S8FGV1 · LAC2_FOMSC
- ProteinLaccase-2
- GeneLCC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids530 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Cofactor
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).
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 μM | 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) | 3.0 | 30 | |||
22.4 μM | 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) | 5.0 | 30 | |||
64.4 μM | 2,6-dimethoxy-phenol | 3.0 | 30 | |||
8 μM | 2,6-dimethoxy-phenol | 5.0 | 30 | |||
1790 μM | guaiacol | 3.0 | 30 | |||
918 μM | guaiacol | 5.0 | 30 |
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 88 | Cu cation 1 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 90 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 133 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 135 | Cu cation 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 428 | Cu cation 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 431 | Cu cation 1 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 433 | Cu cation 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 484 | Cu cation 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 485 | Cu cation 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 486 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 490 | Cu cation 4 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | copper ion binding | |
Molecular Function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLaccase-2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Fomitopsis
Accessions
- Primary accessionS8FGV1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MLLSSAFVGSCLAILNFAAAVSA | ||||||
Chain | PRO_5004563660 | 24-530 | Laccase-2 | |||
Sequence: QGGLSRTTLNIVNKVISPDGYSRDSVLANGIHPGPLISGNKGDTFQINVNNQLHDNSMNTSTTVHWHGIDQHHTNWADGPAFVTQCPIVPEHSFLYNFTVPDQAGTFWYHSHESVQYCDGLRGPLVVYDPEDPHKDLYDVDDDTTIISLSDWYHSPAHELLPGPIPPNSTLINSLGRPDGSDLPVTIIEVDPTKRYRFRLISMACHPYFDFSIDGHNMTIIEADGSNTEPLSDIDQIRIYPAQRYSFVLEPNQTPGDYWIRAAPLQLGNTSNPDTTTSLGLAILRYTNRSGYAQAASVDPYDISQTPIPVNPLLEQNLHAYGDVPELDEECDDCKLTFDFAFNFTAVDFTVNGTSYVNPTVPVLLQILNGTYTAQELLPHHSVYTLPRNKTIEITMPGAVTGGPHPMHLHGHSFYVIQSMGSDTTNTVNPVLRDTVAVGGATGDNVVIRFRTDNPGPWIMHCHIDFHLALGFAVVLAEAPQDVAEYVSPIPTWDELCPIWDNAPSHN | ||||||
Glycosylation | 82 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 109↔520 | |||||
Sequence: CPIVPEHSFLYNFTVPDQAGTFWYHSHESVQYCDGLRGPLVVYDPEDPHKDLYDVDDDTTIISLSDWYHSPAHELLPGPIPPNSTLINSLGRPDGSDLPVTIIEVDPTKRYRFRLISMACHPYFDFSIDGHNMTIIEADGSNTEPLSDIDQIRIYPAQRYSFVLEPNQTPGDYWIRAAPLQLGNTSNPDTTTSLGLAILRYTNRSGYAQAASVDPYDISQTPIPVNPLLEQNLHAYGDVPELDEECDDCKLTFDFAFNFTAVDFTVNGTSYVNPTVPVLLQILNGTYTAQELLPHHSVYTLPRNKTIEITMPGAVTGGPHPMHLHGHSFYVIQSMGSDTTNTVNPVLRDTVAVGGATGDNVVIRFRTDNPGPWIMHCHIDFHLALGFAVVLAEAPQDVAEYVSPIPTWDELC | ||||||
Glycosylation | 120 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 141↔228 | |||||
Sequence: CDGLRGPLVVYDPEDPHKDLYDVDDDTTIISLSDWYHSPAHELLPGPIPPNSTLINSLGRPDGSDLPVTIIEVDPTKRYRFRLISMAC | ||||||
Glycosylation | 191 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 240 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 292 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 311 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 366 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 375 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 392 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 412 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-154 | Plastocyanin-like 1 | ||||
Sequence: NKVISPDGYSRDSVLANGIHPGPLISGNKGDTFQINVNNQLHDNSMNTSTTVHWHGIDQHHTNWADGPAFVTQCPIVPEHSFLYNFTVPDQAGTFWYHSHESVQYCDGLRGPLVVYDPE | ||||||
Domain | 167-311 | Plastocyanin-like 2 | ||||
Sequence: TTIISLSDWYHSPAHELLPGPIPPNSTLINSLGRPDGSDLPVTIIEVDPTKRYRFRLISMACHPYFDFSIDGHNMTIIEADGSNTEPLSDIDQIRIYPAQRYSFVLEPNQTPGDYWIRAAPLQLGNTSNPDTTTSLGLAILRYTN | ||||||
Domain | 379-504 | Plastocyanin-like 3 | ||||
Sequence: YVNPTVPVLLQILNGTYTAQELLPHHSVYTLPRNKTIEITMPGAVTGGPHPMHLHGHSFYVIQSMGSDTTNTVNPVLRDTVAVGGATGDNVVIRFRTDNPGPWIMHCHIDFHLALGFAVVLAEAPQ |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length530
- Mass (Da)58,324
- Last updated2013-10-16 v1
- Checksum669A0729701DA387
Keywords
- Technical term