AROA_PETHY
ID AROA_PETHY Reviewed; 516 AA.
AC P11043;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic {ECO:0000303|PubMed:3346248};
DE EC=2.5.1.19 {ECO:0000269|PubMed:1939260};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000303|PubMed:3346248};
DE Short=EPSP synthase {ECO:0000303|PubMed:3346248};
DE Flags: Precursor;
GN Name=EPSPS {ECO:0000303|PubMed:3346248};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Mitchell;
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).
RN [2]
RP MUTAGENESIS OF GLY-173, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=1939260; DOI=10.1016/s0021-9258(18)54580-4;
RA Padgette S.R., Re D.B., Gasser C.S., Eicholtz D.A., Frazier R.B.,
RA Hironaka C.M., Levine E.B., Shah D.M., Fraley R.T., Kishore G.M.;
RT "Site-directed mutagenesis of a conserved region of the 5-
RT enolpyruvylshikimate-3-phosphate synthase active site.";
RL J. Biol. Chem. 266:22364-22369(1991).
RN [3]
RP FUNCTION, AND INDUCTION BY ODO1.
RC STRAIN=cv. W115;
RX PubMed=15805488; DOI=10.1105/tpc.104.028837;
RA Verdonk J.C., Haring M.A., van Tunen A.J., Schuurink R.C.;
RT "ODORANT1 regulates fragrance biosynthesis in petunia flowers.";
RL Plant Cell 17:1612-1624(2005).
RN [4]
RP INDUCTION BY EOBI.
RC STRAIN=cv. W115;
RX PubMed=23275577; DOI=10.1105/tpc.112.105247;
RA Spitzer-Rimon B., Farhi M., Albo B., Cna'ani A., Ben Zvi M.M., Masci T.,
RA Edelbaum O., Yu Y., Shklarman E., Ovadis M., Vainstein A.;
RT "The R2R3-MYB-like regulatory factor EOBI, acting downstream of EOBII,
RT regulates scent production by activating ODO1 and structural scent-related
RT genes in petunia.";
RL Plant Cell 24:5089-5105(2012).
RN [5]
RP REPRESSION BY LHY.
RX PubMed=26124104; DOI=10.1073/pnas.1422875112;
RA Fenske M.P., Hewett Hazelton K.D., Hempton A.K., Shim J.S., Yamamoto B.M.,
RA Riffell J.A., Imaizumi T.;
RT "Circadian clock gene LATE ELONGATED HYPOCOTYL directly regulates the
RT timing of floral scent emission in Petunia.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:9775-9780(2015).
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 (By similarity). Involved in the accumulation of volatile
CC benzoides in flowers, scent attracting pollinators (e.g. the night-
CC active hawkmoth pollinator Manduca sexta) (PubMed:15805488).
CC {ECO:0000250|UniProtKB:P0A6D3, ECO:0000269|PubMed:15805488}.
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:0000269|PubMed:1939260};
CC -!- ACTIVITY REGULATION: Repressed by glyphosate in a competitive
CC inhibition manner. {ECO:0000269|PubMed:1939260}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for phosphoenolpyruvate {ECO:0000269|PubMed:1939260};
CC KM=7.8 uM for 3-phosphoshikimate {ECO:0000269|PubMed:1939260};
CC KM=1.9 uM for 5-O-(1-carboxyvinyl)-3-phosphoshikimate
CC {ECO:0000269|PubMed:1939260};
CC KM=0.59 mM for phosphate {ECO:0000269|PubMed:1939260};
CC Note=kcat is 36 sec(-1). {ECO:0000269|PubMed:1939260};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000269|PubMed:1939260}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower petals, and, to a lower
CC extent, in roots, stems and anthers, but barely in leaves.
CC {ECO:0000269|PubMed:3346248}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring at the end
CC of the light period in flowers; this expression is monitored by ODO1-
CC mediated induction and by LHY binding and repression to cis-regulatory
CC evening elements in its promoter (PubMed:15805488, PubMed:26124104).
CC Triggered by EOBI in flowers (PubMed:23275577).
CC {ECO:0000269|PubMed:15805488, ECO:0000269|PubMed:23275577,
CC ECO:0000269|PubMed:26124104}.
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. {ECO:0000303|PubMed:1939260}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000305}.
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DR EMBL; M21084; AAA33699.1; -; mRNA.
DR PIR; A28198; XUPJVS.
DR AlphaFoldDB; P11043; -.
DR SMR; P11043; -.
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 GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
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 Herbicide resistance; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:1939260"
FT CHAIN 73..516
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase,
FT chloroplastic"
FT /id="PRO_0000002290"
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"
FT MUTAGEN 173
FT /note="G->A: Resistance to glyphosate due to a lower
FT affinity. Slight reduction in EPSP synthase activity."
FT /evidence="ECO:0000269|PubMed:1939260"
SQ SEQUENCE 516 AA; 55537 MW; 1A753E717BE7BAF8 CRC64;
MAQINNMAQG IQTLNPNSNF HKPQVPKSSS FLVFGSKKLK NSANSMLVLK KDSIFMQKFC
SFRISASVAT AQKPSEIVLQ PIKEISGTVK LPGSKSLSNR ILLLAALSEG TTVVDNLLSS
DDIHYMLGAL KTLGLHVEED SANQRAVVEG CGGLFPVGKE SKEEIQLFLG NAGTAMRPLT
AAVTVAGGNS RYVLDGVPRM RERPISDLVD GLKQLGAEVD CFLGTKCPPV RIVSKGGLPG
GKVKLSGSIS SQYLTALLMA APLALGDVEI EIIDKLISVP YVEMTLKLME RFGISVEHSS
SWDRFFVRGG QKYKSPGKAF VEGDASSASY FLAGAAVTGG TITVEGCGTN SLQGDVKFAE
VLEKMGAEVT WTENSVTVKG PPRSSSGRKH LRAIDVNMNK MPDVAMTLAV VALYADGPTA
IRDVASWRVK ETERMIAICT ELRKLGATVE EGPDYCIITP PEKLNVTDID TYDDHRMAMA
FSLAACADVP VTINDPGCTR KTFPNYFDVL QQYSKH
