Domain

Cellulose-binding domain, family II, bacterial-type (IPR001919)

Short name: Cellulose-bd_dom_fam2_bac

Domain relationships

Description

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) [PMID: 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 [PMID: 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 [PMID: 1812490, PMID: 10973978].

           +-------------------------------------------------+
           |                                                 |
          xCxxxxWxxxxxNxxxWxxxxxxxWxxxxxxxxWNxxxxxGxxxxxxxxxxCx

'C': conserved cysteine involved in a disulphide bond.

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0030246 carbohydrate binding
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles
SMART
Pfam