ID   LAC_AGAPC               Reviewed;          15 AA.
AC   B3EWI3;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   11-DEC-2019, entry version 8.
DE   RecName: Full=Laccase {ECO:0000303|PubMed:23093860};
DE            EC=1.10.3.2 {ECO:0000269|PubMed:23093860};
DE   Flags: Fragment;
OS   Agaricus placomyces (Mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=182818;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Fruiting body {ECO:0000303|PubMed:23093860};
RX   PubMed=23093860; DOI=10.1155/2012/736472;
RA   Sun J., Chen Q.J., Cao Q.Q., Wu Y.Y., Xu L.J., Zhu M.J., Ng T.B.,
RA   Wang H.X., Zhang G.Q.;
RT   "A laccase with antiproliferative and HIV-I reverse transcriptase
RT   inhibitory activities from the mycorrhizal fungus Agaricus placomyces.";
RL   J. Biomed. Biotechnol. 2012:736472-736472(2012).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (By similarity). Active against a variety of substrates
CC       including the benzenediols hydroquinone and catechol, the benzenetriol
CC       pyrogallol, the methoxy-substituted phenol 2-methylcatechol, the
CC       aromatic diamine N,N-dimethyl-1,4-phenylenediamine and the nonphenolic
CC       heterocyclic compound ABTS (PubMed:23093860). Shows highest degradative
CC       activity towards hydroquinone with lower activity against ABTS and N,N-
CC       dimethyl-1,4-phenylenediamine (PubMed:23093860). Activity towards
CC       pyrogallol, catechol and 2-methyl-catechol is considerably attenuated
CC       (PubMed:23093860). Shows no activity against tyrosine
CC       (PubMed:23093860). {ECO:0000250|UniProtKB:P86351,
CC       ECO:0000269|PubMed:23093860}.
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:23093860};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:Q12718};
CC       Note=Binds 4 Cu cations per monomer (By similarity). Copper is
CC       inhibitory at concentrations of 1.25-5.0 mM (PubMed:23093860).
CC       {ECO:0000250|UniProtKB:Q12718, ECO:0000269|PubMed:23093860};
CC   -!- ACTIVITY REGULATION: Activity is enhanced by Al(3+) at concentrations
CC       of 1.25-2.5 mM (PubMed:23093860). Activity is reduced in the presence
CC       of Cu(2+), Hg(2+), Pb(2+), Fe(3+) and EDTA at concentrations of 1.25-
CC       5.0 mM (PubMed:23093860). Activity is not significantly affected by the
CC       presence of cations such as K(+), Ca(2+), Mg(2+), Mn(2+) or Zn(2+) at
CC       concentrations of 1.25-5.0 mM (PubMed:23093860).
CC       {ECO:0000269|PubMed:23093860}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.392 mM for hydroquinone {ECO:0000269|PubMed:23093860};
CC         KM=0.775 mM for ABTS {ECO:0000269|PubMed:23093860};
CC       pH dependence:
CC         Optimum pH is 5.2 with ABTS as substrate. Optimum pH is 6.8 with
CC         hydroquinone as substrate. {ECO:0000269|PubMed:23093860};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius. Activity declines sharply
CC         as the temperature is increased from 40 to 80 degrees Celsius and is
CC         abolished at 80 degrees Celsius. {ECO:0000269|PubMed:23093860};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12718}.
CC   -!- MISCELLANEOUS: Displays antiproliferative activity against a number of
CC       human tumor cell lines and inhibitory activity against HIV-1 reverse
CC       transcriptase. {ECO:0000269|PubMed:23093860}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Secreted.
FT   CHAIN           1..>15
FT                   /note="Laccase"
FT                   /id="PRO_0000417451"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|PubMed:23093860"
SQ   SEQUENCE   15 AA;  1569 MW;  CFF7C40A165E6882 CRC64;
     DVIGPQAQVT LANQD