id: Pfam:PF02675
pfam_id: PF02675
name: S-adenosylmethionine decarboxylase
short_name: AdoMet_dc
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF02675
counters:
  proteins: 7560
  matches: 7574
  proteomes: 6298
  taxa: 10257
  structures: 7
  alphafold_models: 5065
  domain_architectures: 27
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:IPR003826
description: This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and
  archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis
  of spermidine and spermine, is first synthesised as a proenzyme, which is cleaved post translationally
  to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived
  from serine that is essential for activity [[cite:PUB00019108],[cite:PUB00019109]].