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- *********************************************
- * Glycosyl hydrolases family 10 active site *
- *********************************************
-
- 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]. 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).
- - Butyrivibrio fibrisolvens xylanase 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 (cex).
- - Clostridium thermocellum xylanase Z (xynZ).
- - Cryptococcus albidus xylanase.
- - 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.
-
- 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.
-
- -Consensus pattern: [GT]-x(2)-[IVN]-x-[LIVMF]-[ST]-E-[LIVMFY]-[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: NONE.
-
- -Expert(s) to contact by email: Beguin P.
- phycel@pasteur.bitnet
- Henrissat B.
- bernie@cermav.grenet.fr
-
- -Last update: June 1994 / Text revised.
-
- [ 1] Beguin P.
- Annu. Rev. Microbiol. 44:219-248(1990).
- [ 2] Gilkes N.R., Henrissat B., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
- Microbiol. Rev. 55:303-315(1991).
- [ 3] Henrissat B., Claeyssens M., Tomme P., Lemesle L., Mornon J.P.
- Gene 81:83-95(1991).
- [ 4] Henrissat B.
- Biochem. J. 280:309-316(1991).
- [ 5] Tull D., Withers S.G., Gilkes N.R., Kilburn D.G., Warren R.A.J.,
- Aebersold R.
- J. Biol. Chem. 266:15621-15625(1991).
-