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LAC1_CRYPA
ID   LAC1_CRYPA              Reviewed;         591 AA.
AC   Q03966;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=Urishiol oxidase;
DE   Flags: Precursor;
GN   Name=LAC-1;
OS   Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC   Cryphonectria-Endothia species complex; Cryphonectria.
OX   NCBI_TaxID=5116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1535523; DOI=10.1094/mpmi-5-119;
RA   Choi G.H., Larson T.G., Nuss D.L.;
RT   "Molecular analysis of the laccase gene from the chestnut blight fungus and
RT   selective suppression of its expression in an isogenic hypovirulent
RT   strain.";
RL   Mol. Plant Microbe Interact. 5:119-128(1992).
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}.
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DR   EMBL; M73257; AAA33105.1; -; Genomic_DNA.
DR   EMBL; S38903; AAA09235.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q03966; -.
DR   SMR; Q03966; -.
DR   CAZy; AA1; Auxiliary Activities 1.
DR   OMA; WTINGTS; -.
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; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Copper; Disulfide bond; Glycoprotein; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..591
FT                   /note="Laccase"
FT                   /id="PRO_0000002920"
FT   DOMAIN          66..189
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          198..356
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          416..551
FT                   /note="Plastocyanin-like 3"
FT   BINDING         126
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         128
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         171
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         173
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         463
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         466
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         468
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         533
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         534
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         535
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         539
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        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        147..571
FT                   /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT   DISULFID        332..366
FT                   /evidence="ECO:0000250|UniProtKB:Q70KY3"
SQ   SEQUENCE   591 AA;  64696 MW;  B2F44CB2AAD77701 CRC64;
     MPSFFRALFS GLIASQLSWA APSLLHPLEP RQQPNCNTAS NRACWISGSY DITTDYEVKT
     PLTGVVRQYD LTLTQAENWL GPDGVVKEDV MLVNGNILGP VIHAQWGDTI SVTVTNNLKY
     NGTTIHWHGI RQLNTNLQDG VNGITECPIP PNGGSKTYTF IAHQYGTSWY HSHFSAQYGN
     GIVGAIQIDG PASLPYDIDL GPLVLSDYYY KTADELVVYT QSNAPPASDN VLFNGTNINP
     ANTTQGQYKT ITLTPGKRHR LRIINTSVEN NFQVSIVGHS MTVIESDFVP VDSFTTDSLF
     VGIGQRYDVT IDASQATDNY WMNVTFGGGG FCGKSNNPYP AAIIHYNGAS NSHPTNKGVA
     PADHECLDLL NLVPVVPRSI PTSGFVAASD NTLDVQLSTT TRKWTINGST LDVDWGHPIT
     QYVINKSTAW PSTDNVWLVE EANQWAYWLI ENDPTATGNA LPHPIHLHGH DFVVLGRSPN
     VSPTAQTPYT FTSSDVSSLN GNNPIRRDVV MLPPKGWLLI AFQTTNPGAW LMHCHIAWHV
     SAGLGNTFLE QPSAFVAGLN TNDVNQLNSQ CKSWNAYYPS KDIFKQDDSG V
 
 
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