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Protein

Laccase

Gene

LAC

Organism
Phlebia radiata (White-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Most probably plays an important role in lignin degradation.

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactori

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Copper 1; type 2By similarity
Metal bindingi87 – 871Copper 2; type 3By similarity
Metal bindingi130 – 1301Copper 2; type 3By similarity
Metal bindingi132 – 1321Copper 3; type 3By similarity
Metal bindingi418 – 4181Copper 4; type 1By similarity
Metal bindingi421 – 4211Copper 1; type 2By similarity
Metal bindingi423 – 4231Copper 3; type 3By similarity
Metal bindingi473 – 4731Copper 3; type 3By similarity
Metal bindingi474 – 4741Copper 4; type 1By similarity
Metal bindingi475 – 4751Copper 2; type 3By similarity
Metal bindingi479 – 4791Copper 4; type 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase
Diphenol oxidase
Ligninolytic phenoloxidase
Urishiol oxidase
Gene namesi
Name:LAC
OrganismiPhlebia radiata (White-rot fungus)
Taxonomic identifieri5308 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhlebia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 520499LaccasePRO_0000002928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ01679.
SMRiQ01679. Positions 22-520.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 148127Plastocyanin-like 1Add
BLAST
Domaini160 – 304145Plastocyanin-like 2Add
BLAST
Domaini373 – 496124Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01679-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHTFLRSTAL VVAGLSARAL ASIGPVTDFH IVNAAVSPDG FSRQAVLAEG
60 70 80 90 100
VFPGPLIAGN KGDNFQINVI DELTNATMLK TTTIHWHGFF QHGTNWADGP
110 120 130 140 150
AFINQCPIAS GDSFLYNFQV PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP
160 170 180 190 200
ADPYLDQYDV DDDSTVITLA DWYHTAARLG SPFPAADTTL INGLGRCGEA
210 220 230 240 250
GCPVSDLAVI SVTKGKRYRF RLVSISCDSF FTFSIDGHSL NVIEVDATNH
260 270 280 290 300
QPLTVDELTI YAGQRYSFIL TADQDVDNYW IRANPGIGIT TGFAGGINSA
310 320 330 340 350
ILRYDGADVV EPTTTQATSP VVLSESNLAP LTNAAAPGLP EVGGVDLALN
360 370 380 390 400
FNLTFDGPSL KFQINGVTFV PPTVPVLLQI LSGAQSAADL LPSGSVYALP
410 420 430 440 450
SNATIELSLP AGALGGPHPF HLHGHTFSVV RPAGSTTYNY VNPVQRDVVS
460 470 480 490 500
IGNTGDNVTI RFDTNNPGPW FLHCHIDWHL EAGFAVVFAE DIPDVASINP
510 520
VPQDWSNLCP IYNALDASDH
Length:520
Mass (Da):55,704
Last modified:May 10, 2004 - v2
Checksum:iB566CE3CA2791D36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52134 Genomic DNA. Translation: CAA36379.2.
PIRiS18746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52134 Genomic DNA. Translation: CAA36379.2.
PIRiS18746.

3D structure databases

ProteinModelPortaliQ01679.
SMRiQ01679. Positions 22-520.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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.

Entry informationi

Entry nameiLAC1_PHLRA
AccessioniPrimary (citable) accession number: Q01679
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 10, 2004
Last modified: January 7, 2015
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.