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PROSITE documentation PDOC00097 [for PROSITE entry PS00104]

EPSP synthase signatures





Description

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) (EC 2.5.1.19) catalyzes the sixth step in the biosynthesis from chorismate of the aromatic amino acids (the shikimate pathway) in bacteria (gene aroA), plants and fungi (where it is part of a multifunctional enzyme which catalyzes five consecutive steps in this pathway) [1]. EPSP synthase has been extensively studied as it is the target of the potent herbicide glyphosate which inhibits the enzyme.

The sequence of EPSP from various biological sources shows that the structure of the enzyme has been well conserved throughout evolution. We selected two conserved regions as signature patterns. The first pattern corresponds to a region that is part of the active site and which is also important for the resistance to glyphosate [2]. The second pattern is located in the C-terminal part of the protein and contains a conserved lysine which seems to be important for the activity of the enzyme.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

April 2006 / Pattern revised.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

EPSP_SYNTHASE_1, PS00104; EPSP synthase signature 1  (PATTERN)

EPSP_SYNTHASE_2, PS00885; EPSP synthase signature 2  (PATTERN)


References

1AuthorsStallings W.C. Abdel-Meguid S.S. Lim L.W. Shieh H.-S. Dayringer H.E. Leimgruber N.K. Stegeman R.A. Anderson K.S. Sikorski J.A. Padgette S.R. Kishore G.M.
TitleStructure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold.
SourceProc. Natl. Acad. Sci. U.S.A. 88:5046-5050(1991).
PubMed ID11607190

2AuthorsPadgette S.R. Re D.B. Gaser C.S. Eicholtz D.A. Frazier R.B. Hironaka C.M. Levine E.B. Shah D.M. Fraley R.T. Kishore G.M.
TitleSite-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site.
SourceJ. Biol. Chem. 266:22364-22369(1991).
PubMed ID1939260



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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