AROA_BRANA
ID AROA_BRANA Reviewed; 516 AA.
AC P17688;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Westar;
RX PubMed=2339069; DOI=10.1093/nar/18.9.2821;
RA Gasser C.S., Klee H.J.;
RT "A Brassica napus gene encoding 5-enolpyruvylshikimate-3-phosphate
RT synthase.";
RL Nucleic Acids Res. 18:2821-2821(1990).
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; X51475; CAA35839.1; -; Genomic_DNA.
DR PIR; S12744; S12744.
DR AlphaFoldDB; P17688; -.
DR SMR; P17688; -.
DR UniPathway; UPA00053; UER00089.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase 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; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Plastid; Transferase; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..516
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase,
FT chloroplastic"
FT /id="PRO_0000002288"
FT REGION 171..174
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT ACT_SITE 403
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT ACT_SITE 431
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 95..96
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 100
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 203
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 250..252
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 278
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 430
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 434
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 476
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT BINDING 501
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000250|UniProtKB:P0A6D3"
SQ SEQUENCE 516 AA; 55030 MW; 86804B4DE4D0DF57 CRC64;
MAQSSRICHG VQNPCVIISN LSKSNQNKSP FSVSLKTHQP RASSWGLKKS GTMLNGSVIR
PVKVTASVST SEKASEIVLQ PIREISGLIK LPGSKSLSNR ILLLAALSEG TTVVDNLLNS
DDINYMLDAL KKLGLNVERD SVNNRAVVEG CGGIFPASLD SKSDIELYLG NAGTAMRPLT
AAVTAAGGNA SYVLDGVPRM RERPIGDLVV GLKQLGADVE CTLGTNCPPV RVNANGGLPG
GKVKLSGSIS SQYLTALLMA APLALGDVEI EIIDKLISVP YVEMTLKLME RFGVSAEHSD
SWDRFFVKGG QKYKSPGNAY VEGDASSASY FLAGAAITGE TVTVEGCGTT SLQGDVKFAE
VLEKMGCKVS WTENSVTVTG PSRDAFGMRH LRAVDVNMNK MPDVAMTLAV VALFADGPTT
IRDVASWRVK ETERMIAICT ELRKLGATVE EGSDYCVITP PAKVKPAEID TYDDHRMAMA
FSLAACADVP VTIKDPGCTR KTFPDYFQVL ESITKH
