CBM_2Starch binding domain
|SMART accession number:||SM01065|
|Interpro abstract (IPR002044):|
A carbohydrate-binding module (CBM) is defined as a contiguous amino acid sequence within a carbohydrate-active enzyme with a discreet fold having carbohydrate-binding activity. A few exceptions are CBMs in cellulosomal scaffolding proteins and rare instances of independent putative CBMs. The requirement of CBMs existing as modules within larger enzymes sets this class of carbohydrate-binding protein apart from other non-catalytic sugar binding proteins such as lectins and sugar transport proteins.
CBMs were previously classified as cellulose-binding domains (CBDs) based on the initial discovery of several modules that bound cellulose [(PUBMED:3338453), (PUBMED:3134347)]. However, additional modules in carbohydrate-active enzymes are continually being found that bind carbohydrates other than cellulose yet otherwise meet the CBM criteria, hence the need to reclassify these polypeptides using more inclusive terminology.
Previous classification of cellulose-binding domains were based on amino acid similarity. Groupings of CBDs were called "Types" and numbered with roman numerals (e.g. Type I or Type II CBDs). In keeping with the glycoside hydrolase classification, these groupings are now called families and numbered with Arabic numerals. Families 1 to 13 are the same as Types I to XIII. For a detailed review on the structure and binding modes of CBMs see [(PUBMED:15214846)].
This entry represents which binds starch. The crystal structure of CBM20 has been solved [(PUBMED:1826034)]. It consists of seven beta-stands forming an open-sided distorted beta-barrel. Several aromatic residues, especially the well-conserved Trp and Tyr residues, participate in granular starch binding.
|GO function:||starch binding (GO:2001070)|
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Structure (3D structures containing this domain)
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