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Protein

N-acyl homoserine lactonase AiiB

Gene

aiiB

Organism
Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Kineticsi

  1. KM=15 mM for N-butyryl-(RS)-homoserine lactone (with zinc as cofactor)1 Publication
  2. KM=1.6 mM for N-hexanoyl-(S)-homoserine lactone (with zinc as cofactor)1 Publication
  3. KM=4.6 mM for N-(beta-ketocaproyl)-(RS)-homoserine lactone (with zinc as cofactor)1 Publication
  4. KM=1.0 mM for N-octanoyl-(S)-homoserine lactone (with zinc as cofactor)1 Publication
  5. KM=2.5 mM for N-(3-oxo-octanoyl)-(S)-homoserine lactone (with zinc as cofactor)1 Publication
  6. KM=0.11 mM for N-decanoyl-(S)-homoserine lactone (with zinc as cofactor)1 Publication
  7. KM=7.7 mM for N-t-butyloxycarbonyl-(RS)-homoserine lactone (with zinc as cofactor)1 Publication
  8. KM=0.77 mM for N-carbobenzyloxy-(S)-homoserine lactone (with zinc as cofactor)1 Publication
  9. KM=5.9 mM for N-hexanoyl-(S)-homoserine lactone (with cobalt as cofactor)1 Publication
  10. KM=7.3 mM for N-(beta-ketocaproyl)-(RS)-homoserine lactone (with cobalt as cofactor)1 Publication
  11. KM=7.0 mM for N-(3-oxo-octanoyl)-(S)-homoserine lactone (with cobalt as cofactor)1 Publication
  12. KM=1.6 mM for N-carbobenzyloxy-(S)-homoserine lactone (with cobalt as cofactor)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi111 – 1111Zinc 1; via tele nitrogen1 Publication
    Metal bindingi113 – 1131Zinc 1; via pros nitrogen1 Publication
    Metal bindingi116 – 1161Zinc 2; via tele nitrogen1 Publication
    Metal bindingi191 – 1911Zinc 1; via tele nitrogen1 Publication
    Metal bindingi213 – 2131Zinc 11 Publication
    Metal bindingi213 – 2131Zinc 21 Publication
    Metal bindingi259 – 2591Zinc 2; via tele nitrogen1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciAGRO:ATU6071-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acyl homoserine lactonase AiiB1 Publication (EC:3.1.1.81)
    Short name:
    AHL-lactonase AiiB1 Publication
    Gene namesi
    Name:aiiBImported
    Ordered Locus Names:Atu6071
    ORF Names:AGR_pTi_140
    Encoded oniPlasmid pTiC58CuratedImported
    OrganismiAgrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
    Taxonomic identifieri176299 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
    Proteomesi
    • UP000000813 Componenti: Plasmid Ti

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 276276N-acyl homoserine lactonase AiiBPRO_0000405125Add
    BLAST

    Structurei

    Secondary structure

    1
    276
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1613Combined sources
    Helixi17 – 204Combined sources
    Beta strandi29 – 313Combined sources
    Beta strandi38 – 4912Combined sources
    Beta strandi54 – 574Combined sources
    Helixi74 – 796Combined sources
    Helixi90 – 967Combined sources
    Helixi101 – 1033Combined sources
    Beta strandi105 – 1084Combined sources
    Turni114 – 1163Combined sources
    Helixi120 – 1223Combined sources
    Beta strandi124 – 1318Combined sources
    Helixi132 – 14312Combined sources
    Beta strandi148 – 1514Combined sources
    Helixi153 – 1597Combined sources
    Beta strandi166 – 1694Combined sources
    Beta strandi175 – 1795Combined sources
    Beta strandi182 – 20120Combined sources
    Beta strandi203 – 2053Combined sources
    Beta strandi207 – 2126Combined sources
    Helixi218 – 2214Combined sources
    Beta strandi222 – 2243Combined sources
    Helixi234 – 25017Combined sources
    Beta strandi254 – 2596Combined sources
    Helixi261 – 2666Combined sources
    Turni270 – 2723Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R2DX-ray1.75A/B/C/D/E/F1-276[»]
    ProteinModelPortaliA9CKY2.
    SMRiA9CKY2. Positions 1-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA9CKY2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the metallo-beta-lactamase superfamily.Curated

    Phylogenomic databases

    HOGENOMiHOG000094710.
    OrthoDBiEOG6T1WQ8.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Metallo-B-lactamas.
    [Graphical view]
    PfamiPF00753. Lactamase_B. 1 hit.
    [Graphical view]
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A9CKY2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGNKLFVLDL GEIRVDENFI IANSTFVTPQ KPTVSSRLID IPVSAYLIQC
    60 70 80 90 100
    TDATVLYDTG CHPECMGTNG RWPAQSQLNA PYIGASECNL PERLRQLGLS
    110 120 130 140 150
    PDDISTVVLS HLHNDHAGCV EYFGKSRLIA HEDEFATAVR YFATGDHSSP
    160 170 180 190 200
    YIVKDIEAWL ATPRNWDLVG RDERERELAP GVNLLNFGTG HASGMLGLAV
    210 220 230 240 250
    RLEKQPGFLL VSDACYTATN YGPPARRAGV LHDTIGYDRT VSHIRQYAES
    260 270
    RSLTVLFGHD REQFASLIKS TDGFYE
    Length:276
    Mass (Da):30,562
    Last modified:January 15, 2008 - v1
    Checksum:i6AD213ADB02C7DA3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE007871 Genomic DNA. Translation: AAK91031.1.
    PIRiAE3236.
    RefSeqiNP_396590.1. NC_003065.3.
    WP_010974862.1. NC_003065.3.

    Genome annotation databases

    EnsemblBacteriaiAAK91031; AAK91031; Atu6071.
    GeneIDi1137394.
    KEGGiatu:Atu6071.
    PATRICi20820368. VBIAgrTum91616_5278.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE007871 Genomic DNA. Translation: AAK91031.1.
    PIRiAE3236.
    RefSeqiNP_396590.1. NC_003065.3.
    WP_010974862.1. NC_003065.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R2DX-ray1.75A/B/C/D/E/F1-276[»]
    ProteinModelPortaliA9CKY2.
    SMRiA9CKY2. Positions 1-276.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK91031; AAK91031; Atu6071.
    GeneIDi1137394.
    KEGGiatu:Atu6071.
    PATRICi20820368. VBIAgrTum91616_5278.

    Phylogenomic databases

    HOGENOMiHOG000094710.
    OrthoDBiEOG6T1WQ8.

    Enzyme and pathway databases

    BioCyciAGRO:ATU6071-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiA9CKY2.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Metallo-B-lactamas.
    [Graphical view]
    PfamiPF00753. Lactamase_B. 1 hit.
    [Graphical view]
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C58 / ATCC 33970.
    2. "Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens."
      Liu D., Thomas P.W., Momb J., Hoang Q.Q., Petsko G.A., Ringe D., Fast W.
      Biochemistry 46:11789-11799(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiAHLLB_AGRFC
    AccessioniPrimary (citable) accession number: A9CKY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: January 15, 2008
    Last modified: May 11, 2016
    This is version 49 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Plasmid, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.