id: Pfam:PF13427
pfam_id: PF13427
name: Aminoglycoside adenylyltransferase, C-terminal domain
short_name: AadA_C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF13427
counters:
  proteins: 2850
  matches: 2850
  proteomes: 1991
  taxa: 3364
  structures: 9
  alphafold_models: 1883
  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:IPR025184
description: 'This domain is found at the C-terminal end of Aminoglycoside adenylyltransferase from Salmonella
  typhimurium (AadA) and other proteins associated with methicillin-resistant bacteria. AadA adenylates
  the 3''''-hydroxyl group of the streptomycin glucosamine ring and the 9-hydroxyl group of the spectinomycin
  actinamine ring, mediating bacterial resistance to these antibiotics. This enzyme is organised into
  two domains: a N-terminal domain with a nucleotidyltransferase fold ([pfam:PF01909]) and a C-terminal
  domain (this entry) which consists of five alpha-helices forming an up-and-down alpha-helical bundle.
  This domain undergoes small conformational changes upon binding of ATP and magnesium that play a key
  role in the binding of the antibiotic compounds [[cite:PUB00091136],[cite:PUB00100854]].'