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Entry version 111 (12 Aug 2020)
Sequence version 1 (21 Jun 2005)
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Protein

Proofreading thioesterase EntH

Gene

entH

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

Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs.5 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=16 µM for 2,3-DHB-EntB1 Publication
  2. KM=116 µM for 2,3-DHB-EntB1 Publication
  3. KM=21 µM for 4-hydroxybenzoyl-CoA1 Publication
  4. KM=190 µM for 4-hydroxybenzoyl-CoA1 Publication
  5. KM=25 µM for 2,4-DHB-EntB1 Publication
  6. KM=32 µM for lauroyl-EntB1 Publication
  7. KM=35 µM for 3-hydroxybenzoyl-CoA1 Publication
  8. KM=265 µM for 3-hydroxybenzoyl-CoA1 Publication
  9. KM=37 µM for 3-HPA-CoA1 Publication
  10. KM=45 µM for lauroyl-CoA1 Publication
  11. KM=49 µM for decanoyl-CoA1 Publication
  12. KM=55 µM for palmitoyl-CoA1 Publication
  13. KM=4.25 µM for palmitoyl-CoA1 Publication
  14. KM=161 µM for 2,3-dihydroxybenzoyl-CoA1 Publication
  15. KM=176 µM for salicylyl-CoA1 Publication
  16. KM=212 µM for 3,4-dihydroxybenzoyl-CoA1 Publication
  17. KM=219 µM for 2,4-dihydroxybenzoyl-CoA1 Publication
  18. KM=256 µM for 3,5-dihydroxybenzoyl-CoA1 Publication
  19. KM=272 µM for salicylyl-EntB1 Publication
  20. KM=350 µM for hexanoyl-CoA1 Publication
  21. KM=400 µM for propionyl-CoA1 Publication
  22. KM=475 µM for benzoyl-CoA1 Publication
  23. KM=800 µM for acetyl-CoA1 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: enterobactin biosynthesis

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

    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 sitei48Substrate1 Publication1
    <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 sitei63Nucleophile or proton acceptor1 PublicationUniRule annotation1 Publication1
    Binding sitei82Substrate; via carbonyl oxygen1 Publication1

    <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

    • enterobactin biosynthetic process Source: EcoCyc

    <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

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG11105-MONOMER
    ECOL316407:JW0589-MONOMER
    MetaCyc:EG11105-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.2.2, 2026

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

    More...
    UniPathwayi
    UPA00017

    <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:
    Proofreading thioesterase EntHUniRule annotation (EC:3.1.2.-UniRule annotation)
    Alternative name(s):
    Enterobactin synthase component HUniRule annotation
    p15
    <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:entH1 PublicationUniRule annotation
    Synonyms:ybdB
    Ordered Locus Names:b0597, JW0589
    <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

    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

    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>Mutagenesisi48Q → A: Loss of activity. 2 Publications1
    Mutagenesisi48Q → N: 290-fold decrease in activity toward salicylyl-CoA. 1 Publication1
    Mutagenesisi54H → A: 229-fold decrease in activity toward salicylyl-CoA. Loss of activity toward benzoyl-CoA. 2 Publications1
    Mutagenesisi63E → A, D or Q: Loss of activity. 2 Publications1
    Mutagenesisi64T → S: 13-fold decrease in activity toward salicylyl-CoA. 1 Publication1
    Mutagenesisi67S → A: 140-fold decrease in activity toward salicylyl-CoA. 1 Publication1
    Mutagenesisi67S → C: 104-fold decrease in activity toward salicylyl-CoA. 1 Publication1
    Mutagenesisi68M → A: 130-fold decrease in activity toward salicylyl-CoA. 1 Publication1
    Mutagenesisi68M → V: 47-fold increase in catalytic efficiency toward 1,4-dihydroxy-2-naphthoyl-CoA and 10-fold increase in catalytic efficiency toward lauroyl-CoA. Does not affect catalytic efficiency toward benzoyl-CoA. 2 Publications1

    <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_00001566761 – 137Proofreading thioesterase EntHAdd BLAST137

    Proteomic databases

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

    More...
    PaxDbi
    P0A8Y8

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A8Y8

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

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

    Induced by iron starvation.1 Publication

    <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

    Homotetramer. Dimer of dimers.

    Interacts specifically with the aryl carrier protein (ArCP) domain of EntB.

    UniRule annotation3 Publications

    <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

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4260982, 15 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-11343N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A8Y8, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0597

    <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

    1137
    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
    P0A8Y8

    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
    P0A8Y8

    <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>Regioni54 – 55Substrate binding1 Publication2
    Regioni89 – 92Substrate binding1 Publication4

    <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 thioesterase PaaI family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG2050, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_089876_13_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A8Y8

    KEGG Orthology (KO)

    More...
    KOi
    K24147

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A8Y8

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00907, Thioesterase_EntH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029069, HotDog_dom_sf
    IPR003736, PAAI_dom
    IPR026576, Thioesterase_EntH
    IPR006683, Thioestr_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03061, 4HBT, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF54637, SSF54637, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00369, unchar_dom_1, 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.

    P0A8Y8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF
    60 70 80 90 100
    GLLHGGASAA LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG
    110 120 130
    VCQPLHLGRQ NQSWEIVVFD EQGRRCCTCR LGTAVLG
    Length:137
    Mass (Da):14,970
    Last modified:June 21, 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:iC8DF8DE63815F206
    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
    M24148 Unassigned DNA Translation: AAA16104.1
    M24143 Genomic DNA Translation: AAA76837.1
    U82598 Genomic DNA Translation: AAB40797.1
    U00096 Genomic DNA Translation: AAC73698.1
    AP009048 Genomic DNA Translation: BAE76352.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B91904, Q3ECEA

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415129.1, NC_000913.3
    WP_000637953.1, NZ_STEB01000047.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73698; AAC73698; b0597
    BAE76352; BAE76352; BAE76352

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    52075916
    945215

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0589
    eco:b0597

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1672

    <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
    M24148 Unassigned DNA Translation: AAA16104.1
    M24143 Genomic DNA Translation: AAA76837.1
    U82598 Genomic DNA Translation: AAB40797.1
    U00096 Genomic DNA Translation: AAC73698.1
    AP009048 Genomic DNA Translation: BAE76352.1
    PIRiB91904, Q3ECEA
    RefSeqiNP_415129.1, NC_000913.3
    WP_000637953.1, NZ_STEB01000047.1

    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
    1VH9X-ray2.15A/B2-137[»]
    4K4CX-ray1.85A/B/C/D1-137[»]
    4K4DX-ray2.17A/B1-137[»]
    SMRiP0A8Y8
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260982, 15 interactors
    DIPiDIP-11343N
    IntActiP0A8Y8, 2 interactors
    STRINGi511145.b0597

    Proteomic databases

    PaxDbiP0A8Y8
    PRIDEiP0A8Y8

    Genome annotation databases

    EnsemblBacteriaiAAC73698; AAC73698; b0597
    BAE76352; BAE76352; BAE76352
    GeneIDi52075916
    945215
    KEGGiecj:JW0589
    eco:b0597
    PATRICifig|1411691.4.peg.1672

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1097

    Phylogenomic databases

    eggNOGiCOG2050, Bacteria
    HOGENOMiCLU_089876_13_1_6
    InParanoidiP0A8Y8
    KOiK24147
    PhylomeDBiP0A8Y8

    Enzyme and pathway databases

    UniPathwayiUPA00017
    BioCyciEcoCyc:EG11105-MONOMER
    ECOL316407:JW0589-MONOMER
    MetaCyc:EG11105-MONOMER
    BRENDAi3.1.2.2, 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A8Y8

    Protein Ontology

    More...
    PROi
    PR:P0A8Y8

    Family and domain databases

    HAMAPiMF_00907, Thioesterase_EntH, 1 hit
    InterProiView protein in InterPro
    IPR029069, HotDog_dom_sf
    IPR003736, PAAI_dom
    IPR026576, Thioesterase_EntH
    IPR006683, Thioestr_dom
    PfamiView protein in Pfam
    PF03061, 4HBT, 1 hit
    SUPFAMiSSF54637, SSF54637, 1 hit
    TIGRFAMsiTIGR00369, unchar_dom_1, 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 nameiENTH_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: P0A8Y8
    Secondary accession number(s): P15050, Q2MBK4
    <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 21, 2005
    Last sequence update: June 21, 2005
    Last modified: August 12, 2020
    This is version 111 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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