AHLLM_RHIRD
ID AHLLM_RHIRD Reviewed; 263 AA.
AC Q8VPD5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=N-acyl homoserine lactonase AttM {ECO:0000303|PubMed:11930013};
DE Short=AHL-lactonase AttM {ECO:0000303|PubMed:11930013};
DE EC=3.1.1.81;
GN Name=attM;
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL13075.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=A6 {ECO:0000312|EMBL:AAL13075.1};
RX PubMed=11930013; DOI=10.1073/pnas.022056699;
RA Zhang H.B., Wang L.H., Zhang L.H.;
RT "Genetic control of quorum-sensing signal turnover in Agrobacterium
RT tumefaciens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4638-4643(2002).
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:11930013};
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 -!- DEVELOPMENTAL STAGE: Expression increases in the stationary phase of
CC growth. {ECO:0000269|PubMed:11930013}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; AY052389; AAL13075.1; -; Genomic_DNA.
DR RefSeq; WP_038496768.1; NZ_JAANRY010000036.1.
DR AlphaFoldDB; Q8VPD5; -.
DR SMR; Q8VPD5; -.
DR PATRIC; fig|358.67.peg.5041; -.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Plasmid; Zinc.
FT CHAIN 1..263
FT /note="N-acyl homoserine lactonase AttM"
FT /id="PRO_0000403305"
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; 29335 MW; D9C926FD25FF2FC8 CRC64;
MTDIRLYMLQ SGTLKCKVHN IKMNQGNGAD YEIPVPFFLI THPGGHTVID GGNAIEVATD
PRGHWGGICD VYWPVLDKDQ GCVDQIKALG FDPADVKYVV QSHLHLDHTG AIGRFPNATH
IVQRSEYEYA FTPDWFAGGG YIRKDFDKPG LKWQFLNGTQ DDYYDVYGDG TLTTIFTPGH
APGHQSLLVR LPNSKPLLLT IDAAYTLDHW EEKALPGFLA STVDTVRSVQ KLRTYAEKHD
ATVVTGHDPD AWANFKKAPE FYA
