{PDOC00120} {PS00129; GLYCOSYL_HYDROL_F31_1} {PS00707; GLYCOSYL_HYDROL_F31_2} {BEGIN} ******************************************** * Glycosyl hydrolases family 31 signatures * ******************************************** It has been shown [1,2,3,E1] that the following glycosyl hydrolases can be, on the basis of sequence similarities, classified into a single family: - Lysosomal alpha-glucosidase (EC 3.2.1.20) (acid maltase) is a vertebrate glycosidase active at low pH, which hydrolyzes alpha(1->4) and alpha(1->6) linkages in glycogen, maltose, and isomaltose. - Alpha-glucosidase (EC 3.2.1.20) from the yeast Candida tsukunbaensis. - Alpha-glucosidase (EC 3.2.1.20) (gene malA) from the archebacteria Sulfolobus solfataricus. - Intestinal sucrase-isomaltase (EC 3.2.1.48 / EC 3.2.1.10) is a vertebrate membrane-bound, multifunctional enzyme complex which hydrolyzes sucrose, maltose and isomaltose. The sucrase and isomaltase domains of the enzyme are homologous (41% of amino acid identity) and have most probably evolved by duplication. - Glucoamylase 1 (EC 3.2.1.3) (glucan 1,4-alpha-glucosidase) from various fungal species. - Yeast hypothetical protein YBR229c. - Fission yeast hypothetical protein SpAC30D11.01c. An aspartic acid has been implicated [4] in the catalytic activity of sucrase, isomaltase, and lysosomal alpha-glucosidase. The region around this active residue is highly conserved and can be used as a signature pattern. We have used a second region, which contains two conserved cysteines, as an additional signature pattern. -Consensus pattern: [GFY]-[LIVMF]-W-x-D-M-[NSA]-E [D is the active site residue] -Sequences known to belong to this class detected by the pattern: ALL, except for SpAC30D11.01c. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: G-[AVP]-[DT]-[LIVMTAS]-[CG]-G-[FY]-x(3)-[STP]-x(3)-L-[CL]- x-R-W-x(2)-[LVMI]-[GSA]-[SA]-[FY]-x-P-[FY]-x-R-[DNA] -Sequences known to belong to this class detected by the pattern: ALL, except for YBR229c which lacks the two cysteines, rat sucrase-isomaltase and malA. -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] Kinsella B.T., Hogan S., Larkin A., Cantwell B.A. "Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase." Eur. J. Biochem. 202:657-664(1991). PubMed=1761061 [ 3] Naim H.Y., Niermann T., Kleinhans U., Hollenberg C.P., Strasser A.W.M. "Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene." FEBS Lett. 294:109-112(1991). PubMed=1743281 [ 4] Hermans M.M.P., Kroos M.A., van Beeumen J., Oostra B.A., Reuser A.J. "Human lysosomal alpha-glucosidase. Characterization of the catalytic site." J. Biol. Chem. 266:13507-13512(1991). PubMed=1856189 [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}