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MERB_ECOLX
ID   MERB_ECOLX              Reviewed;         212 AA.
AC   P77072;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Alkylmercury lyase;
DE            EC=4.99.1.2;
DE   AltName: Full=Organomercurial lyase;
GN   Name=merB;
OS   Escherichia coli.
OG   Plasmid IncM R831b.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tolle C., Totis P., Summers A.O.;
RT   "Nucleotide sequence of the organomercury resistance (OMR) locus.";
RL   Submitted (DEC-1996) 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 (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the MerB family. {ECO:0000305}.
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DR   EMBL; U77087; AAB49639.1; -; Genomic_DNA.
DR   PDB; 1S6L; NMR; -; A=1-212.
DR   PDB; 3F0O; X-ray; 1.76 A; A/B=1-212.
DR   PDB; 3F0P; X-ray; 1.64 A; A/B=1-212.
DR   PDB; 3F2F; X-ray; 1.98 A; A/B=1-212.
DR   PDB; 3F2G; X-ray; 1.78 A; A/B=1-212.
DR   PDB; 3F2H; X-ray; 2.00 A; A/B=1-212.
DR   PDB; 3FN8; X-ray; 1.88 A; A/B=1-212.
DR   PDB; 5C0T; X-ray; 1.96 A; A/B=1-212.
DR   PDB; 5C0U; X-ray; 1.87 A; A/B=1-212.
DR   PDB; 5DSF; X-ray; 1.95 A; A/B=1-212.
DR   PDB; 5U79; X-ray; 1.60 A; A/B=1-212.
DR   PDB; 5U7A; X-ray; 1.53 A; A/B=1-212.
DR   PDB; 5U7B; X-ray; 2.00 A; A/B=1-212.
DR   PDB; 5U7C; X-ray; 1.75 A; A/B=1-212.
DR   PDB; 5U82; X-ray; 1.85 A; A/B=1-212.
DR   PDB; 5U83; X-ray; 1.61 A; A/B=1-212.
DR   PDB; 5U88; X-ray; 1.80 A; A/B=1-212.
DR   PDBsum; 1S6L; -.
DR   PDBsum; 3F0O; -.
DR   PDBsum; 3F0P; -.
DR   PDBsum; 3F2F; -.
DR   PDBsum; 3F2G; -.
DR   PDBsum; 3F2H; -.
DR   PDBsum; 3FN8; -.
DR   PDBsum; 5C0T; -.
DR   PDBsum; 5C0U; -.
DR   PDBsum; 5DSF; -.
DR   PDBsum; 5U79; -.
DR   PDBsum; 5U7A; -.
DR   PDBsum; 5U7B; -.
DR   PDBsum; 5U7C; -.
DR   PDBsum; 5U82; -.
DR   PDBsum; 5U83; -.
DR   PDBsum; 5U88; -.
DR   AlphaFoldDB; P77072; -.
DR   BMRB; P77072; -.
DR   SMR; P77072; -.
DR   BioCyc; MetaCyc:MON-3304; -.
DR   BRENDA; 4.99.1.2; 2026.
DR   EvolutionaryTrace; P77072; -.
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   DisProt; DP00575; -.
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; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lyase; Mercuric resistance; Mercury; Plasmid.
FT   CHAIN           1..212
FT                   /note="Alkylmercury lyase"
FT                   /id="PRO_0000220356"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   HELIX           20..31
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   HELIX           39..46
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   HELIX           50..59
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:1S6L"
FT   STRAND          71..79
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   HELIX           97..107
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          111..116
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:3F0P"
FT   HELIX           155..161
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   HELIX           168..176
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:1S6L"
FT   STRAND          185..188
FT                   /evidence="ECO:0007829|PDB:5U7A"
FT   HELIX           189..205
FT                   /evidence="ECO:0007829|PDB:5U7A"
SQ   SEQUENCE   212 AA;  23035 MW;  7FE9DFA8A95F490A CRC64;
     MKLAPYILEL LTSVNRTNGT ADLLVPLLRE LAKGRPVSRT TLAGILDWPA ERVAAVLEQA
     TSTEYDKDGN IIGYGLTLRE TSYVFEIDDR RLYAWCALDT LIFPALIGRT ARVSSHCAAT
     GAPVSLTVSP SEIQAVEPAG MAVSLVLPQE AADVRQSFCC HVHFFASVPT AEDWASKHQG
     LEGLAIVSVH EAFGLGQEFN RHLLQTMSSR TP
 
 
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