{PDOC00946} {PS01232; PNP_UDP_1} {BEGIN} ****************************************************** * Purine and other phosphorylases family 1 signature * ****************************************************** The following phosphorylases belongs to the same family: - Purine nucleoside phosphorylase (EC 2.4.2.1) (PNP) from most bacteria (gene deoD). This enzyme catalyzes the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [1]. - Uridine phosphorylase (EC 2.4.2.3) (UdRPase) from bacteria (gene udp) and mammals. Catalyzes the cleavage of uridine into uracil and ribose-1- phosphate. The products of the reaction are used either as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis [2]. - 5'-methylthioadenosine phosphorylase (EC 2.4.2.28) (MTA phosphorylase) from Sulfolobus solfataricus [3]. As a signature pattern, we selected a conserved region in the central part of these enzymes. -Consensus pattern: [GST]-x-G-[LIVM]-G-x-[PA]-S-x-[GSTAL]-[IL]-x(3)-E-L -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: It should be noted that mammalian and some bacterial PNP as well as eukaryotic MTA phosphorylase belong to a different family of phosphorylases (see ). -Last update: December 2004 / Pattern and text revised. [ 1] Takehara M., Ling F., Izawa S., Inoue Y., Kimura A. "Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp." Biosci. Biotechnol. Biochem. 59:1987-1990(1995). PubMed=8534998 [ 2] Watanabe S.-I., Hino A., Wada K., Eliason J.F., Uchida T. "Purification, cloning, and expression of murine uridine phosphorylase." J. Biol. Chem. 270:12191-12196(1995). PubMed=7744869 [ 3] Cacciapuoti G., Porcelli M., Bertoldo C., De Rosa M., Zappia V. "Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds." J. Biol. Chem. 269:24762-24769(1994). PubMed=7929153 -------------------------------------------------------------------------------- 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}