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Reviewed, UniProtKB/Swiss-Prot Q70KY3 (LAC1_MELAO)

Last modified December 15, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-1
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 1
    Urishiol oxidase 1
    Diphenol oxidase 1
    Ligninolytic phenoloxidase
Gene names
Name: LAC1
OrganismMelanocarpus albomyces
Taxonomic identifier204285 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariales incertae sedis › Melanocarpus

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Protein attributes

Sequence length623 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

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:

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

Abs(max)=280 nm Ref.2

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

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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 Ref.3

Traceable author statement. Source: UniProtKB

lignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextraorganismal space Ref.2

Inferred from direct assay. Source: UniProtKB

   Molecular functioncopper ion binding Ref.4

Inferred from direct assay. Source: UniProtKB

laccase activity Ref.2

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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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

1 .................................................................................................. 623
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q70KY3-1 [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

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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: 14711635] [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: 12111146] [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: 15474046] [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: 12118243] [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.

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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[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.10.3.2. 259648.

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.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: December 15, 2009
This is version 40 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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