AHLLM_AZOC5
ID AHLLM_AZOC5 Reviewed; 263 AA.
AC A8IQD2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=N-acyl homoserine lactonase AttM {ECO:0000250|UniProtKB:Q8VPD5};
DE Short=AHL-lactonase AttM {ECO:0000250|UniProtKB:Q8VPD5};
DE EC=3.1.1.81;
GN Name=attM {ECO:0000250|UniProtKB:Q8VPD5}; OrderedLocusNames=AZC_0767;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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:Q8VPD5};
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 -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AP009384; BAF86765.1; -; Genomic_DNA.
DR RefSeq; WP_012169298.1; NC_009937.1.
DR AlphaFoldDB; A8IQD2; -.
DR SMR; A8IQD2; -.
DR EnsemblBacteria; BAF86765; BAF86765; AZC_0767.
DR KEGG; azc:AZC_0767; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_030571_3_2_5; -.
DR OMA; HEEEFKH; -.
DR OrthoDB; 1815576at2; -.
DR Proteomes; UP000000270; Chromosome.
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; Plasmid; Reference proteome; Zinc.
FT CHAIN 1..263
FT /note="N-acyl homoserine lactonase AttM"
FT /id="PRO_0000403297"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
SQ SEQUENCE 263 AA; 29317 MW; 67994DAE371A1AC9 CRC64;
MTDIRLYMLQ SGSLKCKVHN IKMNQGNGAD YEIPVPFFLI THPKGHTIID GGNAVEVATD
PRGHWGGVCD VYWPVMREDE GCVAQVKALG IDPADVKYVV QSHLHLDHTG AIGRFPNATH
IVQRREYEYA FTPDWFAGGG YIRKDFDRPG LRWQFLNADV DDYYDIYGDG TLTTVFSPGH
APGHQSFLVR LPKSGPLLLT IDAAYTLDHW NEQALPGFLA STVDTVRSVQ KLRTLAERTG
AQVVTGHDPD AWPSFKKAPG YYD