id: Pfam:PF04412
pfam_id: PF04412
name: Aconitase X first domain
short_name: AcnX
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF04412
counters:
  proteins: 2037
  matches: 2040
  proteomes: 1846
  taxa: 3243
  structures: 5
  alphafold_models: 1460
  domain_architectures: 22
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:IPR060004
description: This entry represents the first domain of aconitase X (AcnX), which corresponds to domain
  2 in the canonical four-domain architecture of the aconitase superfamily. This domain contains a central
  parallel beta-sheet linked by alpha-helices, similar to nucleotide-binding domains of dehydrogenases
  [[cite:PUB00161781]]. The AcnX subfamily includes bacterial Type I enzymes that function as cis-3-hydroxy-L-proline
  dehydratases and archaeal Type II enzymes that act as mevalonate 5-phosphate dehydratases. Unlike other
  aconitase family members that contain [4Fe-4S] clusters, AcnX enzymes utilise [2Fe-2S] or [3Fe-4S] clusters
  for catalysis [[cite:PUB00088769],[cite:PUB00161781]]. This domain forms part of the active site architecture
  but does not directly coordinate the iron-sulphur cluster.