{PDOC00565} {PS00659; GLYCOSYL_HYDROL_F5} {BEGIN} ****************************************** * Glycosyl hydrolases family 5 signature * ****************************************** The microbial degradation of cellulose and xylans requires several types of enzymes such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) (exoglucanases), or xylanases (EC 3.2.1.8) [1,2]. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. One of these families is known as the cellulase family A [3] or as the glycosyl hydrolases family 5 [4,E1]. The enzymes which are currently known to belong to this family are listed below. - Endoglucanases from various species and strains of Bacillus. - Butyrivibrio fibrisolvens endoglucanases 1 (end1) and A (celA). - Caldocellum saccharolyticum bifunctional endoglucanase/exoglucanase (celB). This protein consists of two domains; it is the C-terminal domain, which has endoglucanase activity, which belongs to this family. - Clostridium acetobutylicum endoglucanase (eglA). - Clostridium cellulolyticum endoglucanases A (celccA) and D (celccD). - Clostridium cellulovorans endoglucanase B (engB) and D (engD). - Clostridium thermocellum endoglucanases B (celB), C (celC), E (celE), G (celG) and H (celH). - Erwinia chrysanthemi endoglucanase Z (celZ). - Fibrobacter succinogenes endoglucanase 3 (cel-3). - Pseudomonas fluorescens endoglucanase C (celC). - Pseudomonas solanacearum endoglucanase (egl). - Robillarda strain Y-20 endoglucanase I. - Ruminococcus albus endoglucanases I (EG-I), A (celA), and B (celB). - Ruminococcus flavefaciens cellodextrinase A (celA). - Ruminococcus flavefaciens endoglucanase E (celE). - Streptomyces lividans endoglucanase. - Thermomonospora fusca endoglucanase E-5 (celE). - Trichoderma reesei endoglucanase II (EGLII). - Xanthomonas campestris endoglucanase (engxcA). As well as: - Baker's yeast glucan 1,3-beta-glucosidase I/II (EC 3.2.1.58) (EXG1). - Baker's yeast glucan 1,3-beta-glucosidase 2 (EC 3.2.1.58) (EXG2). - Baker's yeast sporulation-specific glucan 1,3-beta-glucosidase (SPR1). - Caldocellum saccharolyticum beta-mannanase (EC 3.2.1.78) (manA). - Yeast hypothetical protein YBR056w. - Yeast hypothetical protein YIR007w. One of the conserved regions in these enzymes contains a conserved glutamic acid residue which is potentially involved [5] in the catalytic mechanism. We use this region as a signature pattern. -Consensus pattern: [LIV]-[LIVMFYWGA](2)-[DNEQG]-[LIVMGST]-{SENR}-N-E-[PV]- [RHDNSTLIVFY] [E may be an active site residue] -Sequences known to belong to this class detected by the pattern: ALL, except for Robillarda Y-20 endoglucanase I whose sequence is known to be incorrect and yeast YBR056w. -Other sequence(s) detected in Swiss-Prot: 28. -Expert(s) to contact by email: Henrissat B.; bernie@afmb.cnrs-mrs.fr -Last update: December 2004 / Pattern and text revised. [ 1] Beguin P. "Molecular biology of cellulose degradation." Annu. Rev. Microbiol. 44:219-248(1990). PubMed=2252383; DOI=10.1146/annurev.mi.44.100190.001251 [ 2] Gilkes N.R., Henrissat B., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. "Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families." Microbiol. Rev. 55:303-315(1991). PubMed=1886523 [ 3] Henrissat B., Claeyssens M., Tomme P., Lemesle L., Mornon J.-P. "Cellulase families revealed by hydrophobic cluster analysis." Gene 81:83-95(1989). PubMed=2806912 [ 4] Henrissat B. "A classification of glycosyl hydrolases based on amino acid sequence similarities." Biochem. J. 280:309-316(1991). PubMed=1747104 [ 5] Py B., Bortoli-German I., Haiech J., Chippaux M., Barras F. "Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis." Protein Eng. 4:325-333(1991). PubMed=1677466 [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}