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Entry version 126 (17 Jun 2020)
Sequence version 1 (10 May 2005)
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Protein

D-aminoacyl-tRNA deacylase

Gene

dtd

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

An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs, has no observable editing activity on tRNAs charged with cognate L-amino acid (PubMed:10383414, PubMed:4292198, PubMed:10918062, PubMed:24302572, PubMed:27224426). Edits mischarged glycyl-tRNA(Ala) more efficiently than AlaRS (PubMed:28362257). Acts via tRNA-based rather than protein-based catalysis (PubMed:24302572, PubMed:27224426, PubMed:28362257). Rejects correctly charged L-amino acid-tRNAs from its binding site rather than specifically recognizing incorrectly charged D-amino acid-tRNAs (PubMed:27224426). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly); GTP-bound EF-Tu (tested with T.thermophilus EF-Tu AC Q5SHN6) protects charged glycyl-tRNA(Gly) from hydrolysis, while increasing Dtd levels or inactivating EF-Tu decreases protection (PubMed:27224426). Hydrolyzes mischarged glycyl-tRNA(Ala) (but not seryl-tRNA(Ala)) even in the presence of EF-Tu, edits about 4-fold better than the editing domain of AlaRS (PubMed:28362257). Has greater activity on glycyl-tRNA(Ala) than glycyl-tRNA(Gly) due in part to its recognition of the conserved tRNA(Ala) G3.U70 wobble base pair (PubMed:28362257). Binds D-amino acids but not L-amino acids (PubMed:16902403). Overexpression of E.coli or P.falciparum Dtd is toxic in E.coli, toxicity can be rescued by supplementation with Gly (PubMed:27224426). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality (PubMed:15292242). Hydrolyzes D-tyrosyl-tRNA(Tyr) (PubMed:4292198, PubMed:10383414, PubMed:24302572, PubMed:27224426). Hydrolyzes D-phenylalanyl-tRNA(Phe) (PubMed:4292198, PubMed:24302572). Hydrolyzes D-aspartyl-tRNA(Asp) (PubMed:10918062). Hydrolyzes D-tryptophanyl-tRNA(Trp) (PubMed:10918062). Hydrolyzes glycyl-tRNA(Gly) (PubMed:27224426). Hydrolyzes glycyl-tRNA(Ala) (PubMed:28362257).9 Publications

Caution

Initially the conserved reside Thr-80 was thought to be a nucleophile; mutagenesis in this organism and P.falciparum indicates it is not.1 Publication

<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 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/KM is 6 µM(-1)s(-1) for D-tyrosyl-tRNA(Tyr) (PubMed:10383414). kcat/KM is 2.8 µM(-1)s(-1) for D-tryptophanyl-tRNA(Trp) (PubMed:10918062). kcat/KM is 12 µM(-1)s(-1) for D-aspartyl-tRNA(Asp) (PubMed:10918062). kcat/KM is 10 µM (-1)s(-1) for glycyl-tRNA(Gly) (PubMed:27224426).3 Publications
  1. KM=1.0 µM for D-tyrosyl-tRNA(Tyr)1 Publication
  2. KM=1.0 µM for glycyl-tRNA(Gly)1 Publication

    <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 functionHydrolase, RNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG11852-MONOMER
    ECOL316407:JW3858-MONOMER
    MetaCyc:EG11852-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.1.96 2026

    <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:
    D-aminoacyl-tRNA deacylase1 PublicationUniRule annotation (EC:3.1.1.96UniRule annotation3 Publications)
    Short name:
    DTDUniRule annotation
    Alternative name(s):
    D-tyrosyl RNA deacylase1 Publication
    D-tyrosyl-tRNA(Tyr) deacylase1 Publication
    Gly-tRNA(Ala) deacylase1 PublicationUniRule annotation
    Gly-tRNA(Gly) deacylase1 Publication
    <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:dtd1 PublicationUniRule annotation
    Synonyms:yihZ
    Ordered Locus Names:b3887, JW3858
    <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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

    • cytoplasm Source: GO_Central

    Keywords - Cellular componenti

    Cytoplasm

    <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

    No phenotype in rich or minimal medium, decreased growth rate in the presence of excess D-tyrosine (PubMed:10383414). A double dtd-dadA deletion mutant has a more pronounced growth defect in the presence of D-Tyr (in strain K12 / EC989) (PubMed:10383414). In a dtd deletion mutant about 40% of tRNA(Tyr) is D-tyrosyl-tRNA(Tyr); overexpressing the gene for tRNA(Tyr) suppresses the toxicity of D-Tyr by increasing the levels of L-tyrosyl-tRNA(Tyr) available for translation (PubMed:15292242). Decreased growth in the presence of D-Asp, D-Ser, D-Gln and D-Trp (PubMed:10918062). Poor growth on 20 mg/ml D-Tyr, no growth on 500 mg/ml D-Tyr or 20 mg/ml D-Trp (PubMed:25441601). Overexpression of genes for tRNA(Asp) or tRNA(Trp) suppresses the toxicity of their respective D-amino acids (PubMed:15292242). No effect seen when grown in 3 or 10 mM Gly; in a mutant that no longer edits mischarged glycyl-tRNA(Ala) or seryl-tRNA(Ala) (triple mutation in alaS) Gly becomes toxic, but excess Ala restores growth (PubMed:28362257).5 Publications

    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>Mutagenesisi77S → A or P: Wild-type deacylation of D-tyrosyl-tRNA(Tyr). 1 Publication1
    Mutagenesisi78Q → A: Wild-type deacylation of D-tyrosyl-tRNA(Tyr). 1 Publication1
    Mutagenesisi80T → A: Wild-type deacylation of D-tyrosyl-tRNA(Tyr). 1 Publication1
    Mutagenesisi102A → F: Loss of deacylation of D-tyrosyl-tRNA(Tyr), loss of deacylation of glycyl-tRNA(Gly), not toxic upon overexpression. 2 Publications1
    Mutagenesisi125F → A: Loss of deacylation of D-tyrosyl-tRNA(Tyr), loss of deacylation of glycyl-tRNA(Gly). 2 Publications1
    Mutagenesisi129M → K: Alters stereospecificity, confers binding of L-amino acids while slightly decreasing binding of D-amino acids. 1 Publication1
    Mutagenesisi137G → A: Loss of deacylation of D-tyrosyl-tRNA(Tyr). 1 Publication1
    Mutagenesisi138P → A: Loss of deacylation of D-tyrosyl-tRNA(Tyr). 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_00001645371 – 145D-aminoacyl-tRNA deacylaseAdd BLAST145

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0A6M4

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

    More...
    PaxDbi
    P0A6M4

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A6M4

    <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.

    UniRule annotation2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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
    4262640, 2 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-47962N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A6M4, 9 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b3887

    <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

    1145
    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
    P0A6M4

    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
    P0A6M4

    <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

    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>Motifi137 – 138Gly-cisPro motif, important for rejection of L-amino acidsUniRule annotation1 Publication2

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids (PubMed:24302572, PubMed:27224426).UniRule annotation2 Publications

    <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 DTD family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108YYA Bacteria
    COG1490 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_076901_1_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A6M4

    KEGG Orthology (KO)

    More...
    KOi
    K07560

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A6M4

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00563 Dtyr_deacylase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.50.80.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00518 Deacylase_Dtd, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003732 Daa-tRNA_deacyls_DTD
    IPR023509 DTD-like_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10472 PTHR10472, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02580 Tyr_Deacylase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF69500 SSF69500, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00256 TIGR00256, 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.

    P0A6M4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIALIQRVTR ASVTVEGEVT GEIGAGLLVL LGVEKDDDEQ KANRLCERVL
    60 70 80 90 100
    GYRIFSDAEG KMNLNVQQAG GSVLVVSQFT LAADTERGMR PSFSKGASPD
    110 120 130 140
    RAEALYDYFV ERCRQQEMNT QTGRFAADMQ VSLVNDGPVT FWLQV
    Length:145
    Mass (Da):15,950
    Last modified:May 10, 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:i5CF0C0DB0819EC9B
    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
    L19201 Genomic DNA Translation: AAB03020.1
    U00096 Genomic DNA Translation: AAD13449.1
    AP009048 Genomic DNA Translation: BAE77422.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S40831

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418323.1, NC_000913.3
    WP_000560983.1, NZ_STEB01000017.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAD13449; AAD13449; b3887
    BAE77422; BAE77422; BAE77422

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948378

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3858
    eco:b3887

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2824

    <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
    L19201 Genomic DNA Translation: AAB03020.1
    U00096 Genomic DNA Translation: AAD13449.1
    AP009048 Genomic DNA Translation: BAE77422.1
    PIRiS40831
    RefSeqiNP_418323.1, NC_000913.3
    WP_000560983.1, NZ_STEB01000017.1

    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
    1JKEX-ray1.55A/B/C/D1-145[»]
    SMRiP0A6M4
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4262640, 2 interactors
    DIPiDIP-47962N
    IntActiP0A6M4, 9 interactors
    STRINGi511145.b3887

    Proteomic databases

    jPOSTiP0A6M4
    PaxDbiP0A6M4
    PRIDEiP0A6M4

    Genome annotation databases

    EnsemblBacteriaiAAD13449; AAD13449; b3887
    BAE77422; BAE77422; BAE77422
    GeneIDi948378
    KEGGiecj:JW3858
    eco:b3887
    PATRICifig|1411691.4.peg.2824

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1798

    Phylogenomic databases

    eggNOGiENOG4108YYA Bacteria
    COG1490 LUCA
    HOGENOMiCLU_076901_1_0_6
    InParanoidiP0A6M4
    KOiK07560
    PhylomeDBiP0A6M4

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11852-MONOMER
    ECOL316407:JW3858-MONOMER
    MetaCyc:EG11852-MONOMER
    BRENDAi3.1.1.96 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A6M4

    Protein Ontology

    More...
    PROi
    PR:P0A6M4

    Family and domain databases

    CDDicd00563 Dtyr_deacylase, 1 hit
    Gene3Di3.50.80.10, 1 hit
    HAMAPiMF_00518 Deacylase_Dtd, 1 hit
    InterProiView protein in InterPro
    IPR003732 Daa-tRNA_deacyls_DTD
    IPR023509 DTD-like_sf
    PANTHERiPTHR10472 PTHR10472, 1 hit
    PfamiView protein in Pfam
    PF02580 Tyr_Deacylase, 1 hit
    SUPFAMiSSF69500 SSF69500, 1 hit
    TIGRFAMsiTIGR00256 TIGR00256, 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 nameiDTD_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: P0A6M4
    Secondary accession number(s): P32147, Q2M8I4
    <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: May 10, 2005
    Last sequence update: May 10, 2005
    Last modified: June 17, 2020
    This is version 126 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
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