{PDOC00787} {PS01027; GLYCOSYL_HYDROL_F39} {BEGIN} ****************************************************** * Glycosyl hydrolases family 39 putative active site * ****************************************************** It has been shown [1,E1] that the following glycosyl hydrolases can be classified into a single family on the basis of sequence similarities: - Mammalian lysosomal alpha-L-iduronidase (EC 3.2.1.76). - Caldocellum saccharolyticum and Thermoanaerobacter saccharolyticum beta- xylosidase (EC 3.2.1.37) (gene xynB). The best conserved regions in these enzymes is located in the N-terminal section. It contains a glutamic acid residue which, on the basis of similarities with other families of glycosyl hydrolases [2], probably acts as the proton donor in the catalytic mechanism. We use this region as a signature pattern. -Consensus pattern: W-x-F-E-x-W-N-E-P-[DN] [The second E may be the active site residue] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Expert(s) to contact by email: Henrissat B.; bernie@afmb.cnrs-mrs.fr -Last update: May 2004 / Text revised. [ 1] Henrissat B., Bairoch A. "New families in the classification of glycosyl hydrolases based on amino acid sequence similarities." Biochem. J. 293:781-788(1993). PubMed=8352747 [ 2] Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.-P., Davies G. "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases." Proc. Natl. Acad. Sci. U.S.A. 92:7090-7094(1995). PubMed=7624375 [E1] https://www.uniprot.org/docs/glycosid -------------------------------------------------------------------------------- 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}