W4KMP1 · LP9B_HETIT
- ProteinAA9 family lytic polysaccharide monooxygenase B
- GeneLPMO9B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids244 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 specifically C1 oxidation product (PubMed:29660793).
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 (PubMed:29660793).
Displays catalytic activity on insoluble cellulose using I-beta microfibril model substrate (PubMed:29660793).
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 (PubMed:29660793).
Displays catalytic activity on insoluble cellulose using I-beta microfibril model substrate (PubMed:29660793).
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 | 20 | Cu2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 39 | (1,4-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 99 | Cu2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 178 | O2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 184 | O2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 186 | Cu2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: Y | ||||||
Binding site | 224 | (1,4-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 226 | (1,4-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 229 | (1,4-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | hydrolase activity, acting on glycosyl bonds | |
Molecular Function | metal ion binding | |
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 B
- EC number
- Short namesLPMO9B
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Russulales > Bondarzewiaceae > Heterobasidion > Heterobasidion annosum species complex
Accessions
- Primary accessionW4KMP1
Proteomes
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MFLVPLLAALSLSAPKVAA | ||||||
Chain | PRO_5004844531 | 20-244 | AA9 family lytic polysaccharide monooxygenase B | |||
Sequence: HGGVLAYSLAGTWYNGFVPYNTPTGQSTIQREWDTYNPITDPTDASISCNINGASLGSAQKSATVAAGSSVTAYWNQWPHTIGPVMVYMANCGGDCTTATTSSLEWFKINQVGLVSGTLTSGTWGMGQLVANNNSWTTSIPSSLAAGNYILRHELLAIHTSNQPQFYPECAQLIVTGGEGATPPASYLVKLPGAYSMSDPGVNIDIYSHETETNYTIPGPAVWQG | ||||||
Disulfide bond | 68↔189 | |||||
Sequence: CNINGASLGSAQKSATVAAGSSVTAYWNQWPHTIGPVMVYMANCGGDCTTATTSSLEWFKINQVGLVSGTLTSGTWGMGQLVANNNSWTTSIPSSLAAGNYILRHELLAIHTSNQPQFYPEC | ||||||
Disulfide bond | 111↔115 | |||||
Sequence: CGGDC | ||||||
Glycosylation | 152 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 233 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length244
- Mass (Da)25,744
- Last updated2014-03-19 v1
- Checksum0B9FD48C83A7538A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KI925454 EMBL· GenBank· DDBJ | ETW87087.1 EMBL· GenBank· DDBJ | Genomic DNA |