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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 E [3] or as the glycosyl hydrolases family 9 [4,E1]. The enzymes which are currently known to belong to this family are listed below.

• Butyrivibrio fibrisolvens cellodextrinase 1 (ced1).
• Cellulomonas fimi endoglucanases B (cenB) and C (cenC).
• Clostridium cellulolyticum endoglucanase G (celCCG).
• Clostridium cellulovorans endoglucanase C (engC).
• Clostridium stercoararium endoglucanase Z (avicelase I) (celZ).
• Clostridium thermocellum endoglucanases D (celD), F (celF) and I (celI).
• Fibrobacter succinogenes endoglucanase A (endA).
• Pseudomonas fluorescens endoglucanase A (celA).
• Streptomyces reticuli endoglucanase 1 (cel1).
• Thermomonospora fusca endoglucanase E-4 (celD).
• Dictyostelium discoideum spore germination specific endoglucanase 270-6. This slime mold enzyme may digest the spore cell wall during germination, to release the enclosed amoeba.
• Endoglucanases from plants such as Avocado or French bean. In plants this enzyme may be involved the fruit ripening process.

Two of the most conserved regions in these enzymes are centered on conserved residues which have been shown [5,6], in the endoglucanase D from Cellulomonas thermocellum, to be important for the catalytic activity. The first region contains an active site histidine and the second region contains two catalytically important residues: an aspartate and a glutamate. We have used both regions as signature patterns.

Henrissat B.

November 1997 / Text revised.

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

GLYCOSYL_HYDROL_F9_1, PS00592; Glycosyl hydrolases family 9 active sites signature 1  (PATTERN)

Consensus pattern: [STV]-x-[LIVMFY]-[STV]-x(2)-G-x-[NKR]-x(4)-[PLIVM]-H-x-R H is an active site residue Sequences known to belong to this class detected by the pattern: ALL, except for Cellulomonas fimi cenC and Streptomyces reticuli cel1 Other sequence(s) detected in Swiss-Prot: 2.

• 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 PS00592 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00592 • Scan Swiss-Prot/TrEMBL entries against PS00592 • view ligand binding statistics

Matching PDB structures: 1CLC 1G87 1GA2 1JS4 ... [ALL]

GLYCOSYL_HYDROL_F9_2, PS00698; Glycosyl hydrolases family 9 active sites signature 2  (PATTERN)

Consensus pattern: [FYW]-x-D-x(4)-[FYW]-x(3)-E-x-[STA]-x(3)-N-[STA] D and E are active site residues Sequences known to belong to this class detected by the pattern: ALL, except for Fibrobacter succinogenes endA whose sequence seems to be incorrect Other sequence(s) detected in Swiss-Prot: NONE.

• 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 PS00698 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00698 • Scan Swiss-Prot/TrEMBL entries against PS00698 • view ligand binding statistics

Matching PDB structures: 1CLC 1G87 1GA2 1JS4 ... [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	Tomme P., Chauvaux S., Beguin P., Millet J., Aubert J.-P., Claeyssens M.
	Title	Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum.
	Source	J. Biol. Chem. 266:10313-10318(1991).
	PubMed ID	2037583

6	Authors	Tomme P., van Beeumen J., Claeyssens M.
	Title	Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum.
	Source	Biochem. J. 285:319-324(1992).
	PubMed ID	1637316

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

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