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.
TauD | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | TauD | ||||||||
Pfam | PF02668 | ||||||||
Pfam clan | CL0029 | ||||||||
InterPro | IPR003819 | ||||||||
SCOP2 | 1gy9 / SCOPe / SUPFAM | ||||||||
|
Function
editThis 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
editThis structure has a number of alpha helices and beta sheets.
References
edit- ^ Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T (September 1997). "Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli". J. Biol. Chem. 272 (37): 23031–6. doi:10.1074/jbc.272.37.23031. PMID 9287300.
- ^ Suwa Y, Wright AD, Fukimori F, Nummy KA, Hausinger RP, Holben WE, Forney LJ (July 1996). "Characterization of a chromosomally encoded 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. strain RASC". Appl. Environ. Microbiol. 62 (7): 2464–9. Bibcode:1996ApEnM..62.2464S. doi:10.1128/AEM.62.7.2464-2469.1996. PMC 168028. PMID 8779585.
- ^ Streber WR, Timmis KN, Zenk MH (July 1987). "Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134". J. Bacteriol. 169 (7): 2950–5. doi:10.1128/jb.169.7.2950-2955.1987. PMC 212332. PMID 3036764.