{PDOC01048} {PS01350; ISPF} {BEGIN} ****************************************************************** * 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature * ****************************************************************** The bacterial ispF protein [1] catalyzes the fifth step of the deoxyxylulose- 5-phosphate pathway (DXP) of isoprenoid biosynthesis; the conversion of 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate into 2C-methyl-D- erythritol 2,4-cyclodiphosphate and CMP. It can also converts 4- diphosphocytidyl-2C-methyl-D-erythritol into 2C-methyl-D-erythritol 3,4- cyclophosphate and CMP. In addition to bacterial ispF, this family also includes: - Plasmodium falciparum hypothetical protein PfB0420W. These are proteins of around 20 kDa whose sequence is well conserved. As a signature pattern, we selected a well conserved region located in the N- terminal part of these proteins. -Consensus pattern: S-[DN]-[GA]-D-[LIVAP]-[LIVAG]-x-H-[STAC]-x(2)-[DNT]-[SAG]- x(2)-[SGA] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2006 / Pattern revised. [ 1] Rohdich F., Wungsintaweekul J., Fellermeier M., Sagner S., Herz S., Kis K., Eisenreich W., Bacher A., Zenk M.H. "Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol." Proc. Natl. Acad. Sci. U.S.A. 96:11758-11763(1999). PubMed=10518523; -------------------------------------------------------------------------------- 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 -------------------------------------------------------------------------------- {END}