TauD protein domain
protein family
In molecular biology, TauD refers to a protein domain that in many enteric bacteria is used to break down taurine (2-aminoethanesulfonic acid) as a source of sulfur 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-aminoethanesulfonic acid) as a sulfur source and is expressed only under conditions of sulfate starvation. TauD is an alpha-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulfite 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.
Structure
This structure has a number of alpha helices and beta sheets.
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This entry incorporates text from “TauD protein domain” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.