PROSITE documentation PDOC00097EPSP synthase signatures
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.
Last update:April 2006 / Pattern revised.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Stallings 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. |
| Title | Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 88:5046-5050(1991). | |
| PubMed ID | 11607190 |
| 2 | Authors | Padgette 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. |
| Title | Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site. | |
| Source | J. Biol. Chem. 266:22364-22369(1991). | |
| PubMed ID | 1939260 |
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.
View entry in original PROSITE document format
View entry in raw text format (no links)