ID   A0A058ZTN6_EUCGR        Unreviewed;       556 AA.
AC   A0A058ZTN6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   02-DEC-2020, entry version 37.
DE   RecName: Full=Laccase {ECO:0000256|ARBA:ARBA00012297, ECO:0000256|RuleBase:RU361119};
DE            EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297, 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW44721.1, ECO:0000313|Proteomes:UP000030711};
RN   [1] {ECO:0000313|Proteomes:UP000030711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BRASUZ1 {ECO:0000313|Proteomes:UP000030711};
RX   PubMed=24919147; DOI=10.1038/nature13308;
RA   Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA   Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA   Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA   van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA   Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA   Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA   Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA   Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA   Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA   Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA   Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA   Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA   Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA   Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA   Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT   "The genome of Eucalyptus grandis.";
RL   Nature 510:356-362(2014).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. {ECO:0000256|RuleBase:RU361119}.
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:0000256|ARBA:ARBA00000349,
CC         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. {ECO:0000256|RuleBase:RU361119};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|ARBA:ARBA00004271, ECO:0000256|RuleBase:RU361119}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609, ECO:0000256|RuleBase:RU361119}.
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DR   EMBL; KK199087; KCW44721.1; -; Genomic_DNA.
DR   RefSeq; XP_010041000.1; XM_010042698.1.
DR   STRING; 71139.XP_010041000.1; -.
DR   GeneID; 104429900; -.
DR   KEGG; egr:104429900; -.
DR   eggNOG; KOG1263; Eukaryota.
DR   OrthoDB; 454773at2759; -.
DR   Proteomes; UP000030711; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd13849; CuRO_1_LCC_plant; 1.
DR   CDD; cd13875; CuRO_2_LCC_plant; 1.
DR   CDD; cd13897; CuRO_3_LCC_plant; 1.
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; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034288; CuRO_1_LCC.
DR   InterPro; IPR034285; CuRO_2_LCC.
DR   InterPro; IPR034289; CuRO_3_LCC.
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|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU361119};
KW   Copper {ECO:0000256|RuleBase:RU361119};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lignin degradation {ECO:0000256|ARBA:ARBA00023185,
KW   ECO:0000256|RuleBase:RU361119};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361119};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030711};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119};
KW   Signal {ECO:0000256|RuleBase:RU361119}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361119"
FT   CHAIN           22..556
FT                   /note="Laccase"
FT                   /evidence="ECO:0000256|RuleBase:RU361119"
FT                   /id="PRO_5005102132"
FT   DOMAIN          32..143
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          156..305
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          414..539
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
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
//