Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P08337 (MUTT_ECOLI)

Entry version 185 (23 Feb 2022)
Sequence version 1 (01 Aug 1988)
Previous versions | rss
Add a publicationFeedback
Protein

8-oxo-dGTP diphosphatase

Gene

mutT

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

Specifically hydrolyzes both 8-oxo-deoxyguanosine triphosphate (8-oxo-dGTP) and 8-oxo-guanosine triphosphate (8-oxo-GTP) to the related monophosphates, thereby cleaning up the nucleotide pools and preventing misincorporation of 8-oxoGua into DNA and RNA (PubMed:1309939, PubMed:9311918, PubMed:15850400).

It prevents replicational errors by removing an oxidatively damaged form of guanine (8-oxo-dGTP) from DNA and the nucleotide pool (PubMed:1309939).

8-oxo-dGTP can be inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (PubMed:1309939).

MutT may also ensure transcriptional fidelity, removing 8-oxo-GTP from the ribonucleotide triphosphate pool (PubMed:9311918).

However, due to the lower efficiency of RNA polymerase 8-oxo-GTP incorporation, MutT is probably not a major contributor to transcriptional fidelity (PubMed:25294823).

It also hydrolyzes 8-oxo-dGDP and 8-oxo-GDP to their monophosphate form (PubMed:15850400).

In vitro, can also use dGTP, dGDP and other various nucleoside di- and triphosphates, with much lower efficiency (PubMed:1851162, PubMed:1309939, PubMed:15850400).

Works cooperatively with MutM and MutY to prevent accumulation in the DNA of oxidized guanine residues (PubMed:7739614).

6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mg2+4 Publications

<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=0.058 µM for 8-oxo-dGDP1 Publication
  2. KM=0.081 µM for 8-oxo-dGTP1 Publication
  3. KM=0.48 µM for 8-oxo-dGTP1 Publication
  4. KM=0.045 µM for 8-oxo-GDP1 Publication
  5. KM=0.26 µM for 8-oxo-GTP1 Publication
  6. KM=170 µM for dGDP1 Publication
  7. KM=1100 µM for dGTP2 Publications
  8. KM=1500 µM for dGTP1 Publication
  9. KM=2200 µM for dCTP1 Publication
  10. KM=1700 µM for dCTP1 Publication
  11. KM=1800 µM for dTTP1 Publication
  12. KM=350 µM for GDP1 Publication
  13. KM=1000 µM for GTP1 Publication
  14. KM=1200 µM for GTP1 Publication
  1. Vmax=3.7 pmol/min/ng enzyme toward 8-oxo-dGDP1 Publication
  2. Vmax=20 pmol/min/ng enzyme toward 8-oxo-dGTP1 Publication
  3. Vmax=4.8 pmol/min/ng enzyme toward 8-oxo-GDP1 Publication
  4. Vmax=22 pmol/min/ng enzyme toward 8-oxo-GTP1 Publication
  5. Vmax=5.9 pmol/min/ng enzyme toward dGDP1 Publication
  6. Vmax=44 pmol/min/ng enzyme toward dGTP1 Publication
  7. Vmax=3.5 pmol/min/mg enzyme toward GDP1 Publication
  8. Vmax=24 pmol/min/mg enzyme toward GTP1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei238-oxo-dGTP1 Publication1
Binding sitei288-oxo-dGTP1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi37Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi57Magnesium1 Publication1
Binding sitei1198-oxo-dGTP2 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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • DNA repair Source: GO_Central
  • DNA replication Source: UniProtKB-KW
Complete GO annotation on QuickGO ...

<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 functionHydrolase, Mutator protein
Biological processDNA damage, DNA repair, DNA replication
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10626-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.1.55, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P08337

<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%5Fand%5Ftaxonomy%5Fsection">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:
8-oxo-dGTP diphosphatase (EC:3.6.1.553 Publications)
Short name:
8-oxo-dGTPase
Alternative name(s):
7,8-dihydro-8-oxoguanine-triphosphatase
Mutator protein MutT
dGTP pyrophosphohydrolase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:mutT1 Publication
Ordered Locus Names:b0099, JW0097
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 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 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 the gene increases the rates of A:T to C:G transversion a thousandfold over the wild type level.1 Publication

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02023, 8-oxo-dGMP

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000569431 – 1298-oxo-dGTP diphosphataseAdd BLAST129

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P08337

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

More...PaxDbi		P08337

PRoteomics IDEntifications database

More...PRIDEi		P08337

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261888, 366 interactors
849225, 4 interactors

Database of interacting proteins

More...DIPi		DIP-10288N

Protein interaction database and analysis system

More...IntActi		P08337, 5 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0099

<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

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P08337

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

More...SMRi		P08337

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		P08337

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 129Nudix hydrolasePROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni34 – 378-oxo-dGTP binding1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi38 – 59Nudix boxPROSITE-ProRule annotationAdd BLAST22

<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 Nudix hydrolase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0494, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_037162_19_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08337

Database for complete collections of gene phylogenies

More...PhylomeDBi		P08337

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003561, Mutator_MutT
IPR020476, Nudix_hydrolase
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00293, NUDIX, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01401, MUTATORMUTT
PR00502, NUDIXFAMILY

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55811, SSF55811, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00586, mutt, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51462, NUDIX, 1 hit
PS00893, NUDIX_BOX, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P08337-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKLQIAVGI IRNENNEIFI TRRAADAHMA NKLEFPGGKI EMGETPEQAV 
        60         70         80         90        100
VRELQEEVGI TPQHFSLFEK LEYEFPDRHI TLWFWLVERW EGEPWGKEGQ 
       110        120 
PGEWMSLVGL NADDFPPANE PVIAKLKRL
Length:129
Mass (Da):14,927
Last modified:August 1, 1988 - v1
<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:i626287828DCEA53E
GO

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
X04831 Genomic DNA Translation: CAA28523.1
M20791 Genomic DNA Translation: AAA24620.1
X55034 Genomic DNA Translation: CAA38876.1
U00096 Genomic DNA Translation: AAC73210.1
AP009048 Genomic DNA Translation: BAB96667.1

Protein sequence database of the Protein Information Resource

More...PIRi		A27890, MVECMT

NCBI Reference Sequences

More...RefSeqi		NP_414641.1, NC_000913.3
WP_000736007.1, NZ_SSZK01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73210; AAC73210; b0099
BAB96667; BAB96667; BAB96667

Database of genes from NCBI RefSeq genomes

More...GeneIDi		944824

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0097
eco:b0099

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2181

<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
X04831 Genomic DNA Translation: CAA28523.1
M20791 Genomic DNA Translation: AAA24620.1
X55034 Genomic DNA Translation: CAA38876.1
U00096 Genomic DNA Translation: AAC73210.1
AP009048 Genomic DNA Translation: BAB96667.1
PIRiA27890, MVECMT
RefSeqiNP_414641.1, NC_000913.3
WP_000736007.1, NZ_SSZK01000004.1

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
1MUTNMR-A1-129[»]
1PPXNMR-A1-129[»]
1PUNNMR-A1-129[»]
1PUQNMR-A1-129[»]
1PUSNMR-A1-129[»]
1TUMNMR-A1-129[»]
3A6SX-ray1.80A/B1-129[»]
3A6TX-ray1.96A1-129[»]
3A6UX-ray2.56A1-129[»]
3A6VX-ray2.00A/B1-129[»]
BMRBiP08337
SMRiP08337
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261888, 366 interactors
849225, 4 interactors
DIPiDIP-10288N
IntActiP08337, 5 interactors
STRINGi511145.b0099

Chemistry databases

DrugBankiDB02023, 8-oxo-dGMP

Proteomic databases

jPOSTiP08337
PaxDbiP08337
PRIDEiP08337

Genome annotation databases

EnsemblBacteriaiAAC73210; AAC73210; b0099
BAB96667; BAB96667; BAB96667
GeneIDi944824
KEGGiecj:JW0097
eco:b0099
PATRICifig|1411691.4.peg.2181

Organism-specific databases

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

More...EchoBASEi		EB0621

Phylogenomic databases

eggNOGiCOG0494, Bacteria
HOGENOMiCLU_037162_19_2_6
InParanoidiP08337
PhylomeDBiP08337

Enzyme and pathway databases

BioCyciEcoCyc:EG10626-MONOMER
BRENDAi3.6.1.55, 2026
SABIO-RKiP08337

Miscellaneous databases

EvolutionaryTraceiP08337

Protein Ontology

More...PROi		PR:P08337

Family and domain databases

InterProiView protein in InterPro
IPR003561, Mutator_MutT
IPR020476, Nudix_hydrolase
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom
PfamiView protein in Pfam
PF00293, NUDIX, 1 hit
PRINTSiPR01401, MUTATORMUTT
PR00502, NUDIXFAMILY
SUPFAMiSSF55811, SSF55811, 1 hit
TIGRFAMsiTIGR00586, mutt, 1 hit
PROSITEiView protein in PROSITE
PS51462, NUDIX, 1 hit
PS00893, NUDIX_BOX, 1 hit

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 nameiMUTT_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: P08337
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: February 23, 2022
This is version 185 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again