LAC2_THACU
ID LAC2_THACU Reviewed; 599 AA.
AC Q02075;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Laccase-2;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 2;
DE AltName: Full=Diphenol oxidase 2;
DE AltName: Full=Urishiol oxidase 2;
DE Flags: Precursor;
GN Name=LCC2;
OS Thanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Thanatephorus.
OX NCBI_TaxID=107832;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=R22 / IMI 358730 / AG-6;
RX PubMed=8598061; DOI=10.1007/bf02208621;
RA Wahleithner J.A., Xu F., Brown K.M., Brown S.H., Golightly E.J.,
RA Halkier T., Kauppinen S., Pederson A., Schneider P.;
RT "The identification and characterization of four laccases from the plant
RT pathogenic fungus Rhizoctonia solani.";
RL Curr. Genet. 29:395-403(1996).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000250|UniProtKB:Q70KY3}.
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:0000250|UniProtKB:Q70KY3};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q70KY3};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99046}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- TISSUE SPECIFICITY: In mycelia, at a lower level than LCC4.
CC {ECO:0000269|PubMed:8598061}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; Z54276; CAA91041.1; -; Genomic_DNA.
DR PIR; S68118; S68118.
DR AlphaFoldDB; Q02075; -.
DR SMR; Q02075; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 2.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Lignin degradation; Metal-binding;
KW Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..599
FT /note="Laccase-2"
FT /id="PRO_0000002936"
FT DOMAIN 21..145
FT /note="Plastocyanin-like 1"
FT DOMAIN 157..307
FT /note="Plastocyanin-like 2"
FT DOMAIN 450..567
FT /note="Plastocyanin-like 3"
FT BINDING 82
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 BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 127
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 129
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 BINDING 497
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 500
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 BINDING 502
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 BINDING 549
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 BINDING 550
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 551
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 555
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..588
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
SQ SEQUENCE 599 AA; 66540 MW; F01DD5C52D0CBB91 CRC64;
MARSTTSLFA LSLVASAFAR VVDYGFDVAN GAVAPDGVTR NAVLVNGRFP GPLITANKGD
TLKITVRNKL SDPTMRRSTT IHWHGLLQHR TAEEDGPAFV TQCPIPPQES YTYTMPLGEQ
TGTYWYHSHL SSQYVDGLRG PIVIYDPHDP YRNYYDVDDE RTVFTLADWY HTPSEAIIAT
HDVLKTIPDS GTINGKGKYD PASANTNNTT LENLYTLKVK RGKRYRLRII NASAIASFRF
GVQGHKCTII EADGVLTKPI EVDAFDILAG QRYSCILKAD QDPDSYWINA PITNVLNTNV
QALLVYEDDK RPTHYPWKPF LTWKISNEII QYWQHKHGSH GHKGKGHHHK VRAIGGVSGL
SSRVKSRASD LSKKAVELAA ALVAGEAELD KRQNEDNSTI VLDETKLIAL VQPGAPGGSR
PADVVVPLDF GLNFANGLWT INNVSYSPPD VPTLLKILTD KDKVDASDFT ADEHTYILPK
NQVVELHIKG QALGIVHPLH LHGHAFDVVQ FGDNAPNYVN PPRRDVVGVT DAGVRIQFRT
DNPGPWFLHC HIDWHLEEGF AMVFAEAPED IKKGSQSVKP DGQWKKLCEK YEKLPEALQ
