LACC1_CERUI
ID LACC1_CERUI Reviewed; 63 AA.
AC P86328;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Laccase-C1;
DE EC=1.10.3.2 {ECO:0000269|PubMed:20175123};
DE AltName: Full=Benzenediol:oxygen oxidoreductase C1 {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Diphenol oxidase C1 {ECO:0000250|UniProtKB:Q12718};
DE AltName: Full=Lac C1;
DE AltName: Full=Urishiol oxidase C1 {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=35 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid)
CC (ABTS) {ECO:0000269|PubMed:20175123};
CC KM=1.529 mM for 2-methoxyphenol {ECO:0000269|PubMed:20175123};
CC KM=1.582 mM for hydroquinone {ECO:0000269|PubMed:20175123};
CC KM=17.6 uM for 2,6-dimethoxyphenol {ECO:0000269|PubMed:20175123};
CC KM=265 uM for pyrogallol {ECO:0000269|PubMed:20175123};
CC Vmax=138.9 umol/min/mg enzyme toward ABTS
CC {ECO:0000269|PubMed:20175123};
CC Vmax=1.4 umol/min/mg enzyme toward 2-methoxyphenol
CC {ECO:0000269|PubMed:20175123};
CC Vmax=9.9 umol/min/mg enzyme toward hydroquinone
CC {ECO:0000269|PubMed:20175123};
CC Vmax=11.9 umol/min/mg enzyme toward 2,6-dimethoxyphenol
CC {ECO:0000269|PubMed:20175123};
CC Vmax=8.5 umol/min/mg enzyme toward pyrogallol
CC {ECO:0000269|PubMed:20175123};
CC pH dependence:
CC Optimum pH is 4.4 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 55 degrees Celsius. Half-life at 70 degrees
CC Celsius is 30 minutes. {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 16% carbohydrates.
CC {ECO:0000269|PubMed:20175123}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC 4.05, its MW is: 75 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; P86328; -.
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..>63
FT /note="Laccase-C1"
FT /id="PRO_0000381738"
FT UNSURE 15
FT /note="L or I"
FT UNSURE 20
FT /note="Q or K"
FT UNSURE 22
FT /note="L or I"
FT UNSURE 23
FT /note="L or I"
FT UNSURE 34
FT /note="L or I"
FT UNSURE 35
FT /note="Q or K"
FT UNSURE 38
FT /note="K or Q"
FT UNSURE 49
FT /note="L or I"
FT UNSURE 51
FT /note="L or I"
FT UNSURE 53
FT /note="L or K"
FT UNSURE 54
FT /note="W or GE"
FT UNSURE 56
FT /note="Q or K"
FT UNSURE 61
FT /note="W or GE"
FT UNSURE 62
FT /note="L or I"
FT NON_CONS 10..11
FT /evidence="ECO:0000305"
FT NON_CONS 24..25
FT /evidence="ECO:0000305"
FT NON_CONS 39..40
FT /evidence="ECO:0000305"
FT NON_CONS 50..51
FT /evidence="ECO:0000305"
FT NON_TER 63
SQ SEQUENCE 63 AA; 7148 MW; 2E1D1E2EDDD6131E CRC64;
AIGPVADIDI DVVSLGMVDQ SLLREMHEVS NVALQAMKGS DEYDFNANLR LVLWNQPDFM
WLR
