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P37610 (TAUD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-ketoglutarate-dependent taurine dioxygenase

EC=1.14.11.17
Alternative name(s):
2-aminoethanesulfonate dioxygenase
Sulfate starvation-induced protein 3
Short name=SSI3
Gene names
Name:tauD
Synonyms:ssiD, yaiG
Ordered Locus Names:b0368, JW0360
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2. Ref.9 Ref.10

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.9 Ref.10

Enzyme regulation

Activated by ascorbate and inhibited by divalent metal ions such as zinc, copper and cobalt.

Pathway

Organosulfur degradation; taurine degradation via aerobic pathway; aminoacetaldehyde and sulfite from taurine: step 1/1.

Subunit structure

Homodimer. Ref.9 Ref.10

Induction

Repressed by sulfate or cysteine.

Sequence similarities

Belongs to the TfdA dioxygenase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.9.

Sequence caution

The sequence M24488 differs from that shown. Reason: Frameshift at position 244.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 283282Alpha-ketoglutarate-dependent taurine dioxygenase
PRO_0000194016

Sites

Metal binding991Iron; catalytic
Metal binding1011Iron; catalytic
Metal binding2551Iron; catalytic
Binding site701Substrate
Binding site731Substrate
Binding site951Substrate
Binding site1021Substrate; via amide nitrogen
Binding site12612-oxoglutarate
Binding site24012-oxoglutarate
Binding site26612-oxoglutarate
Binding site27012-oxoglutarate
Binding site2701Substrate

Amino acid modifications

Modified residue12813-hydroxytryptophan; by autocatalysis
Modified residue24013-hydroxytryptophan; by autocatalysis
Modified residue24813-hydroxytryptophan; by autocatalysis

Secondary structure

...................................................... 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37610 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7ADEB0CDC9CEEB57

FASTA28332,410
        10         20         30         40         50         60 
MSERLSITPL GPYIGAQISG ADLTRPLSDN QFEQLYHAVL RHQVVFLRDQ AITPQQQRAL 

        70         80         90        100        110        120 
AQRFGELHIH PVYPHAEGVD EIIVLDTHND NPPDNDNWHT DVTFIETPPA GAILAAKELP 

       130        140        150        160        170        180 
STGGDTLWTS GIAAYEALSV PFRQLLSGLR AEHDFRKSFP EYKYRKTEEE HQRWREAVAK 

       190        200        210        220        230        240 
NPPLLHPVVR THPVSGKQAL FVNEGFTTRI VDVSEKESEA LLSFLFAHIT KPEFQVRWRW 

       250        260        270        280 
QPNDIAIWDN RVTQHYANAD YLPQRRIMHR ATILGDKPFY RAG 

« Hide

References

« Hide 'large scale' references
[1]"Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source."
van der Ploeg J.R., Weiss M.A., Saller E., Nashimoto H., Saito N., Kertesz M.A., Leisinger T.
J. Bacteriol. 178:5438-5446(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The structure of the Escherichia coli hemB gene."
Li J.-M., Russell C.S., Cosloy S.D.
Gene 75:177-184(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-283.
Strain: K12.
[6]"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."
Quadroni M., Staudenmann W., Kertesz M.A., James P.
Eur. J. Biochem. 239:773-781(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11; 42-46 AND 59-63, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[7]"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
Borodovsky M., Rudd K.E., Koonin E.V.
Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[8]"Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli."
Eichhorn E., van der Ploeg J.R., Kertesz M.A., Leisinger T.
J. Biol. Chem. 272:23031-23036(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates."
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.
Biochemistry 41:5185-5192(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON; 2-OXOGLUTARATE AND TAURINE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
[10]"Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure."
O'Brien J.R., Schuller D.J., Yang V.S., Dillard B.D., Lanzilotta W.N.
Biochemistry 42:5547-5554(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IRON; 2-OXOGLUTARATE AND TAURINE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85613 Genomic DNA. Translation: BAA12841.1.
U73857 Genomic DNA. Translation: AAB18091.1.
U00096 Genomic DNA. Translation: AAC73471.1.
AP009048 Genomic DNA. Translation: BAE76149.1.
M24488 Genomic DNA. No translation available.
PIRH64764. S78607.
RefSeqNP_414902.1. NC_000913.3.
YP_488661.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQWX-ray3.00A/B1-283[»]
1GY9X-ray2.50A/B1-283[»]
1OS7X-ray2.50A/B/C/D1-283[»]
1OTJX-ray1.90A/B/C/D1-283[»]
ProteinModelPortalP37610.
SMRP37610. Positions 2-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10966N.
IntActP37610. 4 interactions.
MINTMINT-8299483.
STRING511145.b0368.

Proteomic databases

PRIDEP37610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73471; AAC73471; b0368.
BAE76149; BAE76149; BAE76149.
GeneID12930836.
945021.
KEGGecj:Y75_p0357.
eco:b0368.
PATRIC32115875. VBIEscCol129921_0379.

Organism-specific databases

EchoBASEEB2322.
EcoGeneEG12423. tauD.

Phylogenomic databases

eggNOGCOG2175.
HOGENOMHOG000165071.
KOK03119.
OMALTATHDF.
OrthoDBEOG6M0T37.
PhylomeDBP37610.
ProtClustDBPRK09553.

Enzyme and pathway databases

BioCycEcoCyc:MONOMER0-147.
ECOL316407:JW0360-MONOMER.
MetaCyc:MONOMER0-147.
SABIO-RKP37610.
UniPathwayUPA00336; UER00542.

Gene expression databases

GenevestigatorP37610.

Family and domain databases

InterProIPR003819. Taurine_dOase.
[Graphical view]
PfamPF02668. TauD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP37610.
PROP37610.

Entry information

Entry nameTAUD_ECOLI
AccessionPrimary (citable) accession number: P37610
Secondary accession number(s): P77797, Q2MC57, Q47540
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene