AROA1_TOBAC
ID AROA1_TOBAC Reviewed; 518 AA.
AC P23981;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase 1, chloroplastic;
DE EC=2.5.1.19;
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase 1;
DE Short=EPSP synthase 1;
DE Flags: Precursor;
GN Name=EPSPS-1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1932690; DOI=10.1007/bf00028730;
RA Wang Y., Jones J., Weller S., Goldsbrough P.B.;
RT "Expression and stability of amplified genes encoding 5-
RT enolpyruvylshikimate-3-phosphate synthase in glyphosate-tolerant tobacco
RT cells.";
RL Plant Mol. Biol. 17:1127-1138(1991).
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}.
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; M61904; AAA34071.1; -; mRNA.
DR PIR; S18353; S18353.
DR RefSeq; NP_001312842.1; NM_001325913.1.
DR AlphaFoldDB; P23981; -.
DR SMR; P23981; -.
DR STRING; 4097.P23981; -.
DR ProMEX; P23981; -.
DR GeneID; 107813883; -.
DR KEGG; nta:107813883; -.
DR PhylomeDB; P23981; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000084051; Unplaced.
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..74
FT /note="Chloroplast"
FT CHAIN 75..518
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase 1,
FT chloroplastic"
FT /id="PRO_0000002291"
FT REGION 173..176
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT ACT_SITE 405
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT ACT_SITE 433
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 97..98
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 102
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 205
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 252..254
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 280
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 432
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 436
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 478
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 503
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
SQ SEQUENCE 518 AA; 55711 MW; 4F03C514EAFE1681 CRC64;
MAQISSMGQG IRTPNLNSYL PKTQKVPLFS HSIFIGSKKI TQNSAKSLWV SKEDSVLRVA
KSPFRISASV VTAQKPNEIV LQPIKDISGT VKLPGSKSLS NRILLLAALS KGRTVVDNLL
SSDDIHYMLG ALKTLGLHVE DDNENQRAIV EGCGGQFPVG KKSEEEIQLF LGNAGTAMRP
LTAAVTVAGG HSRYVLDGVP RMRERPIGDL VDGLKQLGAE VDCFLGTNCP PVRIVSKGGL
PGGKVKLSGS ISSQYLTALL MAAPLALGDV EIEIIDKLIS VPYVEMTLKL MERFGVSVEH
TSSWDKFLVR GGQKYKSPGK AYVEGDASSA SYFLAGAAVT GGTVTVEGCG TSSLQGDVKF
AEVLEKMGAE VTWTENSVTV KGPPRNSSGM KHLRAVDVNM NKMPDVAMTL AVVALFADGP
TAIRDVASWR VKETERMIAI CTELRKLGAT VVEGSDYCII TPPEKLNVTE IDTYDDHRMA
MAFSLAACAD VPVTIKDPGC TRKTFPNYFD VLQQYSKH
