ID   LAC2_PLEOS              Reviewed;         533 AA.
AC   Q12739;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Laccase-2;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 2;
DE   AltName: Full=Urishiol oxidase 2;
DE   AltName: Full=Diphenol oxidase 2;
DE   Flags: Precursor;
GN   Name=POX2;
OS   Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Homobasidiomycetes; Agaricomycetidae; Agaricales; Pleurotaceae;
OC   Pleurotus.
OX   NCBI_TaxID=5322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], GLYCOSYLATION AT ASN-467,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Mycelium;
RX   MEDLINE=96184523; PubMed=8654395;
RX   DOI=10.1111/j.1432-1033.1996.00508.x;
RA   Giardina P., Aurilia V., Cannio R., Marzullo L., Amoresano A.,
RA   Siciliano R., Pucci P., Sannia G.;
RT   "The gene, protein and glycan structures of laccase from Pleurotus
RT   ostreatus.";
RL   Eur. J. Biochem. 235:508-515(1996).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=Florida; TISSUE=Mycelium;
RX   MEDLINE=93356991; PubMed=7763931; DOI=10.1007/BF00205066;
RA   Palmieri G., Giardina P., Marzullo L., Desiderio B., Nitti G.,
RA   Cannio R., Sannia G.;
RT   "Stability and activity of a phenol oxidase from the ligninolytic
RT   fungus Pleurotus ostreatus.";
RL   Appl. Microbiol. Biotechnol. 39:632-636(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   -!- PTM: N-glycosylated at Asn-467; contains a high-mannose glycan
CC       with a varying number of mannose residues.
CC   -!- MISCELLANEOUS: POX2 isozyme is the most abundant laccase of
CC       P.ostreatus under various growth conditions.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 3 plastocyanin-like domains.
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DR   EMBL; Z49075; CAA88895.1; -; Genomic_DNA.
DR   EMBL; Z34848; CAA84357.1; -; mRNA.
DR   PIR; S62371; S62371.
DR   HSSP; Q12718; 1GYC.
DR   BRENDA; 1.10.3.2; 16687.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
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; Glycoprotein; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Repeat; Secreted; Signal.
FT   SIGNAL        1     23
FT   CHAIN        24    533       Laccase-2.
FT                                /FTId=PRO_0000002930.
FT   DOMAIN       25    171       Plastocyanin-like 1.
FT   DOMAIN      173    336       Plastocyanin-like 2.
FT   DOMAIN      382    501       Plastocyanin-like 3.
FT   METAL        98     98       Copper 1; type 2 (By similarity).
FT   METAL       100    100       Copper 2; type 3 (By similarity).
FT   METAL       143    143       Copper 2; type 3 (By similarity).
FT   METAL       145    145       Copper 3; type 3 (By similarity).
FT   METAL       427    427       Copper 4; type 1 (By similarity).
FT   METAL       430    430       Copper 1; type 2 (By similarity).
FT   METAL       432    432       Copper 3; type 3 (By similarity).
FT   METAL       483    483       Copper 3; type 3 (By similarity).
FT   METAL       484    484       Copper 4; type 1 (By similarity).
FT   METAL       485    485       Copper 2; type 3 (By similarity).
FT   METAL       489    489       Copper 4; type 1 (By similarity).
FT   CARBOHYD    467    467       N-linked (GlcNAc...) (high mannose).
SQ   SEQUENCE   533 AA;  56767 MW;  7233C41D47E19AE6 CRC64;
     MFPGARILAT LTLALHLLHG AHAAIGPAGN MYIVNEDVSP DGFARSAVVA RSVPATDPTP
     ATASIPGVLV QGNKGDNFQL NVVNQLSDTT MLKTTSIHWH GFFQAGSSWA DGPAFVTQCP
     VASGDSFLYN FNVPDQAGTF WYHSHLSTQY CDGLRGPFVV YDPSDPHLSL YDIDNADTVI
     TLEDWYHIVA PQNAAIPTPD STLINGKGRY AGGPTSPLAI INVESNKRYR FRLVSMSCDP
     NFTFSIDGHS LLVIEADAVN IVPITVDSIQ IFAGQRYSFV LTANQAVDNY WIRANPNLGS
     TGFVGGINSA ILRYAGATED DPTTTSSTST PLLETNLVPL ENPGAPGPPV PGGADININL
     AMAFDFTTFE LTINGVPFLP PTAPVLLQIL SGASTAASLL PSGSIYELEA NKVVEISMPA
     LAVGGPHPFH LHGHTFDVIR SAGSTTYNFD TPARRDVVNT GTGANDNVTI RFVTDNPGPW
     FLHCHIDWHL EIGLAVVFAE DVTSISAPPA AWDDLCPIYN ALSDNDKGGI VPS
//