PROSITE documentation PDOC00794

Glycosyl hydrolases family 16 signature

Description:

It has been shown [1] that the following glycosyl hydrolases can be classified into a single family on the basis of sequence similarities:

  • Bacterial β-1,3-1,4-glucanases, or lichenases, (EC 3.2.1.73) mainly from Bacillus but also from Clostridium thermocellum (gene licB), Fibrobacter succinogenes and Rhodothermus marinus (gene bglA).
  • Bacillus circulans β-1,3-glucanase A1 (EC 3.2.1.39) (gene glcA).
  • Streptomyces coelicolor agarase (EC 3.2.1.81) (gene dagA).
  • Alteromonas carrageenovora kappa-carrageenase (EC 3.2.1.83) (gene cgkA).
  • Rhizobium meliloti endo-1,3-1,4-β-glycanase exoK.

Two closely clustered conserved glutamates have been shown [2] to be involved in the catalytic activity of Bacillus licheniformis lichenase. We used the region that contains these residues as a signature pattern.

Expert(s) to contact by email:

Henrissat B.

Last update:

May 2004 / Text revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

GLYCOSYL_HYDROL_F16, PS01034Glycosyl hydrolases family 16 active sites  (PATTERN)
Consensus pattern: E-[LIV]-D-[LIVF]-x(0,1)-E-x(2)-[GQ]-[KRNF]-x-[PSTA]
The 2 E's are active site residues
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: 4.
• Retrieve an alignment of Swiss-Prot true positive hits:
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Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01034
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01034
Scan Swiss-Prot/TrEMBL entries against PS01034
view ligand binding statistics
Matching PDB structures: 1AJK 1AJO 1AXK 1BYH ... [ALL]

References:

1 AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104
2 AuthorsJuncosa M., Pons J., Dot T., Querol E., Planas A.
TitleIdentification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis.
SourceJ. Biol. Chem. 269:14530-14535(1994).
PubMed ID8182059

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