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Entry version 156 (13 Nov 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Alpha-ketoglutarate-dependent taurine dioxygenase

Gene

tauD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the alpha-ketoglutarate-dependent hydroxylation of taurine yielding sulfite and aminoacetaldehyde after decomposition of an unstable intermediate (PubMed:9287300). Is required for the utilization of taurine (2-aminoethanesulfonate) as an alternative sulfur source for growth in the absence of sulfate (PubMed:8808933). To a lesser extent, pentanesulfonate, 3-(N-morpholino)propanesulfonate and 1,3-dioxo-2-isoindolineethanesulfonate are also desulfonated by this enzyme in vitro; however, desulfonation by TauD of organosulfonates other than taurine seem to be of little or no importance for sulfur metabolism in vivo (PubMed:9287300).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+3 PublicationsNote: Binds 1 Fe2+ ion per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by ascorbate and inhibited by divalent metal ions such as zinc, copper and cobalt.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=55 µM for taurine (at pH 6.9)1 Publication
  2. KM=11 µM for 2-oxoglutarate (at pH 6.9)1 Publication
  3. KM=1490 µM for butanesulfonate (at pH 6.9)1 Publication
  4. KM=590 µM for pentanesulfonate (at pH 6.9)1 Publication
  5. KM=1510 µM for hexanesulfonate (at pH 6.9)1 Publication
  6. KM=145 µM for 3-(N-morpholino)propanesulfonate (at pH 6.9)1 Publication
  7. KM=485 µM for 1,3-dioxo-2-isoindolineethanesulfonate (at pH 6.9)1 Publication
  1. Vmax=4.1 µmol/min/mg enzyme with taurine as substrate (at pH 6.9)1 Publication
  2. Vmax=1.3 µmol/min/mg enzyme with butanesulfonate as substrate (at pH 6.9)1 Publication
  3. Vmax=1.9 µmol/min/mg enzyme with pentanesulfonate as substrate (at pH 6.9)1 Publication
  4. Vmax=2.2 µmol/min/mg enzyme with hexanesulfonate as substrate (at pH 6.9)1 Publication
  5. Vmax=2.0 µmol/min/mg enzyme with 3-(N-morpholino)propanesulfonate as substrate (at pH 6.9)1 Publication
  6. Vmax=3.8 µmol/min/mg enzyme with 1,3-dioxo-2-isoindolineethanesulfonate as substrate (at pH 6.9)1 Publication

pH dependencei

Optimum pH is 6.9.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: taurine degradation via aerobic pathway

This protein is involved in step 1 of the subpathway that synthesizes aminoacetaldehyde and sulfite from taurine.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Alpha-ketoglutarate-dependent taurine dioxygenase (tauD)
This subpathway is part of the pathway taurine degradation via aerobic pathway, which is itself part of Organosulfur degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes aminoacetaldehyde and sulfite from taurine, the pathway taurine degradation via aerobic pathway and in Organosulfur degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei70Taurine2 Publications1
Binding sitei73Taurine2 Publications1
Binding sitei95Taurine2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi99Iron; catalytic2 Publications1
Metal bindingi101Iron; catalytic2 Publications1
Binding sitei102Taurine; via amide nitrogen2 Publications1
Binding sitei1262-oxoglutarate2 Publications1
Metal bindingi255Iron; catalytic2 Publications1
Binding sitei2552-oxoglutarate2 Publications1
Binding sitei2662-oxoglutarate2 Publications1
Binding sitei2702-oxoglutarate2 Publications1
Binding sitei270Taurine2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDioxygenase, Oxidoreductase
LigandIron, Metal-binding, Vitamin C

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:MONOMER0-147
ECOL316407:JW0360-MONOMER
MetaCyc:MONOMER0-147

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.11.17 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P37610

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00336;UER00542

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alpha-ketoglutarate-dependent taurine dioxygenase1 Publication (EC:1.14.11.173 Publications)
Alternative name(s):
2-aminoethanesulfonate dioxygenase
Sulfate starvation-induced protein 3
Short name:
SSI3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tauD
Synonyms:ssiD, yaiG
Ordered Locus Names:b0368, JW0360
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Taurine dioxygenase can be used for enzymatic determination of taurine concentration in food quality control, biological research, and medical diagnosis.1 Publication

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Disruption of this gene leads to a loss of the ability to utilize taurine as a source of sulfur, but does not affect the utilization of a range of other aliphatic sulfonates as sulfur sources.1 Publication

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB01956 Taurine

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001940162 – 283Alpha-ketoglutarate-dependent taurine dioxygenaseAdd BLAST282

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1283-hydroxytryptophan; by autocatalysis1 Publication1
Modified residuei2403-hydroxytryptophan; by autocatalysis1 Publication1
Modified residuei2483-hydroxytryptophan; by autocatalysis1 Publication1

Keywords - PTMi

Hydroxylation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P37610

PRoteomics IDEntifications database

More...
PRIDEi
P37610

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Is only expressed during growth in the absence of sulfate or cysteine.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:11955067, PubMed:12741810, PubMed:9287300). Was later shown to be a homotetramer arranged as a dimer of two dimers (PubMed:22221834).

4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259830, 13 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2120 Taurine dioxygenase complex, tetrameric
CPX-3190 Taurine dioxygenase complex, dimeric

Database of interacting proteins

More...
DIPi
DIP-10966N

Protein interaction database and analysis system

More...
IntActi
P37610, 4 interactors

Molecular INTeraction database

More...
MINTi
P37610

STRING: functional protein association networks

More...
STRINGi
511145.b0368

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1283
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P37610

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P37610

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TfdA dioxygenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105E2B Bacteria
COG2175 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000165071

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P37610

KEGG Orthology (KO)

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KOi
K03119

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P37610

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.130.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR042098 TauD-like_sf
IPR003819 TauD/TfdA-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02668 TauD, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7ADEB0CDC9CEEB57
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence M24488 differs from that shown. Reason: Frameshift.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

Protein sequence database of the Protein Information Resource

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PIRi
S78607 H64764

NCBI Reference Sequences

More...
RefSeqi
NP_414902.1, NC_000913.3
WP_000004027.1, NZ_SSZK01000009.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73471; AAC73471; b0368
BAE76149; BAE76149; BAE76149

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945021

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0360
eco:b0368

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1911

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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.
PIRiS78607 H64764
RefSeqiNP_414902.1, NC_000913.3
WP_000004027.1, NZ_SSZK01000009.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
6EDHX-ray1.73A/B1-283[»]
SMRiP37610
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4259830, 13 interactors
ComplexPortaliCPX-2120 Taurine dioxygenase complex, tetrameric
CPX-3190 Taurine dioxygenase complex, dimeric
DIPiDIP-10966N
IntActiP37610, 4 interactors
MINTiP37610
STRINGi511145.b0368

Chemistry databases

DrugBankiDB01956 Taurine

Proteomic databases

PaxDbiP37610
PRIDEiP37610

Genome annotation databases

EnsemblBacteriaiAAC73471; AAC73471; b0368
BAE76149; BAE76149; BAE76149
GeneIDi945021
KEGGiecj:JW0360
eco:b0368
PATRICifig|1411691.4.peg.1911

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2322

Phylogenomic databases

eggNOGiENOG4105E2B Bacteria
COG2175 LUCA
HOGENOMiHOG000165071
InParanoidiP37610
KOiK03119
PhylomeDBiP37610

Enzyme and pathway databases

UniPathwayiUPA00336;UER00542
BioCyciEcoCyc:MONOMER0-147
ECOL316407:JW0360-MONOMER
MetaCyc:MONOMER0-147
BRENDAi1.14.11.17 2026
SABIO-RKiP37610

Miscellaneous databases

EvolutionaryTraceiP37610

Protein Ontology

More...
PROi
PR:P37610

Family and domain databases

Gene3Di3.60.130.10, 1 hit
InterProiView protein in InterPro
IPR042098 TauD-like_sf
IPR003819 TauD/TfdA-like
PfamiView protein in Pfam
PF02668 TauD, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTAUD_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P37610
Secondary accession number(s): P77797, Q2MC57, Q47540
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: November 13, 2019
This is version 156 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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