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| PROSITE documentation PDOC00510 |
Glycosyl hydrolases family 10 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 F [3] or as the glycosyl hydrolases
family 10 [4,E1]. The enzymes which are currently known to belong to this
family are listed below.
- Aspergillus awamori xylanase A (xynA).
- Bacillus sp. strain 125 xylanase (xynA).
- Bacillus stearothermophilus xylanase.
- Butyrivibrio fibrisolvens xylanases A (xynA) and B (xynB).
- Caldocellum saccharolyticum bifunctional endoglucanase/exoglucanase (celB).
This protein consists of two domains; it is the N-terminal domain, which
has exoglucanase activity, which belongs to this family.
- Caldocellum saccharolyticum xylanase A (xynA).
- Caldocellum saccharolyticum ORF4. This hypothetical protein is encoded in
the xynABC operon and is probably a xylanase.
- Cellulomonas fimi exoglucanase/xylanase (cex).
- Clostridium stercorarium thermostable celloxylanase.
- Clostridium thermocellum xylanases Y (xynY) and Z (xynZ).
- Cryptococcus albidus xylanase.
- Penicillium chrysogenum xylanase (gene xylP).
- Pseudomonas fluorescens xylanases A (xynA) and B (xynB).
- Ruminococcus flavefaciens bifunctional xylanase XYLA (xynA). This protein
consists of three domains: a N-terminal xylanase catalytic domain that
belongs to family 11 of glycosyl hydrolases; a central domain composed of
short repeats of Gln, Asn an Trp, and a C-terminal xylanase catalytic
domain that belongs to family 10 of glycosyl hydrolases.
- Streptomyces lividans xylanase A (xlnA).
- Thermoanaerobacter saccharolyticum endoxylanase A (xynA).
- Thermoascus aurantiacus xylanase.
- Thermophilic bacterium Rt8.B4 xylanase (xynA).
One of the conserved regions in these enzymes is centered on a conserved
glutamic acid residue which has been shown [5], in the exoglucanase from
Cellulomonas fimi, to be directly involved in glycosidic bond cleavage by
acting as a nucleophile. We have used this region as a signature pattern.
Expert(s) to contact by email:
Henrissat B.
Last update:
April 2006 / Pattern revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| GLYCOSYL_HYDROL_F10, PS00591; Glycosyl hydrolases family 10 active site (PATTERN) |
| Consensus pattern: |
[GTA]-{QNAG}-{GSV}-[LIVN]-x-[IVMF]-[ST]-E-[LIY]-[DN]-[LIVMF]
E is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL, except for Thermoascus aurantiacus xylanase whose sequence seems to be incorrect |
| Other sequence(s) detected in Swiss-Prot: |
16. |
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| Matching PDB structures:
1B30 1B31 1B3V 1B3W ... [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 | Tull D., Withers S.G., Gilkes N.R., Kilburn D.G., Warren R.A.J., Aebersold R. |
| Title | Glutamic acid 274 is the nucleophile in the active site of a 'retaining' exoglucanase from Cellulomonas fimi. |
| Source | J. Biol. Chem. 266:15621-15625(1991). |
| PubMed ID | 1678739 |
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