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AROC_EDWI9
ID   AROC_EDWI9              Reviewed;         361 AA.
AC   C5BAF2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=NT01EI_2754;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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; CP001600; ACR69922.1; -; Genomic_DNA.
DR   RefSeq; WP_015872023.1; NC_012779.2.
DR   AlphaFoldDB; C5BAF2; -.
DR   SMR; C5BAF2; -.
DR   STRING; 67780.B6E78_05740; -.
DR   EnsemblBacteria; ACR69922; ACR69922; NT01EI_2754.
DR   GeneID; 7959964; -.
DR   KEGG; eic:NT01EI_2754; -.
DR   PATRIC; fig|634503.3.peg.2465; -.
DR   HOGENOM; CLU_034547_0_2_6; -.
DR   OMA; MLSINAV; -.
DR   OrthoDB; 981870at2; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000001485; 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..361
FT                   /note="Chorismate synthase"
FT                   /id="PRO_1000204948"
FT   BINDING         48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         54
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         238..239
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         278
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         293..297
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         319
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ   SEQUENCE   361 AA;  38712 MW;  A613BC33D6857A5E CRC64;
     MAGNSIGQVF RVTTFGESHG AALGCIVDGV PPGMALSEAD LQHDLDRRRP GASRYTTARR
     EADRVRILSG VFEGVTTGTS IGLLIENTDQ RSQDYSAIKD LFRPGHADYS YEQKYGLRDY
     RGGGRSSARE TAMRVAAGAI AKKYLQQQHG IVIRACLSRM GDIVCRQYDW AQVEQNPFFC
     PDAQQLEALD ALMRDLKKCG DSIGAEVTVM ATGVPPGLGD PVFDRLDADL AHALMSINAV
     KGVEIGDGFA VVGQRGSEHR DEISPSGFLS NHAGGILGGI SSGQPLLARL ALKPTSSIMV
     PGQTITRAGE ATTIVTHGRH DPCVGIRAVP IAEAMMALVL MDHLLRQRAQ CADVACTVPR
     W
 
 
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