ID   LACC_LEPMG              Reviewed;          10 AA.
AC   B3EWG2;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 1.
DT   29-SEP-2021, entry version 12.
DE   RecName: Full=Laccase {ECO:0000303|Ref.1};
DE            EC=1.10.3.2 {ECO:0000269|Ref.1};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000250|UniProtKB:P86351};
DE   AltName: Full=Diphenol oxidase {ECO:0000250|UniProtKB:P86351};
DE   AltName: Full=Urishiol oxidase {ECO:0000250|UniProtKB:P86351};
DE   Flags: Fragment;
OS   Lepiota magnispora (Mushroom) (Lepiota ventriosospora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Lepiota.
OX   NCBI_TaxID=182864;
RN   [1]
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   TISSUE=Fruiting body {ECO:0000269|Ref.1};
RX   DOI=10.1016/j.molcatb.2012.08.001;
RA   Zhang G.-Q., Chen Q.-J., Wang H.-X., Ng T.B.;
RT   "A laccase with inhibitory activity against HIV-1 reverse transcriptase
RT   from the mycorrhizal fungus Lepiota ventriosospora.";
RL   J. Mol. Catal., B Enzym. 85:31-36(2013).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (By similarity). In vitro, has activity towards 2,2'-azino-
CC       bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), catechol and
CC       hydroquinone but not towards 2,6-dimethoxy-phenol or guaiacol.
CC       {ECO:0000250|UniProtKB:P86351, ECO:0000269|Ref.1}.
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|Ref.1};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:Q12718};
CC       Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q12718};
CC   -!- ACTIVITY REGULATION: Inhibited by NaN(3) and SDS. Partially inhibited
CC       by Fe(2+), Fe(3+) and Hg(2+) but not by other metal ions at a
CC       concentration of 10 mM. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=54.9 uM for ABTS (at pH 4) {ECO:0000269|Ref.1};
CC         KM=10.2 uM for catechol (at pH 4) {ECO:0000269|Ref.1};
CC         KM=12.6 uM for hydroquinone (at pH 4) {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is 4. Activity decreases at higher pH and is lost at pH 6.
CC         {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. After incubation at 80
CC         degrees Celsius or 20 degrees Celsius for 5 minutes 50% activity
CC         remains. Activity is lost after incubation at 100 degrees Celsius for
CC         5 minutes. After incubation at 60 degrees Celsius for 1 hour 18%
CC         activity remains. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86351}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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..>10
FT                   /note="Laccase"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000416968"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   10 AA;  1018 MW;  1CE1BFA87B133870 CRC64;
     VTIGKEGTLT