id: Pfam:PF11852
pfam_id: PF11852
name: Alpha-1,6-glucosidases, pullulanase-type, C-terminal
short_name: Pullul_strch_C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF11852
counters:
  proteins: 3239
  matches: 3256
  proteomes: 2756
  taxa: 4152
  structures: 28
  alphafold_models: 1099
  domain_architectures: 143
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:IPR024561
description: This entry represents the uncharacterised C-terminal domain of secreted (or membrane-anchored)
  pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants [[cite:PUB00097791]].
  Both enzymes hydrolyse alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important
  polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes
  that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although
  pullulan itself may not be the natural substrate.