id: Pfam:PF06155
pfam_id: PF06155
name: Gamma-butyrobetaine hydroxylase-like, N-terminal
short_name: GBBH-like_N
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF06155
counters:
  proteins: 11413
  matches: 11424
  proteomes: 7190
  taxa: 14088
  structures: 19
  alphafold_models: 8604
  domain_architectures: 122
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:IPR010376
description: This domain is found in several proteins including gamma-butyrobetaine dioxygenase, Fe-S
  cluster assembly factor HCF101 and trimethyllysine dioxygenase proteins. Gamma-butyrobetaine hydroxylase
  (GBBH) is a alpha-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine
  by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic
  double-stranded beta-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound
  Zn ion, which is coordinated by three cysteines and one histidine. The N-terminal domain could facilitate
  dimer formation, but its precise function is not known [[cite:PUB00075680]]. Other family members have
  been suggested to be involved in FeS cluster maintenance (see Supplementary note 5 in [[cite:PUB00093610]].)