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Entry version 50 (18 Sep 2019)
Sequence version 1 (01 Oct 2000)
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Protein

N-acyl homoserine lactonase

Gene

aiiA

Organism
Bacillus sp.
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

Hydrolyzes acyl homoserine lactones with varying lengths of acyl chains, with a slight preference for substrates without 3-oxo substitution at the C3 position. Has only residual activity towards non-acyl lactones, and no activity towards non-cyclic esters.1 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 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+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

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

Completely inhibited by Cu2+ and Ag+. Partially inhibited by Cr2+, Pb2+ and Fe2+. Mg2+, Ca2+, Mn2+, Co2+, Ni2+, Zn2+ and Cd2+ have no effect on activity. The chelating agents EDTA, 2,2'bipyridine and o-phenanthroline have no effect on 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=4.07 mM for 3-oxo-C4-HSL1 Publication
  2. KM=2.95 mM for 3-oxo-C6-HSL1 Publication
  3. KM=2.28 mM for 3-oxo-C8-HSL1 Publication
  4. KM=1.43 mM for 3-oxo-C10-HSL1 Publication
  5. KM=5.11 mM for C4-HSL1 Publication
  6. KM=3.83 mM for C6-HSL1 Publication
  7. KM=2.61 mM for C8-HSL1 Publication
  8. KM=7.51 mM for 3-HO-C4-HSL1 Publication

    pH dependencei

    Optimum pH is 8.0 with 3-oxo-C8-HSL as substrate. Activity increases with increase in pH from 6.0 to 8.0, and declines slightly at pH 9.0. Little or no activity at pH 5.0 or below.1 Publication

    Temperature dependencei

    Stable below 37 degrees Celsius, activity decreases sharply after incubation for 2 hours at 45 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi104Zinc 1By similarity1
    Metal bindingi106Zinc 1By similarity1
    Metal bindingi108Zinc 2By similarity1
    Metal bindingi109Zinc 2By similarity1
    Metal bindingi169Zinc 1By similarity1
    Metal bindingi191Zinc 1By similarity1
    Metal bindingi191Zinc 2By similarity1
    Metal bindingi235Zinc 2By similarity1

    <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
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-14588

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.1.81 691

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9L8R8

    <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:
    N-acyl homoserine lactonaseBy similarity (EC:3.1.1.81)
    Short name:
    AHL-lactonase2 Publications
    Short name:
    Acyl-homoserine lactonase1 Publication
    <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:aiiAImported
    <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>OrganismiBacillus sp.
    <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 identifieri1409 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    <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_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>Mutagenesisi104H → L: Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 38.6%; when associated with L-106 and L-108. Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 62.1%; when associated with L-106, L-108 and L-109. 1 Publication1
    Mutagenesisi104H → S: No effect on activity on N-beta-oxooctanoyl-L-homoserine lactone. Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 48.9%; when associated with S-106. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-106 and S-109. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-106, S-108 and S-109. 1 Publication1
    Mutagenesisi106H → L: Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 38.6%; when associated with L-104 and L-108. Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 62.1%; when associated with L-104, L-108 and L-109. 2 Publications1
    Mutagenesisi106H → S: Results in a conformational change. Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 38.6%. Reduces activity on acyl homoserine lactone by 47% and decreases enzyme affinity. Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 48.9%; when associated with S-104. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-104 and S-109. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-104, S-108 and S-109. 2 Publications1
    Mutagenesisi108D → E: Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 9.2%. 2 Publications1
    Mutagenesisi108D → L: Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 38.6%; when associated with L-104 and L-106. Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 62.1%; when associated with L-104, L-106 and L-109. 2 Publications1
    Mutagenesisi108D → S: Results in a conformational change. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone and acyl homoserine lactone. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-109. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-104, S-106 and S-109. 2 Publications1
    Mutagenesisi109H → L: Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 62.1%; when associated with L-104, L-106 and L-108. 2 Publications1
    Mutagenesisi109H → S: Results in a conformational change. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone and acyl homoserine lactone. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-108. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-104 and S-106. Abolishes activity on N-beta-oxooctanoyl-L-homoserine lactone; when associated with S-104, S-106 and S-108. 2 Publications1
    Mutagenesisi169H → S: Results in a conformational change. Reduces activity on N-beta-oxooctanoyl-L-homoserine lactone by 38.6%. Reduces activity on acyl homoserine lactone by 47% and decreases enzyme affinity. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004032991 – 250N-acyl homoserine lactonaseAdd BLAST250

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9L8R8

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    By similarity

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

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

    More...
    SMRi
    Q9L8R8

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <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

    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>. 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_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.

    Q9L8R8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTVKKLYFVP AGRCMLDHSS VNSTLTPGEL LDLPVWCYLL ETEEGPILVD
    60 70 80 90 100
    TGMPESAVNN EGLFNGTFVE GQVLPKMTEE DRIVNILKRV GYEPEDLLYI
    110 120 130 140 150
    ISSHLHFDHA GGNGAFINTP IIVQRAEYEA AQHSEEYLKE CILPNLNYKI
    160 170 180 190 200
    IEGDYEVVPG VQLLHTPGHT PGHQSLLIET EKSGPVLLTI DASYTKENFE
    210 220 230 240 250
    NEVPFAGFDS ELALSSIKRL KEVVMKEKPI VFFGHDIEQE RGCKVFPEYI
    Length:250
    Mass (Da):28,037
    Last modified:October 1, 2000 - 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:i6E5D32E1E8818272
    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
    AF196486 Genomic DNA Translation: AAF62398.1

    <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
    AF196486 Genomic DNA Translation: AAF62398.1

    3D structure databases

    SMRiQ9L8R8
    ModBaseiSearch...

    Proteomic databases

    PRIDEiQ9L8R8

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14588
    BRENDAi3.1.1.81 691
    SABIO-RKiQ9L8R8

    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...

    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 nameiAHLL_BACSP
    <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: Q9L8R8
    <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: January 11, 2011
    Last sequence update: October 1, 2000
    Last modified: September 18, 2019
    This is version 50 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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