LAC1_PHLRA
ID LAC1_PHLRA Reviewed; 520 AA.
AC Q01679;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 95.
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;
GN Name=LAC;
OS Phlebia radiata (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Phlebia.
OX NCBI_TaxID=5308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 64658 / 79;
RX PubMed=1955850; DOI=10.1099/00221287-137-7-1537;
RA Saloheimo M., Niku-Paavola M.L., Knowles J.K.;
RT "Isolation and structural analysis of the laccase gene from the lignin-
RT degrading fungus Phlebia radiata.";
RL J. Gen. Microbiol. 137:1537-1544(1991).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Saloheimo M.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; X52134; CAA36379.2; -; Genomic_DNA.
DR PIR; S18746; S18746.
DR AlphaFoldDB; Q01679; -.
DR SMR; Q01679; -.
DR CAZy; AA1; Auxiliary Activities 1.
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_0000002928"
FT DOMAIN 22..148
FT /note="Plastocyanin-like 1"
FT DOMAIN 160..304
FT /note="Plastocyanin-like 2"
FT DOMAIN 373..496
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 418
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 421
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 423
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 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..509
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 138..227
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
SQ SEQUENCE 520 AA; 55704 MW; B566CE3CA2791D36 CRC64;
MHTFLRSTAL VVAGLSARAL ASIGPVTDFH IVNAAVSPDG FSRQAVLAEG VFPGPLIAGN
KGDNFQINVI DELTNATMLK TTTIHWHGFF QHGTNWADGP AFINQCPIAS GDSFLYNFQV
PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP ADPYLDQYDV DDDSTVITLA DWYHTAARLG
SPFPAADTTL INGLGRCGEA GCPVSDLAVI SVTKGKRYRF RLVSISCDSF FTFSIDGHSL
NVIEVDATNH QPLTVDELTI YAGQRYSFIL TADQDVDNYW IRANPGIGIT TGFAGGINSA
ILRYDGADVV EPTTTQATSP VVLSESNLAP LTNAAAPGLP EVGGVDLALN FNLTFDGPSL
KFQINGVTFV PPTVPVLLQI LSGAQSAADL LPSGSVYALP SNATIELSLP AGALGGPHPF
HLHGHTFSVV RPAGSTTYNY VNPVQRDVVS IGNTGDNVTI RFDTNNPGPW FLHCHIDWHL
EAGFAVVFAE DIPDVASINP VPQDWSNLCP IYNALDASDH
