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, PS00591Glycosyl 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:

1 AuthorsBeguin P.
TitleMolecular biology of cellulose degradation.
SourceAnnu. Rev. Microbiol. 44:219-248(1990).
PubMed ID2252383
DOI10.1146/annurev.mi.44.100190.001251
2 AuthorsGilkes N.R., Henrissat B., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
TitleDomains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
SourceMicrobiol. Rev. 55:303-315(1991).
PubMed ID1886523
3 AuthorsHenrissat B., Claeyssens M., Tomme P., Lemesle L., Mornon J.-P.
TitleCellulase families revealed by hydrophobic cluster analysis.
SourceGene 81:83-95(1989).
PubMed ID2806912
4 AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104
5 AuthorsTull D., Withers S.G., Gilkes N.R., Kilburn D.G., Warren R.A.J., Aebersold R.
TitleGlutamic acid 274 is the nucleophile in the active site of a 'retaining' exoglucanase from Cellulomonas fimi.
SourceJ. Biol. Chem. 266:15621-15625(1991).
PubMed ID1678739
E1
Sourcehttp://www.expasy.org/cgi-bin/lists?glycosid.txt

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