id: Pfam:PF04016
pfam_id: PF04016
name: Putative heavy-metal chelation
short_name: DUF364
seed_status: UNKNOWN_CANDIDATE
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF04016
counters:
  proteins: 1766
  matches: 1766
  proteomes: 1491
  taxa: 2706
  structures: 2
  alphafold_models: 1247
  domain_architectures: 6
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:IPR007161
description: This domain of unknown function has a PLP-dependent transferase-like fold. Its genomic context
  suggests that it may have a role in anaerobic vitamin B12 biosynthesis. This domain is often found at
  the C-terminus of proteins containing DUF4213, [pfam:PF13938]. The structure of UnioProtKB:B8FUJ5, PDB:3l5o,
  suggests that the protein has an enolase N-terminal-like fold and this Rossmann-like C-terminal domain.
  Structural and bioinformatic analyses reveal partial similarities to Rossmann-like methyltransferases,
  with residues from the enolase-like fold combining to form a unique active site that is likely to be
  involved in the condensation or hydrolysis of molecules implicated in the synthesis of flavins, pterins
  or other siderophores. The protein may be playing a role in heavy-metal chelation [[cite:PUB00075371]].