AROA_ECOLI
ID AROA_ECOLI Reviewed; 427 AA.
AC P0A6D3; P07638; P78222;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
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, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556, ECO:0000269|PubMed:6229418};
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, ECO:0000303|Ref.1};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|Ref.1};
GN OrderedLocusNames=b0908, JW0891;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Duncan K., Lewendon A., Coggins J.R.;
RT "The complete amino acid sequence of Escherichia coli 5-
RT enolpyruvylshikimate 3-phosphate synthase.";
RL FEBS Lett. 170:59-63(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 380-427.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Palma C.A., Allen E., Araujo R., Aparicio A.M., Botstein D., Cherry M.,
RA Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Kim K.,
RA Komp C., Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=6229418; DOI=10.1016/0014-5793(84)80027-7;
RA Duncan K., Lewendon A., Coggins J.R.;
RT "The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an
RT overproducing strain of Escherichia coli.";
RL FEBS Lett. 165:121-127(1984).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=1899181; DOI=10.1016/0003-9861(91)90316-b;
RA Huynh Q.K.;
RT "5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli -- the
RT substrate analogue bromopyruvate inactivates the enzyme by modifying Cys-
RT 408 and Lys-411.";
RL Arch. Biochem. Biophys. 284:407-412(1991).
RN [8]
RP PHOTO-OXIDATION AT HIS-385.
RX PubMed=8452542; DOI=10.1042/bj2900525;
RA Huynh Q.K.;
RT "Photo-oxidation of 5-enolpyruvoylshikimate-3-phosphate synthase from
RT Escherichia coli: evidence for a reactive imidazole group (His385) at the
RT herbicide glyphosate-binding site.";
RL Biochem. J. 290:525-530(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=11607190; DOI=10.1073/pnas.88.11.5046;
RA Stallings W.C., Abdel-Meguid S.S., Lim L.W., Shieh H.-S., Dayringer H.E.,
RA Leimgruber N.K., Stegeman R.A., Anderson K.S., Sikorski J.A.,
RA Padgette S.R., Kishore G.M.;
RT "Structure and topological symmetry of the glyphosate target 5-enol-
RT pyruvylshikimate-3-phosphate synthase: a distinctive protein fold.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5046-5050(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOG.
RX PubMed=11171958; DOI=10.1073/pnas.98.4.1376;
RA Schonbrunn E., Eschenburg S., Shuttleworth W.A., Schloss J.V., Amrhein N.,
RA Evans J.N., Kabsch W.;
RT "Interaction of the herbicide glyphosate with its target enzyme 5-
RT enolpyruvylshikimate 3-phosphate synthase in atomic detail.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1376-1380(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-96 IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-96,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=12430021; DOI=10.1007/s00425-002-0908-0;
RA Eschenburg S., Healy M.L., Priestman M.A., Lushington G.H., Schonbrunn E.;
RT "How the mutation glycine96 to alanine confers glyphosate insensitivity to
RT 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli.";
RL Planta 216:129-135(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANT ALA-313 IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP ASP-313, ACTIVE SITE, AND REACTION MECHANISM.
RX PubMed=13129913; DOI=10.1074/jbc.m309741200;
RA Eschenburg S., Kabsch W., Healy M.L., Schonbrunn E.;
RT "A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl
RT transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA)
RT derived from X-ray structures of their tetrahedral reaction intermediate
RT states.";
RL J. Biol. Chem. 278:49215-49222(2003).
RN [13]
RP STRUCTURE BY NMR OF 25-240.
RA Young J.K., Stauffer M.E., Kim H.J., Helms G.L., Evans J.N.S.;
RT "Letter: Substrate-induced structural changes to the isolated N-terminal
RT domain of 5-enolpyruvylshikimate-3-phosphate synthase.";
RL Submitted (MAY-2003) to the PDB data bank.
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE ANALOGS, ACTIVITY REGULATION, ACTIVE SITE, AND
RP REACTION MECHANISM.
RX PubMed=15736934; DOI=10.1021/bi048198d;
RA Priestman M.A., Healy M.L., Becker A., Alberg D.G., Bartlett P.A.,
RA Lushington G.H., Schonbrunn E.;
RT "Interaction of phosphonate analogues of the tetrahedral reaction
RT intermediate with 5-enolpyruvylshikimate-3-phosphate synthase in atomic
RT detail.";
RL Biochemistry 44:3241-3248(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16225867; DOI=10.1016/j.febslet.2005.09.066;
RA Priestman M.A., Healy M.L., Funke T., Becker A., Schonbrunn E.;
RT "Molecular basis for the glyphosate-insensitivity of the reaction of 5-
RT enolpyruvylshikimate 3-phosphate synthase with shikimate.";
RL FEBS Lett. 579:5773-5780(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE ANALOGS, FUNCTION, ACTIVE SITE, AND ACTIVITY
RP REGULATION.
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).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS L101 AND S101 IN COMPLEX
RP WITH SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF PRO-101, ACTIVE SITE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17855366; DOI=10.1074/jbc.m705624200;
RA Healy-Fried M.L., Funke T., Priestman M.A., Han H., Schonbrunn E.;
RT "Structural basis of glyphosate tolerance resulting from mutations of
RT Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase.";
RL J. Biol. Chem. 282:32949-32955(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF THR-97 AND PRO-101, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19211556; DOI=10.1074/jbc.m809771200;
RA Funke T., Yang Y., Han H., Healy-Fried M., Olesen S., Becker A.,
RA Schonbrunn E.;
RT "Structural basis of glyphosate resistance resulting from the double
RT mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-
RT phosphate synthase from Escherichia coli.";
RL J. Biol. Chem. 284:9854-9860(2009).
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:12430021, ECO:0000269|PubMed:13129913,
CC ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366,
CC ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556,
CC ECO:0000269|PubMed:6229418}.
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, ECO:0000269|PubMed:12430021,
CC ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:16225867,
CC ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399,
CC ECO:0000269|PubMed:19211556, ECO:0000269|PubMed:6229418};
CC -!- ACTIVITY REGULATION: Competitively inhibited by glyphosate
CC (PubMed:12430021, PubMed:6229418). Inhibited by (S)- and (R)-
CC phosphonates analogs (PubMed:15736934). Inhibited by (R)-difluoromethyl
CC analogs of the tetrahedral reaction intermediate (PubMed:16225867).
CC Inhibited by bromopyruvate (PubMed:1899181).
CC {ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:15736934,
CC ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17958399,
CC ECO:0000269|PubMed:1899181, ECO:0000269|PubMed:6229418}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0035 mM for S3P (at pH 7 and 25 degrees Celsius
CC {ECO:0000269|PubMed:6229418};
CC KM=0.015 mM for PEP (at pH 7 and 25 degrees Celsius
CC {ECO:0000269|PubMed:6229418};
CC KM=0.045 mM for PEP (at pH 7.5 and 25 degrees Celsius
CC {ECO:0000269|PubMed:19211556};
CC KM=0.048 mM for S3P (at pH 7.5 and 25 degrees Celsius
CC {ECO:0000269|PubMed:19211556};
CC KM=0.06 mM for PEP (at pH 7.5 and 25 degrees Celsius
CC {ECO:0000269|PubMed:17855366};
CC KM=0.06 mM for S3P (at pH 7.5 and 25 degrees Celsius
CC {ECO:0000269|PubMed:17855366};
CC KM=0.088 mM for PEP (at pH 6.8 and 20 degrees Celsius
CC {ECO:0000269|PubMed:12430021};
CC KM=0.09 mM for S3P (at pH 5.5 and 20 degrees Celsius
CC {ECO:0000269|PubMed:16225867};
CC KM=0.1 mM for PEP (at pH 5.5 and 20 degrees Celsius
CC {ECO:0000269|PubMed:16225867};
CC KM=0.12 mM for S3P (at pH 6.8 and 20 degrees Celsius
CC {ECO:0000269|PubMed:12430021};
CC Vmax=50 umol/min/ug enzyme (at pH 7.5 and 25 degrees Celsius
CC {ECO:0000269|PubMed:17855366};
CC Vmax=53 umol/min/ug enzyme (at pH 5.5 and 20 degrees Celsius
CC {ECO:0000269|PubMed:16225867};
CC Vmax=57 umol/min/ug enzyme (at pH 7.5 and 25 degrees Celsius
CC {ECO:0000269|PubMed:19211556};
CC pH dependence:
CC Optimum pH is between 6 and 6.5. {ECO:0000269|PubMed:12430021,
CC ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366,
CC ECO:0000269|PubMed:19211556, ECO:0000269|PubMed:6229418};
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 ECO:0000269|PubMed:6229418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210,
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 EMBL; X00557; CAA25223.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73994.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35643.1; -; Genomic_DNA.
DR EMBL; U31523; AAA81514.1; -; Genomic_DNA.
DR PIR; C64830; XUECVS.
DR RefSeq; NP_415428.1; NC_000913.3.
DR RefSeq; WP_000445231.1; NZ_STEB01000006.1.
DR PDB; 1EPS; X-ray; 3.00 A; A=1-427.
DR PDB; 1G6S; X-ray; 1.50 A; A=1-427.
DR PDB; 1G6T; X-ray; 1.60 A; A=1-427.
DR PDB; 1MI4; X-ray; 1.70 A; A=1-427.
DR PDB; 1P88; NMR; -; A=25-240.
DR PDB; 1P89; NMR; -; A=25-240.
DR PDB; 1Q36; X-ray; 1.60 A; A=1-427.
DR PDB; 1X8R; X-ray; 1.50 A; A=1-427.
DR PDB; 1X8T; X-ray; 1.90 A; A=1-427.
DR PDB; 2AA9; X-ray; 1.50 A; A=1-427.
DR PDB; 2AAY; X-ray; 1.55 A; A=1-427.
DR PDB; 2PQ9; X-ray; 1.60 A; A=1-427.
DR PDB; 2QFQ; X-ray; 1.50 A; A=1-427.
DR PDB; 2QFS; X-ray; 1.55 A; A=1-427.
DR PDB; 2QFT; X-ray; 1.55 A; A=1-427.
DR PDB; 2QFU; X-ray; 1.60 A; A=1-427.
DR PDB; 3FJX; X-ray; 1.75 A; A=1-427.
DR PDB; 3FJZ; X-ray; 1.70 A; A=1-427.
DR PDB; 3FK0; X-ray; 1.70 A; A=1-427.
DR PDB; 3FK1; X-ray; 1.70 A; A=1-427.
DR PDBsum; 1EPS; -.
DR PDBsum; 1G6S; -.
DR PDBsum; 1G6T; -.
DR PDBsum; 1MI4; -.
DR PDBsum; 1P88; -.
DR PDBsum; 1P89; -.
DR PDBsum; 1Q36; -.
DR PDBsum; 1X8R; -.
DR PDBsum; 1X8T; -.
DR PDBsum; 2AA9; -.
DR PDBsum; 2AAY; -.
DR PDBsum; 2PQ9; -.
DR PDBsum; 2QFQ; -.
DR PDBsum; 2QFS; -.
DR PDBsum; 2QFT; -.
DR PDBsum; 2QFU; -.
DR PDBsum; 3FJX; -.
DR PDBsum; 3FJZ; -.
DR PDBsum; 3FK0; -.
DR PDBsum; 3FK1; -.
DR AlphaFoldDB; P0A6D3; -.
DR SMR; P0A6D3; -.
DR BioGRID; 4260011; 10.
DR DIP; DIP-48256N; -.
DR IntAct; P0A6D3; 3.
DR STRING; 511145.b0908; -.
DR BindingDB; P0A6D3; -.
DR ChEMBL; CHEMBL5033; -.
DR DrugBank; DB03116; 5-(1-Carboxy-1-Phosphonooxy-Ethoxyl)-Shikimate-3-Phosphate.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB04539; Glyphosate.
DR DrugBank; DB04328; Shikimate-3-Phosphate.
DR SWISS-2DPAGE; P0A6D3; -.
DR jPOST; P0A6D3; -.
DR PaxDb; P0A6D3; -.
DR PRIDE; P0A6D3; -.
DR EnsemblBacteria; AAC73994; AAC73994; b0908.
DR EnsemblBacteria; BAA35643; BAA35643; BAA35643.
DR GeneID; 58462003; -.
DR GeneID; 945528; -.
DR KEGG; ecj:JW0891; -.
DR KEGG; eco:b0908; -.
DR PATRIC; fig|1411691.4.peg.1368; -.
DR EchoBASE; EB0071; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_0_6; -.
DR InParanoid; P0A6D3; -.
DR OMA; YEDHRMA; -.
DR PhylomeDB; P0A6D3; -.
DR BioCyc; EcoCyc:AROA-MON; -.
DR BioCyc; MetaCyc:AROA-MON; -.
DR BRENDA; 2.5.1.19; 2026.
DR SABIO-RK; P0A6D3; -.
DR UniPathway; UPA00053; UER00089.
DR EvolutionaryTrace; P0A6D3; -.
DR PRO; PR:P0A6D3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IDA:UniProtKB.
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; IDA:EcoCyc.
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; Reference proteome; Transferase.
FT CHAIN 1..427
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088253"
FT REGION 94..97
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021,
FT ECO:0000269|PubMed:15736934, ECO:0000269|PubMed:16225867,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399,
FT ECO:0000269|PubMed:19211556"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:15736934, ECO:0000305|PubMed:11171958"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021,
FT ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934,
FT ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366,
FT ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021,
FT ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399,
FT ECO:0000269|PubMed:19211556"
FT BINDING 124
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556"
FT BINDING 169..171
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021,
FT ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934,
FT ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366,
FT ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556"
FT BINDING 197
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021,
FT ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399,
FT ECO:0000269|PubMed:19211556"
FT BINDING 336
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021,
FT ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399,
FT ECO:0000269|PubMed:19211556"
FT BINDING 340
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:12430021,
FT ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:15736934,
FT ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366,
FT ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556"
FT BINDING 344
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556"
FT BINDING 386
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556"
FT BINDING 411
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|PubMed:11171958, ECO:0000269|PubMed:16225867,
FT ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:19211556"
FT SITE 408
FT /note="Modified by bromopyruvate"
FT /evidence="ECO:0000269|PubMed:11171958"
FT SITE 411
FT /note="Modified by bromopyruvate"
FT /evidence="ECO:0000269|PubMed:11171958"
FT MUTAGEN 96
FT /note="G->A: Insensitive to glyphosate with unaltered
FT affinity for its first substrate S3P, but displays a 30-
FT fold lower affinity for its second substrate PEP."
FT /evidence="ECO:0000269|PubMed:12430021"
FT MUTAGEN 97
FT /note="T->I: This mutant is sensitive to glyphosate and
FT causes a substantial decrease in the affinity for PEP.
FT Insensitive to glyphosate but maintains high affinity for
FT PEP. It causes a shift of residue G96 toward the glyphosate
FT binding site, impairing efficient binding of glyphosate,
FT while the side chain of I97 points away from the substrate
FT binding site, facilitating PEP utilization; when associated
FT with S-101."
FT /evidence="ECO:0000269|PubMed:19211556"
FT MUTAGEN 101
FT /note="P->A: Displays a slight decrease of the affinity
FT binding for both S3P and PEP. Decreases the binding
FT affinity of glyphosate, reducing the potency of this
FT inhibitor."
FT /evidence="ECO:0000269|PubMed:17855366,
FT ECO:0000269|PubMed:19211556"
FT MUTAGEN 101
FT /note="P->G: Displays a slight decrease of the affinity
FT binding for both S3P and PEP. Decreases the binding
FT affinity of glyphosate, reducing the potency of this
FT inhibitor."
FT /evidence="ECO:0000269|PubMed:17855366,
FT ECO:0000269|PubMed:19211556"
FT MUTAGEN 101
FT /note="P->L: Displays a 2-fold lower affinity binding for
FT both S3P and PEP. Decreases the binding affinity of
FT glyphosate, reducing the potency of this inhibitor."
FT /evidence="ECO:0000269|PubMed:17855366,
FT ECO:0000269|PubMed:19211556"
FT MUTAGEN 101
FT /note="P->S: Displays a slight decrease of the affinity
FT binding for both S3P and PEP. Decreases the binding
FT affinity of glyphosate, reducing the potency of this
FT inhibitor. Insensitive to glyphosate but maintains high
FT affinity for PEP. It causes a shift of residue G96 toward
FT the glyphosate binding site, impairing efficient binding of
FT glyphosate, while the side chain of I97 points away from
FT the substrate-binding site, facilitating PEP utilization;
FT when associated with I-97."
FT /evidence="ECO:0000269|PubMed:17855366,
FT ECO:0000269|PubMed:19211556"
FT MUTAGEN 313
FT /note="D->A: The enolpyruvyl transfer reaction is halted
FT after formation of the tetrahedral adduct of the
FT substrates."
FT /evidence="ECO:0000269|PubMed:13129913"
FT CONFLICT 23
FT /note="S -> T (in Ref. 1; CAA25223)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="T -> R (in Ref. 1; CAA25223)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1P88"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1P88"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1G6S"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1G6S"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:1G6S"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:1G6S"
FT HELIX 416..423
FT /evidence="ECO:0007829|PDB:1G6S"
SQ SEQUENCE 427 AA; 46096 MW; B1F55469EB4D9F97 CRC64;
MESLTLQPIA RVDGTINLPG SKSVSNRALL LAALAHGKTV LTNLLDSDDV RHMLNALTAL
GVSYTLSADR TRCEIIGNGG PLHAEGALEL FLGNAGTAMR PLAAALCLGS NDIVLTGEPR
MKERPIGHLV DALRLGGAKI TYLEQENYPP LRLQGGFTGG NVDVDGSVSS QFLTALLMTA
PLAPEDTVIR IKGDLVSKPY IDITLNLMKT FGVEIENQHY QQFVVKGGQS YQSPGTYLVE
GDASSASYFL AAAAIKGGTV KVTGIGRNSM QGDIRFADVL EKMGATICWG DDYISCTRGE
LNAIDMDMNH IPDAAMTIAT AALFAKGTTT LRNIYNWRVK ETDRLFAMAT ELRKVGAEVE
EGHDYIRITP PEKLNFAEIA TYNDHRMAMC FSLVALSDTP VTILDPKCTA KTFPDYFEQL
ARISQAA
