ID A0A251T5V5_HELAN Unreviewed; 565 AA.
AC A0A251T5V5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 Name=LAC4 {ECO:0000313|EMBL:OTG05886.1};
GN ORFNames=HannXRQ_Chr12g0378591 {ECO:0000313|EMBL:OTG05886.1},
GN HanXRQr2_Chr12g0553521 {ECO:0000313|EMBL:KAF5778942.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG05886.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|EMBL:KAF5778942.1, ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5778942.1};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
RN [2] {ECO:0000313|EMBL:OTG05886.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaves {ECO:0000313|EMBL:OTG05886.1};
RA Langlade N., Munos S.;
RT "Sunflower complete genome.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF5778942.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5778942.1};
RA Gouzy J., Langlade N., Munos S.;
RT "Helianthus annuus Genome sequencing and assembly Release 2.";
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNCJ02000327; KAF5778942.1; -; Genomic_DNA.
DR EMBL; CM007901; OTG05886.1; -; Genomic_DNA.
DR STRING; 4232.A0A251T5V5; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr12g0553521; mRNA:HanXRQr2_Chr12g0553521; HanXRQr2_Chr12g0553521.
DR Gramene; mRNA:HanXRQr2_Chr12g0553521; mRNA:HanXRQr2_Chr12g0553521; HanXRQr2_Chr12g0553521.
DR InParanoid; A0A251T5V5; -.
DR OMA; HRDHEHG; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000215914; Chromosome 12.
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 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:SF417; LACCASE-17; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000215914};
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..565
FT /note="Laccase"
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT /id="PRO_5041471974"
FT DOMAIN 31..144
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 157..308
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 424..547
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 565 AA; 62602 MW; FA6BA1078F19BF77 CRC64;
MVGFVRTLVA ITLLVSVYSV AGTTRHYEFN IQLQNVTRLC HTRSMVTVNG KFPGPPIVAR
EGDRLLIKVT NNVSNNITIH WHGIRQLRSG WADGPAYVTQ CPIQTGQSYV YNYTVIGQRG
TLFWHAHISW LRASLYGPLI ILPKLSVPYP FTKPYKEVPI IFGEWFNTDP EAIIAEATQT
GGGPNVSDAY TFNGLPGPFY NCSAKDTLKL KVKHAKTYLL RLINAALNDE LFFSIANHTL
TVVEVDAIYT KPFDTETLIL APGQTTNVLL KTKLKFPGAN FVMSARPYVT GQGTFDNSTV
AGILEYESSI PMKNLPLFKP ALPPLNDTSF VTQFSNRLRS LASAQFPANV PQKIDRHLFF
TVGLGTSPCE KNKTCQGPNG TRFAASINNV SFVQPSVALL QSHYSGQSEG VYSPYFPITP
FHRFNYTGTP PNNTFVSNGT KLMVLPFNTS VELVLQDTSI LGVESHPLHL HGFNFFVVGQ
GFGNYDPNKD PKNFNLVDPI ERNTVGVPSG GWVAIRFLAD NPGVWFMHCH LEVHTSWGLK
MAWLVLDGKL PNQKLLPPPV DLPKC
//
