A0A384JXL6 · LP9F_BOTFB
- ProteinAA9 family lytic polysaccharide monooxygenase F
- GeneAA9F
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids250 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H2O2 or O2 as a cosubstrate (Probable).
Catalytic activity
Cofactor
Note: Binds 1 copper ion per subunit.
Biotechnology
Lignocellulose is the most abundant polymeric composite on Earth and is a recalcitrant but promising renewable substrate for industrial biotechnology applications. Together with cellobiose dehydrogenases (CDHs) an enzymatic system capable of oxidative cellulose cleavage is formed, which increases the efficiency of cellulases and put LPMOs at focus of biofuel research.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 19 | Cu2+ (UniProtKB | ChEBI) | |||
Binding site | 108 | Cu2+ (UniProtKB | ChEBI) | |||
Binding site | 185 | O2 (UniProtKB | ChEBI) | |||
Binding site | 194 | O2 (UniProtKB | ChEBI) | |||
Binding site | 196 | Cu2+ (UniProtKB | ChEBI) | |||
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 nameAA9 family lytic polysaccharide monooxygenase F
- EC number
- Short namesAA9F
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Sclerotiniaceae > Botrytis
Accessions
- Primary accessionA0A384JXL6
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-18 | ||||
Chain | PRO_5016863723 | 19-250 | AA9 family lytic polysaccharide monooxygenase F | ||
Glycosylation | 24 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 70↔199 | ||||
Glycosylation | 85 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 146 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 169↔250 | ||||
Keywords
- PTM
Expression
Induction
Expression is increased 8-fold in cellulose-inducible conditions (in Avicel- and wheat bran-containing complex medium).
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length250
- Mass (Da)26,371
- Last updated2018-11-07 v1
- Checksum1474C1E7B5E3C3A2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP009815 EMBL· GenBank· DDBJ | ATZ55262.1 EMBL· GenBank· DDBJ | Genomic DNA |