id: Pfam:PF03781
pfam_id: PF03781
name: Sulfatase-modifying factor enzyme 1-like domain
short_name: FGE-sulfatase
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF03781
counters:
  proteins: 38188
  matches: 41371
  proteomes: 14430
  taxa: 23526
  structures: 65
  alphafold_models: 25146
  domain_architectures: 587
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:IPR005532
description: This domain is found in eukaryotic proteins [[cite:PUB00019471]] required for post-translational
  sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase
  deficiency (MSD) [[cite:PUB00033658]]. The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating
  enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate
  esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases [[cite:PUB00038408]].
  FGE is localised to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form
  of newly synthesised sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary
  structure that adopts a unique fold which is stabilised by two Ca2+ ions. The effect of all mutations
  found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active
  disulfide bond is present in the active site of FGE. An oxidised cysteine residue, possibly cysteine
  sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly
  formation from cysteine residues in all sulfatases [[cite:PUB00055960]]. In Mycobacteria and Treponema
  denticola this enzyme functions as an iron(II)-dependent oxidoreductase [[cite:PUB00060032],[cite:PUB00066766]].
  This domain is also found in the Serine/threonine-protein kinase Pkn1 from Chlamydia trachomatis which
  is a multidomain protein. Pkn1 plays a role in specific interactions with host proteins during host
  intracellular growth.