id: Pfam:PF01796
pfam_id: PF01796
name: ChsH2, C-terminal OB-fold domain
short_name: OB_ChsH2_C
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01796
counters:
  proteins: 14915
  matches: 16307
  proteomes: 4357
  taxa: 6361
  structures: 12
  alphafold_models: 9479
  domain_architectures: 41
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:IPR002878
description: 'This domain is found at the C-terminal end of the probable enoyl -CoA hydratase alpha subunit
  from Thermomonospora curvata (ChsH2) and similar archaeal and bacterial proteins. ChsH2 is likely to
  be involved in bile acid degradation. The C-terminal region of this protein is organised into two domains:
  an N-terminal zinc finger domain ([pfam:PF12172]) and an OB-fold domain (this entry) that consists of
  a five-stranded beta-barrel [[cite:PUB00155451]]. This domain is also found in 3-oxo-4,17- pregnadiene-20-carboxyl-CoA
  hydratase alpha subunit from Mycobacterium tuberculosis that is involved in cholesterol side chain degradation
  [[cite:PUB00154876]]. It is also found in Methanothermococcus thermolithotrophicus HMGCS, an enzyme
  complex comprising the thiolase and 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase, that catalyses the
  second reaction in the mevalonate pathway-the exergonic condensation of acetoacetyl-CoA and acetyl-CoA
  to HMG-CoA [[cite:PUB00154878]].'