id: Pfam:PF05899
pfam_id: PF05899
name: EutQ-like cupin domain
short_name: Cupin_3
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF05899
counters:
  proteins: 11191
  matches: 11372
  proteomes: 5435
  taxa: 8650
  structures: 19
  alphafold_models: 7292
  domain_architectures: 78
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:IPR008579
description: This entry represents the cupin domain, with a conserved jelly roll-like beta-barrel fold
  capable of homodimerisation found in bacteria, plant and fungi. It is present in EutQ family from the
  eut operon, involved in ethanolamine degradation. EutQ is essential during anoxic growth and has acetate
  kinase activity [[cite:PUB00096913]]. The cupin domain from EutQ does not possess the His residues responsible
  for metal coordination in other classes of cupins [[cite:PUB00063996]]. This domain is also found in
  (S)-ureidoglycine aminohydrolase (UGlyAH) from E.coli, which is involved in the anaerobic nitrogen utilisation
  via the assimilation of allantoin. It catalyses the deamination of allantoin to produce S-ureidoglycolate
  and ammonia from S-ureidoglycine [[cite:PUB00078751],[cite:PUB00096858]].