ID L7KT22_9ACTN Unreviewed; 452 AA.
AC L7KT22;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 05-FEB-2025, entry version 32.
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=GOACH_45_00030 {ECO:0000313|EMBL:GAC51102.1};
OS Gordonia aichiensis NBRC 108223.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Gordoniaceae; Gordonia.
OX NCBI_TaxID=1220583 {ECO:0000313|EMBL:GAC51102.1, ECO:0000313|Proteomes:UP000010988};
RN [1] {ECO:0000313|EMBL:GAC51102.1, ECO:0000313|Proteomes:UP000010988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108223 {ECO:0000313|EMBL:GAC51102.1,
RC ECO:0000313|Proteomes:UP000010988};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia aichiensis NBRC 108223.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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:GAC51102.1}.
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DR EMBL; BANR01000045; GAC51102.1; -; Genomic_DNA.
DR AlphaFoldDB; L7KT22; -.
DR STRING; 1220583.GOACH_45_00030; -.
DR eggNOG; ENOG503058G; Bacteria.
DR Proteomes; UP000010988; Unassembled WGS sequence.
DR GO; GO:0018836; F:alkylmercury lyase activity; IEA:UniProtKB-EC.
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; IPR053717; MerB_lyase_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF12324; HTH_15; 1.
DR Pfam; PF03243; 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:GAC51102.1};
KW Mercuric resistance {ECO:0000256|ARBA:ARBA00022466};
KW Mercury {ECO:0000256|ARBA:ARBA00022914};
KW Reference proteome {ECO:0000313|Proteomes:UP000010988}.
FT DOMAIN 17..74
FT /note="Alkylmercury lyase helix-turn-helix"
FT /evidence="ECO:0000259|Pfam:PF12324"
FT REGION 260..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..355
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 51741 MW; C0CE6DF015F81549 CRC64;
MSTDNLTADV FAKILPAGRD RALMRAALRL LAHGTPVTVT ELAAAAGVPD LDPAQTPIGA
DVEYDEAGRI VGWGLTLNPT PHRFSVGGHQ LYTWCAPDTL IFPAVIGAPA CIESDCPITG
TTVRLTIDPV TGVSDLEPAT AMVAFVDPDR IPAFEGLARQ AAAHRRQEPP PLRRQHRHVQ
LIRAQVAQEH QLLDLGLHRG RRRLHRAGRQ PPQPRHLDRR VDDQQRIQFL TPLRRELARQ
PVVGLPLRPR ASVRDPADHR FRARPDHPRR DQVLTRQPEQ QRRRIVLHRP RQQKLIQLLQ
LHRPGRPPPQ ILGHQPHMLG PRLRPLAIRT KLRCIDIQLI RQPGHRHRRR RRHLVRHEPQ
PRQGAQRHRQ AQTDRRAPAL RSNKRQIRRG QREVPEQLLT TDLRELPQAL QLLVREYPRR
HEPQPPTRRP TSSADKPSTN HPGPQPEPRN RR
//
