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tauD:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

TauD

Synonyms

taurine dioxygenase, 2-oxoglutarate-dependent[1], B0368[2][1], YaiG[2][1], SsiD[2][1], TauD[2][1]

Product description

TauD[2][3];

Component of taurine dioxygenase[3]

Taurine/alpha-ketoglutarate dioxygenase[4]

EC number (for enzymes)

Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc [5]

complete

GO:0031418

L-ascorbic acid binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0847

F

Seeded from EcoCyc [5]

complete

GO:0016702

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0223

F

Seeded from EcoCyc [5]

complete

GO:0016491

oxidoreductase activity

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR003819
SP_KW:KW-0560

F

Seeded from EcoCyc [5]

complete

GO:0005506

iron ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0408

F

Seeded from EcoCyc [5]

complete

GO:0000908

taurine dioxygenase activity

GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.14.11.17

F

Seeded from EcoCyc [5]

complete

GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required fields missing

GO:0009055

electron carrier activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003819

F

Seeded from EcoCyc [5]

complete

GO:0055114

oxidation reduction

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc [5]

complete

GO:0009310

amine catabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006790

sulfur metabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0005506

iron ion binding

PMID:11955067[6]

IPI: Inferred from Physical Interaction

F

complete

GO:0005515

protein binding

PMID:11955067[6]

IPI: Inferred from Physical Interaction

F

complete

GO:0005737

cytoplasm

PMID:16165092[7]

IDA: Inferred from Direct Assay

C

complete

GO:0000908

taurine dioxygenase activity

PMID:16165092[7]

IDA: Inferred from Direct Assay

F

complete

GO:0006790

sulfur metabolic process

PMID:8808933[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0000908

taurine dioxygenase activity

PMID:9287300[9]

IDA: Inferred from Direct Assay

F

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner TypePartnerNotesReferencesEvidence

Protein

Subunits of taurine dioxygenase

could be indirect

Protein

greA

PMID:16606699[10]

Experiment(s):EBI-1136388

Protein

rplJ

PMID:16606699[10]

Experiment(s):EBI-1136388

Protein

talA

PMID:16606699[10]

Experiment(s):EBI-1136388

Protein

rpsD

PMID:16606699[10]

Experiment(s):EBI-1136388

Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

CompartmentDescriptionEvidenceSourceNotes

Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc

MSERLSITPL GPYIGAQISG ADLTRPLSDN QFEQLYHAVL RHQVVFLRDQ AITPQQQRAL
AQRFGELHIH PVYPHAEGVD EIIVLDTHND NPPDNDNWHT DVTFIETPPA GAILAAKELP
STGGDTLWTS GIAAYEALSV PFRQLLSGLR AEHDFRKSFP EYKYRKTEEE HQRWREAVAK
NPPLLHPVVR THPVSGKQAL FVNEGFTTRI VDVSEKESEA LLSFLFAHIT KPEFQVRWRW
QPNDIAIWDN RVTQHYANAD YLPQRRIMHR ATILGDKPFY RAG
Length

283

Mol. Wt

32.409 kDa

pI

6.8 (calculated)

Extinction coefficient

46,410 (calc based on 9 Y, 6 W, and C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

TypeResiduesDescriptionNotesReferences

Initiator Methionine

1

Removed

UniProt:P37610



rectanglemotifs

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures
Models

View models at:

Structure figures

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource typeSourceNotes/Reference

Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:MONOMER0-147

UniProt (EcoliWiki Page)

UniProt:P37610

PFAM (EcoliWiki Page)

PFAM:PF02668

RefSeq (EcoliWiki Page)

RefSeq:NP_414902


Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 3.2 3.3 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. 6.0 6.1 Elkins JM et al. (2002) X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates. Biochemistry 41: 5185-92 PubMed EcoliWiki page
  7. 7.0 7.1 Kalliri E et al. (2005) Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/alpha-ketoglutarate dioxygenase, TauD. Biochem Biophys Res Commun 338: 191-7 PubMed EcoliWiki page
  8. van der Ploeg JR et al. (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: 5438-46 PubMed EcoliWiki page
  9. Eichhorn E et al. (1997) Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli. J Biol Chem 272: 23031-6 PubMed EcoliWiki page
  10. 10.0 10.1 10.2 10.3 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page

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