PROSITE documentation PDOC00640

Glycosyl hydrolases family 8 signature

Description

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 D [3] or as the glycosyl hydrolases family 8 [4,E1]. The enzymes which are currently known to belong to this family are listed below.

  • Acetobacter xylinum endonuclease cmcAX.
  • Bacillus strain KSM-330 acidic endonuclease K (Endo-K).
  • Cellulomonas josui endoglucanase 2 (celB).
  • Cellulomonas uda endoglucanase.
  • Clostridium cellulolyticum endoglucanases C (celcCC).
  • Clostridium thermocellum endoglucanases A (celA).
  • Erwinia chrysanthemi minor endoglucanase y (celY).
  • Bacillus circulans β-glucanase (EC 3.2.1.73).
  • Escherichia coli hypothetical protein yhjM.

The most conserved region in these enzymes is a stretch of about 20 residues that contains two conserved aspartate. The first asparatate is thought [5] to act as the nucleophile in the catalytic mechanism. We have used this region as a signature pattern.

Expert(s) to contact by email:

Henrissat B.

Last update:

November 1997 / Text revised.

Technical section

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

GLYCOSYL_HYDROL_F8, PS00812Glycosyl hydrolases family 8 signature  (PATTERN)
Consensus pattern: A-[ST]-D-[AG]-D-x(2)-[IM]-A-x-[SA]-[LIVM]-[LIVMG]-x-A-x(3)-[FW]
The first D is an active site residue
Sequences known to belong to this class detected by the pattern: ALL
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 PS00812
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00812
Scan Swiss-Prot/TrEMBL entries against PS00812
view ligand binding statistics
Matching PDB structures: 1CEM 1IS9 1KWF 1WZZ ... [ALL]

References

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 Alzari P.M., Souchon H., Dominguez R.
Title The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum.
Source Structure 4:265-275(1996).
PubMed ID 8805535
E1
Source http://www.uniprot.org/docs/glycosid

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