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P37610

- TAUD_ECOLI

UniProt

P37610 - TAUD_ECOLI

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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

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

Fe2+2 PublicationsNote: Binds 1 Fe(2+) 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
Complete GO annotation...

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
Complete GO annotation...

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 – 149Combined sources
Beta strandi16 – 205Combined sources
Beta strandi23 – 253Combined sources
Helixi29 – 4214Combined sources
Beta strandi43 – 475Combined sources
Helixi54 – 629Combined sources
Beta strandi71 – 733Combined sources
Beta strandi79 – 8810Combined sources
Turni101 – 1044Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi109 – 11810Combined sources
Beta strandi126 – 1305Combined sources
Helixi131 – 1366Combined sources
Helixi140 – 1467Combined sources
Beta strandi150 – 1534Combined sources
Helixi155 – 1584Combined sources
Helixi161 – 1633Combined sources
Helixi168 – 18013Combined sources
Beta strandi184 – 1918Combined sources
Turni193 – 1953Combined sources
Beta strandi198 – 2003Combined sources
Turni204 – 2063Combined sources
Beta strandi207 – 2137Combined sources
Helixi215 – 22814Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2384Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi266 – 2749Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP37610.
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

        10         20         30         40         50
MSERLSITPL GPYIGAQISG ADLTRPLSDN QFEQLYHAVL RHQVVFLRDQ
60 70 80 90 100
AITPQQQRAL AQRFGELHIH PVYPHAEGVD EIIVLDTHND NPPDNDNWHT
110 120 130 140 150
DVTFIETPPA GAILAAKELP STGGDTLWTS GIAAYEALSV PFRQLLSGLR
160 170 180 190 200
AEHDFRKSFP EYKYRKTEEE HQRWREAVAK NPPLLHPVVR THPVSGKQAL
210 220 230 240 250
FVNEGFTTRI VDVSEKESEA LLSFLFAHIT KPEFQVRWRW QPNDIAIWDN
260 270 280
RVTQHYANAD YLPQRRIMHR ATILGDKPFY RAG
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P37610.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 127 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