AROA_ARATH
ID AROA_ARATH Reviewed; 520 AA.
AC P05466; O22142; Q501E1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic;
DE EC=2.5.1.19 {ECO:0000250|UniProtKB:P11043, ECO:0000305|PubMed:3481024};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000303|PubMed:3481024};
DE Short=EPSP synthase {ECO:0000303|PubMed:3481024};
DE Short=EPSPs {ECO:0000303|PubMed:3481024};
DE Flags: Precursor;
GN OrderedLocusNames=At2g45300; ORFNames=F4L23.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=3481024; DOI=10.1007/bf00327194;
RA Klee H.J., Muskopf Y.M., Gasser C.S.;
RT "Cloning of an Arabidopsis thaliana gene encoding 5-enolpyruvylshikimate-3-
RT phosphate synthase: sequence analysis and manipulation to obtain
RT glyphosate-tolerant plants.";
RL Mol. Gen. Genet. 210:437-442(1987).
RN [2]
RP SEQUENCE REVISION.
RA Gasser C.S.;
RL Submitted (OCT-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000250|UniProtKB:P11043, ECO:0000305|PubMed:3481024};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000250|UniProtKB:P11043, ECO:0000305|PubMed:3481024}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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; X06613; CAA29828.1; -; Genomic_DNA.
DR EMBL; AC002387; AAB82633.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10536.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62712.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62713.1; -; Genomic_DNA.
DR EMBL; BT022026; AAY25438.1; -; mRNA.
DR EMBL; AK227120; BAE99170.1; -; mRNA.
DR PIR; H84888; H84888.
DR PIR; S01061; XUMUVS.
DR RefSeq; NP_001318428.1; NM_001337122.1.
DR RefSeq; NP_001324852.1; NM_001337123.1.
DR RefSeq; NP_182055.1; NM_130093.3.
DR AlphaFoldDB; P05466; -.
DR SMR; P05466; -.
DR BioGRID; 4474; 3.
DR IntAct; P05466; 1.
DR STRING; 3702.AT2G45300.1; -.
DR iPTMnet; P05466; -.
DR PaxDb; P05466; -.
DR PRIDE; P05466; -.
DR ProteomicsDB; 246988; -.
DR EnsemblPlants; AT2G45300.1; AT2G45300.1; AT2G45300.
DR EnsemblPlants; AT2G45300.2; AT2G45300.2; AT2G45300.
DR EnsemblPlants; AT2G45300.4; AT2G45300.4; AT2G45300.
DR GeneID; 819138; -.
DR Gramene; AT2G45300.1; AT2G45300.1; AT2G45300.
DR Gramene; AT2G45300.2; AT2G45300.2; AT2G45300.
DR Gramene; AT2G45300.4; AT2G45300.4; AT2G45300.
DR KEGG; ath:AT2G45300; -.
DR Araport; AT2G45300; -.
DR TAIR; locus:2050812; AT2G45300.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_024321_0_0_1; -.
DR InParanoid; P05466; -.
DR OMA; SAACYFY; -.
DR OrthoDB; 692572at2759; -.
DR PhylomeDB; P05466; -.
DR BioCyc; ARA:AT2G45300-MON; -.
DR UniPathway; UPA00053; UER00089.
DR PRO; PR:P05466; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P05466; baseline and differential.
DR Genevisible; P05466; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IMP:TAIR.
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; IMP:TAIR.
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 1: Evidence at protein 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_0000002287"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT CONFLICT 333
FT /note="S -> C (in Ref. 1; CAA29828)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="P -> S (in Ref. 1; CAA29828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 55734 MW; 79418663170D0809 CRC64;
MAQVSRICNG VQNPSLISNL SKSSQRKSPL SVSLKTQQHP RAYPISSSWG LKKSGMTLIG
SELRPLKVMS SVSTAEKASE IVLQPIREIS GLIKLPGSKS LSNRILLLAA LSEGTTVVDN
LLNSDDINYM LDALKRLGLN VETDSENNRA VVEGCGGIFP ASIDSKSDIE LYLGNAGTAM
RPLTAAVTAA GGNASYVLDG VPRMRERPIG DLVVGLKQLG ADVECTLGTN CPPVRVNANG
GLPGGKVKLS GSISSQYLTA LLMSAPLALG DVEIEIVDKL ISVPYVEMTL KLMERFGVSV
EHSDSWDRFF VKGGQKYKSP GNAYVEGDAS SASYFLAGAA ITGETVTVEG CGTTSLQGDV
KFAEVLEKMG CKVSWTENSV TVTGPPRDAF GMRHLRAIDV NMNKMPDVAM TLAVVALFAD
GPTTIRDVAS WRVKETERMI AICTELRKLG ATVEEGSDYC VITPPKKVKT AEIDTYDDHR
MAMAFSLAAC ADVPITINDP GCTRKTFPDY FQVLERITKH
