Q4WEH3 · LP11B_ASPFU
- ProteinAA11 family lytic polysaccharide monooxygenase B
- GeneAA11B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids418 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Lytic polysaccharide monooxygenase (LPMO)-like protein that acts as a strict peroxygenase and does not catalyze a monooxygenase reaction (PubMed:34567832).
It is indeed hardly active on chitin, while being very active on soluble oligomers of N-acetylglucosamine (PubMed:34567832).
Cleaves the glycosidic bonds byoxidizing the C1 position (PubMed:34567832).
Also unable to oxidize cellopentaose (PubMed:34738811).
Probably breaks glycosidic bonds in non-polymeric substrates possibly carbohydrates in the cell wall of the fungus or its competitors (PubMed:34567832).
In the presence of chitotetraose, the enzyme can withstand considerable amounts of H2O2, which it uses to efficiently and stoichiometrically convert this substrate (PubMed:34567832).
It is indeed hardly active on chitin, while being very active on soluble oligomers of N-acetylglucosamine (PubMed:34567832).
Cleaves the glycosidic bonds byoxidizing the C1 position (PubMed:34567832).
Also unable to oxidize cellopentaose (PubMed:34738811).
Probably breaks glycosidic bonds in non-polymeric substrates possibly carbohydrates in the cell wall of the fungus or its competitors (PubMed:34567832).
In the presence of chitotetraose, the enzyme can withstand considerable amounts of H2O2, which it uses to efficiently and stoichiometrically convert this substrate (PubMed:34567832).
Cofactor
Note: Binds 1 copper ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.8 μM | H2O2 |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 22 | Cu+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 82 | Cu+ (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | metal ion binding | |
Molecular Function | monooxygenase activity | |
Biological Process | cellulose catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAA11 family lytic polysaccharide monooxygenase B
- EC number
- Short namesLPMO11B
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionQ4WEH3
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-21 | ||||
Chain | PRO_5004246172 | 22-418 | AA11 family lytic polysaccharide monooxygenase B | ||
Disulfide bond | 50↔165 | ||||
Disulfide bond | 87↔113 | ||||
Glycosylation | 120 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 134 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 206↔240 | ||||
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 226-345 | Disordered | |||
Compositional bias | 245-297 | Polar residues | |||
Compositional bias | 309-345 | Polar residues | |||
Sequence similarities
Belongs to the polysaccharide monooxygenase AA11 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length418
- Mass (Da)42,802
- Last updated2005-07-05 v1
- Checksum58213D755A30F6A1
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 245-297 | Polar residues | |||
Compositional bias | 309-345 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHF01000011 EMBL· GenBank· DDBJ | EAL86004.1 EMBL· GenBank· DDBJ | Genomic DNA |