Gamma-butyrobetaine hydroxylase-like, N-terminal (IPR010376)

Short name: GBH-like_N

Overlapping homologous superfamilies

Domain relationships



This domain is found in 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 [PMID: 20599753].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.