ID   AROA2_TOBAC             Reviewed;         338 AA.
AC   P23281;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase 2;
DE            EC=2.5.1.19;
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase 2;
DE            Short=EPSP synthase 2;
DE   Flags: Fragment;
GN   Name=EPSPS-2;
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}.
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DR   EMBL; M61905; AAA34072.1; -; mRNA.
DR   PIR; S18354; S18354.
DR   AlphaFoldDB; P23281; -.
DR   SMR; P23281; -.
DR   STRING; 4097.P23281; -.
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   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; 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.
FT   CHAIN           <1..338
FT                   /note="3-phosphoshikimate 1-carboxyvinyltransferase 2"
FT                   /id="PRO_0000088341"
FT   ACT_SITE        225
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT   ACT_SITE        253
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT   BINDING         25
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT   BINDING         72..74
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         252
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT   BINDING         256
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT   BINDING         298
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT   BINDING         323
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6D3"
FT   NON_TER         1
SQ   SEQUENCE   338 AA;  36319 MW;  569E90218AD68B89 CRC64;
     LTAAVAVAGG NSRYVLDGVP RMRERPIGDL VDGLKQLGAE VDCFLGTKCP PVRIVSKGGL
     PGGKVKLSGS ISSQYLTALL MAAPLALGDV EIEIIDKLIS VLYVEMTLKL MERFGISVEH
     SSSWDRFVVR GGQKYKSPGK AYVEGDASSA SYFLAGAAVT GGTVTVEGCG TSSLQGDVKF
     AEVLEQMGAE VTWTENSVTV KGPPRNSSAM KHLRAIDVNM NKMPDVAMTL AVVALFADGP
     TAIRDVASWR VKETERMIAI CTELRKLGAT VEEGPDYCII TPPEKLNVTE IDTYDDHRMA
     MAFSLAACAD VPVTINDPGC TRKTFPNYFD VLQQYSKH