Alpha-ketoglutarate-dependent taurine dioxygenase

NameAlpha-ketoglutarate-dependent taurine dioxygenase
Synonyms
  • 1.14.11.17
  • 2-aminoethanesulfonate dioxygenase
  • SSI3
  • ssiD
  • Sulfate starvation-induced protein 3
  • yaiG
Gene NametauD
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0002747|Alpha-ketoglutarate-dependent taurine dioxygenase
MSERLSITPLGPYIGAQISGADLTRPLSDNQFEQLYHAVLRHQVVFLRDQAITPQQQRAL
AQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTFIETPPAGAILAAKELP
STGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHDFRKSFPEYKYRKTEEEHQRWREAVAK
NPPLLHPVVRTHPVSGKQALFVNEGFTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRW
QPNDIAIWDNRVTQHYANADYLPQRRIMHRATILGDKPFYRAG
Number of residues283
Molecular Weight32409.26
Theoretical pI6.76
GO Classification
Functions
  • metal ion binding
  • L-ascorbic acid binding
  • taurine dioxygenase activity
Processes
  • sulfur compound metabolic process
Components
  • cytoplasm
General FunctionTaurine dioxygenase activity
Specific FunctionCatalyzes 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
Transmembrane RegionsNot Available
GenBank Protein ID1384060
UniProtKB IDP37610
UniProtKB Entry NameTAUD_ECOLI
Cellular LocationNot 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
GenBank Gene IDD85613
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. 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. 8808933
  2. 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. 9278503
  3. 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. 16738553
  4. Li JM, Russell CS, Cosloy SD: The structure of the Escherichia coli hemB gene. Gene. 1989 Jan 30;75(1):177-84. 2656410
  5. 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. 8774726
  6. 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. 7984428
  7. 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. 9287300
  8. 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. 11955067
  9. 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. 12741810