Glucoamylase, CBM20 domain (IPR034836)

Short name: CBM20_glucoamylase

Overlapping homologous superfamilies

Domain relationships


Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two [PMID: 11150611].

This entry represents the glucoamylase, starch-binding, C-terminal CBM20 (carbohydrate-binding module, family 20) domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:2001070 starch binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.