ID F5BQA4_SALDU Unreviewed; 168 AA.
AC F5BQA4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=Alkylmercury lyase {ECO:0000256|ARBA:ARBA00018180};
DE EC=4.99.1.2 {ECO:0000256|ARBA:ARBA00013237};
DE AltName: Full=Organomercurial lyase {ECO:0000256|ARBA:ARBA00031271};
GN ORFNames=pSD853_88_70 {ECO:0000313|EMBL:AEA95534.1};
OS Salmonella dublin.
OG Plasmid pSD_88 {ECO:0000313|EMBL:AEA95534.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=98360 {ECO:0000313|EMBL:AEA95534.1};
RN [1] {ECO:0000313|EMBL:AEA95534.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=853 {ECO:0000313|EMBL:AEA95534.1};
RC PLASMID=pSD_88 {ECO:0000313|EMBL:AEA95534.1};
RA Han J., Lynne A.M., David D.E., Nayak R., Foley S.L.;
RT "Sequencing of plasmids from a multi-antimicrobial resistant Salmonella
RT enterica serovar Dublin strain.";
RL Food Res. Intern. 45:931-934(2012).
CC -!- FUNCTION: Cleaves the carbon-mercury bond of organomercurials such as
CC phenylmercuric acetate. One product is Hg(2+), which is subsequently
CC detoxified by the mercuric reductase. {ECO:0000256|ARBA:ARBA00025326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alkylmercury + H(+) = an alkane + Hg(2+);
CC Xref=Rhea:RHEA:18777, ChEBI:CHEBI:15378, ChEBI:CHEBI:16793,
CC ChEBI:CHEBI:18310, ChEBI:CHEBI:83725; EC=4.99.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000165};
CC -!- SIMILARITY: Belongs to the MerB family.
CC {ECO:0000256|ARBA:ARBA00009443}.
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DR EMBL; JF267652; AEA95534.1; -; Genomic_DNA.
DR RefSeq; YP_006954830.1; NC_019105.1.
DR AlphaFoldDB; F5BQA4; -.
DR GO; GO:0018836; F:alkylmercury lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046413; P:organomercury catabolic process; IEA:InterPro.
DR GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-KW.
DR Gene3D; 3.30.450.410; -; 1.
DR InterPro; IPR004927; MerB.
DR InterPro; IPR024259; MerB_HTH_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF12324; HTH_15; 1.
DR Pfam; PF03243; MerB; 1.
DR PIRSF; PIRSF001458; MerB; 1.
DR PRINTS; PR01699; ORGNOHGLYASE.
DR SUPFAM; SSF160387; NosL/MerB-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AEA95534.1};
KW Mercuric resistance {ECO:0000256|ARBA:ARBA00022466};
KW Mercury {ECO:0000256|ARBA:ARBA00022914};
KW Plasmid {ECO:0000313|EMBL:AEA95534.1}.
FT DOMAIN 8..75
FT /note="Alkylmercury lyase helix-turn-helix"
FT /evidence="ECO:0000259|Pfam:PF12324"
SQ SEQUENCE 168 AA; 18180 MW; D99449C4D0025471 CRC64;
MKLAPYILER LTSVNRTNGT ADLLVPLLRE LAKGRPVSRT TLAGILDWPA ERVAAVLEQA
TSTEYDKDGN IIGYGLTLRE TSYVFEIDDR RLYAWCALDT LIFPALIGRT ARVSSHCAAT
GAPVSLTVSP SEIQAVEPAG MAVSLVLPQE AADVRQSFCS GTVANSRW
//
