ID B1N7B5_9NOCA Unreviewed; 323 AA.
AC B1N7B5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 28-JUN-2023, entry version 24.
DE SubName: Full=QsdA {ECO:0000313|EMBL:ABQ42704.1};
GN Name=qsdA {ECO:0000313|EMBL:ABQ42704.1};
OS Rhodococcus sp. MP50.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=441624 {ECO:0000313|EMBL:ABQ42704.1};
RN [1] {ECO:0000313|EMBL:ABQ42704.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP50 {ECO:0000313|EMBL:ABQ42704.1};
RX PubMed=18192419; DOI=10.1128/AEM.02014-07;
RA Uroz S., Oger P.M., Chapelle E., Adeline M.T., Faure D., Dessaux Y.;
RT "A Rhodococcus qsdA-encoded enzyme defines a novel class of large-spectrum
RT quorum-quenching lactonases.";
RL Appl. Environ. Microbiol. 74:1357-1366(2008).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR601559-51};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR601559-51};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000256|PROSITE-ProRule:PRU00679}.
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DR EMBL; EF218066; ABQ42704.1; -; Genomic_DNA.
DR AlphaFoldDB; B1N7B5; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PHOSPHOTRIESTERASE-RELATED; 1.
DR PANTHER; PTHR10819:SF3; PHOSPHOTRIESTERASE-RELATED PROTEIN; 1.
DR Pfam; PF02126; PTE; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601559-51}.
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT MOD_RES 147
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-50,
FT ECO:0000256|PROSITE-ProRule:PRU00679"
SQ SEQUENCE 323 AA; 35592 MW; D43C72831E504165 CRC64;
MSSVQTVRGP VDTADLGKVL MHEHVFVLGE ELRQNYPDYP EPWDEEVRVA DAVAKLTEVK
SRGISTIVDP TVIGLGRYIP RIVRINEQVD LNIIVATGIY TYNDIPFQFH YTGPGLLFDG
PEPMVELFVK DIREGIAGTG VRASFLKCAI EEPGLTPGVE RVMRAVGQSQ VETGVPITVH
TNPHTESGLV AQKVLAEEGA DLTKVVIGHS GDTTDLDYLC ALADAGSLLG MDRFGLEPFL
SFEDRVNTVV EMARRGYAEK MVLAHDASCF IDYFPSAARE AALPNWNYTH ISDDVIPALL
ERGVTEDQVK AMLVDNPRRY FES
//
