LACC2_CERUI
ID LACC2_CERUI Reviewed; 62 AA.
AC P86327;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Laccase-C2;
DE EC=1.10.3.2 {ECO:0000269|PubMed:20175123};
DE AltName: Full=Benzenediol:oxygen oxidoreductase C2 {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Diphenol oxidase C2 {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Lac C2;
DE AltName: Full=Urishiol oxidase C2 {ECO:0000250|UniProtKB:Q12718};
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]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION,
RP AND GLYCOSYLATION.
RC STRAIN=VKM F-3196;
RX PubMed=20175123; DOI=10.1002/jobm.200900382;
RA Lisova Z.A., Lisov A.V., Leontievsky A.A.;
RT "Two laccase isoforms of the basidiomycete Cerrena unicolor VKMF-3196.
RT Induction, isolation and properties.";
RL J. Basic Microbiol. 50:72-82(2010).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products (Probable). Oxidation of a broad range of substrates including
CC mono-, di- and polyphenols, aromatic amines and methoxy-substituted
CC phenols accompanied by reduction of oxygen to water.
CC {ECO:0000269|PubMed:20175123, 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|PubMed:20175123};
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.
CC {ECO:0000269|PubMed:20175123}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid)
CC (ABTS) {ECO:0000269|PubMed:20175123};
CC KM=127 uM for 2-methoxyphenol {ECO:0000269|PubMed:20175123};
CC KM=518 uM for hydroquinone {ECO:0000269|PubMed:20175123};
CC KM=4.9 uM for 2,6-dimethoxyphenol {ECO:0000269|PubMed:20175123};
CC KM=140 uM for pyrogallol {ECO:0000269|PubMed:20175123};
CC Vmax=92.6 umol/min/mg enzyme toward 2,2'-azino-bis(3-
CC ethylbenzthiazoline-6-sulphonic acid) (ABTS)
CC {ECO:0000269|PubMed:20175123};
CC Vmax=2.4 umol/min/mg enzyme toward 2-methoxyphenol
CC {ECO:0000269|PubMed:20175123};
CC Vmax=16.4 umol/min/mg enzyme toward hydroquinone
CC {ECO:0000269|PubMed:20175123};
CC Vmax=0.1 umol/min/mg enzyme toward 2,6-dimethoxyphenol
CC {ECO:0000269|PubMed:20175123};
CC Vmax=8.3 umol/min/mg enzyme toward pyrogallol
CC {ECO:0000269|PubMed:20175123};
CC pH dependence:
CC Optimum pH is 3.8 with 2,6-dimethoxyphenol as substrate, and less
CC than 2.7 with ABTS as substrate. {ECO:0000269|PubMed:20175123};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Half-life at 60 degrees
CC Celsius is 20 minutes. Half-life at 70 degrees Celsius is 3 minutes.
CC {ECO:0000269|PubMed:20175123};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20175123}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20175123}.
CC -!- INDUCTION: By copper ions. {ECO:0000269|PubMed:20175123}.
CC -!- PTM: Glycosylated; contains 6% carbohydrates.
CC {ECO:0000269|PubMed:20175123}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC 3.85, its MW is: 67 kDa.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
CC -!- CAUTION: The order of the peptides is unknown. {ECO:0000305}.
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DR AlphaFoldDB; P86327; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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..>62
FT /note="Laccase-C2"
FT /id="PRO_0000381739"
FT BINDING 54
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT UNSURE 14
FT /note="Q or K"
FT UNSURE 15
FT /note="L or I"
FT UNSURE 22
FT /note="K or Q"
FT UNSURE 23
FT /note="W or GE"
FT UNSURE 26
FT /note="L or I"
FT UNSURE 36
FT /note="L or I"
FT UNSURE 53
FT /note="L or I"
FT UNSURE 55
FT /note="L or I"
FT UNSURE 58
FT /note="L or I"
FT NON_CONS 10..11
FT /evidence="ECO:0000305"
FT NON_CONS 22..23
FT /evidence="ECO:0000305"
FT NON_CONS 31..32
FT /evidence="ECO:0000305"
FT NON_CONS 47..48
FT /evidence="ECO:0000305"
FT NON_TER 62
SQ SEQUENCE 62 AA; 6626 MW; 9A35C2CCBFB7F179 CRC64;
AIGPVADLDI VNDQLTDASM IKWDCLPYDV RSPNPLGTTG FAGGNYRSVP ADLHLTTLAD
PR
