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| PROSITE documentation PDOC00511 |
Glycosyl hydrolases family 9 active sites 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 E [3] or as the glycosyl hydrolases
family 9 [4,E1]. The enzymes which are currently known to belong to this
family are listed below.
- Butyrivibrio fibrisolvens cellodextrinase 1 (ced1).
- Cellulomonas fimi endoglucanases B (cenB) and C (cenC).
- Clostridium cellulolyticum endoglucanase G (celCCG).
- Clostridium cellulovorans endoglucanase C (engC).
- Clostridium stercoararium endoglucanase Z (avicelase I) (celZ).
- Clostridium thermocellum endoglucanases D (celD), F (celF) and I (celI).
- Fibrobacter succinogenes endoglucanase A (endA).
- Pseudomonas fluorescens endoglucanase A (celA).
- Streptomyces reticuli endoglucanase 1 (cel1).
- Thermomonospora fusca endoglucanase E-4 (celD).
- Dictyostelium discoideum spore germination specific endoglucanase 270-6.
This slime mold enzyme may digest the spore cell wall during germination,
to release the enclosed amoeba.
- Endoglucanases from plants such as Avocado or French bean. In plants this
enzyme may be involved the fruit ripening process.
Two of the most conserved regions in these enzymes are centered on conserved
residues which have been shown [5,6], in the endoglucanase D from Cellulomonas
thermocellum, to be important for the catalytic activity. The first region
contains an active site histidine and the second region contains two
catalytically important residues: an aspartate and a glutamate. We have used
both regions as signature patterns.
Expert(s) to contact by email:
Henrissat B.
Last update:
November 1997 / Text revised.
Technical section:
PROSITE methods (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F9_1, PS00592; Glycosyl hydrolases family 9 active sites signature 1 (PATTERN) |
| Consensus pattern: |
[STV]-x-[LIVMFY]-[STV]-x(2)-G-x-[NKR]-x(4)-[PLIVM]-H-x-R
H is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL, except for Cellulomonas fimi cenC and Streptomyces reticuli cel1 |
| Other sequence(s) detected in Swiss-Prot: |
2. |
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| Matching PDB structures:
1CLC 1G87 1GA2 1JS4 ... [ALL] |
| GLYCOSYL_HYDROL_F9_2, PS00698; Glycosyl hydrolases family 9 active sites signature 2 (PATTERN) |
| Consensus pattern: |
[FYW]-x-D-x(4)-[FYW]-x(3)-E-x-[STA]-x(3)-N-[STA]
D and E are active site residues |
| Sequences known to belong to this class detected by the pattern: |
ALL, except for Fibrobacter succinogenes endA whose sequence seems to be incorrect |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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|
| Matching PDB structures:
1CLC 1G87 1GA2 1JS4 ... [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 | Tomme P., Chauvaux S., Beguin P., Millet J., Aubert J.-P., Claeyssens M. |
| Title | Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum. |
| Source | J. Biol. Chem. 266:10313-10318(1991). |
| PubMed ID | 2037583 |
| 6 |
Authors | Tomme P., van Beeumen J., Claeyssens M. |
| Title | Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum. |
| Source | Biochem. J. 285:319-324(1992). |
| PubMed ID | 1637316 |
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