id: Pfam:PF12568
pfam_id: PF12568
name: Acetyltransferase (GNAT) domain, PanZ
short_name: PanZ
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12568
counters:
  proteins: 899
  matches: 899
  proteomes: 895
  taxa: 1212
  structures: 5
  alphafold_models: 531
  domain_architectures: 4
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:IPR040448
description: This domain family is found in bacteria, and is approximately 40 amino acids in length. The
  proteins in this family are members of the acetyltransferases of the GNAT family. Family members such
  as PanZ has been shown to be involved in the biosynthesis of Coenzyme A (CoA). CoA is a ubiquitous and
  essential cofactor, synthesized from the precursor pantothenate. In all organisms, the final step in
  pantothenate biosynthesis relies on the presence of beta-alanine, which comes from different sources
  in bacteria, yeast, and plants. In bacteria, beta-alanine is derived by the action of alpha-decarboxylase
  (ADC) enzyme. PanZ promotes the activation of the zymogen, PanD, to form aspartate alpha-decarboxylase
  (ADC) in a CoA-dependent manner. Thereby, playing an essential role in the biosynthetic pathway to pantothenate
  and the regulation of CoA biosynthesis. Structure and function studies show that direct interaction
  of PanD with the PanZ Arg43-Leu46 loop promotes PanD to adopt a reactive conformation, which leads to
  activation [[cite:PUB00091022]].