ID M5XKH4_PRUPE Unreviewed; 558 AA.
AC M5XKH4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=PRUPE_2G245800 {ECO:0000313|EMBL:ONI24545.1};
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:ONI24545.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI24545.1, 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 -!- 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; CM007652; ONI24545.1; -; Genomic_DNA.
DR RefSeq; XP_007220829.1; XM_007220767.1.
DR AlphaFoldDB; M5XKH4; -.
DR SMR; M5XKH4; -.
DR STRING; 3760.M5XKH4; -.
DR EnsemblPlants; ONI24545; ONI24545; PRUPE_2G245800.
DR GeneID; 18787612; -.
DR Gramene; ONI24545; ONI24545; PRUPE_2G245800.
DR KEGG; pper:18787612; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR OMA; DMGCMPP; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000006882; Chromosome g2.
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:SF317; LACCASE; 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:UP000006882};
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..25
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT CHAIN 26..558
FT /note="Laccase"
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT /id="PRO_5005141109"
FT DOMAIN 37..147
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 160..309
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 408..541
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 558 AA; 61240 MW; 302FD7125F85C43D CRC64;
MESCRLHLRA MLLLVAFLYP AFVQSLVRHY KFSVVFKNTT KLCSSKPTIT VNGKFPGPTL
YAREDDTVIV RVINHVNHNL TIHWHGVRQL GTAWADGPAY ITQCPIQPGQ NFIYNFTLTG
QRGTLLWHAH TSWLRATLHG AIVILPKRGT PYPFPTPDEE KTVILAEWWK SDVEAVVNQS
IKSGLPPNVS DAHTINGHAG PVPGCSSQGG YTLHVESGKT YLLRIINAAL NDDLFFKIAG
HNLTVVEVDA SYTKPFQTDT IFISPGQTTN AILTANRGIG KYLIAASPFM DAPVGFDNLT
SIASLLYKGT PANPKAFLTS IPPQNATPVT NTFMDSLRSL NSKQYPANVP LTIDHSLFFT
IAVGVNPCAT CVNGSKLVAA FNNVSFVMPT IALLQAYYYN TKGVFTLDFP ANPPIPFNYT
GNSTANMQTT NGTRLYRLGY NSTVQIVLQG TAVIAPESHP THLHGFNFFV VGKGIGNFDP
KKDPKTFNLV DPVERNTISV PTGGWTAIRF RADNPGIWFL HCHLEVHTTW GLKMPFLVEN
GKGPNETLRP PPADLPTC
//
