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Database: UniProt
Entry: A0A2T7DJB2_9POAL
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ID   A0A2T7DJB2_9POAL        Unreviewed;       525 AA.
AC   A0A2T7DJB2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   08-NOV-2023, entry version 21.
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=GQ55_5G231000 {ECO:0000313|EMBL:PUZ55670.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ55670.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ55670.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CM009753; PUZ55670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7DJB2; -.
DR   EnsemblPlants; PUZ55670; PUZ55670; GQ55_5G231000.
DR   Gramene; PUZ55670; PUZ55670; GQ55_5G231000.
DR   Proteomes; UP000244336; Chromosome 5.
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: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, 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361119};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244336};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119}.
FT   DOMAIN          2..111
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          128..274
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          375..508
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   525 AA;  57129 MW;  301287D83540F59B CRC64;
     MSNVSRLCHA KSMVTVNGSF PGPTLYAREG DRVVVTVTNR AAHNVTIHWH GLKQRRNGWA
     DGPAYVTQCP IRPGGSYVYD FNVTGQRGTL WWHAHIAWLR ATVHGAIVVL PARGVPYPFP
     KPDAEAEIIL GEWWHADVEA VEEQGRMLGM APNTSDAHTI NGKPGPLFPC SEKHTYALEV
     QWGRTYLLRI VNAAVNDELF FSIAGHIMTV VEIDATYTKP LTASTIHLSP GQTTNVLVRA
     DRRPGRYFMA VKPFNDVPVP ADNKTATAIL QYAGVPASVL PAAPQLMPDA NGTGFVAAFH
     DRLRSLNSAR YPAAVPLAVD RHLLYTIGLN IDPCASCPNG SRLAASLNNI TFVMPRVALL
     QAHYGGLRGV FAADFPDRPP ARFNYTGAPL TAGLGTSPGT RLSRVAYNAS VELVLQDTSL
     LSVESHPFHL HGYNFFVVGR GAGNFDPSRD PAKYNLVDPP ERNTVGVPAG GWAAIRFRAD
     NPGIWFLHCH LEVHTSWGLK MAFLVEDGDG PDESVVPPPK DLPEC
//
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