id: Pfam:PF04978
pfam_id: PF04978
name: Mycothiol-S-transferase
short_name: MST
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF04978
counters:
  proteins: 16967
  matches: 16983
  proteomes: 3797
  taxa: 4695
  structures: 3
  alphafold_models: 9298
  domain_architectures: 45
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:IPR007061
description: This entry, previously known as DUF664, represents the Mycothiol S-transferase (MST) from
  Mycobacterium tuberculosis and related proteins mainly found in Actinobacteria. MST binds to and is
  responsible for the transfer of Mycothiol (MSH) to xenobiotic acceptors. The ability of MST to catalyse
  this reaction depends on the presence of divalent metal ions and this enzyme exhibits only a residual
  activity in metal absence [[cite:PUB00158836]]. MST is a member of the DinB-like superfamily. It folds
  into a canonical four-helical bundle that creates a metal binding site using a combination of three
  coordinating highly conserved histidine and aspartate residues. It was shown that MST uses Fe2+ as the
  catalytic metal in vivo [[cite:PUB00158836]].