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Database: UniProt
Entry: F6I398_VITVI
LinkDB: F6I398_VITVI
Original site: F6I398_VITVI 
ID   F6I398_VITVI            Unreviewed;       497 AA.
AC   F6I398;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|ARBA:ARBA00012450, ECO:0000256|RuleBase:RU004164};
DE            EC=2.5.1.19 {ECO:0000256|ARBA:ARBA00012450, ECO:0000256|RuleBase:RU004164};
GN   OrderedLocusNames=VIT_15s0048g00360 {ECO:0000313|EMBL:CCB61416.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB61416.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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:0000256|ARBA:ARBA00001901,
CC         ECO:0000256|RuleBase:RU004164};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       6/7. {ECO:0000256|ARBA:ARBA00004811, ECO:0000256|RuleBase:RU004164}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|ARBA:ARBA00009948, ECO:0000256|RuleBase:RU004164}.
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DR   EMBL; FN596739; CCB61416.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6I398; -.
DR   STRING; 29760.F6I398; -.
DR   PaxDb; 29760-VIT_15s0048g00360-t01; -.
DR   EnsemblPlants; Vitvi15g01491_t001; Vitvi15g01491_P001; Vitvi15g01491.
DR   Gramene; Vitvi15g01491_t001; Vitvi15g01491_P001; Vitvi15g01491.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_024321_0_0_1; -.
DR   InParanoid; F6I398; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000009183; Chromosome 15.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR   CDD; cd01556; EPSP_synthase; 1.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 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   NCBIfam; TIGR01356; aroA; 1.
DR   PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   PIRSF; PIRSF000505; EPSPS; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU004164};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU004164};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004164}.
FT   DOMAIN          85..494
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
SQ   SEQUENCE   497 AA;  52791 MW;  928078F7CA1F4AFA CRC64;
     MAQVTRIISG GVQNGPLLPN LSKPHKPTPP FTTPFLRSGP NVSSFSLKHE RAVSNSVVSV
     RAPFRVSASV ATKEKLSTVP EIVLQPIKEI SGTITLPGSK SLSNRILLLA ALSEGTTVVD
     NLLNSEDVHY MLGALRTLGL QVEEQSENKR VIVQGCGGQF PVGNGSVDQV QLFLGNCATA
     TRALTAAVTA AGGNASYVLD GVLRMRERPI GDLVTGLKQL GADVNCFLGT NCPPVYVNGN
     GGLPGGKVKL SGSISSQYLT ALLMAAPLAL GDVEIEIIDR LISIPYVEMT LKVMERFGVS
     VEHGNTWDRR FLIRGGKKYN ASYFLAGAAV TGGTVTVEGC GTSSLQGDVK FAEVLEQTGA
     KVSWTENSVT VTGPPRDSSG RKHLRAIDVN MNEMPDVAIT LAVVALYADG PTAIRDVASW
     RVKETERMIA ICTELRKLGA TVVEGPDYCV ITPPEKLNVT SIDTYDDHRM AMAFSLAACA
     DVPVTIKDPG CTKEKLP
//
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