LAC2_PLEOS
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 03-AUG-2022, entry version 98.
DE RecName: Full=Laccase-2;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 2;
DE AltName: Full=Diphenol oxidase 2;
DE AltName: Full=Urishiol oxidase 2;
DE Flags: Precursor;
GN Name=POX2;
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], GLYCOSYLATION AT ASN-467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mycelium;
RX PubMed=8654395; 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 PubMed=7763931; DOI=10.1007/bf00205066;
RA Palmieri G., Giardina P., Marzullo L., Desiderio B., Nitti G., Cannio R.,
RA Sannia G.;
RT "Stability and activity of a phenol oxidase from the ligninolytic fungus
RT Pleurotus ostreatus.";
RL Appl. Microbiol. Biotechnol. 39:632-636(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 -!- PTM: N-glycosylated at Asn-467; contains a high-mannose glycan with a
CC varying number of mannose residues. {ECO:0000269|PubMed:8654395}.
CC -!- MISCELLANEOUS: POX2 isozyme is the most abundant laccase of P.ostreatus
CC under various growth conditions.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; Z49075; CAA88895.1; -; Genomic_DNA.
DR EMBL; Z34848; CAA84357.1; -; mRNA.
DR PIR; S62371; S62371.
DR AlphaFoldDB; Q12739; -.
DR SMR; Q12739; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR iPTMnet; Q12739; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1089723; -.
DR BRENDA; 1.10.3.2; 4912.
DR SABIO-RK; Q12739; -.
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; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Disulfide bond; Glycoprotein; Lignin degradation; Metal-binding;
KW Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT CHAIN 24..533
FT /note="Laccase-2"
FT /id="PRO_0000002930"
FT DOMAIN 25..171
FT /note="Plastocyanin-like 1"
FT DOMAIN 173..336
FT /note="Plastocyanin-like 2"
FT DOMAIN 382..501
FT /note="Plastocyanin-like 3"
FT BINDING 98
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 100
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 143
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 145
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 427
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 430
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 432
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 483
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 484
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 485
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 489
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 467
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:8654395"
FT DISULFID 119..516
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 151..238
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
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
