ID   AROC_CAPSE              Reviewed;         447 AA.
AC   P27793;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Chorismate synthase, chloroplastic;
DE            EC=4.2.3.5;
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase;
DE   Flags: Precursor;
OS   Capnoides sempervirens (Rock-harlequin) (Corydalis sempervirens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Fumarioideae;
OC   Capnoides.
OX   NCBI_TaxID=3464;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 267-276 AND 307-320.
RX   PubMed=1718979; DOI=10.1016/s0021-9258(18)54657-3;
RA   Schaller A., Schmid J., Leibinger U., Amrhein N.;
RT   "Molecular cloning and analysis of a cDNA coding for chorismate synthase
RT   from the higher plant Corydalis sempervirens Pers.";
RL   J. Biol. Chem. 266:21434-21438(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 306-320.
RX   PubMed=2146922; DOI=10.1016/0003-9861(90)90141-k;
RA   Schaller A., Windhofer V., Amrhein N.;
RT   "Purification of chorismate synthase from a cell culture of the higher
RT   plant Corydalis sempervirens Pers.";
RL   Arch. Biochem. Biophys. 282:437-442(1990).
CC   -!- FUNCTION: Catalyzes the last common step of the biosynthesis of
CC       aromatic amino acids, produced via the shikimic acid pathway.
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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       7/7.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the chorismate synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X60544; CAA43034.1; -; mRNA.
DR   PIR; A41197; A41197.
DR   AlphaFoldDB; P27793; -.
DR   SMR; P27793; -.
DR   BRENDA; 4.2.3.5; 1634.
DR   UniPathway; UPA00053; UER00090.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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   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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW   Direct protein sequencing; Lyase; Plastid; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..447
FT                   /note="Chorismate synthase, chloroplastic"
FT                   /id="PRO_0000002295"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48100 MW;  7CACAFD93A6BAEF8 CRC64;
     MASSLSTKPF LSGSRRRSTT DGSGWSYFQT SDLRQLSNQS VQISVRRQTA PLKLVVQASG
     SSFGKVFQVT TYGESHGGGV GCVIDGCPPR FPISEADIQS DLDRRRPGQS RITTPRKETD
     TCKIYSGVAD GFTTGSPIHI SVPNTDQRGN DYSEMAKAYR PSHADATYDF KYGVRSVQGG
     GRSSARETIG RVAAGALAKK ILKAYAGTEV LAYVSQAHKV VLPEGLVDHE TLSLEQIESN
     IVRCPDSEYA EKMIAAIDAV RVKGDSVGGV VTCIMRNVPR GLGSPVFDKL EAELAKACMS
     LPATKGFEFG SGFSGTFLTG SEHNDEFYTD ENGRIRTRTN RSGGIQGGIS NGEIINMRIA
     FKPTSTIGKK QNTVTREREE IELIARGRHD PCVVPRAVPM VEAMVALVLL DQLMLQHAQG
     NLFSINPALQ EPLSETVSSA AASLQGV