Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P0A847 (TGT_ECOLI)

Entry version 122 (07 Oct 2020)
Sequence version 1 (07 Jun 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Queuine tRNA-ribosyltransferase

Gene

tgt

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 base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).UniRule annotation2 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

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit.UniRule annotation1 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

kcat is 0.00121 sec(-1) with tRNA(Tyr) and guanine as substrates.1 Publication
  1. KM=0.12 µM for tRNA(Tyr)1 Publication
  2. KM=0.1 µM for guanine1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tRNA-queuosine biosynthesis

    This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.UniRule annotation1 Publication
    View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei89Proton acceptorUniRule annotation1 Publication1
    <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 sitei143SubstrateUniRule annotation1
    Binding sitei187SubstrateUniRule annotation1
    Binding sitei214Substrate; via amide nitrogenUniRule annotation1
    Active sitei264NucleophileUniRule annotation1 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 bindingi302ZincUniRule annotation1 Publication1
    Metal bindingi304ZincUniRule annotation1 Publication1
    Metal bindingi307ZincUniRule annotation1 Publication1
    Metal bindingi333Zinc; via pros nitrogenUniRule annotation1

    <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

    • queuosine biosynthetic process Source: EcoCyc
    • tRNA-guanine transglycosylation Source: InterPro
    • tRNA wobble guanine modification Source: EcoCyc
    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 functionGlycosyltransferase, Transferase
    Biological processQueuosine biosynthesis, tRNA processing
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:EG10996-MONOMER
    MetaCyc:EG10996-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.4.2.29, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P0A847

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

    More...    UniPathwayi    		UPA00392

    <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:
    Queuine tRNA-ribosyltransferaseUniRule annotation (EC:2.4.2.29UniRule annotation2 Publications)
    Alternative name(s):
    Guanine insertion enzymeUniRule annotation
    tRNA-guanine transglycosylaseUniRule annotation
    <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:tgtUniRule annotation
    Ordered Locus Names:b0406, JW0396
    <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 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

    Complete GO annotation on QuickGO ...

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi28C → A: Slight loss of activity. 1 Publication1
    Mutagenesisi89D → E: Reduces catalytic activity by 51%. 1 Publication1
    Mutagenesisi90S → A: Loss of activity. 1 Publication1
    Mutagenesisi90S → C: Loss of activity. 1 Publication1
    Mutagenesisi90S → F: Loss of activity. 1 Publication1
    Mutagenesisi145C → A: No loss of activity. 1 Publication1
    Mutagenesisi232C → A: Slight loss of activity. 1 Publication1
    Mutagenesisi264D → A, N, Q, K or H: Loss of catalytic activity. 1 Publication1
    Mutagenesisi264D → E: Reduces catalytic activity by 88%. 1 Publication1
    Mutagenesisi265C → A: Significant loss of activity. 1 Publication1
    Mutagenesisi302C → A: Loss of activity. 1 Publication1
    Mutagenesisi304C → A: Loss of activity. 1 Publication1
    Mutagenesisi307C → A: Loss of activity. 1 Publication1
    Mutagenesisi316H → A: Slight loss of activity. 1 Publication1
    Mutagenesisi317H → A: Loss of activity. 1 Publication1
    Mutagenesisi321C → A: No loss of activity. 1 Publication1

    <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_00001354711 – 375Queuine tRNA-ribosyltransferaseAdd BLAST375

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0A847

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

    More...    PaxDbi    		P0A847

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0A847

    <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

    Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.

    UniRule annotation

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4263531, 21 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-36020N

    Protein interaction database and analysis system

    More...    IntActi    		P0A847, 39 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0406

    <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

    3D structure databases

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

    More...    SMRi    		P0A847

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    <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

    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>Regioni89 – 93Substrate bindingUniRule annotation5
    Regioni245 – 251RNA bindingUniRule annotation7
    Regioni269 – 273RNA binding; important for wobble base 34 recognitionUniRule annotation5

    <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 queuine tRNA-ribosyltransferase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0343, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_022060_0_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A847

    KEGG Orthology (KO)

    More...    KOi    		K00773

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A847

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.20.20.105, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00168, Q_tRNA_Tgt, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR004803, TGT
    IPR036511, TGT-like_sf
    IPR002616, tRNA_ribo_trans-like

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01702, TGT, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF51713, SSF51713, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00430, Q_tRNA_tgt, 1 hit
    TIGR00449, tgt_general, 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.

    P0A847-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG 
            60         70         80         90        100
    AQIILGNTFH LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD 
           110        120        130        140        150
    IRKITEQGVH FRNPINGDPI FLDPEKSMEI QYDLGSDIVM IFDECTPYPA 
           160        170        180        190        200
    DWDYAKRSME MSLRWAKRSR ERFDSLGNKN ALFGIIQGSV YEDLRDISVK 
           210        220        230        240        250
    GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP RYLMGVGKPE 
           260        270        280        290        300
    DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP 
           310        320        330        340        350
    ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE 
           360        370 
    EGKLESFVTD FYQRQGREVP PLNVD
    Length:375
    Mass (Da):42,594
    Last modified:June 7, 2005 - 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:i40271CA08D8A8820
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti54 – 55IL → MV (PubMed:1706703).Curated2
    Sequence conflicti54 – 55IL → MV (PubMed:8323579).Curated2

    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
    		M63939 Genomic DNA Translation: AAA24667.1
    U00096 Genomic DNA Translation: AAC73509.1
    AP009048 Genomic DNA Translation: BAE76186.1
    U82664 Genomic DNA Translation: AAB40162.1
    X56175 Genomic DNA Translation: CAA39631.1 Sequence problems.
    X56175 Genomic DNA Translation: CAA39632.1 Sequence problems.
    S68715 Genomic DNA Translation: AAC60467.2

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		C38530

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414940.1, NC_000913.3
    WP_000667319.1, NZ_STEB01000007.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73509; AAC73509; b0406
    BAE76186; BAE76186; BAE76186

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		49585797
    949130

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0396
    eco:b0406

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1871

    <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
    		M63939 Genomic DNA Translation: AAA24667.1
    U00096 Genomic DNA Translation: AAC73509.1
    AP009048 Genomic DNA Translation: BAE76186.1
    U82664 Genomic DNA Translation: AAB40162.1
    X56175 Genomic DNA Translation: CAA39631.1 Sequence problems.
    X56175 Genomic DNA Translation: CAA39632.1 Sequence problems.
    S68715 Genomic DNA Translation: AAC60467.2
    PIRiC38530
    RefSeqiNP_414940.1, NC_000913.3
    WP_000667319.1, NZ_STEB01000007.1

    3D structure databases

    SMRiP0A847
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi4263531, 21 interactors
    DIPiDIP-36020N
    IntActiP0A847, 39 interactors
    STRINGi511145.b0406

    Proteomic databases

    jPOSTiP0A847
    PaxDbiP0A847
    PRIDEiP0A847

    Genome annotation databases

    EnsemblBacteriaiAAC73509; AAC73509; b0406
    BAE76186; BAE76186; BAE76186
    GeneIDi49585797
    949130
    KEGGiecj:JW0396
    eco:b0406
    PATRICifig|1411691.4.peg.1871

    Organism-specific databases

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

    More...    EchoBASEi    		EB0989

    Phylogenomic databases

    eggNOGiCOG0343, Bacteria
    HOGENOMiCLU_022060_0_1_6
    InParanoidiP0A847
    KOiK00773
    PhylomeDBiP0A847

    Enzyme and pathway databases

    UniPathwayiUPA00392
    BioCyciEcoCyc:EG10996-MONOMER
    MetaCyc:EG10996-MONOMER
    BRENDAi2.4.2.29, 2026
    SABIO-RKiP0A847

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P0A847

    Family and domain databases

    Gene3Di3.20.20.105, 1 hit
    HAMAPiMF_00168, Q_tRNA_Tgt, 1 hit
    InterProiView protein in InterPro
    IPR004803, TGT
    IPR036511, TGT-like_sf
    IPR002616, tRNA_ribo_trans-like
    PfamiView protein in Pfam
    PF01702, TGT, 1 hit
    SUPFAMiSSF51713, SSF51713, 1 hit
    TIGRFAMsiTIGR00430, Q_tRNA_tgt, 1 hit
    TIGR00449, tgt_general, 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 nameiTGT_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: P0A847
    Secondary accession number(s): P19675
    , P19676, P78226, Q2MC20, Q47627
    <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: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 7, 2020
    This is version 122 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

    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. 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