S8FGV1 · LAC2_FOMSC

Function

function

In vitro, has activity towards 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), 2,6-dimethoxy-phenol, and guaiacol (PubMed:34116754).
Although brown rot fungi preferentially degrade hemicellulose and cellulose, the enzyme may contribute to generating small amounts of lignin breakdown products required for catalytic reactions (PubMed:34116754).

Catalytic activity

Cofactor

Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds 4 Cu cations per monomer.

Activity regulation

Inhibited by chloride ions (PubMed:34116754).
Inhibited by citrate (PubMed:34116754).
Inhibited by oxalate (PubMed:34116754).
Activated by acetate (PubMed:34116754).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
20.1 μM2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS)3.030
22.4 μM2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS)5.030
64.4 μM2,6-dimethoxy-phenol3.030
8 μM2,6-dimethoxy-phenol5.030
1790 μMguaiacol3.030
918 μMguaiacol5.030
kcat is 315 sec-1 with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate (at pH 3.0 and 30 degrees Celsius). kcat is 42.6 sec-1 with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) as substrate (at pH 5.0 and 30 degrees Celsius). kcat is 155 sec-1 with 2,6-dimethoxy-phenol as substrate (at pH 3.0 and 30 degrees Celsius). kcat is 14.8 sec-1 with 2,6-dimethoxy-phenol as substrate (at pH 5.0 and 30 degrees Celsius). cat is 48 sec-1 with guaiacol as substrate (at pH 3.0 and 30 degrees Celsius). kcat is 16.7 sec-1 with guaiacol as substrate (at pH 5.0 and 30 degrees Celsius).

pH Dependence

Optimum pH is 2.5 or below with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) or 2,6-dimethoxy-phenol as substrate, and 3.5 with guaiacol as substrate.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site88Cu cation 1 (UniProtKB | ChEBI); type 2 copper site
Binding site90Cu cation 2 (UniProtKB | ChEBI); type 3 copper site
Binding site133Cu cation 2 (UniProtKB | ChEBI); type 3 copper site
Binding site135Cu cation 3 (UniProtKB | ChEBI); type 3 copper site
Binding site428Cu cation 4 (UniProtKB | ChEBI); type 1 copper site
Binding site431Cu cation 1 (UniProtKB | ChEBI); type 2 copper site
Binding site433Cu cation 3 (UniProtKB | ChEBI); type 3 copper site
Binding site484Cu cation 3 (UniProtKB | ChEBI); type 3 copper site
Binding site485Cu cation 4 (UniProtKB | ChEBI); type 1 copper site
Binding site486Cu cation 2 (UniProtKB | ChEBI); type 3 copper site
Binding site490Cu cation 4 (UniProtKB | ChEBI); type 1 copper site

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncopper ion binding
Molecular Functionoxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Laccase-2
  • EC number
  • Alternative names
    • FpLCC2

Gene names

    • Name
      LCC2
    • ORF names
      FOMPIDRAFT_51906

Organism names

Accessions

  • Primary accession
    S8FGV1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_500456366024-530Laccase-2
Glycosylation82N-linked (GlcNAc...) asparagine
Disulfide bond109↔520
Glycosylation120N-linked (GlcNAc...) asparagine
Disulfide bond141↔228
Glycosylation191N-linked (GlcNAc...) asparagine
Glycosylation240N-linked (GlcNAc...) asparagine
Glycosylation292N-linked (GlcNAc...) asparagine
Glycosylation311N-linked (GlcNAc...) asparagine
Glycosylation366N-linked (GlcNAc...) asparagine
Glycosylation375N-linked (GlcNAc...) asparagine
Glycosylation392N-linked (GlcNAc...) asparagine
Glycosylation412N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Expression

Induction

Expressed during growth on spruce wood (at protein level).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain36-154Plastocyanin-like 1
Domain167-311Plastocyanin-like 2
Domain379-504Plastocyanin-like 3

Sequence similarities

Belongs to the multicopper oxidase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    530
  • Mass (Da)
    58,324
  • Last updated
    2013-10-16 v1
  • Checksum
    669A0729701DA387
MLLSSAFVGSCLAILNFAAAVSAQGGLSRTTLNIVNKVISPDGYSRDSVLANGIHPGPLISGNKGDTFQINVNNQLHDNSMNTSTTVHWHGIDQHHTNWADGPAFVTQCPIVPEHSFLYNFTVPDQAGTFWYHSHESVQYCDGLRGPLVVYDPEDPHKDLYDVDDDTTIISLSDWYHSPAHELLPGPIPPNSTLINSLGRPDGSDLPVTIIEVDPTKRYRFRLISMACHPYFDFSIDGHNMTIIEADGSNTEPLSDIDQIRIYPAQRYSFVLEPNQTPGDYWIRAAPLQLGNTSNPDTTTSLGLAILRYTNRSGYAQAASVDPYDISQTPIPVNPLLEQNLHAYGDVPELDEECDDCKLTFDFAFNFTAVDFTVNGTSYVNPTVPVLLQILNGTYTAQELLPHHSVYTLPRNKTIEITMPGAVTGGPHPMHLHGHSFYVIQSMGSDTTNTVNPVLRDTVAVGGATGDNVVIRFRTDNPGPWIMHCHIDFHLALGFAVVLAEAPQDVAEYVSPIPTWDELCPIWDNAPSHN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KE504147
EMBL· GenBank· DDBJ
EPT00641.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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