ID K3ZHT5_SETIT Unreviewed; 597 AA.
AC K3ZHT5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN Name=101762817 {ECO:0000313|EnsemblPlants:KQK95582};
GN ORFNames=SETIT_8G209600v2 {ECO:0000313|EMBL:RCV39267.1};
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:RCV39267.1};
RN [1] {ECO:0000313|EMBL:RCV39267.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK95582,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV39267.1};
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:RCV39267.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV39267.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK95582}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK95582};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000256|ARBA:ARBA00002075}.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; AGNK02005183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003535; RCV39267.1; -; Genomic_DNA.
DR RefSeq; XP_004980796.2; XM_004980739.2.
DR AlphaFoldDB; K3ZHT5; -.
DR EnsemblPlants; KQK95582; KQK95582; SETIT_026137mg.
DR GeneID; 101762817; -.
DR Gramene; KQK95582; KQK95582; SETIT_026137mg.
DR KEGG; sita:101762817; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR InParanoid; K3ZHT5; -.
DR OMA; MAPSNLC; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000004995; Chromosome VIII.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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; 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 PANTHER; PTHR11709:SF253; LACCASE; 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};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..597
FT /note="laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010127829"
FT DOMAIN 38..151
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 162..291
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 442..576
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 597 AA; 65338 MW; 8258EDC2DCFD5DFC CRC64;
MAKFSMAASN LCVAIVALAA VAAAAVGEAA AVEHTFVVSE MKMTHLCNET LVTVVNGQLP
GPAIEVTEGD SVAVHVVNKS PHNITIHWHG LKQRLNCWAD GVPMVTQCPI RPGHNFTYRL
NVTGQEGTLW WHAHVSCLRA SLHGAFIIRP RHAYPFPKPD KEIPIVIGEW WSMNLAQLAK
NMEDGYYDDS SSATTINGKL GDLYNCSGVV EDGLVLDVEP GKTYLLRLLN AALYSEYYVK
IAGHEFTVVS ADANYVRPFT TDVVAIGPGE TLDALVVANA IPGRYYMVAV GGQAPKPDIQ
IPETRSRATV RYAIGAGNGD EAAPPVAPEM PDQHDFMVSF NFHGNLSSLN RPGSPPVPAT
ADESLFVVLR MGSICRRGRL SCKRSGSKES IIVETMNNVS FQLPAVAAAT PLLEELYYDH
RRNGTVGGSG LDQLYTLPDR PARPFNYTDR ALIPWGPNEA WLEPTEKAAL ARRFRHGAVV
DIVFQNAAMM DTDNHPMHLH GHDMFVLAQG HDNYDTVRDV ARYNLVDPPL KNTVLVPRLG
WAAVRFLADN PGVWYMHCHY ELHVSIGMAA VFIIEDGPTL ESALPPPPVD FPKCDQQ
//
