id: Pfam:PF04768
pfam_id: PF04768
name: NAT, N-acetyltransferase, of N-acetylglutamate synthase
short_name: NAT
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF04768
counters:
  proteins: 4045
  matches: 4354
  proteomes: 2336
  taxa: 5183
  structures: 10
  alphafold_models: 3250
  domain_architectures: 68
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:IPR006855
description: 'This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate
  synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the
  putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora
  crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal
  to the amino acid kinase region ([pfam:PF00696]) in some fungal acetylglutamate kinase enzymes [[cite:PUB00110296]].
  it stabilises the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition
  by arginine [[cite:PUB00059379]]. This domain is found to be the N-acetyltransferase (NAT) domain, and
  it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25
  Angstrom away from the L-arginine binding site in the N-terminal domain [pfam:PF00696] [[cite:PUB00074836]].'