ID A0A0E0CAC8_9ORYZ Unreviewed; 1115 AA.
AC A0A0E0CAC8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G34380.3};
RN [1] {ECO:0000313|EnsemblPlants:OMERI01G34380.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI01G34380.3};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI01G34380.3}
RP IDENTIFICATION.
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; A0A0E0CAC8; -.
DR EnsemblPlants; OMERI01G34380.3; OMERI01G34380.3; OMERI01G34380.
DR Gramene; OMERI01G34380.3; OMERI01G34380.3; OMERI01G34380.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_0_0_1; -.
DR Proteomes; UP000008021; Chromosome 1.
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; 2.
DR CDD; cd13875; CuRO_2_LCC_plant; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 6.
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; IPR017761; Laccase.
DR NCBIfam; TIGR03389; laccase; 2.
DR PANTHER; PTHR11709:SF339; LACCASE-6; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 2.
DR Pfam; PF07731; Cu-oxidase_2; 2.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR SUPFAM; SSF49503; Cupredoxins; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 2.
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:UP000008021};
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..1115
FT /note="Laccase"
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT /id="PRO_5005116237"
FT DOMAIN 45..147
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 159..313
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 424..562
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT DOMAIN 593..707
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 719..870
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 967..1097
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 1115 AA; 119945 MW; 8F1CBE92BB42E808 CRC64;
MSCSWMIPVF AVLAFVASVA QADVVEHTFN VAILSLPRIC QPGNTSVTAV NGRVPGPQVE
AREGDTVVIH VINDSPYNVT VHWHGVFQRG TPWADGPAMV TQCPIRPGHR YTYRFAVAGQ
EGTLWWHAHS SYMRATVYGA LVIRPRRAGG YPFPTPYEEK TVLLGEWWNG DPVALESQSF
STGIPAPNAD AYTINGMPGD SYLCPETTNR IAKFEVRRDK TYLLRIINAA LNTAFFFKVA
GHTFTVVAAD ASYTEPYATD VIVIAPGQTV DALMAADASP GCYHMAISSY QSAIPFPPRP
AGFNGNTTTA VVEYVDPAAT TDAASPVLPV MPKPNDTYTA NQFYTSLTAL IRPGRRTVPL
TVDTRMLVTV GLGFSSCQAA QTQCNRSAPV VLANMNNVSF ALPNTVSMLE ALYRNTADGV
YTRDFPDQPP VAFDYTSRGL LGNSPLASTG SPSTKVKTLR YNATVEMVLQ NTALVGLESH
PMHLHGFNFF MVAQGFGNYD GEAAGAGEFN LVNPQERNTV AVPTGGWAVI RFVADNPGMW
AMHCHIDSHF AIGLAMVFEV ESGPTPGTTL PPPPPDLPQS VADAATANYT FTVESMRVSR
LCNSTDIIAV NGQLPGPTIE VNEGDAVAVE VINGSPYNLT IHWHGILQLL TPWADGPSMV
TQCPIQPNSS YTYRFNVTGQ EGTLWWHAHS SFLRATVYGA LIIRPRNGSA YPFPAPDQEV
PIVLGEWWSR NVVDIESDAV SSGQLPRESD AFTVNGVTGE LYQCANETFT VDVQPNTTVL
LRVINAGLNT HLFFKVAGHA FTVVAVDACY TANYTTDTLV LAPGHTVDAL MVTNASAGSY
YMAVQAYDSL SPTTMAVTDD TTATAIVRYN TTSTKKNATP VMPTMPQSSD SATANAFYFG
LRGPPSPSAP AVPTKVDVNM TIELGLGQLP CDSTQSSCSG KSVAAAMNGV SFRLPSQMSL
LEAQFNRTPG VYTADFPDAP QPSGTPMVEG TKVRRLKYNS TVEIVLQNPT AFPSENHPIH
LHGFNFFVLA QGLGNFTPGN VSGYNLVDPI SRNTLAVPTG GWAVIRFVAN NPGMWFFHCH
LDAHVPMGLG MVFAVDNGTT PDSFLPPPPA DLPKC
//
