AROA_AGRSC
ID AROA_AGRSC Reviewed; 455 AA.
AC Q9R4E4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|Ref.1};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210};
OS Agrobacterium sp. (strain CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC unclassified Agrobacterium.
OX NCBI_TaxID=268951;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-28; 47-61 AND
RP 321-333.
RA Barry G.F., Kishore G.M., Padgette S.R., Stallings W.C.;
RT "Glyphosate-tolerant 5-enolpyruvylshikimate-3-phosphate synthases.";
RL Patent number US5633435, 27-MAY-1997.
RN [2]
RP PROTEIN SEQUENCE OF 1-15.
RX PubMed=8598558; DOI=10.1093/jn/126.3.728;
RA Harrison L.A., Bailey M.R., Naylor M.W., Ream J.E., Hammond B.G.,
RA Nida D.L., Burnette B.L., Nickson T.E., Mitsky T.A., Taylor M.L.,
RA Fuchs R.L., Padgette S.R.;
RT "The expressed protein in glyphosate-tolerant soybean, 5-
RT enolpyruvylshikimate-3-phosphate synthase from Agrobacterium sp. strain
RT CP4, is rapidly digested in vitro and is not toxic to acutely gavaged
RT mice.";
RL J. Nutr. 126:728-740(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF WILD-TYPE AND MUTANT GLY-100 IN
RP COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOG,
RP FUNCTION, AND MUTAGENESIS OF ALA-100.
RX PubMed=16916934; DOI=10.1073/pnas.0603638103;
RA Funke T., Han H., Healy-Fried M.L., Fischer M., Schonbrunn E.;
RT "Molecular basis for the herbicide resistance of Roundup Ready crops.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13010-13015(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 6-450 OF WILD-TYPE AND MUTANT
RP GLY-100 IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE ANALOGS, FUNCTION, ACTIVE
RP SITE, AND ACTIVITY REGULATION.
RC STRAIN=CP4;
RX PubMed=17958399; DOI=10.1021/bi701095u;
RA Funke T., Healy-Fried M.L., Han H., Alberg D.G., Bartlett P.A.,
RA Schonbrunn E.;
RT "Differential inhibition of class I and class II 5-enolpyruvylshikimate-3-
RT phosphate synthases by tetrahedral reaction intermediate analogues.";
RL Biochemistry 46:13344-13351(2007).
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:0000255|HAMAP-Rule:MF_00210,
CC ECO:0000269|PubMed:16916934, ECO:0000269|PubMed:17958399}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00210};
CC -!- ACTIVITY REGULATION: Competitively inhibited by glyphosate, (R)-
CC difluoromethyl and (R)-phosphonate analogs of the tetrahedral reaction
CC intermediate. {ECO:0000269|PubMed:17958399}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
CC glyphosate-tolerant soybean, canola, cotton and maize by Monsanto.
CC Developed to provide new weed-control options for farmers. Expression
CC of this protein in plants imparts high levels of glyphosate tolerance.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00210, ECO:0000305}.
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DR PDB; 2GG4; X-ray; 2.10 A; A=1-455.
DR PDB; 2GG6; X-ray; 1.64 A; A=1-455.
DR PDB; 2GGA; X-ray; 1.70 A; A=1-455.
DR PDB; 2GGD; X-ray; 1.70 A; A=1-455.
DR PDB; 2PQB; X-ray; 1.80 A; A=6-450.
DR PDB; 2PQC; X-ray; 1.60 A; A=6-450.
DR PDB; 2PQD; X-ray; 1.77 A; A=6-450.
DR PDBsum; 2GG4; -.
DR PDBsum; 2GG6; -.
DR PDBsum; 2GGA; -.
DR PDBsum; 2GGD; -.
DR PDBsum; 2PQB; -.
DR PDBsum; 2PQC; -.
DR PDBsum; 2PQD; -.
DR AlphaFoldDB; Q9R4E4; -.
DR SMR; Q9R4E4; -.
DR BRENDA; 2.5.1.19; 206.
DR UniPathway; UPA00053; UER00089.
DR EvolutionaryTrace; Q9R4E4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
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: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 PIRSF; PIRSF000505; EPSPS; 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 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cytoplasm; Direct protein sequencing; Genetically modified food;
KW Herbicide resistance; Transferase.
FT CHAIN 1..455
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088215"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..101
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:16916934"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000305|PubMed:17958399"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000305|PubMed:17958399"
FT BINDING 28..29
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:16916934, ECO:0000269|PubMed:17958399"
FT BINDING 33
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:16916934, ECO:0000269|PubMed:17958399"
FT BINDING 128
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:16916934"
FT BINDING 353
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:16916934, ECO:0000269|PubMed:17958399"
FT BINDING 357
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:16916934"
FT BINDING 405
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:16916934"
FT MUTAGEN 100
FT /note="A->G: Confers resistance to glyphosate."
FT /evidence="ECO:0000269|PubMed:16916934"
FT CONFLICT 2
FT /note="S -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2PQC"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 276..284
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 299..307
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:2PQC"
FT HELIX 436..443
FT /evidence="ECO:0007829|PDB:2PQC"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:2PQC"
SQ SEQUENCE 455 AA; 47588 MW; 236580D08D6EF422 CRC64;
MSHGASSRPA TARKSSGLSG TVRIPGDKSI SHRSFMFGGL ASGETRITGL LEGEDVINTG
KAMQAMGARI RKEGDTWIID GVGNGGLLAP EAPLDFGNAA TGCRLTMGLV GVYDFDSTFI
GDASLTKRPM GRVLNPLREM GVQVKSEDGD RLPVTLRGPK TPTPITYRVP MASAQVKSAV
LLAGLNTPGI TTVIEPIMTR DHTEKMLQGF GANLTVETDA DGVRTIRLEG RGKLTGQVID
VPGDPSSTAF PLVAALLVPG SDVTILNVLM NPTRTGLILT LQEMGADIEV INPRLAGGED
VADLRVRSST LKGVTVPEDR APSMIDEYPI LAVAAAFAEG ATVMNGLEEL RVKESDRLSA
VANGLKLNGV DCDEGETSLV VRGRPDGKGL GNASGAAVAT HLDHRIAMSF LVMGLVSENP
VTVDDATMIA TSFPEFMDLM AGLGAKIELS DTKAA
