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LAC2_BOTFU
ID   LAC2_BOTFU              Reviewed;         581 AA.
AC   Q96WM9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Laccase-2;
DE            EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 2;
DE   AltName: Full=Diphenol oxidase 2;
DE   AltName: Full=Urishiol oxidase 2;
DE   Flags: Precursor;
GN   Name=lcc2;
OS   Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=40559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=SAS56;
RX   PubMed=11929539; DOI=10.1046/j.1365-2958.2002.02801.x;
RA   Schouten A., Wagemakers L., Stefanato F.L., van der Kaaij R.M.,
RA   van Kan J.A.L.;
RT   "Resveratrol acts as a natural profungicide and induces self-intoxication
RT   by a specific laccase.";
RL   Mol. Microbiol. 43:883-894(2002).
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   -!- INDUCTION: By resveratrol and tannins. {ECO:0000269|PubMed:11929539}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR   EMBL; AF243855; AAK77953.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96WM9; -.
DR   SMR; Q96WM9; -.
DR   CAZy; AA1; Auxiliary Activities 1.
DR   OMA; QNEQHPF; -.
DR   PHI-base; PHI:552; -.
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   2: Evidence at transcript level;
KW   Copper; Disulfide bond; Glycoprotein; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..581
FT                   /note="Laccase-2"
FT                   /id="PRO_0000267638"
FT   DOMAIN          74..191
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          197..353
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          413..547
FT                   /note="Plastocyanin-like 3"
FT   BINDING         125
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         127
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         169
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="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT   BINDING         464
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         467
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         469
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         526
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         527
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         528
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         532
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        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        146..562
FT                   /evidence="ECO:0000250|UniProtKB:Q70KY3"
SQ   SEQUENCE   581 AA;  63434 MW;  674947DAFD6BC757 CRC64;
     MKYSTVFTAL TALFAQASAT AIPAVRSPLA PRQSTTASCA NSATSRSCWG EYSIDTNWYD
     VTPNTGVTRE YWLSVENSTI TPDGYTRSAM TFNGTVPGPA ITADWGDNLI IHVTNNLQHN
     GTSIHWHGIR QLGSLEYDGV PGVTQCPIAP GDTLTYKFQA TQYGTTWYHS HFSLQYADGL
     FGPLIINGPA TADYDEDVGA IFLQDWAHKS VFEIWDSARQ GAPPALENTL MNGTNIYDCS
     ASTDANCVGG GKKFELTFVE GTKYRLRLIN VGIDSHFEFA IDNHTLTVIA NDLVPIVPYT
     TDTLLIGIGQ RYDVIVEANA AADNYWIRGN WGTTCSSNSE AANATGILRY DSSSTVDPTS
     VGVTPRGTCA DEPVASLVPH LALDVGGYSL VDEQVSFAFT NYFTWTINSS SLLLDWSSPT
     TLKIFNNETI FPTDYNVVAL NQTDANEEWV VYVIEDLTGF GIWHPIHLHG HDFYVVAQET
     DVFSATKSPA NFNLVNPPRR DVAALPGNGY LAIAFKLDNP GSWLLHCHIA WHASEGLAMQ
     FVESQSSIAI GMSDTDIFED TCANWNAYTP TELFAEDDSG I
 
 
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