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| PROSITE documentation PDOC00507 |
Glycosyl hydrolases family 17 signature
Description:
It has been shown [1,2] that the following glycosyl hydrolases can be
classified into a single family on the basis of sequence similarities:
- Glucan endo-1,3-β-D-glucosidases (EC 3.2.1.39) (endo-(1->3)-β-
glucanase) from various plants. This enzyme may be involved in the defense
of plants against pathogens through its ability to degrade fungal cell wall
polysaccharides.
- Glucan 1,3-β-glucosidase (EC 3.2.1.58) (exo-(1->3)-β-glucanase) from
yeast (gene BGL2). This enzyme may play a role in cell expansion during
growth, in cell-cell fusion during mating, and in spore release during
sporulation.
- Lichenases (EC 3.2.1.73) (endo-(1->3,1->4)-β-glucanase) from various
plants.
The best conserved region in the sequence of these enzymes is located in their
central section. This region contains a conserved tryptophan residue which
could be involved in the interaction with the glucan substrates [2] and it
also contains a conserved glutamate which has been shown [3] 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:
December 2004 / Pattern and text revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F17, PS00587; Glycosyl hydrolases family 17 signature (PATTERN) |
| Consensus pattern: |
[LIVMKS]-x-[LIVMFYWA](3)-[STAG]-E-[STACVI]-G-[WY]-P-[STN]-x-[SAGQ]
E 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:
1AQ0 1GHR 1GHS [ALL] |
References:
| 1 |
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 |
| 2 |
Authors | Ori N., Sessa G., Lotan T., Himmelhoch S., Fluhr R. |
| Title | A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass. |
| Source | EMBO J. 9:3429-3436(1990). |
| PubMed ID | 2120041 |
| 3 |
Authors | Varghese J.N., Garrett T.P.J., Colman P.M., Chen L., Hoj P.B., Fincher G.B. |
| Title | Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities. |
| Source | Proc. Natl. Acad. Sci. U.S.A. 91:2785-2789(1994). |
| PubMed ID | 8146192 |
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