ID V4L8Y9_EUTSA Unreviewed; 558 AA. AC V4L8Y9; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-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=EUTSA_v10015593mg {ECO:0000313|EMBL:ESQ40099.1}; OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema. OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ40099.1, ECO:0000313|Proteomes:UP000030689}; RN [1] {ECO:0000313|EMBL:ESQ40099.1, ECO:0000313|Proteomes:UP000030689} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23518688; DOI=10.3389/fpls.2013.00046; RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J., RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A., RA Mitchell-Olds T., Schumaker K.S., Wang X.; RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum."; RL Front. Plant Sci. 4:46-46(2013). 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; KI517464; ESQ40099.1; -; Genomic_DNA. DR RefSeq; XP_006398646.1; XM_006398583.1. DR STRING; 72664.XP_006398646.1; -. DR GeneID; 18019469; -. DR KEGG; eus:EUTSA_v10015593mg; -. DR eggNOG; KOG1263; Eukaryota. DR OrthoDB; 454773at2759; -. DR Proteomes; UP000030689; 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 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:UP000030689}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361119}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|RuleBase:RU361119" FT CHAIN 23..558 FT /note="Laccase" FT /evidence="ECO:0000256|RuleBase:RU361119" FT /id="PRO_5005148428" FT DOMAIN 33..144 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT DOMAIN 158..307 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF00394" FT DOMAIN 425..541 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07731" SQ SEQUENCE 558 AA; 61267 MW; F0C165FE91206415 CRC64; MEFPIRILVI FALLAFPACV HGAIRKYTFN VITKQVTRLC STKQIVTVNG KFPGPTIYAN EDDTILVNVV NNVKYNVSIH WHGIRQLRTG WADGPAYITQ CPIKPGHSYV YNFTVTGQRG TLWWHAHVLW LRATVHGAIV ILPKPGLPYP FPKPHREEVI VLGEWWKSDT ETVVNEALKS GLAPNVSDAH VINGHPGLVP NCPSQGNFKL AVESGKTYML RLVNAAMNEE LFFKIAGHRF TVVEVDAVYV KPFTTDTILI APGQTTTALV SAARPSGQYL IAAAPFQDSA VVAVDNRTAT ATVHYSGTFS ATATKTTSPP PQNATSVANS FVNSLRSLNS ITYPAKVPIT VDHDLLFTVG LGINRCHSCK AGNFSRVVAA INNITFKMPK TALLQAHYFN LTGIYTTDFP AKPRRFFDFT GKPPSNLATM KATKLYKLPY NSTVQVVLQD TGNVAPENHP IHLHGFNFFV VGLGSGNYNS KKDSKKFNLV DPVERNTVGV PSGGWAAIRF RADNPGVWFM HCHLEVHTTW GLKMAFLVEN GKGPNQSILP PPSDLPKC //