ID   AHLL_BACT3              Reviewed;         250 AA.
AC   Q7B8C3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=N-acyl homoserine lactonase {ECO:0000250|UniProtKB:Q7B8B9};
DE            Short=AHL-lactonase {ECO:0000250|UniProtKB:Q7B8B9};
DE            EC=3.1.1.81;
GN   Name=aiiA {ECO:0000312|EMBL:AAM92131.1};
OS   Bacillus thuringiensis subsp. indiana.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180850;
RN   [1] {ECO:0000312|EMBL:AAM92131.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HD-521 {ECO:0000312|EMBL:AAM92131.1};
RX   PubMed=12147491; DOI=10.1128/aem.68.8.3919-3924.2002;
RA   Lee S.J., Park S.Y., Lee J.J., Yum D.Y., Koo B.T., Lee J.K.;
RT   "Genes encoding the N-acyl homoserine lactone-degrading enzyme are
RT   widespread in many subspecies of Bacillus thuringiensis.";
RL   Appl. Environ. Microbiol. 68:3919-3924(2002).
CC   -!- FUNCTION: Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone,
CC       but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl
CC       homoserine lactones with or without 3-oxo substitution at C3, has
CC       maximum activity on C10-AHL (By similarity).
CC       {ECO:0000250|UniProtKB:Q7B8B9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
CC         + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81;
CC         Evidence={ECO:0000250|UniProtKB:Q7B8B9};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q7B8B9};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q7B8B9};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q7B8B9}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF478050; AAM92131.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7B8C3; -.
DR   SMR; Q7B8C3; -.
DR   BRENDA; 3.1.1.81; 711.
DR   GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..250
FT                   /note="N-acyl homoserine lactonase"
FT                   /id="PRO_0000403300"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7B8B9"
SQ   SEQUENCE   250 AA;  28220 MW;  CEBC2FE957707C2E CRC64;
     MTVKKLYFIP AGRCMLDHSS VNSALTPGKL LNLPVWCYLL ETEEGPILVD TGMPESAVNN
     EGLFNGTFVE GQILPKMTEE DRIVNILKRV GYEPDDLLYI ISSHLHFDHA GGNGAFTNTP
     IIVQRTEYEA ALHREEYMKE CILPHLNYKI IEGDYEVVPG VQLLYTPGHS PGHQSLFIET
     EQSGSVLLTI DASYTKENFE DEVPFAGFDP ELALSSIKRL KEVVKKEKPI IFFGHDIEQE
     KSCRVFPEYI