ID   LAC1_HERCO              Reviewed;          10 AA.
AC   B3A0L4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Laccase {ECO:0000303|PubMed:22367940};
DE            EC=1.10.3.2 {ECO:0000269|PubMed:22367940};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000250|UniProtKB:D0VWU3};
DE   AltName: Full=Diphenol oxidase {ECO:0000250|UniProtKB:D0VWU3};
DE   AltName: Full=Urishiol oxidase {ECO:0000250|UniProtKB:D0VWU3};
DE   Flags: Fragment;
OS   Hericium coralloides (Coral tooth fungus) (Hericium ramosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Hericiaceae; Hericium.
OX   NCBI_TaxID=100756;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Fruiting body {ECO:0000269|PubMed:22367940};
RX   PubMed=22367940; DOI=10.1007/s12275-012-1372-6;
RA   Zou Y.J., Wang H.X., Ng T.B., Huang C.Y., Zhang J.X.;
RT   "Purification and characterization of a novel laccase from the edible
RT   mushroom Hericium coralloides.";
RL   J. Microbiol. 50:72-78(2012).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. Has activity towards ABTS and, to a much lesser extent,
CC       towards N,N-dimethyl-1,4-phenylenediamine, catechol and 2-
CC       methylcatechol. {ECO:0000269|PubMed:22367940}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O;
CC         Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
CC         Evidence={ECO:0000269|PubMed:22367940};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:Q70KY3};
CC       Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC   -!- ACTIVITY REGULATION: Strongly activated by Mg(2+) and Al(3+). At
CC       concentrations <50 mM, activated by Ca(2+), Mn(2+), Co(2+) and K(+).
CC       Strongly inhibited by Hg(2+) and, in a concentration-dependent manner,
CC       by Fe(2+). {ECO:0000269|PubMed:22367940}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 2.2. Activity declines sharply with decreases or
CC         increases in pH and is absent above pH 6.6.
CC         {ECO:0000269|PubMed:22367940};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Retains 65% activity at 20
CC         degrees Celsius and 24% activity at 100 degrees Celsius.
CC         {ECO:0000269|PubMed:22367940};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D0VWU3}.
CC   -!- MISCELLANEOUS: Inhibits HIV-1 reverse transcriptase (IC(50)=0.6 uM).
CC       {ECO:0000269|PubMed:22367940}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR   BioCyc; MetaCyc:MON-17210; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046274; P:lignin catabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Secreted.
FT   CHAIN           1..>10
FT                   /note="Laccase"
FT                   /id="PRO_0000414619"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:22367940"
SQ   SEQUENCE   10 AA;  1078 MW;  228933C771AAAAA8 CRC64;
     AVGDDTPQLY