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Laccase-2d (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase) (Diphenol oxidase) (Laccase-IId) (Lac-IId) (Urishiol oxidase) (Fragments)

 LAC2D_CERUI             Reviewed;          47 AA.
P85430;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
25-OCT-2017, entry version 30.
RecName: Full=Laccase-2d {ECO:0000303|PubMed:19283431};
EC=1.10.3.2;
AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000250|UniProtKB:Q99044};
AltName: Full=Diphenol oxidase {ECO:0000250|UniProtKB:Q99044};
AltName: Full=Laccase-IId {ECO:0000303|PubMed:19283431};
Short=Lac-IId {ECO:0000303|PubMed:19283431};
AltName: Full=Urishiol oxidase {ECO:0000250|UniProtKB:Q99044};
Flags: Fragments;
Cerrena unicolor (Canker rot fungus) (Daedalea unicolor).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Cerrenaceae; Cerrena.
NCBI_TaxID=90312;
[1] {ECO:0000305}
PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND GLYCOSYLATION.
STRAIN=MTCC 5159 {ECO:0000269|PubMed:19283431};
PubMed=19283431; DOI=10.1007/s10126-009-9187-0;
D'Souza-Ticlo D., Sharma D., Raghukumar C.;
"A thermostable metal-tolerant laccase with bioremediation potential
from a marine-derived fungus.";
Mar. Biotechnol. 11:725-737(2009).
-!- FUNCTION: Lignin degradation and detoxification of lignin-derived
products (Probable). Has highest activity towards ABTS, also
active towards ferulic acid and guaiacol, but is not active
towards tyrosine, vanillic acid, 2,5-dimethyl aniline, p-anisidine
or violuric acid. {ECO:0000269|PubMed:19283431, ECO:0000305}.
-!- CATALYTIC ACTIVITY: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
H(2)O. {ECO:0000250|UniProtKB:Q99044,
ECO:0000269|PubMed:19283431}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000250|UniProtKB:Q12718};
Note=Binds 4 Cu cations per monomer.
{ECO:0000250|UniProtKB:Q12718};
-!- ENZYME REGULATION: Inhibited by sodium azide, SDS and
mercaptoethanol, but not by 4-hexyl resocinol, L-cysteine and
dithiothreitol. Activity is inhibited by the heavy metal ions Cr,
W, Sn, Ag(+) and Hg(2+), but not by Pb(2+), Fe(3+), Ni(2+),
Li(2+), Co(2+) or Cd(2+). {ECO:0000269|PubMed:19283431}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=54.1 uM for ABTS (at 70 degrees Celsius)
{ECO:0000269|PubMed:19283431};
KM=57.1 uM for ABTS (at 30 degrees Celsius)
{ECO:0000269|PubMed:19283431};
KM=19.2 uM for syringaldizine (at 30 degrees Celsius)
{ECO:0000269|PubMed:19283431};
pH dependence:
Optimum pH is 3.0 at 70 degrees Celsius with ABTS as substrate,
and 6.0 with guaiacol and syringaldazine as substrate.
{ECO:0000269|PubMed:19283431};
Temperature dependence:
Optimum temperature is 70 degrees Celsius at pH 3.0 with ABTS as
substrate. Retains 100% of its activity after 1 hour at 30
degrees Celsius at pH 9.0. Retains more than 60% of its activity
after 180 minutes at 60 degrees Celsius at pH 9.0. Retains
approximately 50% of its activity after 90 minutes at 70 degrees
Celsius at pH 9.0. {ECO:0000269|PubMed:19283431};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99044}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- PTM: N-glycosylated; contains 17% carbohydrates.
{ECO:0000269|PubMed:19283431}.
-!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
5.3, its MW is: 59 kDa. {ECO:0000269|PubMed:19283431}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000255}.
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SMR; P85430; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
1: Evidence at protein level;
Copper; Direct protein sequencing; Glycoprotein; Lignin degradation;
Metal-binding; Oxidoreductase; Repeat; Secreted.
CHAIN 1 >47 Laccase-2d.
/FTId=PRO_0000320022.
DOMAIN 2 >47 Plastocyanin-like. {ECO:0000255}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
NON_CONS 30 31 {ECO:0000303|PubMed:19283431}.
NON_TER 47 47 {ECO:0000303|PubMed:19283431}.
SEQUENCE 47 AA; 4846 MW; DFC1942A188FC2B9 CRC64;
GTGPVADLHI INKDLSPDGF QRPTVVAGGG RDVVSIGRAG DNVTIRF


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