LAC1_PYCCI
ID LAC1_PYCCI Reviewed; 518 AA.
AC O59896; Q8J1Y2; Q8WZN9;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Laccase;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase;
DE AltName: Full=Diphenol oxidase;
DE AltName: Full=Ligninolytic phenoloxidase;
DE AltName: Full=Urishiol oxidase;
DE Flags: Precursor;
GN Name=LCC3-1; Synonyms=LAC3, LCC1;
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 200478 / PB; TISSUE=Mycelium;
RX PubMed=9572949; DOI=10.1128/aem.64.5.1766-1772.1998;
RA Eggert C., LaFayette P.R., Temp U., Eriksson K.-E.L., Dean J.F.D.;
RT "Molecular analysis of a laccase gene from the white rot fungus Pycnoporus
RT cinnabarinus.";
RL Appl. Environ. Microbiol. 64:1766-1772(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Dhawan S., Lal R., Kuhad R.C.;
RT "Cloning, characterization and expression of laccase gene from white rot
RT fungus Pycnoporus cinnabarinus.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE OF 85-131.
RC TISSUE=Mycelium;
RA Luis P., Buscot F.;
RT "Molecular biological monitoring of soil fungi with laccase genes.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 22-42, CHARACTERIZATION, FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 200478 / PB; TISSUE=Mycelium;
RX PubMed=8919775; DOI=10.1128/aem.62.4.1151-1158.1996;
RA Eggert C., Temp U., Eriksson K.-E.L.;
RT "The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus:
RT purification and characterization of the laccase.";
RL Appl. Environ. Microbiol. 62:1151-1158(1996).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products (By similarity). Cleaves the C-C and C-O bonds of some
CC phenolic lignin model compounds (such as O- and P-quinols, aminophenols
CC and phenylenediamine) (PubMed:8919775). May also be involved in
CC synthesis of phenoxazinone pigments (PubMed:9572949).
CC {ECO:0000250|UniProtKB:Q70KY3, ECO:0000269|PubMed:8919775,
CC ECO:0000303|PubMed:9572949}.
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:0000250|UniProtKB:Q70KY3};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q70KY3};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
CC -!- INDUCTION: By lignosulfonate, veratryl alcohol and 2,5-xylidine.
CC {ECO:0000269|PubMed:8919775}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AF025481; AAC39469.1; -; Genomic_DNA.
DR EMBL; AY147188; AAN71597.1; -; Genomic_DNA.
DR EMBL; AJ420334; CAD12461.1; -; mRNA.
DR AlphaFoldDB; O59896; -.
DR SMR; O59896; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR GO; GO:0005576; C:extracellular region; 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 Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:8919775"
FT CHAIN 22..518
FT /note="Laccase"
FT /id="PRO_0000002934"
FT DOMAIN 23..148
FT /note="Plastocyanin-like 1"
FT DOMAIN 160..302
FT /note="Plastocyanin-like 2"
FT DOMAIN 369..489
FT /note="Plastocyanin-like 3"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 132
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 416
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 419
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 421
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 471
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 472
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 473
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT BINDING 477
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..507
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 138..226
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT CONFLICT 348
FT /note="N -> S (in Ref. 2; AAN71597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 55986 MW; 31B4386AFDB8DF9D CRC64;
MSRFQSLLSF VLVSLAAVAN AAIGPVADLT LTNAAVSPDG FSREAVVVNG ITPAPLIAGQ
KGDRFQLNVI DNLTNHTMLK TTSIHWHGFF QHGTNWADGV SFVNQCPIAS GHSFLYDFQV
PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP NDPQASLYDI DNDDTVITLA DWYHVAAKLG
PRFPLGADAT LINGLGRSPG TTTADLAVIK VTQGKRYRFR LVSLSCDPNH TFSIDGHTMT
VIEADSVNTQ PLEVDSIQIF AAQRYSFVLD ASQPVDNYWI RANPAFGNVG FAGGINSAIL
RYDGAPEVEP TTTQTTSTKP LNEADLHPLT PMPVPGRPEA GGVDKPLNMV FNFNGTNFFI
NNHSFVPPSV PVLLQILSGA QAAQDLVPDG SVYVLPSNSS IEISFPATAN APGTPHPFHL
HGHTFAVVRS AGSSEYNYDN PIFRDVVSTG QPGDNVTIRF QTNNPGPWFL HCHIDFHLEA
GFAVVLAEDT PDTAAVNPVP QSWSDLCPIY DALDPSDL
