AC   MF_00300;
DC   Protein; auto
TR   HAMAP; MF_00300; -; 1; level=0
XX
Names: Chorismate_synth
XX
ID   AROC
DE   RecName: Full=Chorismate synthase;
DE            Short=CS;
DE            EC=4.2.3.5;
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase;
GN   Name=aroC;
XX
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.
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   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC       Note=Reduced FMN (FMNH(2)).;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       7/7.
case <OC:Bacteria>
CC   -!- SUBUNIT: Homotetramer.
end case
CC   -!- SIMILARITY: Belongs to the chorismate synthase family.
XX
DR   Pfam; PF01264; Chorismate_synt; 1; trigger=no
DR   PIRSF; PIRSF001456; Chorismate_synth; 1; trigger=no
DR   NCBIfam; TIGR00033; AroC; 1; trigger=no
DR   PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1; trigger=no
DR   PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1; trigger=no
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   FAD
KW   Flavoprotein
KW   FMN
KW   Lyase
KW   NADP
XX
GO   GO:0004107; F:chorismate synthase activity
GO   GO:0009073; P:aromatic amino acid family biosynthetic process
XX
FT   From: AROC_STRPN (P0A2Y6)
FT   BINDING         130..132
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [RH]-x-S
FT   BINDING         251..252
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [NQ]-[AGTS]
FT   BINDING         311..315
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [KH]-x(3)-[TS]
FT   BINDING         39
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: R
FT   BINDING         45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [RK]
FT   BINDING         296
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [GAS]
FT   BINDING         337
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [RN]
XX
Size: 330-422;
Related: None;
Template: P12008; O66493; P56122; P9WPY1; P0A2Y6; Q59803;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACAN, BACC1, BACCR, BACCZ, BACAH, BACHK
Plasmid: None
Comments: None
XX
# Revision 1.38 2023/06/01
//