ID A0A368QHM9_SETIT Unreviewed; 407 AA.
AC A0A368QHM9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SETIT_3G218000v2 {ECO:0000313|EMBL:RCV17413.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV17413.1};
RN [1] {ECO:0000313|EMBL:RCV17413.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV17413.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV17413.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV17413.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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|RuleBase:RU361119}.
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DR EMBL; CM003530; RCV17413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368QHM9; -.
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; cd13875; CuRO_2_LCC_plant; 1.
DR CDD; cd13897; CuRO_3_LCC_plant; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2.
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; IPR034285; CuRO_2_LCC.
DR InterPro; IPR034289; CuRO_3_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 SUPFAM; SSF49503; Cupredoxins; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119}.
FT DOMAIN 1..149
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 259..389
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 407 AA; 43713 MW; C698853FEE109E70 CRC64;
MLGEWFNADP EAVIRQALQT GGGPNVSDAY TFNGLPGPTY NACSAGDTFR LRVRPGRTYM
LRLVNAALND ELFFAVANHT LTVVGADASY VKPFTAATLV ISPGQTMDVL LTAAAATPPS
PAYAIAVAPY TNTVGTFDNT TAVAALEYAP QAALRGLPLP ALPLYNDTGA VANFSANFRS
LASAQYPARV PRTVDRKFFF AVGLGADPCP SRVNGTCQGP NGTRFAASMN NVSFTMPKTS
LLQAHYQRRY SGVLTANFPA MPPMTFNYTG TPPNNTFVTH GTRVVPLRYN TTVEVVLQDT
SILGAESHPL HLHGYDFYVV GTGFGNYDAN NDTAKYNLVD PVQRNTISVP TAGWVAIRFV
ADNPGVWIMH CHLDVHLSWG LAMAWLVNDG PLPNQKLPPP PSDIPKC
//
