LAC3_THACU
ID LAC3_THACU Reviewed; 572 AA.
AC Q02079;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Laccase-3;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 3;
DE AltName: Full=Diphenol oxidase 3;
DE AltName: Full=Urishiol oxidase 3;
DE Flags: Precursor;
GN Name=LCC3;
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; Z54215; CAA90942.1; -; Genomic_DNA.
DR PIR; S68119; S68119.
DR AlphaFoldDB; Q02079; -.
DR SMR; Q02079; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR PRIDE; Q02079; -.
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; 1.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..572
FT /note="Laccase-3"
FT /id="PRO_0000002937"
FT DOMAIN 21..145
FT /note="Plastocyanin-like 1"
FT DOMAIN 157..304
FT /note="Plastocyanin-like 2"
FT DOMAIN 422..540
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 470
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 473
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 475
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 522
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 523
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 524
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 528
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 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..561
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT VARIANT 159
FT /note="D -> N"
FT VARIANT 359
FT /note="R -> H"
FT VARIANT 418
FT /note="H -> Y"
FT VARIANT 448
FT /note="I -> V"
SQ SEQUENCE 572 AA; 63747 MW; DF1E2AF9FF108CE4 CRC64;
MARTTFLVSV SLFVSAVLAR TVEYNLKISN GKIAPDGVER DATLVNGGYP GPLIFANKGD
TLKVKVQNKL TNPDMYRTTS IHWHGLLQHR NADDDGPAFV TQCPIVPQAS YTYTMPLGDQ
TGTYWYHSHL SSQYVDGLRG PLVIYDPKDP HRRLYDIDDE KTVLIIGDWY HTSSKAILAT
GNITLQQPDS ATINGKGRFD PDNTPANPNT LYTLKVKRGK RYRLRVINSS AIASFRMSIQ
GHKMTVIAAD GVSTKPYQVD SFDILAGQRI DAVVEANQEP DTYWINAPLT NVANKTAQAL
LIYEDDRRPY HPPKGPYRKW SVSEAIIKYW KHKHGRGLLS GHGGLKARMM EGSLHLHGRR
DIVKRQNETT TVVMDETKLV PLEHPGAACG SKPADLVIDL TFGVNFTTGH WMINGIPHKS
PDMPTLLKIL TDTDGVTESD FTQPEHTIIL PKNKCVEFNI KGNSGLGIVH PIHLHGHTFD
VVQFGNNPPN YVNPPRRDVV GATDEGVRFQ FKTDNPGPWF LHCHIDWHLE EGFAMVFAEA
PEAIKGGPKS VPVDRQWKDL CRKYGSLPAG FL
