P0CJ63 · AHLLA_BACTK

Function

function

Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
303 mMGBL (with cobalt as cofactor)
0.8 mMC5-HSL (with cobalt as cofactor)
0.15 mMC10-HSL (with cobalt as cofactor)
3.8 mMBOC-HSL (with cobalt as cofactor)
0.48 mMCBZ-HSL (with cobalt as cofactor)

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site104Zn2+ 1 (UniProtKB | ChEBI)
Binding site106Zn2+ 1 (UniProtKB | ChEBI)
Binding site108Zn2+ 2 (UniProtKB | ChEBI)
Binding site109Zn2+ 2 (UniProtKB | ChEBI)
Binding site169Zn2+ 1 (UniProtKB | ChEBI)
Binding site191Zn2+ 1 (UniProtKB | ChEBI)
Binding site191Zn2+ 2 (UniProtKB | ChEBI)
Binding site235Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionacyl-L-homoserine-lactone lactonohydrolase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    N-acyl homoserine lactonase AiiA
  • EC number
  • Short names
    AHL-lactonase AiiA

Gene names

    • Name
      aiiA

Organism names

Accessions

  • Primary accession
    P0CJ63
  • Secondary accessions
    • Q7B8B9
    • Q8RPW7
    • Q8RPW8

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis104Abolishes activity.
Mutagenesis106Abolishes activity.
Mutagenesis108Abolishes activity.
Mutagenesis108Slow substrate turnover.
Mutagenesis109Reduces activity by 85%.
Mutagenesis169Abolishes activity.
Mutagenesis191Abolishes activity.
Mutagenesis191Abolishes activity.
Mutagenesis194Reduces activity by 70%. Slow substrate turnover.
Mutagenesis206Small decrease in KM value for hydrolysis of GBL, C5-HSL and C10-HSL.
Mutagenesis207Small decrease in KM value for hydrolysis of GBL and C10-HSL. Increase in KM value for hydrolysis of C5-HSL.
Mutagenesis207Small decrease in KM value for hydrolysis of GBL and C5-HSL. Larger decrease in KM value for hydrolysis of C10-HSL.
Mutagenesis235Reduces activity by 85%.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003999911-250N-acyl homoserine lactonase AiiA

Interaction

Subunit

Monomer.

Family & Domains

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    250
  • Mass (Da)
    28,220
  • Last updated
    2011-01-11 v1
  • Checksum
    CEBC2FE957707C2E
MTVKKLYFIPAGRCMLDHSSVNSALTPGKLLNLPVWCYLLETEEGPILVDTGMPESAVNNEGLFNGTFVEGQILPKMTEEDRIVNILKRVGYEPDDLLYIISSHLHFDHAGGNGAFTNTPIIVQRTEYEAALHREEYMKECILPHLNYKIIEGDYEVVPGVQLLYTPGHSPGHQSLFIETEQSGSVLLTIDASYTKENFEDEVPFAGFDPELALSSIKRLKEVVKKEKPIIFFGHDIEQEKSCRVFPEYI

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict189in Ref. 1; AAL98717
Sequence conflict237in Ref. 1; AAL98717

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF350928
EMBL· GenBank· DDBJ
AAL98717.1
EMBL· GenBank· DDBJ
Genomic DNA
AF350929
EMBL· GenBank· DDBJ
AAL98718.1
EMBL· GenBank· DDBJ
Genomic DNA
AF478059
EMBL· GenBank· DDBJ
AAM92140.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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