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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 G [3] or as the glycosyl hydrolases family 11 [4,E1]. The enzymes which are currently known to belong to this family are listed below.

• Aspergillus awamori xylanase C (xynC).
• Bacillus circulans, pumilus, stearothermophilus and subtilis xylanase (xynA).
• Clostridium acetobutylicum xylanase (xynB).
• Clostridium stercorarium xylanase A (xynA).
• Fibrobacter succinogenes xylanase C (xynC) which consist of two catalytic domains that both belong to family 10.
• Neocallimastix patriciarum xylanase A (xynA).
• 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.
• Schizophyllum commune xylanase A.
• Streptomyces lividans xylanases B (xlnB) and C (xlnC).
• Trichoderma reesei xylanases I and II.

Two of the conserved regions in these enzymes are centered on glutamic acid residues which have both been shown [5], in Bacillus pumilis xylanase, to be necessary for catalytic activity. We have used both regions as signature patterns.

Henrissat B.

April 2006 / Pattern revised.

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

GLYCOSYL_HYDROL_F11_1, PS00776; Glycosyl hydrolases family 11 active site signature 1  (PATTERN)

Consensus pattern: [PSA]-[LQ]-x-E-[YF]-Y-[LIVM](2)-[DE]-x-[FYWHN] E is an active site residue Sequences known to belong to this class detected by the pattern: ALL, except for Piromyces sp. xynA 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 PS00776 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00776 • Scan Swiss-Prot/TrEMBL entries against PS00776 • view ligand binding statistics

Matching PDB structures: 1AXK 1BCX 1BK1 1BVV ... [ALL]

GLYCOSYL_HYDROL_F11_2, PS00777; Glycosyl hydrolases family 11 active site signature 2  (PATTERN)

Consensus pattern: [LIVMF]-x(2)-E-[AG]-[YWG]-[QRFGS]-[SG]-[STAN]-G-x-[SAF] E is an active site residue Sequences known to belong to this class detected by the pattern: ALL, except for Piromyces sp. xynA Other sequence(s) detected in Swiss-Prot: 3.

• 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 PS00777 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00777 • Scan Swiss-Prot/TrEMBL entries against PS00777 • view ligand binding statistics

Matching PDB structures: 1AXK 1BK1 1BVV 1C5H ... [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	Ko E.P., Akatsuka H., Moriyama H., Shinmyo A., Hata Y., Katsube Y., Urabe I., Okada H.
	Title	Site-directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus.
	Source	Biochem. J. 288:117-121(1992).
	PubMed ID	1359880

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

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