Alpha-ketoglutarate-dependent taurine dioxygenase
Details
- Name
- Alpha-ketoglutarate-dependent taurine dioxygenase
- Synonyms
- 1.14.11.17
- 2-aminoethanesulfonate dioxygenase
- SSI3
- ssiD
- Sulfate starvation-induced protein 3
- yaiG
- Gene Name
- tauD
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0002747|Alpha-ketoglutarate-dependent taurine dioxygenase MSERLSITPLGPYIGAQISGADLTRPLSDNQFEQLYHAVLRHQVVFLRDQAITPQQQRAL AQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTFIETPPAGAILAAKELP STGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHDFRKSFPEYKYRKTEEEHQRWREAVAK NPPLLHPVVRTHPVSGKQALFVNEGFTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRW QPNDIAIWDNRVTQHYANADYLPQRRIMHRATILGDKPFYRAG
- Number of residues
- 283
- Molecular Weight
- 32409.26
- Theoretical pI
- 6.76
- GO Classification
- FunctionsL-ascorbic acid binding / metal ion binding / taurine dioxygenase activityProcessessulfur compound metabolic processComponentscytoplasm
- General Function
- Taurine dioxygenase activity
- Specific Function
- Catalyzes the conversion of taurine and alpha ketoglutarate to sulfite, aminoacetaldehyde and succinate. Required for the utilization of taurine (2-aminoethanesulfonic acid) as an alternative sulfur source. Pentane-sulfonic acid, 3-(N-morpholino)propanesulfonic acid and 1,3-dioxo-2-isoindolineethanesulfonic acid are also substrates for this enzyme.
- Pfam Domain Function
- TauD (PF02668)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0021659|Alpha-ketoglutarate-dependent taurine dioxygenase (tauD) ATGAGTGAACGTCTGAGCATTACCCCGCTGGGGCCGTATATCGGCGCACAAATTTCGGGT GCCGACCTGACGCGCCCGTTAAGCGATAATCAGTTTGAACAGCTTTACCATGCGGTGCTG CGCCATCAGGTGGTGTTTCTACGCGATCAAGCTATTACGCCGCAGCAGCAACGCGCGCTG GCCCAGCGTTTTGGCGAATTGCATATTCACCCTGTTTACCCGCATGCCGAAGGGGTTGAC GAGATCATCGTGCTGGATACCCATAACGATAATCCGCCAGATAACGACAACTGGCATACC GATGTGACATTTATTGAAACGCCACCCGCAGGGGCGATTCTGGCAGCTAAAGAGTTACCT TCGACCGGCGGTGATACGCTCTGGACCAGCGGTATTGCGGCCTATGAGGCGCTCTCTGTT CCCTTCCGCCAGCTGCTGAGTGGGCTGCGTGCGGAGCATGATTTCCGTAAATCGTTCCCG GAATACAAATACCGCAAAACCGAGGAGGAACATCAACGCTGGCGCGAGGCGGTCGCGAAA AACCCGCCGTTGCTACATCCGGTGGTGCGAACGCATCCGGTGAGCGGTAAACAGGCGCTG TTTGTGAATGAAGGCTTTACTACGCGAATTGTTGATGTGAGCGAGAAAGAGAGCGAAGCC TTGTTAAGTTTTTTGTTTGCCCATATCACCAAACCGGAGTTTCAGGTGCGCTGGCGCTGG CAACCAAATGATATTGCGATTTGGGATAACCGCGTGACCCAGCACTATGCCAATGCCGAT TACCTGCCACAGCGACGGATAATGCATCGGGCGACGATCCTTGGGGATAAACCGTTTTAT CGGGCGGGGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P37610 UniProtKB Entry Name TAUD_ECOLI GenBank Protein ID 1384060 GenBank Gene ID D85613 - General References
- van der Ploeg JR, Weiss MA, Saller E, Nashimoto H, Saito N, Kertesz MA, Leisinger T: Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J Bacteriol. 1996 Sep;178(18):5438-46. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Li JM, Russell CS, Cosloy SD: The structure of the Escherichia coli hemB gene. Gene. 1989 Jan 30;75(1):177-84. [Article]
- Quadroni M, Staudenmann W, Kertesz M, James P: Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli. Eur J Biochem. 1996 Aug 1;239(3):773-81. [Article]
- Borodovsky M, Rudd KE, Koonin EV: Intrinsic and extrinsic approaches for detecting genes in a bacterial genome. Nucleic Acids Res. 1994 Nov 11;22(22):4756-67. [Article]
- Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T: Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli. J Biol Chem. 1997 Sep 12;272(37):23031-6. [Article]
- Elkins JM, Ryle MJ, Clifton IJ, Dunning Hotopp JC, Lloyd JS, Burzlaff NI, Baldwin JE, Hausinger RP, Roach PL: X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates. Biochemistry. 2002 Apr 23;41(16):5185-92. [Article]
- O'Brien JR, Schuller DJ, Yang VS, Dillard BD, Lanzilotta WN: Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure. Biochemistry. 2003 May 20;42(19):5547-54. [Article]