ID   LAC2D_CERUI             Reviewed;          47 AA.
AC   P85430;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Laccase-2d {ECO:0000303|PubMed:19283431};
DE            EC=1.10.3.2 {ECO:0000269|PubMed:19283431};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000250|UniProtKB:Q99044};
DE   AltName: Full=Diphenol oxidase {ECO:0000250|UniProtKB:Q99044};
DE   AltName: Full=Laccase-IId {ECO:0000303|PubMed:19283431};
DE            Short=Lac-IId {ECO:0000303|PubMed:19283431};
DE   AltName: Full=Urishiol oxidase {ECO:0000250|UniProtKB:Q99044};
DE   Flags: Fragments;
OS   Cerrena unicolor (Canker rot fungus) (Daedalea unicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Cerrenaceae; Cerrena.
OX   NCBI_TaxID=90312;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
RC   STRAIN=MTCC 5159 {ECO:0000269|PubMed:19283431};
RX   PubMed=19283431; DOI=10.1007/s10126-009-9187-0;
RA   D'Souza-Ticlo D., Sharma D., Raghukumar C.;
RT   "A thermostable metal-tolerant laccase with bioremediation potential from a
RT   marine-derived fungus.";
RL   Mar. Biotechnol. 11:725-737(2009).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (By similarity). Has highest activity towards ABTS, also
CC       active towards ferulic acid and guaiacol, but is not active towards
CC       tyrosine, vanillic acid, 2,5-dimethyl aniline, p-anisidine or violuric
CC       acid (PubMed:19283431). {ECO:0000250|UniProtKB:Q70KY3,
CC       ECO:0000269|PubMed:19283431}.
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:19283431};
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 sodium azide, SDS and
CC       mercaptoethanol, but not by 4-hexyl resocinol, L-cysteine and
CC       dithiothreitol. Activity is inhibited by the heavy metal ions Cr, W,
CC       Sn, Ag(+) and Hg(2+), but not by Pb(2+), Fe(3+), Ni(2+), Li(2+), Co(2+)
CC       or Cd(2+). {ECO:0000269|PubMed:19283431}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=54.1 uM for ABTS (at 70 degrees Celsius)
CC         {ECO:0000269|PubMed:19283431};
CC         KM=57.1 uM for ABTS (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:19283431};
CC         KM=19.2 uM for syringaldizine (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:19283431};
CC       pH dependence:
CC         Optimum pH is 3.0 at 70 degrees Celsius with ABTS as substrate, and
CC         6.0 with guaiacol and syringaldazine as substrate.
CC         {ECO:0000269|PubMed:19283431};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius at pH 3.0 with ABTS as
CC         substrate. Retains 100% of its activity after 1 hour at 30 degrees
CC         Celsius at pH 9.0. Retains more than 60% of its activity after 180
CC         minutes at 60 degrees Celsius at pH 9.0. Retains approximately 50% of
CC         its activity after 90 minutes at 70 degrees Celsius at pH 9.0.
CC         {ECO:0000269|PubMed:19283431};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99044}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: N-glycosylated; contains 17% carbohydrates.
CC       {ECO:0000269|PubMed:19283431}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.3,
CC       its MW is: 59 kDa. {ECO:0000269|PubMed:19283431}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
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   AlphaFoldDB; P85430; -.
DR   SMR; P85430; -.
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; Glycoprotein; Lignin degradation;
KW   Metal-binding; Oxidoreductase; Repeat; Secreted.
FT   CHAIN           1..>47
FT                   /note="Laccase-2d"
FT                   /id="PRO_0000320022"
FT   DOMAIN          2..>47
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000255"
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000303|PubMed:19283431"
FT   NON_TER         47
FT                   /evidence="ECO:0000303|PubMed:19283431"
SQ   SEQUENCE   47 AA;  4846 MW;  DFC1942A188FC2B9 CRC64;
     GTGPVADLHI INKDLSPDGF QRPTVVAGGG RDVVSIGRAG DNVTIRF