id: Pfam:PF01910
pfam_id: PF01910
name: Thiamine-binding protein
short_name: Thiamine_BP
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01910
counters:
  proteins: 9298
  matches: 9331
  proteomes: 8093
  taxa: 12399
  structures: 7
  alphafold_models: 6343
  domain_architectures: 25
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:IPR002767
description: The crystal structure of two of these members shows that this domain has a ferredoxin like
  fold and is likely to exists as at least homodimers. Sulphate ions are are located at the dimer interfaces,
  which are thought to confer additional stability. Although the function of this domain remains to be
  identified, its structure suggests a role in protein-protein interactions possibly regulated by the
  binding of small-molecule ligands [[cite:PUB00019479]]. Solution of the structure of the hyperthermophilic
  anaerobic Thermotoga maritima sequence, UniProtKB:Q9WYV6, shows that this has a beta-alpha-beta-beta-alpha-beta
  ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monmer
  that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl
  pyrimidine. It is proposed that it is transporting charged thiamine around the cytoplasm. Under oxidative
  conditions this bacterium is under stress, and the transcriiptional unit within which this protein is
  expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine
  is part of the response mechanism to such oxidatvie stress, which is mediated by this family [[cite:PUB00055842]].