ID A0A251MVK8_PRUPE Unreviewed; 514 AA.
AC A0A251MVK8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN ORFNames=PRUPE_8G095000 {ECO:0000313|EMBL:ONH91128.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH91128.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONH91128.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; CM007658; ONH91128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251MVK8; -.
DR EnsemblPlants; ONH91128; ONH91128; PRUPE_8G095000.
DR Gramene; ONH91128; ONH91128; PRUPE_8G095000.
DR eggNOG; KOG1263; Eukaryota.
DR Proteomes; UP000006882; Chromosome g8.
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 PANTHER; PTHR11709:SF452; LACCASE-2; 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};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..514
FT /note="laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012738712"
FT DOMAIN 38..152
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 166..295
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 363..496
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 514 AA; 57389 MW; B67262ADC5861ACF CRC64;
MAKTNSFCWG SSAFLFLCLI GFFCTPAKAT LKTYRFDVQV KNVRRLCHSK PIVTVNGMFP
GPTVYAREGD TLLVNVTNHA QYNMSIHWHG LKQHRNGWAD GPAYITQCPI KTGHSYTYNI
TITGQRGTLW WHAHIFWLRA TVYGAIVILP KQGTGFPFLQ PYKEANIVLG EWWNNDVKEV
VKQGNKLGLP PNMSDAHTIN GKPGPLFPCS EKHTYALEVE QGKMYLLRII NAALNDELFF
AIAEIDAVYT KPFASQAILI APGQTTNVLV QANQAPGRYF MAARPFMDAP VSVDNKLPLE
YCMYLFKVDR HLFYTIGLGI NQCTTCLNGT QLTAFLNNIT FVMPQIGLLQ AHYFNTKGVF
TTDFPDRPPT PFNYTGTPLT ASLGTKLGTR LSKLAFNSTV ELVLQDINLL TVESHPFHLH
GYNFFVVGTG VGNFDPKQDP AKYNLVDPPE RNTIGVPTGG WVAIRFRADN PGVWFMHCHL
ELHTSWGLKT AFVVESGKDS DHSILPPPTD LPPC
//
