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| 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, 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. |
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| 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 |
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