C0HLV6 · LACS_TRAHI
- ProteinLaccase-S
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids238 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lignin degradation and detoxification of lignin-derived products (By similarity).
Has activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) (PubMed:34093489).
Has activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) (PubMed:34093489).
Catalytic activity
- 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O
Cofactor
Note: Binds 4 Cu cations per monomer.
Activity regulation
Activity is strongly promoted by toluene (PubMed:34093489).
Activity is promoted by magnesium, potassium, cadmium, zinc, nickel, sodium, lead and manganese ions (PubMed:34093489).
Completely inhibited by IAA (cysteine protease inhibitor), PMSF (serine protease inhibitor), DEP (histidine protease inhibitor) and NAI (tyrosine protease inhibitor) (PubMed:34093489).
Inhibited by ethanol, acetone, SDS, and EDTA (PubMed:34093489).
Activity is strongly inhibited by mercury ions (PubMed:34093489).
Also inhibited by lithium, aluminum, calcium, barium and iron ions (PubMed:34093489).
Activity is promoted by magnesium, potassium, cadmium, zinc, nickel, sodium, lead and manganese ions (PubMed:34093489).
Completely inhibited by IAA (cysteine protease inhibitor), PMSF (serine protease inhibitor), DEP (histidine protease inhibitor) and NAI (tyrosine protease inhibitor) (PubMed:34093489).
Inhibited by ethanol, acetone, SDS, and EDTA (PubMed:34093489).
Activity is strongly inhibited by mercury ions (PubMed:34093489).
Also inhibited by lithium, aluminum, calcium, barium and iron ions (PubMed:34093489).
Biotechnology
Able to metabolize the endocrine disrupting chemical (EDC) 17beta-estradiol (E2), and so could be used in biotechnological and industrial applications that require the biodegradation and bioremediation of the environmental pollutant.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
87.47 μM | ABTS | 6.0 | 50 |
kcat is 129.37 sec-1 for ABTS oxidation (at pH 6.0 and 50 degrees Celsius).
pH Dependence
Optimum pH is 6 at 25 degrees Celsius (PubMed:34093489).
Retains over 60 percent activity in the pH range from 4 to 10 (PubMed:34093489).
Retains activity above 50% after incubation at pH 5-10 for 72 hours (PubMed:34093489).
Retains over 60 percent activity in the pH range from 4 to 10 (PubMed:34093489).
Retains activity above 50% after incubation at pH 5-10 for 72 hours (PubMed:34093489).
Temperature Dependence
Optimum temperature is 50 degrees Celsius (PubMed:34093489).
Retains over 57 percent activity when incubated for 2 hours at temperatures between 30-65 degrees Celsius (PubMed:34093489).
Retains over 57 percent activity when incubated for 2 hours at temperatures between 30-65 degrees Celsius (PubMed:34093489).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 21 | Cu cation 1 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 23 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 66 | Cu cation 2 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H | ||||||
Binding site | 68 | Cu cation 3 (UniProtKB | ChEBI); type 3 copper site | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | copper ion binding | |
Molecular Function | hydroquinone:oxygen oxidoreductase activity | |
Biological Process | lignin catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLaccase-S
- EC number
- Short namesThLacc-S
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Polyporaceae > Trametes
Accessions
- Primary accessionC0HLV6
- Secondary accessions
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453427 | 1-238 | Laccase-S | |||
Sequence: FQLNVIANMNNHTMLKQTSIHWHCHFQKGTNWADGHAFVNACPIASGHSFLYDFTAPDQHGTFWYHSHLSTQYCDGLRGHFVVYDPADPHHDLYDVDDEHTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSCDPNHVFSIDSNHMTVIEADAVSHEHCTVDSIQIYAGQRYSFHLTVDQDVDNYWIRAHPSFGTYSFHDGINSAIARY | ||||||
Glycosylation | 8 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 74↔162 | |||||
Sequence: CDGLRGHFVVYDPADPHHDLYDVDDEHTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSC | ||||||
Glycosylation | 165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-87 | Plastocyanin-like 1 | ||||
Sequence: NVIANMNNHTMLKQTSIHWHCHFQKGTNWADGHAFVNACPIASGHSFLYDFTAPDQHGTFWYHSHLSTQYCDGLRGHFVVYDPA | ||||||
Domain | 100-238 | Plastocyanin-like 2 | ||||
Sequence: HTIITLADWYHVAAKLGHHFQLGADSTLINGSGRFAGDPTAHLTVIYVTQGKRYRFHLVSLSCDPNHVFSIDSNHMTVIEADAVSHEHCTVDSIQIYAGQRYSFHLTVDQDVDNYWIRAHPSFGTYSFHDGINSAIARY |
Sequence similarities
Belongs to the multicopper oxidase family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length238
- Mass (Da)27,055
- Last updated2021-09-29 v1
- Checksum79668D388A8F4456
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: F | ||||||
Non-terminal residue | 238 | |||||
Sequence: Y |
Mass Spectrometry
Keywords
- Technical term