位置:首页 > 蛋白库 > LAC2_AGABI
LAC2_AGABI
ID   LAC2_AGABI              Reviewed;         520 AA.
AC   Q12542;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Laccase II;
DE   AltName: Full=Urishiol oxidase 2;
DE   Flags: Precursor;
GN   Name=lcc2;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=D649;
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}.
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; L10663; AAA17035.1; -; mRNA.
DR   AlphaFoldDB; Q12542; -.
DR   SMR; Q12542; -.
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-2"
FT                   /id="PRO_0000002919"
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        241
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;  57823 MW;  EF100145F0A697AA CRC64;
     MRFSNAFVLV AACISSVLAD TKTFNFDLVN TRLAPDGFER DTVVINGEFP GTLVQVNKGD
     SVRIPVNNKL TSSTMRRSVS IHWHGFFQAR TSGQDGPAFV NQCPQPPNTT FTYEFSVADE
     SGTFWYHSHL STQYCDGLRG AFVVYDPEDP LGHLYDVDDE TTVITLAEWY HVLAPDINNE
     FFSSGIIPVQ DSGLINGKGR FNGGPETPFA VVNVEQGKRY RFRVIAISCR PFFTFSVDNH
     NLTFMEADSV EHDPVEIQNV DIYAAQRVSV ILNANQPVDN YWMRAPMTGG NPDRNPNLNI
     SLTLAILRYK GAPEVEPTTV NVPGHKLLDQ EMHPIAQEGP GKLGDGPPDK HITLNIAQPN
     APFFDINGIS YISPTVPVLL QILSGAKRPE DVLPSEQIFF VPKNSLIEVN IPGEGAHPFH
     LHGHNFDVVL ASNDDTFNFV NPPRRDVYPI NGGNTTFRFF TDNPGAWFLH CHIDWHLEAG
     LAIVFAEAPE DNVSGPQSQI TPQDWLDLCP EYNAIEPEFQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024