PROSITE documentation PDOC00877

Glycosyl hydrolases family 45 active site

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 K or as the glycosyl hydrolases family 45 [3,E1]. The enzymes which are currently known to belong to this family are listed below.

  • Endoglucanase 5 from Humicola insolens.
  • Endoglucanase 5 from Trichoderma reesei (egl5).
  • Endoglucanase K from Fusarium oxysporum.
  • Endoglucanase B from Pseudomonas fluorescens (celB).
  • Endoglucanase 1 from Ustilago maydis (egl1).

The best conserved regions in these enzymes is located in the N-terminal section. It contains an aspartic acid residue which has been shown [4] to act as a nucleophile in the catalytic mechanism. We use this region as a signature pattern.

Expert(s) to contact by email:

Henrissat B.

Last update:

November 1997 / Pattern and text revised.

Technical section

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

GLYCOSYL_HYDROL_F45, PS01140Glycosyl hydrolases family 45 active site  (PATTERN)
Consensus pattern: [STA]-T-R-Y-[FYW]-D-x(5)-[CA]
The 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 PS01140
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01140
Scan Swiss-Prot/TrEMBL entries against PS01140
view ligand binding statistics
Matching PDB structures: 1HD5 2ENG 3ENG [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., Bairoch A.
Title New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.
Source Biochem. J. 293:781-788(1993).
PubMed ID 8352747
4 Authors Davies G.J., Dodson G.G., Hubbard R.E., Tolley S.P., Dauter Z., Wilson K.S., Hjort C., Mikkelsen J.M., Rasmussen G., Schuelein M.
Title Structure and function of endoglucanase V.
Source Nature 365:362-364(1993).
PubMed ID 8377830
DOI 10.1038/365362a0
E1
Source http://www.uniprot.org/docs/glycosid

Copyright

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)