| Activities in Family | Modules of approx. 150 residues which always appear as a threefold internal repeat. The only apparent exception to this, xylanase II of Actinomadura sp. FC7 (GenBank U08894), is in fact not completely sequenced. These modules were first identified in several plant lectins such as ricin or agglutinin of Ricinus communis which bind galactose residues. The three-dimensional structure of a plant lectin has been determined and displays a pseudo-threefold symmetry in accord with the observed sequence threefold repeat. These modules have since been found in a number of other proteins of various functions including glycoside hydrolases and glycosyltransferases. While in the plant lectins this module binds mannose, binding to xylan has been demonstrated in the Streptomyces lividans xylanase A and arabinofuranosidase B. Binding to GalNAc has been shown for the corresponding module of GalNAc transferase 4. For the other proteins, the binding specificity of these modules has not been established. The pseudo three-fold symmetry of the CBM13 module has now been confirmed in the 3-D structure of the intact, two-domain, xylanase of Streptomyces olivaceoviridis. |
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| 3D Structure Status | β-trefoil |
| Note | Previously known as cellulose-binding domain family XIII (CBD XIII). |
| External resources | HOMSTRAD; |
| Statistics | GenBank accession (18440); Uniprot accession (142); PDB accession (171); 3D entries (62); cryst (1) |