|SMART accession number:||SM00637|
|Interpro abstract (IPR001919):|
The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC 184.108.40.206), cellobiohydrolases (EC 220.127.116.11) (exoglucanases), or xylanases (EC 18.104.22.168) [(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)].
|GO process:||carbohydrate metabolic process (GO:0005975)|
|GO function:||carbohydrate binding (GO:0030246), hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)|
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- Evolution (species in which this domain is found)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)