id: Pfam:PF11896
pfam_id: PF11896
name: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase, domain N/S
short_name: GlgE_dom_N_S
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF11896
counters:
  proteins: 5826
  matches: 5835
  proteomes: 5370
  taxa: 6993
  structures: 25
  alphafold_models: 3347
  domain_architectures: 14
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR021828
description: 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, 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 [[cite:PUB00017702]]. In GlgE,
  domain B is fairly typical for a GH13 enzyme [[cite:PUB00060751]] in having a pair of anti-parallel
  strands and one short helix. The C-terminal domain C has a beta-sandwich fold. 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 [[cite:PUB00060749]].