ID   LAC1B_CERUI             Reviewed;           9 AA.
AC   P85308;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Laccase-1b;
DE            EC=1.10.3.2 {ECO:0000269|Ref.1};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 1b;
DE   AltName: Full=Diphenol oxidase 1b;
DE   AltName: Full=Lac Ib;
DE   AltName: Full=Urishiol oxidase 1b;
DE   Flags: Fragment;
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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RA   Checinska A., Janusz G., Rogalski J.M.;
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. {ECO:0000250|UniProtKB:Q12718, ECO:0000305}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.153 mM for syringaldazine {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is 5.3. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12718}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC       4.27, its MW is: 54.49 kDa.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
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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..>9
FT                   /note="Laccase-1b"
FT                   /id="PRO_0000310833"
FT   BINDING         9
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT   NON_TER         9
SQ   SEQUENCE   9 AA;  892 MW;  1CE22AADC2D76870 CRC64;
     AIGPVADLH