id: Pfam:PF13938
pfam_id: PF13938
name: Putative heavy-metal chelation
short_name: DUF4213
seed_status: UNKNOWN_CANDIDATE
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF13938
counters:
  proteins: 843
  matches: 843
  proteomes: 695
  taxa: 1584
  structures: 2
  alphafold_models: 676
  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:IPR025251
description: This domain of unknown function has an enolase N-terminal domain-like fold. Its genomic context
  suggests that it may have a role in anaerobic vitamin B12 biosynthesis. This domain is often found at
  the N-terminus of proteins containing DUF364, [pfam:PF04016]. The structure of UnioProtKB:B8FUJ5, PDB:3l5o,
  suggests that the whole protein has this enolase N-terminal-like fold and an 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]].