id: Pfam:PF09995
pfam_id: PF09995
name: ER-bound oxygenase mpaB/B'/Rubber oxygenase, catalytic domain
short_name: MPAB_Lcp_cat
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF09995
counters:
  proteins: 17931
  matches: 17952
  proteomes: 7118
  taxa: 10739
  structures: 2
  alphafold_models: 10982
  domain_architectures: 79
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:IPR018713
description: This is the catalytic domain found in the endoplasmic reticulum (ER) -bound oxygenases mpaB'
  (MPAB2) and mpaB (MPAB) from Penicillium roqueforti and Penicillium brevicompactum and in the rubber
  oxygenase (Lcp) from Streptomyces sp., which contains highly conserved arginine and histidine residues.
  Structural analysis from Lcp revealed that Arg164, Thr168 and His198 are crucial active site residues
  [[cite:PUB00087009]]. The mpaB and mpaB' are part of the gene cluster that mediates the biosynthesis
  of mycophenolic acid (MPA) [[cite:PUB00096709]]. Lcp (Latex clearing proteins) is a rubber oxygenase
  that catalyses the extracellular cleavage of poly (cis-1,4-isoprene) [[cite:PUB00087009],[cite:PUB00096710]].
  This domain is also present in uncharacterised proteins from Mycobacterium sp. and hypothetical proteins,
  mainly from bacteria and fungi.