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Protein

Isoaspartyl dipeptidase

Gene

iadA

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 hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu.4 Publications

<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+3 Publications, Co2+3 PublicationsNote: Binds 2 Zn2+ ions per subunit. Has highest activity with Zn2+ ions, but is also active with Co2+ ions.3 Publications

<p>This subsection of the ‘Function’ 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

P-hydroxymercuribenzoate causes a slight inhibition (8 to 17 %). Iodoacetamide, o-iodosobenzoate and ammonium persulfate do not inhibit the enzyme activity.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=0.81 mM for beta-aspartylleucine (at pH 8.0)1 Publication

    pH dependencei

    Optimum pH is 7.5. Active over a wide pH range.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi68Zinc 1; via tele nitrogen; catalytic4 Publications1
    Metal bindingi70Zinc 1; via tele nitrogen; catalytic4 Publications1
    <p>This subsection of the ‘Function’ 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 sitei106Substrate3 Publications1
    Binding sitei137Substrate3 Publications1
    Metal bindingi162Zinc 1; via carbamate group; catalytic4 Publications1
    Metal bindingi162Zinc 2; via carbamate group; catalytic4 Publications1
    Binding sitei169Substrate3 Publications1
    Metal bindingi201Zinc 2; via pros nitrogen; catalytic4 Publications1
    Metal bindingi230Zinc 2; via tele nitrogen; catalytic4 Publications1
    Binding sitei233Substrate3 Publications1
    <p>This subsection of the ‘Function’ 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 sitei285Proton acceptor1 Publication1
    Metal bindingi285Zinc 1; catalytic4 Publications1
    Binding sitei289Substrate; via amide nitrogen and carbonyl oxygen3 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

    <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, Metalloprotease, Protease
    LigandCobalt, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7925-MONOMER
    MetaCyc:G7925-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.4.19.5 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P39377

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    M38.001

    <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:
    Isoaspartyl dipeptidase (EC:3.4.19.-)
    <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:iadA
    Synonyms:yjiF
    Ordered Locus Names:b4328, JW4291
    <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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG12567 iadA

    <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

    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 observable phenotype. Does not result in reduced stationary phase or heat shock survival. Approximately 31% of the enzyme activity present.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi77E → D or Q: Reduces activity 100000-fold. 2 Publications1
    Mutagenesisi137Y → A or F: Reduces activity 1000-fold. 2 Publications1
    Mutagenesisi169R → K: Reduces activity 1000-fold. 1 Publication1
    Mutagenesisi169R → M: Loss of activity. 1 Publication1
    Mutagenesisi233R → K: Reduces activity 1000-fold. 1 Publication1
    Mutagenesisi233R → M: Loss of activity. 1 Publication1
    Mutagenesisi285D → A: Reduces activity 100000-fold. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02437 (5r)-5-Amino-6-Hydroxyhexylcarbamic Acid
    DB03801 Lysine Nz-Carboxylic Acid

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000791781 – 390Isoaspartyl dipeptidaseAdd BLAST390

    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 residuei162N6-carboxylysine4 Publications1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Carbamylation allows a single lysine to coordinate two zinc ions (PubMed:12718528, PubMed:12946361, PubMed:15882050, PubMed:16289685).4 Publications

    Proteomic databases

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

    More...
    PaxDbi
    P39377

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P39377

    <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

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261005, 12 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10001N

    Protein interaction database and analysis system

    More...
    IntActi
    P39377, 4 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    316407.85677071

    <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

    1390
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P39377

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

    More...
    SMRi
    P39377

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P39377

    <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>Regioni75 – 77Substrate binding3

    <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 peptidase M38 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105DYB Bacteria
    ENOG410XNTK LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000275891

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P39377

    KEGG Orthology (KO)

    More...
    KOi
    K01305

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P39377

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01308 Isoaspartyl-dipeptidase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.40.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006680 Amidohydro-rel
    IPR033826 Isoaspartyl-dipeptidase
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase
    IPR010229 Pept_M38_dipep

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01979 Amidohydro_1, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001238 IadA, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51338 SSF51338, 2 hits
    SSF51556 SSF51556, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01975 isoAsp_dipep, 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>.<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.

    P39377-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIDYTAAGFT LLQGAHLYAP EDRGICDVLV ANGKIIAVAS NIPSDIVPNC
    60 70 80 90 100
    TVVDLSGQIL CPGFIDQHVH LIGGGGEAGP TTRTPEVALS RLTEAGVTSV
    110 120 130 140 150
    VGLLGTDSIS RHPESLLAKT RALNEEGISA WMLTGAYHVP SRTITGSVEK
    160 170 180 190 200
    DVAIIDRVIG VKCAISDHRS AAPDVYHLAN MAAESRVGGL LGGKPGVTVF
    210 220 230 240 250
    HMGDSKKALQ PIYDLLENCD VPISKLLPTH VNRNVPLFEQ ALEFARKGGT
    260 270 280 290 300
    IDITSSIDEP VAPAEGIARA VQAGIPLARV TLSSDGNGSQ PFFDDEGNLT
    310 320 330 340 350
    HIGVAGFETL LETVQVLVKD YDFSISDALR PLTSSVAGFL NLTGKGEILP
    360 370 380 390
    GNDADLLVMT PELRIEQVYA RGKLMVKDGK ACVKGTFETA
    Length:390
    Mass (Da):41,084
    Last modified:February 1, 1995 - 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:i9CEEC838381545B5
    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
    U15029 Genomic DNA Translation: AAC43299.1
    U14003 Genomic DNA Translation: AAA97224.1
    U00096 Genomic DNA Translation: AAC77284.1
    AP009048 Genomic DNA Translation: BAE78321.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B55889

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_418748.1, NC_000913.3
    WP_000568432.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC77284; AAC77284; b4328
    BAE78321; BAE78321; BAE78321

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948853

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW4291
    eco:b4328

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2361

    <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
    U15029 Genomic DNA Translation: AAC43299.1
    U14003 Genomic DNA Translation: AAA97224.1
    U00096 Genomic DNA Translation: AAC77284.1
    AP009048 Genomic DNA Translation: BAE78321.1
    PIRiB55889
    RefSeqiNP_418748.1, NC_000913.3
    WP_000568432.1, NZ_LN832404.1

    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
    1ONWX-ray1.65A/B1-390[»]
    1ONXX-ray2.10A/B1-390[»]
    1PO9X-ray2.00A/B1-390[»]
    1POJX-ray3.30A/B1-390[»]
    1POKX-ray2.70A/B1-390[»]
    1YBQX-ray2.00A/B1-390[»]
    2AQOX-ray1.95A/B1-390[»]
    2AQVX-ray1.95A/B1-390[»]
    5LP3electron microscopy10.50A/B/C/D/E/F/G/H/I/J/K/L1-390[»]
    ProteinModelPortaliP39377
    SMRiP39377
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261005, 12 interactors
    DIPiDIP-10001N
    IntActiP39377, 4 interactors
    STRINGi316407.85677071

    Chemistry databases

    DrugBankiDB02437 (5r)-5-Amino-6-Hydroxyhexylcarbamic Acid
    DB03801 Lysine Nz-Carboxylic Acid

    Protein family/group databases

    MEROPSiM38.001

    Proteomic databases

    PaxDbiP39377
    PRIDEiP39377

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77284; AAC77284; b4328
    BAE78321; BAE78321; BAE78321
    GeneIDi948853
    KEGGiecj:JW4291
    eco:b4328
    PATRICifig|1411691.4.peg.2361

    Organism-specific databases

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

    More...
    EchoBASEi
    EB2455
    EcoGeneiEG12567 iadA

    Phylogenomic databases

    eggNOGiENOG4105DYB Bacteria
    ENOG410XNTK LUCA
    HOGENOMiHOG000275891
    InParanoidiP39377
    KOiK01305
    PhylomeDBiP39377

    Enzyme and pathway databases

    BioCyciEcoCyc:G7925-MONOMER
    MetaCyc:G7925-MONOMER
    BRENDAi3.4.19.5 2026
    SABIO-RKiP39377

    Miscellaneous databases

    EvolutionaryTraceiP39377

    Protein Ontology

    More...
    PROi
    PR:P39377

    Family and domain databases

    CDDicd01308 Isoaspartyl-dipeptidase, 1 hit
    Gene3Di2.30.40.10, 1 hit
    InterProiView protein in InterPro
    IPR006680 Amidohydro-rel
    IPR033826 Isoaspartyl-dipeptidase
    IPR011059 Metal-dep_hydrolase_composite
    IPR032466 Metal_Hydrolase
    IPR010229 Pept_M38_dipep
    PfamiView protein in Pfam
    PF01979 Amidohydro_1, 1 hit
    PIRSFiPIRSF001238 IadA, 1 hit
    SUPFAMiSSF51338 SSF51338, 2 hits
    SSF51556 SSF51556, 1 hit
    TIGRFAMsiTIGR01975 isoAsp_dipep, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiIADA_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: P39377
    Secondary accession number(s): Q2M5Y5
    <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: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: November 7, 2018
    This is version 155 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, Complete proteome, 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
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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