Alpha-ketoglutarate-dependent taurine dioxygenase (P37610)

Identification
Name:Alpha-ketoglutarate-dependent taurine dioxygenase
Synonyms:
  • 2-aminoethanesulfonate dioxygenase
  • Sulfate starvation-induced protein 3
  • SSI3
Gene Name:tauD
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase 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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0alpha-Ketoglutarate + 1.0Oxygen + 1.0Taurine ↔ 1.0Aminoacetaldehyde + 1.0Carbon dioxide + 1.0Hydrogen ion + 1.0Sulfite + 1.0Succinic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Taurine + 1.0alpha-Ketoglutarate + 1.0Oxygen ↔ 1.0Sulfite + 1.0Aminoacetaldehyde + 1.0Succinic acid + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Sulfite+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Taurine + 1.0Oxoglutaric acid + 1.0Oxygen → 1.0Sulfite + 1.0Succinic acid + 1.0Aminoacetaldehyde + 1.0Carbon dioxide + 1.0Sulfite
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Sulfite+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Taurine + 1.0Oxoglutaric acid + 1.0Oxygen → 1.0Sulfite + 1.0Succinic acid + 1.0Carbon dioxide + 1.0Hydrogen ion + 1.0Aminoacetaldehyde + 1.0Sulfite
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Taurine + 1.0Oxoglutaric acid + 1.0Oxygen → 1.0Hydrogen ion + 1.0Aminoacetaldehyde + 1.0Sulfite + 1.0Succinic acid + 1.0Carbon dioxide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Taurine + 1.0Oxoglutaric acid + 1.0Oxygen → 1.0Sulfite + 1.0Aminoacetaldehyde + 1.0Succinic acid + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB20116AminoacetaldehydeMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB00254Succinic acidMetaboCard
ECMDB00240SulfiteMetaboCard
ECMDB00251TaurineMetaboCard
GO Classification:
Function
catalytic activity
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0368
Gene OrientationClockwise
Centisome Percentage:8.34
Left Sequence End387019
Right Sequence End387870
Gene Sequence:
>852 bp
ATGGCTGAAATTACCGCATCCCTGGTAAAAGAGCTGCGTGAGCGTACTGGCGCAGGCATG
ATGGATTGCAAAAAAGCACTGACTGAAGCTAACGGCGACATCGAGCTGGCAATCGAAAAC
ATGCGTAAGTCCGGTGCTATTAAAGCAGCGAAAAAAGCAGGCAACGTTGCTGCTGACGGC
GTGATCAAAACCAAAATCGACGGCAACTACGGCATCATTCTGGAAGTTAACTGCCAGACT
GACTTCGTTGCAAAAGACGCTGGTTTCCAGGCGTTCGCAGACAAAGTTCTGGACGCAGCT
GTTGCTGGCAAAATCACTGACGTTGAAGTTCTGAAAGCACAGTTCGAAGAAGAACGTGTT
GCGCTGGTAGCGAAAATTGGTGAAAACATCAACATTCGCCGCGTTGCTGCGCTGGAAGGC
GACGTTCTGGGTTCTTATCAGCACGGTGCGCGTATCGGCGTTCTGGTTGCTGCTAAAGGC
GCTGACGAAGAGCTGGTTAAACACATCGCTATGCACGTTGCTGCAAGCAAGCCAGAATTC
ATCAAACCGGAAGACGTATCCGCTGAAGTGGTAGAAAAAGAATACCAGGTACAGCTGGAT
ATCGCGATGCAGTCTGGTAAGCCGAAAGAAATCGCAGAGAAAATGGTTGAAGGCCGCATG
AAGAAATTCACCGGCGAAGTTTCTCTGACCGGTCAGCCGTTCGTTATGGAACCAAGCAAA
ACTGTTGGTCAGCTGCTGAAAGAGCATAACGCTGAAGTGACTGGCTTCATCCGCTTCGAA
GTGGGTGAAGGCATCGAGAAAGTTGAGACTGACTTTGCAGCAGAAGTTGCTGCGATGTCC
AAGCAGTCTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:283
Protein Molecular Weight:32409
Protein Theoretical pI:7
PDB File:1OTJ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Alpha-ketoglutarate-dependent taurine dioxygenase
MSERLSITPLGPYIGAQISGADLTRPLSDNQFEQLYHAVLRHQVVFLRDQAITPQQQRAL
AQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTFIETPPAGAILAAKELP
STGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHDFRKSFPEYKYRKTEEEHQRWREAVAK
NPPLLHPVVRTHPVSGKQALFVNEGFTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRW
QPNDIAIWDNRVTQHYANADYLPQRRIMHRATILGDKPFYRAG
References
External Links:
ResourceLink
Uniprot ID:P37610
Uniprot Name:TAUD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21239025
PDB ID:1OTJ
Ecogene ID:EG12423
Ecocyc:EG12423
ColiBase:b0368
Kegg Gene:b0368
EchoBASE ID:EB2322
CCDB:TAUD_ECOLI
BacMap:16128353
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Borodovsky, M., Rudd, K. E., Koonin, E. V. (1994). "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Nucleic Acids Res 22:4756-4767. Pubmed: 7984428
  • Eichhorn, E., van der Ploeg, J. R., Kertesz, M. A., Leisinger, T. (1997). "Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli." J Biol Chem 272:23031-23036. Pubmed: 9287300
  • Elkins, J. M., Ryle, M. J., Clifton, I. J., Dunning Hotopp, J. C., Lloyd, J. S., Burzlaff, N. I., Baldwin, J. E., Hausinger, R. P., Roach, P. L. (2002). "X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates." Biochemistry 41:5185-5192. Pubmed: 11955067
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Li, J. M., Russell, C. S., Cosloy, S. D. (1989). "The structure of the Escherichia coli hemB gene." Gene 75:177-184. Pubmed: 2656410
  • Quadroni, M., Staudenmann, W., Kertesz, M., James, P. (1996). "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 239:773-781. Pubmed: 8774726
  • van der Ploeg, J. R., Weiss, M. A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M. A., Leisinger, T. (1996). "Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source." J Bacteriol 178:5438-5446. Pubmed: 8808933