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LAC1_AGABI
ID   LAC1_AGABI              Reviewed;         520 AA.
AC   Q12541;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Laccase I;
DE   AltName: Full=Urishiol oxidase 1;
DE   Flags: Precursor;
GN   Name=lcc1;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=D649; TISSUE=Mycelium;
RX   PubMed=8360614; DOI=10.1099/00221287-139-6-1209;
RA   Perry C.R., Smith M., Britnell C.H., Wood D.A., Thurston C.F.;
RT   "Identification of two laccase genes in the cultivated mushroom Agaricus
RT   bisporus.";
RL   J. Gen. Microbiol. 139:1209-1218(1993).
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; L10664; AAC18877.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12541; -.
DR   SMR; Q12541; -.
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; 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   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..19
FT   CHAIN           20..520
FT                   /note="Laccase-1"
FT                   /id="PRO_0000002918"
FT   DOMAIN          21..145
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          157..305
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          375..488
FT                   /note="Plastocyanin-like 3"
FT   BINDING         82
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         84
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         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         129
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         417
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         420
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         422
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         470
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="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT   BINDING         472
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         476
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        108
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        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..509
FT                   /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT   DISULFID        135..229
FT                   /evidence="ECO:0000250|UniProtKB:D0VWU3"
SQ   SEQUENCE   520 AA;  58099 MW;  943DB3F23297B891 CRC64;
     MRLSNALVLV AACISSVVAK TRTFDFDLVN TRLAPDGFER DTVVINGEFP GTLIQVNKGD
     SVRIPLHNKL TSPTMRRSVS IHWHGFFQAR TSGQDGPSFV NQCPQPPNTT FTYEFSVAEQ
     SGTFWYHSHL STQYCDGLRG AFIVYDPRDP LRHLYDVDDE STVITLAEWY HILAPDATNE
     FFSSGIIPVQ DSGLINGKGR FNGGPLTPFA VVNVRRGKRY RLRVIAISCR PFFTFSVDNH
     SLVFMEADGV EHDPVEVQNV DIYAAQRVSV ILHANQPIDN YWIRAPMTGG NPDRNPNLNI
     SLTLAILRYH GARHVEPTTV NVPGHKLLDQ EMHPIRQEGP GKLGDGPPDK HITLNIAQPN
     APFFDINGIS YISPTVPVLL QILSGAKRPE DVLPSEQIFF VPKNSLIEVN IPGEGAHPFH
     LHGHNFDVVL ASNDDTFNFK NPPRRDVYPI NGGNTTFRFF TDNPGAWFLH CHIDWHLEAG
     LAIVFAEAPE DNVSGPQSQI TPQDWLDLCP EYNAIEPEFQ
 
 
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