ID A0A058ZTN6_EUCGR Unreviewed; 556 AA. AC A0A058ZTN6; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 29-MAY-2024, entry version 51. 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}; 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., Rokhsar D.S.; RT "The genome of Eucalyptus grandis."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAK2632305.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2632305.1}; 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). RN [3] {ECO:0000313|EMBL:KAK2632305.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2632305.1}; RA Myburg A., Grattapaglia D., Tuskan G., Hellsten U., Hayes R., Grimwood J., RA Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D., Dubchak I., RA Poliakov A., Mizrachi E., Kullan A., Hussey S., Pinard D., Van D., RA Singh P., Van J., Silva-Junior O., Togawa R., Pappas M., Faria D., RA Sansaloni C., Petroli C., Yang X., Ranjan P., Tschaplinski T., Ye C., RA Li T., Sterck L., Vanneste K., Murat F., Soler M., Clemente H., Saidi N., RA Cassan-Wang H., Dunand C., Hefer C., Bornberg-Bauer E., Kersting A., RA Vining K., Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A., RA Liston A., Spatafora J., Dharmwardhana P., Raja R., Sullivan C., RA Romanel E., Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., RA Kudrna D., Brommonschenkel S., Pasquali G., Byrne M., Rigault P., RA Tibbits J., Spokevicius A., Jones R., Steane D., Vaillancourt R., Potts B., RA Joubert F., Barry K., Pappas G., Strauss S., Jaiswal P., RA Grima-Pettenati J., Salse J., Van D., Rokhsar D., Schmutz J.; RT "WGS assembly of Eucalyptus grandis."; RL Submitted (FEB-2023) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KAK2632305.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2632305.1}; 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 D.M., Singh P., Van J.I., Silva-Junior O.B., Togawa R.C., Pappas M.R., RA Faria D.A., Sansaloni C.P., Petroli C.D., Yang X., Ranjan P., RA Tschaplinski T.J., Ye C.Y., Li T., Sterck L., Vanneste K., Murat F., RA Soler M., 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., Potts B.M., RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P., RA Grima-Pettenati J., Salse J., Van D.P., Rokhsar D.S., Schmutz J.; RL Submitted (JUL-2023) to the EMBL/GenBank/DDBJ databases. 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}. 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; MU848571; KAK2632305.1; -; Genomic_DNA. DR EMBL; KK199087; KCW44721.1; -; Genomic_DNA. DR RefSeq; XP_010041000.1; XM_010042698.1. DR AlphaFoldDB; A0A058ZTN6; -. DR STRING; 71139.A0A058ZTN6; -. DR EnsemblPlants; KCW44721; KCW44721; EUGRSUZ_L01734. DR GeneID; 104429900; -. DR Gramene; KCW44721; KCW44721; EUGRSUZ_L01734. DR KEGG; egr:104429900; -. DR eggNOG; KOG1263; Eukaryota. DR InParanoid; A0A058ZTN6; -. DR OrthoDB; 449862at2759; -. 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; Cupredoxins - blue copper proteins; 3. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR001117; Cu-oxidase_2nd. DR InterPro; IPR011706; Cu-oxidase_C. DR InterPro; IPR045087; Cu-oxidase_fam. 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 NCBIfam; TIGR03389; laccase; 1. DR PANTHER; PTHR11709:SF370; LACCASE-4; 1. DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR SUPFAM; SSF49503; Cupredoxins; 3. 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|ARBA:ARBA00023008, 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 31..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 410..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 //