id: Pfam:PF11892
pfam_id: PF11892
name: Pyrimidine/purine nucleotide monophosphate nucleosidase, C-terminal
short_name: PpnN_C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF11892
counters:
  proteins: 2629
  matches: 2629
  proteomes: 2622
  taxa: 3451
  structures: 9
  alphafold_models: 1597
  domain_architectures: 6
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:IPR021826
description: This domain is found at the C-terminal end of Pyrimidine/purine nucleotide 5'-monophosphate
  nucleosidase from Escherichia coli (PpnN, also known as YgdH) and similar proteins mainly found in gammaproteobacteria.
  PpnN is a nucleosidase that catalyses the hydrolysis of the N-glycosidic bond of diverse pyrimidine
  and purine nucleotide 5'-monophosphates. The binding of (p)ppGpp, an alarmone molecule that plays a
  role in the bacterial stringent response, gives rise to a large conformational change in the terminal
  region that leads to the exposure of the catalytic pocket. This domain shows a completely alpha-helical
  fold with an extension that wraps around the central domain [[cite:PUB00100958],[cite:PUB00084997]].