{PDOC00621} {PS00775; GLYCOSYL_HYDROL_F3} {BEGIN} ******************************************** * Glycosyl hydrolases family 3 active site * ******************************************** It has been shown [1,2] that the following glycosyl hydrolases can be, on the basis of sequence similarities, classified into a single family: - Beta glucosidases (EC 3.2.1.21) from the fungi Aspergillus wentii (A-3), Hansenula anomala, Kluyveromyces fragilis, Saccharomycopsis fibuligera, (BGL1 and BGL2), Schizophyllum commune and Trichoderma reesei (BGL1). - Beta glucosidases from the bacteria Agrobacterium tumefaciens (Cbg1), Butyrivibrio fibrisolvens (bglA), Clostridium thermocellum (bglB), Escherichia coli (bglX), Erwinia chrysanthemi (bgxA) and Ruminococcus albus. - Alteromonas strain O-7 beta-hexosaminidase A (EC 3.2.1.52). - Bacillus subtilis hypothetical protein yzbA. - Escherichica coli hypothetical protein ycfO and HI0959, the corresponding Haemophilus influenzae protein. One of the conserved regions in these enzymes is centered on a conserved aspartic acid residue which has been shown [3], in Aspergillus wentii beta- glucosidase A3, to be implicated in the catalytic mechanism. We have used this region as a signature pattern. -Consensus pattern: [LIVM](2)-[KR]-x-[EQKRD]-x(4)-G-[LIVMFTC]-[LIVT]-[LIVMF]- [ST]-D-x(2)-[SGADNIT] [D is 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: April 2006 / Pattern revised. [ 1] Henrissat B. "A classification of glycosyl hydrolases based on amino acid sequence similarities." Biochem. J. 280:309-316(1991). PubMed=1747104 [ 2] Castle L.A., Smith K.D., Morris R.O. "Cloning and sequencing of an Agrobacterium tumefaciens beta-glucosidase gene involved in modifying a vir-inducing plant signal molecule." J. Bacteriol. 174:1478-1486(1992). PubMed=1537792 [ 3] Bause E., Legler G. "Isolation and structure of a tryptic glycopeptide from the active site of beta-glucosidase A3 from Aspergillus wentii." Biochim. Biophys. Acta 626:459-465(1980). PubMed=6783081 -------------------------------------------------------------------------------- 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}