ID Q9S4I2_ECOLX Unreviewed; 212 AA.
AC Q9S4I2;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 03-MAY-2023, entry version 63.
DE RecName: Full=Alkylmercury lyase {ECO:0000256|ARBA:ARBA00018180, ECO:0000256|HAMAP-Rule:MF_00714};
DE EC=4.99.1.2 {ECO:0000256|ARBA:ARBA00013237, ECO:0000256|HAMAP-Rule:MF_00714};
DE AltName: Full=Organomercurial lyase {ECO:0000256|ARBA:ARBA00031271, ECO:0000256|HAMAP-Rule:MF_00714};
GN Name=merB {ECO:0000256|HAMAP-Rule:MF_00714,
GN ECO:0000313|EMBL:AAD46510.1};
OS Escherichia coli.
OG Plasmid pIAAD-2 {ECO:0000313|EMBL:AAD46510.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAD46510.1};
RN [1] {ECO:0000313|EMBL:AAD46510.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pIAAD-2 {ECO:0000313|EMBL:AAD46510.1};
RX PubMed=16211434; DOI=10.1007/s00284-005-0013-2;
RA Murtaza I., Dutt A., Mushtaq D., Ali A.;
RT "Molecular cloning and genetic analysis of functional merB gene from indian
RT isolates of Escherichia coli.";
RL Curr. Microbiol. 51:297-302(2005).
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 ECO:0000256|HAMAP-Rule:MF_00714}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00714};
CC -!- SIMILARITY: Belongs to the MerB family. {ECO:0000256|ARBA:ARBA00009443,
CC ECO:0000256|HAMAP-Rule:MF_00714}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF144395; AAD46510.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S4I2; -.
DR BRENDA; 4.99.1.2; 2026.
DR GO; GO:0018836; F:alkylmercury lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046413; P:organomercury catabolic process; IEA:InterPro.
DR GO; GO:0046689; P:response to mercury ion; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.450.410; -; 1.
DR HAMAP; MF_00714; MerB; 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:0000256|HAMAP-Rule:MF_00714};
KW Mercuric resistance {ECO:0000256|ARBA:ARBA00022466, ECO:0000256|HAMAP-
KW Rule:MF_00714};
KW Mercury {ECO:0000256|ARBA:ARBA00022914, ECO:0000256|HAMAP-Rule:MF_00714};
KW Plasmid {ECO:0000313|EMBL:AAD46510.1}.
FT DOMAIN 15..75
FT /note="Alkylmercury lyase helix-turn-helix"
FT /evidence="ECO:0000259|Pfam:PF12324"
SQ SEQUENCE 212 AA; 23090 MW; AD505063985766CC CRC64;
MKLAPYILER PTSVNRTNGT ADLLVPLLRE LAKGRPVSRT TLAGILDWPA ERVAAVLEQA
TSTEYDKDGN IIGYGLTLRE TSYVFEIDDR RLYAWCALDT LIFPALIGRT ARVSSHCAAT
GAPVSLTVSP SEIQAVEPAG MAVSLVLPQE AADVRQSFCC HVHFFASVPT AEDWASKHQG
LEGLAIVSVH EAFGLGQEFN RHLLRTMSSR TP
//
