LAC1_THACU
ID LAC1_THACU Reviewed; 576 AA.
AC P56193;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Laccase-1;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 1;
DE AltName: Full=Diphenol oxidase 1;
DE AltName: Full=Urishiol oxidase 1;
DE Flags: Precursor;
GN Name=LCC1;
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], BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:8598061};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z54275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S68117; S68117.
DR AlphaFoldDB; P56193; -.
DR SMR; P56193; -.
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 1: Evidence at protein 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..576
FT /note="Laccase-1"
FT /id="PRO_0000002935"
FT DOMAIN 21..145
FT /note="Plastocyanin-like 1"
FT DOMAIN 157..304
FT /note="Plastocyanin-like 2"
FT DOMAIN 376..576
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 471
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 474
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 476
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="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 524
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 525
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 529
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 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..562
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
SQ SEQUENCE 576 AA; 64377 MW; CE5E32918038AE48 CRC64;
MARTTFLVSV SLFVSAVLAR TVEYGLKISD GEIAPDGVKR NATLVNGGYP GPLIFANKGD
TLKVKVQNKL TNPEMYRTTS IHWHGLLQHR NADDDGPSFV TQCPIVPRES YTYTIPLDDQ
TGTYWYHSHL SSQYVDGLRG PLVIYDPKDP HRRLYDVDDE KTVLIIGDWY HESSKAILAS
GNITRQRPVS ATINGKGRFD PDNTPANPDT LYTLKVKRGK RYRLRVINSS EIASFRFSVE
GHKVTVIAAD GVSTKPYQVD AFDILAGQRI DCVVEANQEP DTYWINAPLT NVPNKTAQAL
LVYEEDRRPY HPPKGPYRKW SVSEAIIKYW NHKHKHGRGL LSGHGGLKAR MIEGSHHLHS
RSVVKRQNET TTVVMDESKL VPLEYPGAAC GSKPADLVLD LTFGLNFATG HWMINGIPYE
SPKIPTLLKI LTDEDGVTES DFTKEEHTVI LPKNKCIEFN IKGNSGIPIT HPVHLHGHTW
DVVQFGNNPP NYVNPPRRDV VGSTDAGVRI QFKTDNPGPW FLHCHIDWHL EEGFAMVFAE
APEAVKGGPK SVAVDSQWEG LCGKYDNWLK SNPGQL
