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LAC5_TRAVE
ID   LAC5_TRAVE              Reviewed;         527 AA.
AC   Q12717;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Laccase-5;
DE            EC=1.10.3.2 {ECO:0000250|UniProtKB:Q70KY3};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 5;
DE   AltName: Full=Diphenol oxidase 5;
DE   AltName: Full=Laccase IV;
DE   AltName: Full=Urishiol oxidase 5;
DE   Flags: Precursor;
GN   Name=LCC5; Synonyms=LCCIV;
OS   Trametes versicolor (White-rot fungus) (Coriolus versicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 20869 / PAP 52 / 52J;
RX   PubMed=9322748; DOI=10.1016/s0378-1119(97)00215-1;
RA   Ong E., Pollock W.B., Smith M.;
RT   "Cloning and sequence analysis of two laccase complementary DNAs from the
RT   ligninolytic basidiomycete Trametes versicolor.";
RL   Gene 196:113-119(1997).
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; U44431; AAC49829.1; -; mRNA.
DR   AlphaFoldDB; Q12717; -.
DR   SMR; Q12717; -.
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; 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.
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..527
FT                   /note="Laccase-5"
FT                   /id="PRO_0000002942"
FT   DOMAIN          25..150
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          162..306
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          373..498
FT                   /note="Plastocyanin-like 3"
FT   BINDING         87
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         89
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         132
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         134
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         480
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="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWU3"
FT   BINDING         482
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         486
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        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
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        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..516
FT                   /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT   DISULFID        140..230
FT                   /evidence="ECO:0000250|UniProtKB:D0VWU3"
SQ   SEQUENCE   527 AA;  56094 MW;  D9597491F1F79825 CRC64;
     MGKFHSFVNV VALSLSLSGR VFGAIGPVTD LTISNADVTP DGITRAAVLA GGVFPGPLIT
     GNKGDEFQIN VIDNLTNETM LKSTTIHWHG IFQAGTNWAD GAAFVNQCPI ATGNSFLYDF
     TVPDQAGTFW YHSHLSTQYC DGLRGPLVVY DPDDANASLY DVDDDTTVIT LADWYHTAAK
     LGPAFPAGPD SVLINGLGRF SGDGGGATNL TVITVTQGKR YRFRLVSISC DPNFTFSIDG
     HNMTIIEVGG VNHEALDVDS IQIFAGQRYS FILNANQSID NYWIRAIPNT GTTDTTGGVN
     SAILRYDTAE EIEPTTNATT SVIPLTETDL VPLDNPAAPG DPQVGGVDLA MSLDFSFNGS
     NFFINNETFV PPTVPVLLQI LSGAQDAASL LPNGSVYTLP SNSTIEISFP IITTDGALNA
     PGAPHPFHLH GHTFSVVRSA GSSTFNYANP VRRDTVSTGN SGDNVTIRFT TDNPGPWFLH
     CHIDFHLDAG FAIVFAEDTA DTASANPVPT AWSDLCPTYD ALDSSDL
 
 
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