AROA_SOLLC
ID AROA_SOLLC Reviewed; 520 AA.
AC P10748;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic;
DE EC=2.5.1.19;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase;
DE Short=EPSP synthase;
DE Flags: Precursor;
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].
RX PubMed=3346248; DOI=10.1016/s0021-9258(18)68922-7;
RA Gasser C.S., Winter J.A., Hironaka C.M., Shah D.M.;
RT "Structure, expression, and evolution of the 5-enolpyruvylshikimate-3-
RT phosphate synthase genes of petunia and tomato.";
RL J. Biol. Chem. 263:4280-4287(1988).
CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate
CC (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic
CC phosphate. {ECO:0000250|UniProtKB:P0A6D3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:145989; EC=2.5.1.19;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: This enzyme is the target of the potent, broad-spectrum
CC herbicide, glyphosate [n-(phosphonomethyl)glycine]. Overproduction of
CC EPSP leads to glyphosate tolerance.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000305}.
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DR EMBL; M21071; AAA34136.1; -; mRNA.
DR PIR; B28198; XUTOVS.
DR STRING; 4081.Solyc01g091190.2.1; -.
DR PaxDb; P10748; -.
DR PRIDE; P10748; -.
DR eggNOG; KOG0692; Eukaryota.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P10748; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd01556; EPSP_synthase; 1.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_00210; EPSP_synth; 1.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR Pfam; PF00275; EPSP_synthase; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR01356; aroA; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 77..520
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase,
FT chloroplastic"
FT /id="PRO_0000002289"
FT REGION 175..178
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 99..100
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 104
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 207
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 254..256
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 282
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 434
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 438
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 480
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 505
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
SQ SEQUENCE 520 AA; 55717 MW; 82B2061B2E8C8F4C CRC64;
MAQISSMAQG IQTLSLNSSN LSKTQKGPLV SNSLFFGSKK LTQISAKSLG VFKKDSVLRV
VRKSSFRISA SVATAEKPHE IVLXPIKDIS GTVKLPGSKS LSNRILLLAA LSEGRTVVDN
LLSSDDIHYM LGALKTLGLH VEDDNENQRA IVEGCGGQFP VGKKSEEEIQ LFLGNAGTAM
RPLTAAVTVA GGHSRYVLDG VPRMRERPIG DLVDGLKQLG AEVDCSLGTN CPPVRIVSKG
GLPGGKVKLS GSISSQYLTA LLMAAPLALG DVEIEIIDKL ISVPYVEMTL KLMERFGVFV
EHSSGWDRFL VKGGQKYKSP GKAFVEGDAS SASYFLAGAA VTGGTVTVEG CGTSSLQGDV
KFAEVLEKMG AEVTWTENSV TVKGPPRNSS GMKHLRAIDV NMNKMPDVAM TLAVVALFAD
GPTTIRDVAS WRVKETERMI AICTELRKLG ATVVEGSDYC IITPPEKLNV TEIDTYDDHR
MAMAFSLAAC ADVPVTIKNP GCTRKTFPDY FEVLQKYSKH
