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P37610

- TAUD_ECOLI

UniProt

P37610 - TAUD_ECOLI

Protein

Alpha-ketoglutarate-dependent taurine dioxygenase

Gene

tauD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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 activityi

    Taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2.2 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.2 Publications

    Enzyme regulationi

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

    pH dependencei

    Optimum pH is 6.9.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei70 – 701Substrate
    Binding sitei73 – 731Substrate
    Binding sitei95 – 951Substrate
    Metal bindingi99 – 991Iron; catalytic2 Publications
    Metal bindingi101 – 1011Iron; catalytic2 Publications
    Binding sitei102 – 1021Substrate; via amide nitrogen
    Binding sitei126 – 12612-oxoglutarate2 Publications
    Binding sitei240 – 24012-oxoglutarate2 Publications
    Metal bindingi255 – 2551Iron; catalytic2 Publications
    Binding sitei266 – 26612-oxoglutarate2 Publications
    Binding sitei270 – 27012-oxoglutarate2 Publications
    Binding sitei270 – 2701Substrate

    GO - Molecular functioni

    1. L-ascorbic acid binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. taurine dioxygenase activity Source: EcoliWiki

    GO - Biological processi

    1. sulfur compound metabolic process Source: EcoliWiki

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BioCyciEcoCyc:MONOMER0-147.
    ECOL316407:JW0360-MONOMER.
    MetaCyc:MONOMER0-147.
    SABIO-RKP37610.
    UniPathwayiUPA00336; UER00542.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:tauD
    Synonyms:ssiD, yaiG
    Ordered Locus Names:b0368, JW0360
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12423. tauD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 283282Alpha-ketoglutarate-dependent taurine dioxygenasePRO_0000194016Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 12813-hydroxytryptophan; by autocatalysis1 Publication
    Modified residuei240 – 24013-hydroxytryptophan; by autocatalysis1 Publication
    Modified residuei248 – 24813-hydroxytryptophan; by autocatalysis1 Publication

    Keywords - PTMi

    Hydroxylation

    Proteomic databases

    PRIDEiP37610.

    Expressioni

    Inductioni

    Repressed by sulfate or cysteine.

    Gene expression databases

    GenevestigatoriP37610.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-10966N.
    IntActiP37610. 4 interactions.
    MINTiMINT-8299483.
    STRINGi511145.b0368.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 149
    Beta strandi16 – 205
    Beta strandi23 – 253
    Helixi29 – 4214
    Beta strandi43 – 475
    Helixi54 – 629
    Beta strandi71 – 733
    Beta strandi79 – 8810
    Turni101 – 1044
    Beta strandi105 – 1073
    Beta strandi109 – 11810
    Beta strandi126 – 1305
    Helixi131 – 1366
    Helixi140 – 1467
    Beta strandi150 – 1534
    Helixi155 – 1584
    Helixi161 – 1633
    Helixi168 – 18013
    Beta strandi184 – 1918
    Turni193 – 1953
    Beta strandi198 – 2003
    Turni204 – 2063
    Beta strandi207 – 2137
    Helixi215 – 22814
    Helixi232 – 2343
    Beta strandi235 – 2384
    Beta strandi245 – 2495
    Beta strandi252 – 2576
    Beta strandi266 – 2749

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GQWX-ray3.00A/B2-283[»]
    1GY9X-ray2.50A/B2-283[»]
    1OS7X-ray2.50A/B/C/D1-283[»]
    1OTJX-ray1.90A/B/C/D1-283[»]
    ProteinModelPortaliP37610.
    SMRiP37610. Positions 2-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37610.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TfdA dioxygenase family.Curated

    Phylogenomic databases

    eggNOGiCOG2175.
    HOGENOMiHOG000165071.
    KOiK03119.
    OMAiEFTIRWR.
    OrthoDBiEOG6M0T37.
    PhylomeDBiP37610.

    Family and domain databases

    InterProiIPR003819. Taurine_dOase.
    [Graphical view]
    PfamiPF02668. TauD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P37610-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSERLSITPL GPYIGAQISG ADLTRPLSDN QFEQLYHAVL RHQVVFLRDQ    50
    AITPQQQRAL AQRFGELHIH PVYPHAEGVD EIIVLDTHND NPPDNDNWHT 100
    DVTFIETPPA GAILAAKELP STGGDTLWTS GIAAYEALSV PFRQLLSGLR 150
    AEHDFRKSFP EYKYRKTEEE HQRWREAVAK NPPLLHPVVR THPVSGKQAL 200
    FVNEGFTTRI VDVSEKESEA LLSFLFAHIT KPEFQVRWRW QPNDIAIWDN 250
    RVTQHYANAD YLPQRRIMHR ATILGDKPFY RAG 283
    Length:283
    Mass (Da):32,410
    Last modified:January 23, 2007 - v3
    Checksum:i7ADEB0CDC9CEEB57
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS78607. H64764.
    RefSeqiNP_414902.1. NC_000913.3.
    YP_488661.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73471; AAC73471; b0368.
    BAE76149; BAE76149; BAE76149.
    GeneIDi12930836.
    945021.
    KEGGiecj:Y75_p0357.
    eco:b0368.
    PATRICi32115875. VBIEscCol129921_0379.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRi S78607. H64764.
    RefSeqi NP_414902.1. NC_000913.3.
    YP_488661.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GQW X-ray 3.00 A/B 2-283 [» ]
    1GY9 X-ray 2.50 A/B 2-283 [» ]
    1OS7 X-ray 2.50 A/B/C/D 1-283 [» ]
    1OTJ X-ray 1.90 A/B/C/D 1-283 [» ]
    ProteinModelPortali P37610.
    SMRi P37610. Positions 2-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10966N.
    IntActi P37610. 4 interactions.
    MINTi MINT-8299483.
    STRINGi 511145.b0368.

    Proteomic databases

    PRIDEi P37610.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73471 ; AAC73471 ; b0368 .
    BAE76149 ; BAE76149 ; BAE76149 .
    GeneIDi 12930836.
    945021.
    KEGGi ecj:Y75_p0357.
    eco:b0368.
    PATRICi 32115875. VBIEscCol129921_0379.

    Organism-specific databases

    EchoBASEi EB2322.
    EcoGenei EG12423. tauD.

    Phylogenomic databases

    eggNOGi COG2175.
    HOGENOMi HOG000165071.
    KOi K03119.
    OMAi EFTIRWR.
    OrthoDBi EOG6M0T37.
    PhylomeDBi P37610.

    Enzyme and pathway databases

    UniPathwayi UPA00336 ; UER00542 .
    BioCyci EcoCyc:MONOMER0-147.
    ECOL316407:JW0360-MONOMER.
    MetaCyc:MONOMER0-147.
    SABIO-RK P37610.

    Miscellaneous databases

    EvolutionaryTracei P37610.
    PROi P37610.

    Gene expression databases

    Genevestigatori P37610.

    Family and domain databases

    InterProi IPR003819. Taurine_dOase.
    [Graphical view ]
    Pfami PF02668. TauD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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, HYDROXYLATION AT TRP-128; TRP-240 AND TRP-248.
    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.

    Entry informationi

    Entry nameiTAUD_ECOLI
    AccessioniPrimary (citable) accession number: P37610
    Secondary accession number(s): P77797, Q2MC57, Q47540
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3