AHLL_BACTU
ID AHLL_BACTU Reviewed; 250 AA.
AC A3FJ64; D3JZ16; Q1WNZ4; Q6JVJ7; Q7B8B9; Q8RPW7; Q8RPW8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=N-acyl homoserine lactonase;
DE Short=AHL-lactonase;
DE EC=3.1.1.81;
DE AltName: Full=Homoserine lactone lactonase;
GN Name=aiiA;
OS Bacillus thuringiensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KCTC 1507;
RA Kim S.-H., Cho Y.-H.;
RT "An AHL-lactonase gene from Bacillus thuringiensis KCTC 1507.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WB12;
RA Huang T., Yao F., Guan X.;
RT "Cloning of novel AHL-lactonase genes from Bacillus cereus group.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Gonzalez A., Correa E., Orduz S.;
RT "Identification of AHL-lactonase from Colombian Bacillus thuringiensis
RT strain.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KACC10171, KACC10175, KACC10180, and KACC10183;
RA Yoon B.S., Nguyen K.T.;
RT "Expression of homoserine lactone lactonase from Bacillus thuringiensis in
RT E. coli.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=15895999; DOI=10.1021/bi050050m;
RA Thomas P.W., Stone E.M., Costello A.L., Tierney D.L., Fast W.;
RT "The quorum-quenching lactonase from Bacillus thuringiensis is a
RT metalloprotein.";
RL Biochemistry 44:7559-7569(2005).
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. {ECO:0000269|PubMed:15895999}.
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:0000269|PubMed:15895999};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15895999};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15895999};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 mM for C6-(S)-HSL {ECO:0000269|PubMed:15895999};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AY300026; AAQ73629.1; -; Genomic_DNA.
DR EMBL; DQ000642; AAY51612.1; -; Genomic_DNA.
DR EMBL; EF379241; ABN51242.1; -; Genomic_DNA.
DR EMBL; GU339169; ADB96947.1; -; Genomic_DNA.
DR EMBL; GU339170; ADB96948.1; -; Genomic_DNA.
DR EMBL; GU339171; ADB96949.1; -; Genomic_DNA.
DR EMBL; GU339172; ADB96950.1; -; Genomic_DNA.
DR RefSeq; WP_000216581.1; NZ_WJDM01000002.1.
DR PDB; 4J5F; X-ray; 1.72 A; A=1-250.
DR PDB; 4J5H; X-ray; 1.45 A; A=1-250.
DR PDB; 5EHT; X-ray; 1.29 A; A=2-250.
DR PDBsum; 4J5F; -.
DR PDBsum; 4J5H; -.
DR PDBsum; 5EHT; -.
DR AlphaFoldDB; A3FJ64; -.
DR SMR; A3FJ64; -.
DR PATRIC; fig|1428.310.peg.4057; -.
DR OrthoDB; 1815576at2; -.
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 GO; GO:1901335; P:lactone catabolic process; IMP:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..250
FT /note="N-acyl homoserine lactonase"
FT /id="PRO_0000403302"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="I -> V (in Ref. 1; AAQ73629 and 3; ABN51242)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="P -> L (in Ref. 4; ADB96950)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="K -> E (in Ref. 4; ADB96950)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> G (in Ref. 1; AAQ73629)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="V -> A (in Ref. 2; AAY51612)"
FT /evidence="ECO:0000305"
FT STRAND 2..17
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5EHT"
FT TURN 61..66
FT /evidence="ECO:0007829|PDB:5EHT"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:5EHT"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:5EHT"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5EHT"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5EHT"
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
