LAC1_TRAHI
ID LAC1_TRAHI Reviewed; 520 AA.
AC Q02497;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Laccase;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase;
DE AltName: Full=Diphenol oxidase;
DE AltName: Full=Ligninolytic phenoloxidase;
DE AltName: Full=Urishiol oxidase;
DE Flags: Precursor;
OS Trametes hirsuta (White-rot fungus) (Coriolus hirsutus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
RP PRO-411.
RC STRAIN=NBRC 4917;
RX PubMed=2394718; DOI=10.1016/s0021-9258(18)77245-1;
RA Kojima Y., Tsukuda Y., Kawai Y., Tsukamoto A., Sugiura J., Sakaino M.,
RA Kita Y.;
RT "Cloning, sequence analysis, and expression of ligninolytic phenoloxidase
RT genes of the white-rot basidiomycete Coriolus hirsutus.";
RL J. Biol. Chem. 265:15224-15230(1990).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products (By similarity). Has activity towards guaiacol
CC (PubMed:2394718). {ECO:0000250|UniProtKB:Q70KY3,
CC ECO:0000269|PubMed:2394718}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- POLYMORPHISM: 2 allelic forms exist in position 111.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; M60560; AAA33103.1; -; Genomic_DNA.
DR EMBL; M60561; AAA33104.1; -; Genomic_DNA.
DR PIR; A35883; A35883.
DR AlphaFoldDB; Q02497; -.
DR SMR; Q02497; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR BRENDA; 1.10.3.2; 1623.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT CHAIN 22..520
FT /note="Laccase"
FT /id="PRO_0000002939"
FT DOMAIN 23..148
FT /note="Plastocyanin-like 1"
FT DOMAIN 160..302
FT /note="Plastocyanin-like 2"
FT DOMAIN 369..491
FT /note="Plastocyanin-like 3"
FT BINDING 85
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 87
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 130
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 132
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 416
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 419
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 421
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 473
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 474
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 475
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 479
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 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..509
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 138..226
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT VARIANT 411
FT /note="A -> P"
FT /evidence="ECO:0000269|PubMed:2394718"
FT CONFLICT 378..379
FT /note="SG -> RR (in Ref. 1; AAA33104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 55688 MW; 977D8DFA551F7929 CRC64;
MSRFQSLLAF VVASLAAVAH AAIGPTADLT ISNAEVSPDG FARQAVVVNN VTPGPLVAGN
KGDRFQLNVI DNLTNHTMLK STSIHWHGFF QKGTNWADGP AFVNQCPISS GHSFLYDFQV
PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP NDPHASLYDV DNDDTVITLA DWYHTAAKLG
PAFPLGADAT LINGLGRSPS TTAADLAVIN VTKGKRYRFR LVSLSCDPNH TFSIDGHDLT
IIEVDSINSQ PLVVDSIQIF AAQRYSFVLN ADQDVGNYWI RANPNFGNVG FAGGINSAIL
RYDGADPVEP TTTQTTPTKP LNEVDLHPLA TMAVPGSPVA GGVDTAINMA FNFNGTNFFI
NGASFVPPTV PVLLQIISGA QNAQDLLPSG SVYSLPSNAD IEISFPATAA APGAPHPFHL
HGHAFAVVRS AGSTVYNYDN PIFRDVVSTG TPAAGDNVTI RFRTDNPGPW FLHCHIDFHL
EAGFAVVFAE DIPDVASANP VPQAWSDLCP IYDALDVNDQ
