPRAVPVA EAMVALVIVD QMISGGLINP
     VSAGAVDASR NR