ID G7ENJ8_9GAMM Unreviewed; 211 AA.
AC G7ENJ8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 Name=merB {ECO:0000313|EMBL:GAA62471.1};
GN ORFNames=P20311_0244 {ECO:0000313|EMBL:GAA62471.1};
OS Pseudoalteromonas sp. BSi20311.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=383911 {ECO:0000313|EMBL:GAA62471.1, ECO:0000313|Proteomes:UP000005146};
RN [1] {ECO:0000313|Proteomes:UP000005146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSi20311 {ECO:0000313|Proteomes:UP000005146};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA62471.1}.
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DR EMBL; BADU01000009; GAA62471.1; -; Genomic_DNA.
DR AlphaFoldDB; G7ENJ8; -.
DR Proteomes; UP000005146; Unassembled WGS sequence.
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:GAA62471.1};
KW Mercuric resistance {ECO:0000256|ARBA:ARBA00022466};
KW Mercury {ECO:0000256|ARBA:ARBA00022914}.
FT DOMAIN 12..80
FT /note="Alkylmercury lyase helix-turn-helix"
FT /evidence="ECO:0000259|Pfam:PF12324"
SQ SEQUENCE 211 AA; 23246 MW; 84B7F70B76D74A97 CRC64;
MKISMKHTRY ITKIAESLTP ANQPQGFGEL FVVLLRELAK GRPVSRTTLA KSLDWPAQQV
NAVLERTTST EYDSDGNIVG YVLTLRETSH IFEIDGRRLY AWCALDTLML PALIGQTARV
TSHCAATGAP VSLTVSPNEI RDIAPTDAAV SLVLPQETAD IRRSFCCHVH FFASAVTAKD
WASKHEGVEI VSVQDGFRLG QELNRHLLQT A
//