LAC1_BOTFU
ID LAC1_BOTFU Reviewed; 561 AA.
AC Q12570; Q96WN0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 03-AUG-2022, entry version 92.
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; Synonyms=lac1;
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=SAS56;
RX PubMed=11929539; DOI=10.1046/j.1365-2958.2002.02801.x;
RA Schouten A., Wagemakers L., Stefanato F.L., van der Kaaij R.M.,
RA van Kan J.A.L.;
RT "Resveratrol acts as a natural profungicide and induces self-intoxication
RT by a specific laccase.";
RL Mol. Microbiol. 43:883-894(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-561.
RC STRAIN=SAS56;
RA Cantone F.A., Staples R.C.;
RT "A laccase cDNA from Botrytis cinerea.";
RL Phytopathology 83:1383-1383(1993).
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 -!- INDUCTION: Not induced by resveratrol or tannins.
CC {ECO:0000269|PubMed:11929539}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB41823.1; Type=Erroneous gene model prediction; Note=The sequence does probably not originate from mRNA or it was not properly spliced.; Evidence={ECO:0000305};
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DR EMBL; AF243854; AAK77952.1; -; Genomic_DNA.
DR EMBL; U20192; AAB41823.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q12570; -.
DR SMR; Q12570; -.
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; IPR002355; Cu_oxidase_Cu_BS.
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.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Lignin degradation; Metal-binding;
KW Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..561
FT /note="Laccase-1"
FT /id="PRO_0000085584"
FT DOMAIN 68..185
FT /note="Plastocyanin-like 1"
FT DOMAIN 191..337
FT /note="Plastocyanin-like 2"
FT DOMAIN 396..525
FT /note="Plastocyanin-like 3"
FT BINDING 119
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 121
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 163
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 165
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 445
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 448
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 450
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 504
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 505
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 506
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 510
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 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..542
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CONFLICT 117..118
FT /note="SI -> TM (in Ref. 2; AAB41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="V -> I (in Ref. 2; AAB41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="N -> K (in Ref. 2; AAB41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="M -> L (in Ref. 2; AAB41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="P -> S (in Ref. 2; AAB41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="A -> V (in Ref. 2; AAB41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="A -> G (in Ref. 2; AAB41823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 60337 MW; 7F366B289EF73C23 CRC64;
MKNSFFSSLA KFASLSLAFA LPTAEVIPSA LEERQSCANT ATTRSCWGQY SASTNSYTTV
PKTGYWLVVQ NTTLSADGVS RPTLNFNGTI PGPQITADWG DDVIVHVTNK LTSNGTSIHW
HGIRQLNNAQ YDGVPGITQC PIAPGGTLTY KFHADNYGSS WYHSHFILQY GDGLFGPLVI
NGPATANYDV DLGMLFLNDW NHVPVQSLWD KAKTGAPPTL LTGLMNGTNT YNGAGKKFQT
TFTPGLKYRI RVVNTAVDGH FQFSIDGHSF QVIAMDFVPI VPYNATSILV SIAQRYDIIV
TANAAVGNYW IRAGWQTACS GNTNAANITG ILRYTGSSST ADPTTTSTVT ASTSCLDEPL
ASLVPFVPIN PVASSIMKTT LTTGGGQWLF NGSSLLLNWT DPTLLTVLNS GNIWPTEYNV
IPIESTTANK GWAVLAISGP NGPNHPIHLH GHDFWTLSQG TGAYTATTAL NLVNPPRRDV
MTLPTGGHLV IAFQIDNPGS WLMHCHIAWH ASEGLALQFV ESESSILPTI GTADVSTFQN
TCAAWKAWTP TEPFPQDDSG I
