AHLL_ARTSP
ID AHLL_ARTSP Reviewed; 273 AA.
AC Q7X3T2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=N-acyl homoserine lactonase {ECO:0000303|PubMed:12777494};
DE Short=AHL-lactonase {ECO:0000303|PubMed:12777494};
DE EC=3.1.1.81;
GN Name=ahlD {ECO:0000312|EMBL:AAP57766.1};
OS Arthrobacter sp.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1667;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP57766.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=IBN110 {ECO:0000312|EMBL:AAP57766.1};
RX PubMed=12777494; DOI=10.1099/mic.0.26269-0;
RA Park S.Y., Lee S.J., Oh T.K., Oh J.W., Koo B.T., Yum D.Y., Lee J.K.;
RT "AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted
RT homologues in other bacteria.";
RL Microbiology 149:1541-1550(2003).
CC -!- FUNCTION: Hydrolyzes the acyl homoserine lactones N-hexanoyl-L-
CC homoserine lactone, N-3-oxohexanoyl-L-homoserine lactone, N-octonoyl-L-
CC homoserine lactone, N-decanoyl-L-homoserine lactone and N-3-
CC oxododecanoyl-L-homoserine lactone. {ECO:0000269|PubMed:12777494}.
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:12777494};
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; AF525800; AAP57766.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7X3T2; -.
DR SMR; Q7X3T2; -.
DR KEGG; ag:AAP57766; -.
DR BRENDA; 3.1.1.81; 457.
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 Direct protein sequencing; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..273
FT /note="N-acyl homoserine lactonase"
FT /id="PRO_0000403296"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7B8B9"
SQ SEQUENCE 273 AA; 30663 MW; F526C32070547C73 CRC64;
MEKDQLKVRV LETGVMEADM AWLLLKPGRI IADRNNKERQ REWGEIPTHA VLIEHPEGRI
LWDTGVPRDW SSRWQESGMD NYFPVKTESS SESGFLDSSL AQVGLEPADI DLLILSHLHL
DHAGNARLFD NGKTKIVANR KELEGVQEIM GSHLGGHLKA DFEGLKIDAI EGDTEIVPGV
SVIDTPGHTW GTMSLQVDLP DDGTKIFTSD AVYLRDSFGP PAIGAAVVWN NLLWLESVEK
LRRIQERTNA EMIFGHESEQ TSQIRWAHQG HYQ
