AHLLM_AGRFC
ID AHLLM_AGRFC Reviewed; 263 AA.
AC Q7D3U0; Q9WWD3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 76.
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:0000312|EMBL:AAD43990.1};
GN Synonyms=blcC {ECO:0000312|EMBL:AAK90512.2}; OrderedLocusNames=Atu5139;
GN ORFNames=AGR_pAT_200;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OG Plasmid AT.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1] {ECO:0000312|EMBL:AAD43990.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10786639; DOI=10.1016/s0167-4781(99)00250-x;
RA Matthysse A.G., Yarnall H., Boles S.B., McMahan S.;
RT "A region of the Agrobacterium tumefaciens chromosome containing genes
RT required for virulence and attachment to host cells.";
RL Biochim. Biophys. Acta 1490:208-212(2000).
RN [2] {ECO:0000312|EMBL:AAK90512.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43990.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK90512.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U59485; AAD43990.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE007872; AAK90512.2; ALT_INIT; Genomic_DNA.
DR PIR; AG3176; AG3176.
DR RefSeq; NP_396071.2; NC_003064.2.
DR RefSeq; WP_019565706.1; NC_003064.2.
DR AlphaFoldDB; Q7D3U0; -.
DR SMR; Q7D3U0; -.
DR STRING; 176299.Atu5139; -.
DR EnsemblBacteria; AAK90512; AAK90512; Atu5139.
DR KEGG; atu:Atu5139; -.
DR PATRIC; fig|176299.10.peg.4827; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_030571_3_2_5; -.
DR Proteomes; UP000000813; Plasmid At.
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_0000403295"
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; 29353 MW; 7090C2A4EEAFC511 CRC64;
MTDIRLYMLQ SGTLKCKVHN IKMNQGNGAD YEIPVPFFLI THPAGHTVID GGNAIEVATD
PRGHWGGICD VYWPVLDKDQ GCVDQIKALG FDPADVKYVV QSHLHLDHTG AIGRFPNATH
IVQRSEYEYA FTPDWFAGGG YIRKDFDKPG LKWQFLNGAQ DDYYDVYGDG TLTTIFTPGH
APGHQSFLVR LPNSKPLLLT IDAAYTLDHW EEKALPGFLA STVDTVRSVQ KLRTYAEKHD
ATVVTGHDPD AWANFKKAPE FYA
