LAC1_PLEOS
ID LAC1_PLEOS Reviewed; 529 AA.
AC Q12729;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Laccase-1;
DE EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE AltName: Full=Benzenediol:oxygen oxidoreductase 1;
DE AltName: Full=Diphenol oxidase 1;
DE AltName: Full=Urishiol oxidase 1;
DE Flags: Precursor;
GN Name=POX1;
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Florida; TISSUE=Mycelium;
RX PubMed=7793961; DOI=10.1128/aem.61.6.2408-2413.1995;
RA Giardina P., Cannio R., Martirani L., Marzullo L., Palmieri G., Sannia G.;
RT "Cloning and sequencing of a laccase gene from the lignin-degrading
RT basidiomycete Pleurotus ostreatus.";
RL Appl. Environ. Microbiol. 61:2408-2413(1995).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products. {ECO:0000250|UniProtKB:Q70KY3}.
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 -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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; Z34847; CAA84356.1; -; mRNA.
DR EMBL; Z22591; CAA80305.1; -; Genomic_DNA.
DR PIR; S49120; S49120.
DR AlphaFoldDB; Q12729; -.
DR SMR; Q12729; -.
DR CAZy; AA1; Auxiliary Activities 1.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1089733; -.
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; IPR002355; Cu_oxidase_Cu_BS.
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; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Lignin degradation; Metal-binding;
KW Oxidoreductase; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..529
FT /note="Laccase-1"
FT /id="PRO_0000002929"
FT DOMAIN 25..159
FT /note="Plastocyanin-like 1"
FT DOMAIN 170..312
FT /note="Plastocyanin-like 2"
FT DOMAIN 380..499
FT /note="Plastocyanin-like 3"
FT BINDING 96
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 98
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 141
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 143
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 425
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 428
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 430
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 481
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 482
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 483
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 487
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 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..514
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT DISULFID 149..236
FT /evidence="ECO:0000250|UniProtKB:D0VWU3"
SQ SEQUENCE 529 AA; 56580 MW; 40110AFC4886882F CRC64;
MFPGARILAT LTLALHLLHG THAAIGPTGD MYIVNEDVSP DGFTRSAVVA RSDPTTNGTS
ETLTGVLVQG NKGDNFQLNV LNQLSDTTML KTTSIHWHGF FQSGSTWADG PAFVNQCPIA
SGNSFLYDFN VPDQAGTFWY HSHLSTQYCD GLRGPFIVYD PSDPHLSLYD VDNADTIITL
EDWYHVVAPQ NAVLPTADST LINGKGRFAG GPTSALAVIN VESNKRYRFR LISMSCDPNF
TFSIDGHSLQ VIEADAVNIV PIVVDSIQIF AGQRYSFVLN ANQTVDNYWI RADPNLGSTG
FDGGINSAIL RYAGATEDDP TTTSSTSTPL EETNLVPLEN PGAPGPAVPG GADININLAM
AFDVTNFELT INGSPFKAPT APVLLQILSG ATTAASLLPS GSIYSLEANK VVEISIPALA
VGGPHPFHLH GHTFDVIRSA GSTTYNFDTP ARRDVVNTGT DANDNVTIRF VTDNPGPWFL
HCHIDWHLEI GLAVVFAEDV TSITAPPAAW DDLCPIYDAL SDSDKGGIA
