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TauD protein domain : ウィキペディア英語版 | TauD protein domain
In molecular biology, TauD refers to a protein domain that in many enteric bacteria is used to break down taurine (2-aminoethanesulphonic acid) as a source of sulphur under stress conditions. In essence, they are domains found in enzymes that provide bacteria with an important nutrient. ==Function== This protein family consists of TauD/TfdA taurine catabolism dioxygenases. The ''Escherichia coli'' tauD gene is required for the utilization 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 catalyzing the oxygenolytic release of sulphite from taurine. The 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from ''Burkholderia sp.'' (strain RASC) also belongs to this family. TfdA from ''Ralstonia eutropha'' (Alcaligenes eutrophus) is a 2,4-D monooxygenase.
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