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Q01679 (LAC1_PHLRA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Laccase
EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase
Diphenol oxidase
Ligninolytic phenoloxidase
Urishiol oxidase
Gene names
Name:LAC
OrganismPhlebia radiata (White-rot fungus)
Taxonomic identifier5308 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Corticiales › Corticiaceae › Phlebia

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Most probably plays an important role in lignin degradation.

Catalytic activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

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

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

hydroquinone:oxygen oxidoreductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 520499Laccase
PRO_0000002928

Regions

Domain22 – 148127Plastocyanin-like 1
Domain160 – 304145Plastocyanin-like 2
Domain373 – 496124Plastocyanin-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 binding4181Copper 4; type 1 By similarity
Metal binding4211Copper 1; type 2 By similarity
Metal binding4231Copper 3; type 3 By similarity
Metal binding4731Copper 3; type 3 By similarity
Metal binding4741Copper 4; type 1 By similarity
Metal binding4751Copper 2; type 3 By similarity
Metal binding4791Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q01679 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: B566CE3CA2791D36

FASTA52055,704
        10         20         30         40         50         60 
MHTFLRSTAL VVAGLSARAL ASIGPVTDFH IVNAAVSPDG FSRQAVLAEG VFPGPLIAGN 

        70         80         90        100        110        120 
KGDNFQINVI DELTNATMLK TTTIHWHGFF QHGTNWADGP AFINQCPIAS GDSFLYNFQV 

       130        140        150        160        170        180 
PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP ADPYLDQYDV DDDSTVITLA DWYHTAARLG 

       190        200        210        220        230        240 
SPFPAADTTL INGLGRCGEA GCPVSDLAVI SVTKGKRYRF RLVSISCDSF FTFSIDGHSL 

       250        260        270        280        290        300 
NVIEVDATNH QPLTVDELTI YAGQRYSFIL TADQDVDNYW IRANPGIGIT TGFAGGINSA 

       310        320        330        340        350        360 
ILRYDGADVV EPTTTQATSP VVLSESNLAP LTNAAAPGLP EVGGVDLALN FNLTFDGPSL 

       370        380        390        400        410        420 
KFQINGVTFV PPTVPVLLQI LSGAQSAADL LPSGSVYALP SNATIELSLP AGALGGPHPF 

       430        440        450        460        470        480 
HLHGHTFSVV RPAGSTTYNY VNPVQRDVVS IGNTGDNVTI RFDTNNPGPW FLHCHIDWHL 

       490        500        510        520 
EAGFAVVFAE DIPDVASINP VPQDWSNLCP IYNALDASDH

« Hide

References

[1]"Isolation and structural analysis of the laccase gene from the lignin-degrading fungus Phlebia radiata."
Saloheimo M., Niku-Paavola M.L., Knowles J.K.
J. Gen. Microbiol. 137:1537-1544(1991) [PubMed: 1955850] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 64658 / 79.
[2]Saloheimo M.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO C-TERMINUS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52134 Genomic DNA. Translation: CAA36379.2.
PIRS18746.

3D structure databases

ProteinModelPortalQ01679.
SMRQ01679. Positions 22-520.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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]
SUPFAMSSF49503. Cupredoxin. 3 hits.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC1_PHLRA
AccessionPrimary (citable) accession number: Q01679
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 10, 2004
Last modified: November 16, 2011
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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