ID A0A058ZTN6_EUCGR Unreviewed; 556 AA. AC A0A058ZTN6; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 11-MAY-2016, entry version 17. 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; Myrtoideae; OC 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]. 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., RA Goodstein D.M., Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., RA Hussey S.G., Pinard D., van der Merwe K., Singh P., van Jaarsveld I., RA Silva-Junior O.B., Togawa R.C., Pappas M.R., Faria D.A., RA Sansaloni C.P., Petroli C.D., Yang X., Ranjan P., Tschaplinski T.J., RA Ye C.Y., Li T., Sterck L., Vanneste K., Murat F., Soler M., RA Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A., RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M., RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W., RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M., RA 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., RA Potts B.M., Joubert F., Barry K., Pappas G.J., Strauss S.H., RA Jaiswal P., Grima-Pettenati J., Salse J., Van de Peer Y., RA Rokhsar D.S., Schmutz J.; RT "The genome of Eucalyptus grandis."; RL Nature 509:356-362(2014). 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, ECO:0000256|SAAS:SAAS00534212}. CC -!- SIMILARITY: Contains 3 plastocyanin-like domains. CC {ECO:0000256|RuleBase:RU361119}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KK199087; KCW44721.1; -; Genomic_DNA. DR RefSeq; XP_010041000.1; XM_010042698.1. DR GeneID; 104429900; -. DR KEGG; egr:104429900; -. DR KO; K05909; -. 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: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; IPR033138; Cu_oxidase_CS. 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 Complete proteome {ECO:0000313|Proteomes:UP000030711}; KW Copper {ECO:0000256|RuleBase:RU361119, ECO:0000256|SAAS:SAAS00524507}; KW Lignin degradation {ECO:0000256|RuleBase:RU361119}; KW Metal-binding {ECO:0000256|RuleBase:RU361119, KW ECO:0000256|SAAS:SAAS00524516}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361119, KW ECO:0000256|SAAS:SAAS00524477}; KW Reference proteome {ECO:0000313|Proteomes:UP000030711}; 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_5005102132. FT DOMAIN 32 143 Plastocyanin-like. {ECO:0000259|Pfam: FT PF07732}. FT DOMAIN 156 305 Plastocyanin-like. {ECO:0000259|Pfam: FT PF00394}. FT DOMAIN 414 539 Plastocyanin-like. {ECO:0000259|Pfam: FT 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 //