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AHLLM_RHIL3
ID   AHLLM_RHIL3             Reviewed;         263 AA.
AC   Q1M813;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=pRL100136;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OG   Plasmid pRL10 {ECO:0000312|EMBL:CAK10359.1}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AM236084; CAK10359.1; -; Genomic_DNA.
DR   RefSeq; WP_011654183.1; NC_008381.1.
DR   AlphaFoldDB; Q1M813; -.
DR   SMR; Q1M813; -.
DR   EnsemblBacteria; CAK10359; CAK10359; pRL100136.
DR   KEGG; rle:pRL100136; -.
DR   HOGENOM; CLU_030571_3_2_5; -.
DR   OMA; HEEEFKH; -.
DR   Proteomes; UP000006575; Plasmid pRL10.
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; Zinc.
FT   CHAIN           1..263
FT                   /note="N-acyl homoserine lactonase AttM"
FT                   /id="PRO_0000403304"
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;  29363 MW;  C6E4B402C5E6C726 CRC64;
     MTDIRLYMLQ SGTLKCKVHN IKMNQGNGAD YEIPVPFYLI THPDGHTIID GGNAIEVATD
     PRGHWGGICD VYWPVLDKDK GCVDQVKALG FDPAEVRYVV QSHLHLDHTG AIGRFPNATH
     IVQRAEYEYA FTPDWFAGGG YIRKDFDRPG LKWQFLNGTQ DDFYDVYGDG TLTTIFSPGH
     AMGHQSFLVR LPSSEPLLLT IDAAYTLDHW EEKALPGFLA STVDTVRSVQ KLRTIAERTG
     ANVVTGHDPA AWSTFKKAPE YYS
 
 
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