InterPro domain: IPR003819

This domain is found in TauD/TfdA taurine catabolism dioxygenases. The Escherichia coli tauD gene is required for the utilisation of taurine (2-aminoethanesulphonic acid) as a sulphur source and is expressed only under conditions of sulphate starvation. TauD is an alpha-ketoglutarate-dependent dioxygenase catalysing the oxygenolytic release of sulphite from taurine [ 1 ]. The 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. (strain RASC) also belongs to this family [ 2 ]. TfdA from Ralstonia eutropha (Alcaligenes eutrophus) is a 2,4-D monooxygenase [ 3 ].

This domain is also found in gamma-butyrobetaine hydroxylase (GBBH), the enzyme responsible for the biosynthesis of L-carnitine, a key molecule of fatty acid metabolism. The GBBH monomer consists of this catalytic double-stranded beta-helix (DBSH) domain, which is found in all 2-ketoglutarate (2KG) oxygenases, and a smaller N-terminal domain [ 4 ].

1. Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli. J. Biol. Chem. 272, 23031-6
2. Characterization of a chromosomally encoded 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. strain RASC. Appl. Environ. Microbiol. 62, 2464-9
3. Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134. J. Bacteriol. 169, 2950-5
4. Crystal structure of human gamma-butyrobetaine hydroxylase. Biochem. Biophys. Res. Commun. 398, 634-9