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Hericium coralloides (Coral tooth fungus) (Hericium ramosum)
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli


Lignin degradation and detoxification of lignin-derived products. Has activity towards ABTS and, to a much lesser extent, towards N,N-dimethyl-1,4-phenylenediamine, catechol and 2-methylcatechol.1 Publication

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.1 Publication


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

Enzyme regulationi

Strongly activated by Mg2+ and Al3+. At concentrations <50 mM, activated by Ca2+, Mn2+, Co2+ and K+. Strongly inhibited by Hg2+ and, in a concentration-dependent manner, by Fe2+.1 Publication

pH dependencei

Optimum pH is 2.2. Activity declines sharply with decreases or increases in pH and is absent above pH 6.6.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius. Retains 65% activity at 20 degrees Celsius and 24% activity at 100 degrees Celsius.1 Publication

GO - Molecular functioni

  • hydroquinone:oxygen oxidoreductase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • lignin catabolic process Source: UniProtKB


Molecular functionOxidoreductase
Biological processLignin degradation
LigandCopper, Metal-binding

Enzyme and pathway databases


Names & Taxonomyi

Protein namesi
Recommended name:
Laccase1 Publication (EC: Publication)
Alternative name(s):
Benzenediol:oxygen oxidoreductaseBy similarity
Diphenol oxidaseBy similarity
Urishiol oxidaseBy similarity
OrganismiHericium coralloides (Coral tooth fungus) (Hericium ramosum)
Taxonomic identifieri100756 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesRussulalesHericiaceaeHericium

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004146191 – ›10Laccase›10


Sequence statusi: Fragment.

Mass (Da):1,078
Last modified:December 14, 2011 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei101 Publication1


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases


Family and domain databases


Entry informationi

Entry nameiLAC1_HERCO
AccessioniPrimary (citable) accession number: B3A0L4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: December 14, 2011
Last modified: January 20, 2016
This is version 9 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program



Inhibits HIV-1 reverse transcriptase (IC50=0.6 µM).1 Publication

Keywords - Technical termi

Direct protein sequencing

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 one 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.