Biology:TauD protein domain

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TauD
PDB 2q4a EBI.jpg
ensemble refinement of the protein crystal structure of gene product from arabidopsis thaliana at3g21360
Identifiers
SymbolTauD
PfamPF02668
Pfam clanCL0029
InterProIPR003819
SCOP21gy9 / SCOPe / SUPFAM

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.[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]

Structure

This structure has a number of alpha helices and beta sheets.

References

This article incorporates text from the public domain Pfam and InterPro: IPR003819