id: Pfam:PF17648
pfam_id: PF17648
name: Luciferase domain
short_name: Luciferase
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF17648
counters:
  proteins: 3012
  matches: 3012
  proteomes: 1997
  taxa: 3597
  structures: 0
  alphafold_models: 2193
  domain_architectures: 28
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:IPR040841
description: This entry describes the luciferase domain found in fungi. This entry also includes uncharacterised
  bacterial sequences. Fungal luciferase is part of the gene cluster that mediates the fungal bioluminescence
  cycle [[cite:PUB00101065]]. It may use the fungal luciferin 3-hydroxyhispidin as a substrate to produce
  an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known
  as caffeoylpyruvate) and light emission. The fungal bioluminescence cycle begins with the hispidin synthetase
  that catalyses the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase,
  yielding the fungal luciferin 3-hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy
  intermediate with decomposition that yields oxyluciferin and light emission. Oxyluciferin can be recycled
  to caffeic acid by caffeoylpyruvate hydrolase [[cite:PUB00101065]].