TauD protein domain explained

Symbol:TauD
TauD
Pfam:PF02668
Pfam Clan:CL0029
Interpro:IPR003819
Scop:1gy9

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.

Notes and References

  1. Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T . Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli . J. Biol. Chem. . 272 . 37 . 23031–6 . September 1997 . 9287300 . 10.1074/jbc.272.37.23031. free .
  2. Suwa Y, Wright AD, Fukimori F, Nummy KA, Hausinger RP, Holben WE, Forney LJ . Characterization of a chromosomally encoded 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. strain RASC . Appl. Environ. Microbiol. . 62 . 7 . 2464–9 . July 1996 . 8779585 . 168028 . 10.1128/AEM.62.7.2464-2469.1996. 1996ApEnM..62.2464S .
  3. Streber WR, Timmis KN, Zenk MH . Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134 . J. Bacteriol. . 169 . 7 . 2950–5 . July 1987 . 3036764 . 212332 . 10.1128/jb.169.7.2950-2955.1987.