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 [1]. Other family members have been suggested to be involved in FeS cluster maintenance (see Supplementary note 5 in [2].) [1]. 20599753. Crystal structure of human gamma-butyrobetaine hydroxylase.. Tars K, Rumnieks J, Zeltins A, Kazaks A, Kotelovica S, Leonciks. A, Sharipo J, Viksna A, Kuka J, Liepinsh E, Dambrova M;. Biochem Biophys Res Commun. 2010;398:634-639.. [2]. 29769716. Mutant phenotypes for thousands of bacterial genes of unknown. function.. Price MN, Wetmore KM, Waters RJ, Callaghan M, Ray J, Liu H,. Kuehl JV, Melnyk RA, Lamson JS, Suh Y, Carlson HK, Esquivel Z,. Sadeeshkumar H, Chakraborty R, Zane GM, Rubin BE, Wall JD, Visel. A, Bristow J, Blow MJ, Arkin AP, Deutschbauer AM;. Nature. 2018;557:503-509. (from Pfam)
- Date:
- 2024-08-14