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Entry version 99 (08 May 2019)
Sequence version 1 (01 Feb 1991)
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Protein

2-aminobenzoylacetyl-CoA thioesterase

Gene

pqsE

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score:

Annotation score:4 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 the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. Catalyzes the hydrolysis of the intermediate 2-aminobenzoylacetyl-CoA (2-ABA-CoA) to form 2-aminobenzoylacetate (2-ABA), the precursor of HHQ. In vitro, can also hydrolyze other substrates such as S-ethyl-acetothioacetate and acetoacetyl-CoA, but is inactive against anthraniloyl-CoA, malonyl-CoA and octanoyl-CoA (PubMed:25960261, PubMed:27082157). Beyond its thioesterase function, is involved in the regulation of diverse genes coding for key virulence determinants and biofilm development (PubMed:27851827).3 Publications

Miscellaneous

As mutant can produce wild-type levels of PQS, it was originally thought that PqsE is not involved in HHQ/PQS biosynthesis (PubMed:12426334, PubMed:18776012). It was shown later that the role of PqsE can be taken over to some extent by the broad-specificity thioesterase TesB, explaining why the pqsE deletion mutant still synthesizes HHQ and PQS (PubMed:25960261).2 Publications1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 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

Thioesterase activity, but not pyocyanine production, is inhibited by 2-(pyridin-3-yl)benzoic acid, 2-(1H-pyrrol-1-yl)benzoic acid and 3-methylthiophene-2-carboxylic acid. Compounds bind to the active center.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

kcat is 0.85 sec(-1) with S-ethyl-acetothioacetate as substrate. kcat is 0.36 sec(-1) with acetoacetyl-CoA as substrate. kcat is 0.022 sec(-1) with cysteamine-S-phosphate as substrate (PubMed:25960261). kcat is 7.2 min(-1) with S-(4-nitrobenzoyl)mercaptoethane as substrate (PubMed:19788310).2 Publications
  1. KM=4.4 mM for S-ethyl-acetothioacetate1 Publication
  2. KM=2.5 mM for acetoacetyl-CoA1 Publication
  3. KM=0.8 mM for cysteamine-S-phosphate1 Publication
  4. KM=14 µM for S-(4-nitrobenzoyl)mercaptoethane1 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 bindingi69Iron 1; via tele nitrogen3 Publications1
    Metal bindingi71Iron 1; via pros nitrogen3 Publications1
    Metal bindingi73Iron 23 Publications1
    Metal bindingi74Iron 2; via tele nitrogen3 Publications1
    Metal bindingi159Iron 1; via tele nitrogen3 Publications1
    Metal bindingi178Iron 13 Publications1
    Metal bindingi178Iron 23 Publications1
    Metal bindingi221Iron 2; via tele nitrogen3 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

    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
    LigandIron, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-19871
    PAER208964:G1FZ6-1019-MONOMER

    <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:
    2-aminobenzoylacetyl-CoA thioesteraseCurated (EC:3.1.2.322 Publications)
    <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:pqsE1 Publication
    Ordered Locus Names:PA1000
    <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>OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    <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 identifieri208964 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    <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
    • UP000002438 <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

    Organism-specific databases

    Pseudomonas genome database

    More...
    PseudoCAPi
    PA1000

    <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

    Mutant is defective in pyocyanine and rhamnolipid production and fails to kill worms efficiently, but can still produce PQS (PubMed:12426334, PubMed:18776012). Deletion mutant produces increased levels of DHQ, resulting from intramolecular cyclization of 2-ABA-CoA (PubMed:25960261).3 Publications

    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>Mutagenesisi182E → A: Strong decrease in kcat with S-(4-nitrobenzoyl)mercaptoethane as substrate. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB07418 bis(4-nitrophenyl) hydrogen phosphate

    <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_00002062491 – 3012-aminobenzoylacetyl-CoA thioesteraseAdd BLAST301

    Proteomic databases

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

    More...
    PaxDbi
    P20581

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P20581

    <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

    1301
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    2Q0IX-ray1.57A1-301[»]
    2Q0JX-ray2.10A/B1-301[»]
    2VW8X-ray1.45A1-301[»]
    3DH8X-ray1.80A1-301[»]
    5HIOX-ray1.90A1-301[»]
    5HIPX-ray1.99A1-301[»]
    5HIQX-ray2.10A1-301[»]
    5HISX-ray1.77A1-301[»]

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

    More...
    SMRi
    P20581

    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
    P20581

    <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

    <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 metallo-beta-lactamase superfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105R2E Bacteria
    ENOG4111ZI3 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000247670

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P20581

    KEGG Orthology (KO)

    More...
    KOi
    K20257

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    MQIRTIA

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.60.15.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001279 Metallo-B-lactamas
    IPR036866 RibonucZ/Hydroxyglut_hydro

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00753 Lactamase_B, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00849 Lactamase_B, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56281 SSF56281, 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.

    P20581-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLRLSAPGQL DDDLCLLGDV QVPVFLLRLG EASWALVEGG ISRDAELVWA
    60 70 80 90 100
    DLCRWVADPS QVHYWLITHK HYDHCGLLPY LCPRLPNVQV LASERTCQAW
    110 120 130 140 150
    KSESAVRVVE RLNRQLLRAE QRLPEACAWD ALPVRAVADG EWLELGPRHR
    160 170 180 190 200
    LQVIEAHGHS DDHVVFYDVR RRRLFCGDAL GEFDEAEGVW RPLVFDDMEA
    210 220 230 240 250
    YLESLERLQR LPTLLQLIPG HGGLLRGRLA ADGAESAYTE CLRLCRRLLW
    260 270 280 290 300
    RQSMGESLDE LSEELHRAWG GQSVDFLPGE LHLGSMRRML EILSRQALPL

    D
    Length:301
    Mass (Da):34,306
    Last modified:February 1, 1991 - 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:iCB78E9103D8F221C
    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
    M33810 Genomic DNA Translation: AAA88447.1
    AE004091 Genomic DNA Translation: AAG04389.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    C35116

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_249691.1, NC_002516.2
    WP_003086247.1, NZ_QZGE01000006.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAG04389; AAG04389; PA1000

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    880721

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    pae:PA1000

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|208964.12.peg.1032

    <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
    M33810 Genomic DNA Translation: AAA88447.1
    AE004091 Genomic DNA Translation: AAG04389.1
    PIRiC35116
    RefSeqiNP_249691.1, NC_002516.2
    WP_003086247.1, NZ_QZGE01000006.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2Q0IX-ray1.57A1-301[»]
    2Q0JX-ray2.10A/B1-301[»]
    2VW8X-ray1.45A1-301[»]
    3DH8X-ray1.80A1-301[»]
    5HIOX-ray1.90A1-301[»]
    5HIPX-ray1.99A1-301[»]
    5HIQX-ray2.10A1-301[»]
    5HISX-ray1.77A1-301[»]
    SMRiP20581
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    DrugBankiDB07418 bis(4-nitrophenyl) hydrogen phosphate

    Proteomic databases

    PaxDbiP20581
    PRIDEiP20581

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG04389; AAG04389; PA1000
    GeneIDi880721
    KEGGipae:PA1000
    PATRICifig|208964.12.peg.1032

    Organism-specific databases

    PseudoCAPiPA1000

    Phylogenomic databases

    eggNOGiENOG4105R2E Bacteria
    ENOG4111ZI3 LUCA
    HOGENOMiHOG000247670
    InParanoidiP20581
    KOiK20257
    OMAiMQIRTIA

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-19871
    PAER208964:G1FZ6-1019-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP20581

    Family and domain databases

    Gene3Di3.60.15.10, 1 hit
    InterProiView protein in InterPro
    IPR001279 Metallo-B-lactamas
    IPR036866 RibonucZ/Hydroxyglut_hydro
    PfamiView protein in Pfam
    PF00753 Lactamase_B, 1 hit
    SMARTiView protein in SMART
    SM00849 Lactamase_B, 1 hit
    SUPFAMiSSF56281 SSF56281, 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 nameiPQSE_PSEAE
    <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: P20581
    <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, 1991
    Last sequence update: February 1, 1991
    Last modified: May 8, 2019
    This is version 99 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, 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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