ID I1PWB0_ORYGL Unreviewed; 513 AA.
AC I1PWB0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA05G0165800.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA05G0165800.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000256|ARBA:ARBA00002075,
CC 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 AlphaFoldDB; I1PWB0; -.
DR STRING; 4538.I1PWB0; -.
DR EnsemblPlants; ORGLA05G0165800.1; ORGLA05G0165800.1; ORGLA05G0165800.
DR Gramene; ORGLA05G0165800.1; ORGLA05G0165800.1; ORGLA05G0165800.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR OMA; FVMPRTS; -.
DR Proteomes; UP000007306; 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 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; IPR008972; Cupredoxin.
DR InterPro; IPR034288; CuRO_1_LCC.
DR InterPro; IPR034285; CuRO_2_LCC.
DR InterPro; IPR017761; Laccase.
DR NCBIfam; TIGR03389; laccase; 1.
DR PANTHER; PTHR11709:SF67; LACCASE-11-RELATED; 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.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU361119};
KW Copper {ECO:0000256|RuleBase:RU361119};
KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185,
KW ECO:0000256|RuleBase:RU361119};
KW Metal-binding {ECO:0000256|RuleBase:RU361119};
KW Oxidoreductase {ECO:0000256|RuleBase:RU361119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119}.
FT DOMAIN 3..112
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 125..279
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 391..497
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 513 AA; 55907 MW; E0D8ADC6C7BDF6A4 CRC64;
MATVTRLCVT KSVPTVNGQF PGPKLVVREG DTLVIRVTNN INNNVTFHWH GIRQVRSGWA
DGPAYITQCP IRPGGSYVYR FTVTGQRGTL WWHAHFSWLR ATLYGPLVIL PPRGVAYPFP
KPHREVPLLL GEWFNADPEA VIKQALQTGG GPNVSDAYTF NGLPGPTYNC SSSNDTFKLR
VRPGKTYLLR LINAALNDEL FFGVANHTLT VVQADASYVK PFAATALVIS PGQTMDVLLT
AAANNPPSRS FAIAVAPYTN TVGTFDNTTA VAVLEYYGAA TSAAALRSLL LPSLPAYNDT
GAVANFSASF RSLASAQYPA RVPRTVDRHF FFAVGLGADP CQSPVNGTCQ GPNNTRFAAS
MNNVSFVMPR TSLLQAHYQR RYNGVLAANF PAAPRTPFNY TGTPPNNTFV THGTRVVPLS
FNTTVEVVLQ DTSILGAESH PLHLHGYDFY VVGTGFGNYD ASNDTAKYNL IDPVQRNTIS
VPTAGWVAIR FVADNPGWLP ALYFYLHLKR EFL
//
