CBD_II |
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| SMART accession number: | SM00637 |
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| Description: | |
| Interpro abstract (IPR001919): | The microbial degradation of cellulose and xylans requires several types of enzyme such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91) (exoglucanases), or xylanases (EC 3.2.1.8) (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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| GO process: | carbohydrate metabolic process (GO:0005975) |
| GO function: | carbohydrate binding (GO:0030246), hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553) |
| Family alignment: |
There are 284 CBD_II domains in 266 proteins in SMART's nrdb database.
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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)

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