id: Pfam:PF05153
pfam_id: PF05153
name: Myo-inositol oxygenase
short_name: MIOX
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF05153
counters:
  proteins: 5483
  matches: 5682
  proteomes: 3279
  taxa: 8215
  structures: 3
  alphafold_models: 4460
  domain_architectures: 97
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:IPR007828
description: MIOX is the enzyme myo-inositol oxygenase. It catalyses the first committed step in the glucuronate-xylulose
  pathway, It is a di-iron oxygenase with a key role in inositol metabolism. The structure reveals a monomeric,
  single-domain protein with a mostly helical fold that is distantly related to the diverse HD domain
  superfamily. The structural core is of five alpha-helices that contribute six ligands, four His and
  two Asp, to the di-iron centre where the two iron atoms are bridged by a putative hydroxide ion and
  one of the Asp ligands. The substrate is myo-inositol is bound in a terminal substrate-binding mode
  to a di-iron cluster [[cite:PUB00041510]]. Within the structure are two additional proteinous lids that
  cover and shield the enzyme's active site [[cite:PUB00047694]].