ID   LAC1_AGABI              Reviewed;         520 AA.
AC   Q12541;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-NOV-2008, entry version 50.
DE   RecName: Full=Laccase-1;
DE            EC=1.10.3.2;
DE   AltName: Full=Laccase I;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 1;
DE   AltName: Full=Urishiol oxidase 1;
DE   AltName: Full=Diphenol oxidase 1;
DE   Flags: Precursor;
GN   Name=lcc1;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=D649; TISSUE=Mycelium;
RX   MEDLINE=93367392; PubMed=8360614;
RA   Perry C.R., Smith M., Britnell C.H., Wood D.A., Thurston C.F.;
RT   "Identification of two laccase genes in the cultivated mushroom
RT   Agaricus bisporus.";
RL   J. Gen. Microbiol. 139:1209-1218(1993).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 4 copper ions per monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 3 plastocyanin-like domains.
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DR   EMBL; L10664; AAC18877.1; -; Genomic_DNA.
DR   HSSP; Q9Y780; 1HFU.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008471; F:laccase activity; IEA:EC.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011706; Cu-oxidase_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 3.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Glycoprotein; Lignin degradation;
KW   Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.
FT   SIGNAL        1     19
FT   CHAIN        20    520       Laccase-1.
FT                                /FTId=PRO_0000002918.
FT   DOMAIN       21    145       Plastocyanin-like 1.
FT   DOMAIN      157    305       Plastocyanin-like 2.
FT   DOMAIN      375    488       Plastocyanin-like 3.
FT   METAL        82     82       Copper 1; type 2 (By similarity).
FT   METAL        84     84       Copper 2; type 3 (By similarity).
FT   METAL       127    127       Copper 2; type 3 (By similarity).
FT   METAL       129    129       Copper 3; type 3 (By similarity).
FT   METAL       417    417       Copper 4; type 1 (By similarity).
FT   METAL       420    420       Copper 1; type 2 (By similarity).
FT   METAL       422    422       Copper 3; type 3 (By similarity).
FT   METAL       470    470       Copper 3; type 3 (By similarity).
FT   METAL       471    471       Copper 4; type 1 (By similarity).
FT   METAL       472    472       Copper 2; type 3 (By similarity).
FT   METAL       476    476       Copper 4; type 1 (By similarity).
FT   CARBOHYD    108    108       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    239    239       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    299    299       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    454    454       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    492    492       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   520 AA;  58099 MW;  943DB3F23297B891 CRC64;
     MRLSNALVLV AACISSVVAK TRTFDFDLVN TRLAPDGFER DTVVINGEFP GTLIQVNKGD
     SVRIPLHNKL TSPTMRRSVS IHWHGFFQAR TSGQDGPSFV NQCPQPPNTT FTYEFSVAEQ
     SGTFWYHSHL STQYCDGLRG AFIVYDPRDP LRHLYDVDDE STVITLAEWY HILAPDATNE
     FFSSGIIPVQ DSGLINGKGR FNGGPLTPFA VVNVRRGKRY RLRVIAISCR PFFTFSVDNH
     SLVFMEADGV EHDPVEVQNV DIYAAQRVSV ILHANQPIDN YWIRAPMTGG NPDRNPNLNI
     SLTLAILRYH GARHVEPTTV NVPGHKLLDQ EMHPIRQEGP GKLGDGPPDK HITLNIAQPN
     APFFDINGIS YISPTVPVLL QILSGAKRPE DVLPSEQIFF VPKNSLIEVN IPGEGAHPFH
     LHGHNFDVVL ASNDDTFNFK NPPRRDVYPI NGGNTTFRFF TDNPGAWFLH CHIDWHLEAG
     LAIVFAEAPE DNVSGPQSQI TPQDWLDLCP EYNAIEPEFQ
//