ID   A0A058ZTN6_EUCGR        Unreviewed;       556 AA.
AC   A0A058ZTN6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   04-FEB-2015, entry version 7.
DE   RecName: Full=Laccase {ECO:0000256|RuleBase:RU361119};
DE            EC=1.10.3.2 {ECO:0000256|RuleBase:RU361119};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000256|RuleBase:RU361119};
DE   AltName: Full=Diphenol oxidase {ECO:0000256|RuleBase:RU361119};
DE   AltName: Full=Urishiol oxidase {ECO:0000256|RuleBase:RU361119};
GN   ORFNames=EUGRSUZ_L01734 {ECO:0000313|EMBL:KCW44721.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Myrtales; Myrtaceae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW44721.1};
RN   [1] {ECO:0000313|EMBL:KCW44721.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW44721.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D.,
RA   Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. {ECO:0000256|RuleBase:RU361119}.
CC   -!- CATALYTIC ACTIVITY: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
CC       H(2)O. {ECO:0000256|RuleBase:RU361119}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU361119};
CC       Note=Binds 4 Cu cations per monomer.
CC       {ECO:0000256|RuleBase:RU361119};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|RuleBase:RU361119}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|RuleBase:RU361119}.
CC   -!- SIMILARITY: Contains 3 plastocyanin-like domains.
CC       {ECO:0000256|RuleBase:RU361119}.
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DR   EMBL; KK199087; KCW44721.1; -; Genomic_DNA.
DR   GO; GO:0048046; C:apoplast; 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_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR017761; Laccase.
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   TIGRFAMs; TIGR03389; laccase; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Apoplast {ECO:0000256|RuleBase:RU361119};
KW   Copper {ECO:0000256|RuleBase:RU361119, ECO:0000256|SAAS:SAAS00056315};
KW   Lignin degradation {ECO:0000256|RuleBase:RU361119};
KW   Metal-binding {ECO:0000256|RuleBase:RU361119,
KW   ECO:0000256|SAAS:SAAS00056267};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361119,
KW   ECO:0000256|SAAS:SAAS00056258};
KW   Repeat {ECO:0000256|RuleBase:RU361119};
KW   Secreted {ECO:0000256|RuleBase:RU361119};
KW   Signal {ECO:0000256|RuleBase:RU361119}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU361119}.
FT   CHAIN        22    556       Laccase. {ECO:0000256|RuleBase:RU361119}.
FT                                /FTId=PRO_5001335908.
SQ   SEQUENCE   556 AA;  60799 MW;  4C85C3843B0922B4 CRC64;
     MDSWLKILVL VACITPAVVE ARVRNYSFNV VMKNKTRLCS SKPIVTVNGK FPGPTLYARE
     DDNVLVRVTN HVKYNVTIHW HGVRQLRTGW ADGPAYITQC PIQTGQSYVY NFTITGQRGT
     LLWHAHILWL RATLHGAIVI LPKRGVPYPF PKPHKEVVVV LGEWWKSDTE AVINQAIKSG
     LAPNVSDAHT INGHPGPSSN CPSQGGFTLP VESGKKYMLR IINAALNEEL FFKIAGHQLT
     IVEVDATYVK PFKTNTIVIA PGQTTNALIS TDQSSGKYMV AASPFMDSPI AVDNMTATAT
     LHYSGTLAAT STTLTKTPPQ NATAVANNFI NSLRSLNSKR YPAKVPLTVD HSLLFTVGLG
     VNPCPSCKAG NGSRVVASMN NVTFVMPSTA LLQAHFFNIS GVFTSDFPGN PRTTFNYTGS
     PPSNLRTTSG TKVFRLHYNS TVQLVLQDTG IIAPENHPIH LHGFNFFTVG KGLGNYNPKV
     DQKNFNLVDP VERNTIGVPS GGWVAIRFRA DNPGVWFMHC HLEIHTTWGL KMAFLVDNGK
     GPNESLPPPP NDLPKC
//