Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase, domain N/S (IPR021828)

Short name: GlgE_dom_N/S

Overlapping homologous superfamilies


Domain relationships



This entry represents domain N and S of GlgE.

GlgE is a homodimer and a member of the GH13_3 CAZy subfamily. Each subunit of GlgE is composed of five domains, four of which have been observed before in members of the GH13 alpha-amylase family of enzymes in the GH-H clan. Domain A is a (beta/alpha)8 barrel, typical of the catalytic domain of this family of enzymes, that forms part of the dimer interface. Domain B corresponds to an insertion after the third beta-strand of domain A, as has been observed in many other members of this family [PMID: 11257505]. In GlgE, domain B is fairly typical for a GH13 enzyme [PMID: 9302327] in having a pair of anti-parallel strands and one short helix. The C-terminal domain C has a beta-sandwich fold. Domain C is thought to help stabilise domain A in other family members and could be involved in substrate binding in some cases [PMID: 11257505]. The N-terminal domain N, which also consists of a beta-sandwich fold, forms the core of the dimer interface. The final domain arises from an insertion within domain N and forms a four-helix bundle where the last helix is discontinuous and slightly kinked. This domain, which will henceforth be referred to as domain S, participates in the dimer interface and interacts directly with domain B of the neighbouring subunit [PMID: 21914799].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

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.