SMART accession number:SM00637
Description: -
Interpro abstract (IPR001919):

The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC, cellobiohydrolases (EC (exoglucanases), or xylanases (EC [(PUBMED:1886523)]. Structurally, cellulases and xylanases generally consist of a catalytic domain joined to a cellulose-binding domain (CBD) by a short linker sequence rich in proline and/or hydroxy-amino acids.

The CBD domain is found either at the N-terminal or at the C-terminal extremity of these enzymes. As it is shown in the following schematic representation, there are two conserved cysteines in this CBD domain - one at each extremity of the domain - which have been shown [(PUBMED:1761039)] to be involved in a disulphide bond. There are also four conserved tryptophan, two are involved in cellulose binding. The CBD of a number of bacterial cellulases has been shown to consist of about 105 amino acid residues [(PUBMED:1812490), (PUBMED:10973978)].

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'C': conserved cysteine involved in a disulphide bond.
GO process:carbohydrate metabolic process (GO:0005975)
GO function:carbohydrate binding (GO:0030246), hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)
Family alignment:
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There are 2411 CBD_II domains in 2323 proteins in SMART's nrdb database.

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