TauD protein domain

TauD

ensemble refinement of the protein crystal structure of gene product from arabidopsis thaliana at3g21360

Identifiers

Symbol

TauD

Pfam clan

1gy9 / SCOPe / SUPFAM

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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

^ 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.

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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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