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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-β-glucosidase I/II (EC 3.2.1.58) (EXG1).
• Baker's yeast glucan 1,3-β-glucosidase 2 (EC 3.2.1.58) (EXG2).
• Baker's yeast sporulation-specific glucan 1,3-β-glucosidase (SPR1).
• Caldocellum saccharolyticum β-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.

Henrissat B.

December 2004 / Pattern and text revised.

PROSITE method (with tools and information) covered by this documentation:

GLYCOSYL_HYDROL_F5, PS00659; Glycosyl hydrolases family 5 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.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00659 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00659 • Scan Swiss-Prot/TrEMBL entries against PS00659 • view ligand binding statistics

Matching PDB structures: 1A3H 1CEC 1CZ1 1E5J ... [ALL]

1	Authors	Beguin P.
	Title	Molecular biology of cellulose degradation.
	Source	Annu. Rev. Microbiol. 44:219-248(1990).
	PubMed ID	2252383
	DOI	10.1146/annurev.mi.44.100190.001251

2	Authors	Gilkes N.R., Henrissat B., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
	Title	Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
	Source	Microbiol. Rev. 55:303-315(1991).
	PubMed ID	1886523

3	Authors	Henrissat B., Claeyssens M., Tomme P., Lemesle L., Mornon J.-P.
	Title	Cellulase families revealed by hydrophobic cluster analysis.
	Source	Gene 81:83-95(1989).
	PubMed ID	2806912

4	Authors	Henrissat B.
	Title	A classification of glycosyl hydrolases based on amino acid sequence similarities.
	Source	Biochem. J. 280:309-316(1991).
	PubMed ID	1747104

5	Authors	Py B., Bortoli-German I., Haiech J., Chippaux M., Barras F.
	Title	Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His98 and Glu133 residues for catalysis.
	Source	Protein Eng. 4:325-333(1991).
	PubMed ID	1677466

E1
Source	http://www.uniprot.org/docs/glycosid

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