Catalyzes the alpha-ketoglutarate-dependent hydroxylation of taurine yielding sulfite and aminoacetaldehyde after decomposition of an unstable intermediate (PubMed:9287300). Is required for the utilization of taurine (2-aminoethanesulfonate) as an alternative sulfur source for growth in the absence of sulfate (PubMed:8808933). To a lesser extent, pentanesulfonate, 3-(N-morpholino)propanesulfonate and 1,3-dioxo-2-isoindolineethanesulfonate are also desulfonated by this enzyme in vitro; however, desulfonation by TauD of organosulfonates other than taurine seem to be of little or no importance for sulfur metabolism in vivo (PubMed:9287300). 2-oxoglutarate + O2 + taurine = aminoacetaldehyde + CO2 + H(+) + succinate + sulfite Binds 1 Fe(2+) ion per subunit. Activated by ascorbate and inhibited by divalent metal ions such as zinc, copper and cobalt. Optimum pH is 6.9. Organosulfur degradation; taurine degradation via aerobic pathway; aminoacetaldehyde and sulfite from taurine: step 1/1. Homodimer (PubMed:11955067, PubMed:12741810, PubMed:9287300). Was later shown to be a homotetramer arranged as a dimer of two dimers (PubMed:22221834). Is only expressed during growth in the absence of sulfate or cysteine. Disruption of this gene leads to a loss of the ability to utilize taurine as a source of sulfur, but does not affect the utilization of a range of other aliphatic sulfonates as sulfur sources. Taurine dioxygenase can be used for enzymatic determination of taurine concentration in food quality control, biological research, and medical diagnosis. Belongs to the TfdA dioxygenase family.