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Database: UniProt
Entry: D7SKM1_VITVI
LinkDB: D7SKM1_VITVI
Original site: D7SKM1_VITVI 
ID   D7SKM1_VITVI            Unreviewed;       566 AA.
AC   D7SKM1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   OrderedLocusNames=VIT_06s0004g04050 {ECO:0000313|EMBL:CBI16199.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI16199.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN594951; CBI16199.3; -; Genomic_DNA.
DR   AlphaFoldDB; D7SKM1; -.
DR   SMR; D7SKM1; -.
DR   STRING; 29760.D7SKM1; -.
DR   PaxDb; 29760-VIT_06s0004g04050-t01; -.
DR   EnsemblPlants; Vitvi06g00405_t001; Vitvi06g00405_P001; Vitvi06g00405.
DR   Gramene; Vitvi06g00405_t001; Vitvi06g00405_P001; Vitvi06g00405.
DR   eggNOG; KOG1263; Eukaryota.
DR   HOGENOM; CLU_006504_6_3_1; -.
DR   InParanoid; D7SKM1; -.
DR   OMA; HWHGQHH; -.
DR   Proteomes; UP000009183; Chromosome 6.
DR   ExpressionAtlas; D7SKM1; baseline and differential.
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:SF417; LACCASE-17; 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:UP000009183};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119}.
FT   DOMAIN          26..139
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          151..301
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          422..548
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   566 AA;  62296 MW;  051870D9AD7592C5 CRC64;
     MALCLLPELA LAQDSGITRH YKFDIKLQNV TRLCHTKSIL TVNGQFPGPR IVAREGDRLL
     IKVVNHVQNN ISIHWHGIRQ LRSGWADGPA YVTQCPIQTG QSYVYNFTVV GQRGTLFWHA
     HISWLRSTLY GPLIILPKRN VPYPFEKPHK EVPIIFGEWW NADTEAVISQ ALQTGGGPNV
     SDAYTINGLP GPLYNCSAKD TFKLRVKASK TYLLRLINAA LNDELFFSIA NHTLTVVDAD
     AIYVKPFETD TLLIAPGQTT NVLLKTKPHF PNAAFLITAR PYVTGLGTFD NSTVAGILEY
     ELPSASPHST VSIKKLPLFK PTLPPLNDTS FATNFTNRLR SLASPQFPAN VPQKVDRHFF
     FTIGLGTSPC DQNQTCQGPN GTKFAASVNN VSFASSTTAL LQAHFSGQSN GVYNPDFPIT
     PIIPFNYTGT PPNNTLVSNG TKVVVLPFNT SVELVMQDTS ILGAESHPLH LHGFNFFVVG
     QGFGNYDPNK DPANFNLVDP IERNTVGVPS GGWVAIRFLA DNPGVWFMHC HLEIHTSWGL
     KMAWVVLDGK LPNQKLLPPP ADLPKC
//
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