| 词条 | TauD protein domain |
| 释义 |
| Symbol = TauD | Name = TauD | image = PDB 2q4a EBI.jpg | width = | caption = ensemble refinement of the protein crystal structure of gene product from arabidopsis thaliana at3g21360 | Pfam = PF02668 | Pfam_clan = CL0029 | InterPro = IPR003819 | SMART = | PROSITE = | MEROPS = | SCOP = 1gy9 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, TauD refers to a protein domain that in many enteric bacteria is used to break down taurine (2-aminoethanesulphonic acid) as a source of sulphur under stress conditions. In essence, they are domains found in enzymes that provide bacteria with an important nutrient. FunctionThis protein family consists of TauD/TfdA taurine catabolism dioxygenases. The Escherichia coli tauD gene is required for the utilization of taurine (2-aminoethanesulphonic acid) as a sulphur source and is expressed only under conditions of sulphate starvation. TauD is an alpha-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulphite 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] StructureThis structure has a number of alpha helices and beta sheets. PDB structure References1. ^{{cite journal | vauthors = Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T | title = Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli | journal = J. Biol. Chem. | volume = 272 | issue = 37 | pages = 23031–6 |date=September 1997 | pmid = 9287300 | doi = 10.1074/jbc.272.37.23031| url = }} {{InterPro content|IPR003819}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{Enzyme-stub}}2. ^{{cite journal | vauthors = Suwa Y, Wright AD, Fukimori F, Nummy KA, Hausinger RP, Holben WE, Forney LJ | title = Characterization of a chromosomally encoded 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. strain RASC | journal = Appl. Environ. Microbiol. | volume = 62 | issue = 7 | pages = 2464–9 |date=July 1996 | pmid = 8779585 | pmc = 168028 | doi = | url = }} 3. ^{{cite journal | vauthors = Streber WR, Timmis KN, Zenk MH | title = Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134 | journal = J. Bacteriol. | volume = 169 | issue = 7 | pages = 2950–5 |date=July 1987 | pmid = 3036764 | pmc = 212332 | doi = | url = }} 3 : Protein families|Protein domains|Oxidoreductases |
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