 |
|
| 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.
Henrissat B.
November 1997 / Pattern and text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F45, PS01140; Glycosyl 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. |
|
|
|
| Matching PDB structures:
1HD5 2ENG 3ENG [ALL] |
References
| 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 |
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)