PROSITE documentation PDOC00622Glycosyl hydrolases family 11 (GH11) active sites signatures and domain profile
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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 (GH11) [4,E1,E2]. Family 11 is monospecific, only consisting of xylanases. 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.
The GH11 domain folds into a jelly-roll shape likened to a partially closed right hand (see <PDB:4HK8>). Several anti-parallel β-strands bend almost 90 degrees to produce a substrate-binding groove characteristic of the GH11 domain active sites. Two catalytic Glu residues face each other from opposite sides of the groove. The hydrolysis reaction is believed to follow a double-displacement mechanism, with one Glu residue acting as a general acid/base catalyst and the other as a nucleophile.
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. We have also developed a profile that covers the entire GH11 domain.
Expert(s) to contact by email: Last update:June 2015 / Text revised; profile added.
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PROSITE methods (with tools and information) covered by this documentation:
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 |
6 | Authors | Wan Q. Zhang Q. Hamilton-Brehm S. Weiss K. Mustyakimov M. Coates L. Langan P. Graham D. Kovalevsky A. |
Title | X-ray crystallographic studies of family 11 xylanase Michaelis and product complexes: implications for the catalytic mechanism. | |
Source | Acta Crystallogr. D 70:11-23(2014). | |
PubMed ID | 24419374 | |
DOI | 10.1107/S1399004713023626 |
E1 | Title | https://www.uniprot.org/docs/glycosid |
E2 | Title | https://www.cazy.org/GH11.html |
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