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Q70KY3 (LAC1_MELAO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laccase-1

EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 1
Diphenol oxidase 1
Ligninolytic phenoloxidase
Urishiol oxidase 1
Gene names
Name:LAC1
OrganismMelanocarpus albomyces
Taxonomic identifier204285 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariales incertae sedisMelanocarpus

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lignin degradation and detoxification of lignin-derived products Probable. Ref.3

Catalytic activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O. Ref.2

Cofactor

Binds 4 copper ions per monomer. Ref.2 Ref.4

Subunit structure

Monomer. Ref.4

Tissue specificity

Secreted protein; extracellular space. Ref.2

Sequence similarities

Belongs to the multicopper oxidase family.

Biophysicochemical properties

Absorption:

Abs(max)=280 nm Ref.2 Ref.4

Exhibits a shoulder at 360 nm, a smaller absorption peak at 450 nm, and a second, larger peak at 590 nm. Ref.4

pH dependence:

Optimum pH is 3.5 with 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) as substrate, 5.0-7.5 with guiacol as substrate, and 6.0-7.0 with syringaldazine as substrate. Ref.2

Temperature dependence:

Optimum temperature is 60-70 degrees Celsius. Ref.2

Ontologies

Keywords
   Biological processLignin degradation
   DomainSignal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Traceable author statement Ref.3. Source: UniProtKB

lignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextraorganismal space

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from direct assay Ref.4. Source: UniProtKB

hydroquinone:oxygen oxidoreductase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 5028
PRO_0000235826
Chain51 – 609559Laccase-1 Ref.4
PRO_0000235827
Propeptide610 – 62314 Ref.4
PRO_0000235828

Sites

Metal binding1431Copper 1 Ref.4
Metal binding1451Copper 2 Ref.4
Metal binding1881Copper 2 Ref.4
Metal binding1901Copper 3 Ref.4
Metal binding4811Copper 4 Ref.4
Metal binding4841Copper 1 Ref.4
Metal binding4861Copper 3 Ref.4
Metal binding5521Copper 3 Ref.4
Metal binding5531Copper 4 Ref.4
Metal binding5541Copper 2 Ref.4
Metal binding5581Copper 4 Ref.4

Amino acid modifications

Glycosylation891N-linked (GlcNAc...) Ref.4
Glycosylation1381N-linked (GlcNAc...) Ref.4
Glycosylation2511N-linked (GlcNAc...) Ref.4
Glycosylation2661N-linked (GlcNAc...) Ref.4
Glycosylation2941N-linked (GlcNAc...) Ref.4
Glycosylation3391N-linked (GlcNAc...) Ref.4
Glycosylation4261N-linked (GlcNAc...) Ref.4
Glycosylation4461N-linked (GlcNAc...) Ref.4
Disulfide bond54 ↔ 62 Ref.4
Disulfide bond164 ↔ 590 Ref.4
Disulfide bond348 ↔ 382 Ref.4

Secondary structure

........................................................................................................ 623
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q70KY3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A322F89B438784E1

FASTA62368,958
        10         20         30         40         50         60 
MKTFTSALAL VVGMLAPGAV VAAPPSTPAQ RDLVELREAR QEGGKDLRPR EPTCNTPSNR 

        70         80         90        100        110        120 
ACWSDGFDIN TDYEVSTPDT GVTQSYVFNL TEVDNWMGPD GVVKEKVMLI NGNIMGPNIV 

       130        140        150        160        170        180 
ANWGDTVEVT VINNLVTNGT SIHWHGIHQK DTNLHDGANG VTECPIPPKG GQRTYRWRAR 

       190        200        210        220        230        240 
QYGTSWYHSH FSAQYGNGVV GTIQINGPAS LPYDIDLGVF PITDYYYRAA DDLVHFTQNN 

       250        260        270        280        290        300 
APPFSDNVLI NGTAVNPNTG EGQYANVTLT PGKRHRLRIL NTSTENHFQV SLVNHTMTVI 

       310        320        330        340        350        360 
AADMVPVNAM TVDSLFLAVG QRYDVVIDAS RAPDNYWFNV TFGGQAACGG SLNPHPAAIF 

       370        380        390        400        410        420 
HYAGAPGGLP TDEGTPPVDH QCLDTLDVRP VVPRSVPVNS FVKRPDNTLP VALDLTGTPL 

       430        440        450        460        470        480 
FVWKVNGSDI NVDWGKPIID YILTGNTSYP VSDNIVQVDA VDQWTYWLIE NDPEGPFSLP 

       490        500        510        520        530        540 
HPMHLHGHDF LVLGRSPDVP AASQQRFVFD PAVDLARLNG DNPPRRDTTM LPAGGWLLLA 

       550        560        570        580        590        600 
FRTDNPGAWL FHCHIAWHVS GGLSVDFLER PADLRQRISQ EDEDDFNRVC DEWRAYWPTN 

       610        620 
PYPKIDSGLK RRRWVEESEW LVR 

« Hide

References

[1]"Molecular cloning and expression in Saccharomyces cerevisiae of a laccase gene from the ascomycete Melanocarpus albomyces."
Kiiskinen L.-L., Saloheimo M.
Appl. Environ. Microbiol. 70:137-144(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces."
Kiiskinen L.-L., Viikari L., Kruus K.
Appl. Microbiol. Biotechnol. 59:198-204(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-78; 214-228 AND 507-517, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Strain: VTT D-96490.
[3]"Laccase from Melanocarpus albomyces binds effectively to cellulose."
Kiiskinen L.-L., Palonen H., Linder M., Viikari L., Kruus K.
FEBS Lett. 576:251-255(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE FUNCTION.
[4]"Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site."
Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., Koivula A., Rouvinen J.
Nat. Struct. Biol. 9:601-605(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-609 IN COMPLEX WITH COFACTOR AND OXYGEN, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION AT ASN-89; ASN-138; ASN-251; ASN-266; ASN-294; ASN-339; ASN-426 AND ASN-446, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ571698 Genomic DNA. Translation: CAE00180.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GW0X-ray2.40A/B51-609[»]
2IH8X-ray2.00A/B51-609[»]
2IH9X-ray2.00A/B51-609[»]
2Q9OX-ray1.30A/B51-609[»]
3DKHX-ray2.40A/B51-608[»]
3FU7X-ray1.67A/B51-609[»]
3FU8X-ray1.80A/B51-609[»]
3FU9X-ray2.00A/B51-609[»]
3QPKX-ray1.90A/B51-609[»]
ProteinModelPortalQ70KY3.
SMRQ70KY3. Positions 51-609.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.420. 3 hits.
InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 3 hits.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ70KY3.

Entry information

Entry nameLAC1_MELAO
AccessionPrimary (citable) accession number: Q70KY3
Secondary accession number(s): Q7SIE6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: July 5, 2004
Last modified: October 16, 2013
This is version 58 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references