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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 F [3] or as the glycosyl hydrolases family 10 [4,E1]. The enzymes which are currently known to belong to this family are listed below.

• Aspergillus awamori xylanase A (xynA).
• Bacillus sp. strain 125 xylanase (xynA).
• Bacillus stearothermophilus xylanase.
• Butyrivibrio fibrisolvens xylanases A (xynA) and B (xynB).
• Caldocellum saccharolyticum bifunctional endoglucanase/exoglucanase (celB). This protein consists of two domains; it is the N-terminal domain, which has exoglucanase activity, which belongs to this family.
• Caldocellum saccharolyticum xylanase A (xynA).
• Caldocellum saccharolyticum ORF4. This hypothetical protein is encoded in the xynABC operon and is probably a xylanase.
• Cellulomonas fimi exoglucanase/xylanase (cex).
• Clostridium stercorarium thermostable celloxylanase.
• Clostridium thermocellum xylanases Y (xynY) and Z (xynZ).
• Cryptococcus albidus xylanase.
• Penicillium chrysogenum xylanase (gene xylP).
• Pseudomonas fluorescens xylanases A (xynA) and B (xynB).
• Ruminococcus flavefaciens bifunctional xylanase XYLA (xynA). This protein consists of three domains: a N-terminal xylanase catalytic domain that belongs to family 11 of glycosyl hydrolases; a central domain composed of short repeats of Gln, Asn an Trp, and a C-terminal xylanase catalytic domain that belongs to family 10 of glycosyl hydrolases.
• Streptomyces lividans xylanase A (xlnA).
• Thermoanaerobacter saccharolyticum endoxylanase A (xynA).
• Thermoascus aurantiacus xylanase.
• Thermophilic bacterium Rt8.B4 xylanase (xynA).

One of the conserved regions in these enzymes is centered on a conserved glutamic acid residue which has been shown [5], in the exoglucanase from Cellulomonas fimi, to be directly involved in glycosidic bond cleavage by acting as a nucleophile. We have used this region as a signature pattern.

Henrissat B.

April 2006 / Pattern revised.

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

GLYCOSYL_HYDROL_F10, PS00591; Glycosyl hydrolases family 10 active site  (PATTERN)

Consensus pattern: [GTA]-{QNAG}-{GSV}-[LIVN]-x-[IVMF]-[ST]-E-[LIY]-[DN]-[LIVMF] E is the active site residue Sequences known to belong to this class detected by the pattern: ALL, except for Thermoascus aurantiacus xylanase whose sequence seems to be incorrect Other sequence(s) detected in Swiss-Prot: 16.

• 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 PS00591 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00591 • Scan Swiss-Prot/TrEMBL entries against PS00591 • view ligand binding statistics

Matching PDB structures: 1B30 1B31 1B3V 1B3W ... [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	Tull D., Withers S.G., Gilkes N.R., Kilburn D.G., Warren R.A.J., Aebersold R.
	Title	Glutamic acid 274 is the nucleophile in the active site of a 'retaining' exoglucanase from Cellulomonas fimi.
	Source	J. Biol. Chem. 266:15621-15625(1991).
	PubMed ID	1678739

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

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