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| PROSITE documentation PDOC00563 |
Glycosyl hydrolases family 6 signatures
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 B [3] or as the glycosyl hydrolases
family 6 [4,E1]. The enzymes which are currently known to belong to this
family are listed below.
- Agaricus bisporus exoglucanase 3 (cel3).
- Cellulomonas fimi endoglucanase A (cenA).
- Cellulomonas fimi exoglucanase A (cbhA).
- Microspora bispora endoglucanase A (celA).
- Streptomyces halstedii endoglucanases A (celA1).
- Streptomyces strain KSM-9 endoglucanase 1 (casA).
- Thermomonospora fusca endoglucanase E-2 (celB).
- Trichoderma reesei exoglucanase II (CBH2).
One of the conserved regions in these enzymes contains a conserved aspartic
acid residue which is potentially involved [5] in the catalytic mechanism;
the aspartate is followed by a cysteine which is involved in a disulfide bond
[6]. A second conserved region contains an aspartate which seems [5] to be the
proton donor in the catalytic mechanism. We have used both regions as
signature patterns.
Henrissat B.
May 2004 / Text revised.
Technical section
PROSITE methods (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F6_1, PS00655; Glycosyl hydrolases family 6 signature 1 (PATTERN) |
| Consensus pattern: |
V-x-Y-x(2)-P-x-R-D-C-[GSAF]-x(2)-[GSA](2)-x-G
D may be an active site residue; C is involved in a disulfide bond |
| Sequences known to belong to this class detected by the pattern: |
ALL, except for celA1 |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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| Matching PDB structures:
1BVW 1GZ1 1HGY 1OC5 ... [ALL] |
| GLYCOSYL_HYDROL_F6_2, PS00656; Glycosyl hydrolases family 6 signature 2 (PATTERN) |
| Consensus pattern: |
[LIVMYA]-[LIVA]-[LIVT]-[LIV]-E-P-D-[SAL]-[LI]-[PSAG]
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:
1BVW 1CB2 1DYS 1GZ1 ... [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., 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 |
Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K., Jones T.A. |
| Title |
Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. |
| Source |
Science 249:380-386(1990). |
| PubMed ID |
2377893 |
| 6 |
Authors |
Gilkes N.R., Claeyssens M., Aebersold R., Henrissat B., Meinke A., Morrison H.D., Kilburn D.G., Warren R.A.J., Miller R.C. Jr. |
| Title |
Structural and functional relationships in two families of beta-1,4-glycanases. |
| Source |
Eur. J. Biochem. 202:367-377(1991). |
| PubMed ID |
1761039 |
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