AROC2_SOLLC
ID AROC2_SOLLC Reviewed; 431 AA.
AC Q42885;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chorismate synthase 2, chloroplastic;
DE EC=4.2.3.5;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase 2;
DE Flags: Precursor;
GN Name=CS2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. UC82B;
RX PubMed=8251624; DOI=10.1007/bf00021526;
RA Goerlach J., Schmid J., Amrheim N.;
RT "Differential expression of tomato (Lycopersicon esculentum L.) genes
RT encoding shikimate pathway isoenzymes. II. Chorismate synthase.";
RL Plant Mol. Biol. 23:707-716(1993).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers and roots and,
CC to a lesser extent, in stems, leaves, and cotyledons.
CC -!- SIMILARITY: Belongs to the chorismate synthase family. {ECO:0000305}.
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DR EMBL; Z21791; CAA79854.1; -; mRNA.
DR PIR; S40409; S40409.
DR RefSeq; NP_001234411.1; NM_001247482.1.
DR AlphaFoldDB; Q42885; -.
DR SMR; Q42885; -.
DR STRING; 4081.Solyc04g009620.2.1; -.
DR PaxDb; Q42885; -.
DR PRIDE; Q42885; -.
DR EnsemblPlants; Solyc04g009620.3.1; Solyc04g009620.3.1; Solyc04g009620.3.
DR GeneID; 544151; -.
DR Gramene; Solyc04g009620.3.1; Solyc04g009620.3.1; Solyc04g009620.3.
DR KEGG; sly:544151; -.
DR eggNOG; KOG4492; Eukaryota.
DR HOGENOM; CLU_034547_0_1_1; -.
DR InParanoid; Q42885; -.
DR OMA; PCIVQRA; -.
DR OrthoDB; 826475at2759; -.
DR PhylomeDB; Q42885; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000004994; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004107; F:chorismate synthase activity; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..431
FT /note="Chorismate synthase 2, chloroplastic"
FT /id="PRO_0000002297"
FT REGION 93..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 46871 MW; D72D26C0F4F6B003 CRC64;
MASSMLTKQF LGAPFSSFGS GQQPSKLCSS NLRFPTHRSQ PKRLEIQAAG NTFGNYFRVT
TFGESHGGGV GCIIDGCPPR LPLSESDMQV ELDRRRPGQS RITTPRKETD TCKISSGTAD
GLTTGSPIKV EVPNTDQRGN DYSEMSLAYR PSHADATYDF KYGVRSVQGG GRSSARETIG
RVAAGAVAKK ILKLYSGTEI LAYVSQVHNV VLPEDLVDNQ IVTLEQIESN IVRCPNPEYA
EKMIGAIDYV RVRGDSVGGV VTCIVRNVPR GLGTPVFDKL EAELAKACMS LPATKGFEFG
SGFAGTFMTG SEHNDEFFMD EHDQIRTKTN RSGGIQGGIS NGEIINMRVA FKPTSTIARK
QHTVSRDKHE TELIARGRHD PCVVPRAVPM VEAMVALVLV DQLMTQYAQC MLFPVNLTLQ
EPLQPSTTKS A