ID A0A0E0IX14_ORYNI Unreviewed; 567 AA.
AC A0A0E0IX14;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA11G00180.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA11G00180.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA11G00180.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA11G00180.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA11G00180.1};
RG EnsemblPlants;
RL Submitted (APR-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; A0A0E0IX14; -.
DR STRING; 4536.A0A0E0IX14; -.
DR EnsemblPlants; ONIVA11G00180.1; ONIVA11G00180.1; ONIVA11G00180.
DR Gramene; ONIVA11G00180.1; ONIVA11G00180.1; ONIVA11G00180.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR OMA; QWPIAPH; -.
DR Proteomes; UP000006591; 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; 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:SF457; LACCASE-17-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.
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 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:UP000006591};
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..22
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT CHAIN 23..567
FT /note="Laccase"
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT /id="PRO_5005115922"
FT DOMAIN 31..144
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 161..309
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 415..549
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 567 AA; 61590 MW; B085385A495488E5 CRC64;
MPSRGCSCWL LSLALLCSLA AAKEQYHEFV IRETTVKRLC KSHNIMTVNG QFPGPTLEIN
EGDSLIINLI NRGRYNMTLH WHGVRQMRTG WSDGPEYVTQ CPVRPGQSYR YRFTVAAQEG
TLWWHAHSSW LRATVYGALL IRPRDGTSYP FDVQPTRELA PILLGEWWDM NPVDVVRAAT
RTGAAPNISD ALTVNAQPGD LYSCSSHDTA VFPVTSGETN LLRFINAALN TELFVSLAGH
NMTVVAADAS YTKPYTTSLL LLAPGQTTDV LVTFDQPPGR YYLAARAYAS AQGVPFDNTT
TTAIFDYGAA NNASSAAIAM PTLPAYNDTT AATAFTTNLR GLRKAELPSR VDESLFFTVG
VGLFNCTNAT AQQCGGPNGT RFAASINNVS FVLPSSTSIL QAHHHGAPGG VFTADFPANP
PVQFDYTAQN VSRALWQPVA GTKVYKLKYG SAVQVVLQGT NIFAGENHPI HLHGYDFYIL
AEGLGNFDAG ADTAKFNMED PPMRNTVGVP VNGWAVIRFV ADNPGVWLMH CHLDVHITWG
LAMAFLVDDG VGELQSLEAP PPDLPLC
//
