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Reviewed, UniProtKB/Swiss-Prot O59896 (LAC1_PYCCI)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Laccase
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase
    Urishiol oxidase
    Diphenol oxidase
    Ligninolytic phenoloxidase
Gene names
Name: LCC3-1
Synonyms: LAC3, LCC1
OrganismPycnoporus cinnabarinus (Cinnabar-red polypore)
Taxonomic identifier5643 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Aphyllophorales › Polyporaceae › Pycnoporus

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Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Most probably plays an important role in lignin degradation. Cleaves the C-C and C-O bonds of some phenolic lignin model compounds (such as O- and P-quinols, aminophenols and phenylenediamine). May also be involved in synthesis of phenoxazinone pigments.

Catalytic activity

4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secreted.

Induction

By lignosulfonate, veratryl alcohol and 2,5-xylidine.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

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Ontologies

Keywords

   Biological processLignin degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 518497Laccase
PRO_0000002934

Regions

Domain23 – 148126Plastocyanin-like 1
Domain160 – 302143Plastocyanin-like 2
Domain369 – 489121Plastocyanin-like 3

Sites

Metal binding851Copper 1; type 2 By similarity
Metal binding871Copper 2; type 3 By similarity
Metal binding1301Copper 2; type 3 By similarity
Metal binding1321Copper 3; type 3 By similarity
Metal binding4161Copper 4; type 1 By similarity
Metal binding4191Copper 1; type 2 By similarity
Metal binding4211Copper 3; type 3 By similarity
Metal binding4711Copper 3; type 3 By similarity
Metal binding4721Copper 4; type 1 By similarity
Metal binding4731Copper 2; type 3 By similarity
Metal binding4771Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation2291N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3481N → S in AAN71597. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
O59896-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 31B4386AFDB8DF9D

FASTA51855,986
        10         20         30         40         50         60 
MSRFQSLLSF VLVSLAAVAN AAIGPVADLT LTNAAVSPDG FSREAVVVNG ITPAPLIAGQ 

        70         80         90        100        110        120 
KGDRFQLNVI DNLTNHTMLK TTSIHWHGFF QHGTNWADGV SFVNQCPIAS GHSFLYDFQV 

       130        140        150        160        170        180 
PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP NDPQASLYDI DNDDTVITLA DWYHVAAKLG 

       190        200        210        220        230        240 
PRFPLGADAT LINGLGRSPG TTTADLAVIK VTQGKRYRFR LVSLSCDPNH TFSIDGHTMT 

       250        260        270        280        290        300 
VIEADSVNTQ PLEVDSIQIF AAQRYSFVLD ASQPVDNYWI RANPAFGNVG FAGGINSAIL 

       310        320        330        340        350        360 
RYDGAPEVEP TTTQTTSTKP LNEADLHPLT PMPVPGRPEA GGVDKPLNMV FNFNGTNFFI 

       370        380        390        400        410        420 
NNHSFVPPSV PVLLQILSGA QAAQDLVPDG SVYVLPSNSS IEISFPATAN APGTPHPFHL 

       430        440        450        460        470        480 
HGHTFAVVRS AGSSEYNYDN PIFRDVVSTG QPGDNVTIRF QTNNPGPWFL HCHIDFHLEA 

       490        500        510 
GFAVVLAEDT PDTAAVNPVP QSWSDLCPIY DALDPSDL

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References

[1]"Molecular analysis of a laccase gene from the white rot fungus Pycnoporus cinnabarinus."
Eggert C., LaFayette P.R., Temp U., Eriksson K.-E.L., Dean J.F.D.
Appl. Environ. Microbiol. 64:1766-1772(1998) [PubMed: 9572949] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 200478 / PB.
Tissue: Mycelium.
[2]"Cloning, characterization and expression of laccase gene from white rot fungus Pycnoporus cinnabarinus."
Dhawan S., Lal R., Kuhad R.C.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Molecular biological monitoring of soil fungi with laccase genes."
Luis P., Buscot F.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 85-131.
Tissue: Mycelium.
[4]"The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase."
Eggert C., Temp U., Eriksson K.-E.L.
Appl. Environ. Microbiol. 62:1151-1158(1996) [PubMed: 8919775] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-42, CHARACTERIZATION, INDUCTION.
Strain: ATCC 200478 / PB.
Tissue: Mycelium.

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Cross-references

Sequence databases

AF025481 Genomic DNA. Translation: AAC39469.1.
AY147188 Genomic DNA. Translation: AAN71597.1.
AJ420334 mRNA. Translation: CAD12461.1.

3D structure databases

HSSPHSSP built from PDB template 1KYA based on UniProtKB Q96UT7.
SMRO59896. Positions 22-517.
ModBaseSearch...

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLAC1_PYCCI
AccessionPrimary (citable) accession number: O59896
Secondary accession number(s): Q8J1Y2, Q8WZN9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: August 1, 1998
Last modified: November 25, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents