A0A2I6QB00 · LP14B_TRAC3
- ProteinAA14 family lytic polysaccharide monooxygenase B
- GeneAA14B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids418 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves xylan with both C1 and C4 regioselectivity and that specifically targets the protective shield made by heteroxylans that cover cellulose microfibrils in wood (PubMed:29377002, PubMed:32793303).
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:29377002).
Cleavage occurs only when xylans are bound to cellulose and not when they are in solution (PubMed:29377002).
Increases the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers via synergistic relationship with xylan-active enzymes, xylobiohydrolases and cellobiohydrolases (PubMed:29377002, PubMed:32793303).
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:29377002).
Cleavage occurs only when xylans are bound to cellulose and not when they are in solution (PubMed:29377002).
Increases the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers via synergistic relationship with xylan-active enzymes, xylobiohydrolases and cellobiohydrolases (PubMed:29377002, PubMed:32793303).
Cofactor
Note: Binds 1 copper ion per subunit.
Biotechnology
The unique enzyme activity of AA14 family LPMOs involved in the degradation of woody biomass in nature offers an innovative solution for improving enzyme cocktails for biorefinery applications.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | metal ion binding | |
Molecular Function | monooxygenase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAA14 family lytic polysaccharide monooxygenase B
- EC number
- Short namesLPMO AA14B
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Polyporaceae > Trametes
Accessions
- Primary accessionA0A2I6QB00
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MIPVFLAAVAAFLPLTSG | ||||||
Chain | PRO_5014319006 | 19-418 | AA14 family lytic polysaccharide monooxygenase B | |||
Sequence: HIAFWHNSMYGFNVTEQTFPYDNRPVVPLQYMTFQEWWFHNHLDYPPHPGDFFDFPAGKAATAELACNKGATTWFNSSEGGNIQNGNDPCPGSPPSEYHTTGIDDVKGCAMAIAYESDVRKIKPEDFTVFSVNQTCVWYRFTDFQVPERMPPCPPGGCHCAWFWIHSPDSGGEQIYMNGFQCNITGSTSHVPLAKPKVARRCGADPDHGKPDAVPGNCTYGAKQPLYWLQKEGNNEFDDYIAPPFYNDLYNFKDGAQNDIFVDSYPDGIPDPSPEQTIVPTPVNAAAVAAATPAPSSSGSSPSSSSPGSSSTASTTSTSGPRPSARGFRRSTGERPPTGVPTPRKSWTQTRKLRYVCLDRARIVLCCKGLALMVHRLALQRGRHQEPSAQGASLAFLAAG | ||||||
Glycosylation | 31 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 85↔108 | |||||
Sequence: CNKGATTWFNSSEGGNIQNGNDPC | ||||||
Glycosylation | 94 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 127↔154 | |||||
Sequence: CAMAIAYESDVRKIKPEDFTVFSVNQTC | ||||||
Glycosylation | 151 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 171↔176 | |||||
Sequence: CPPGGC | ||||||
Disulfide bond | 178↔200 | |||||
Sequence: CAWFWIHSPDSGGEQIYMNGFQC | ||||||
Glycosylation | 201 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 220↔236 | |||||
Sequence: CGADPDHGKPDAVPGNC | ||||||
Glycosylation | 235 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 307-364 | Disordered | ||||
Sequence: AAATPAPSSSGSSPSSSSPGSSSTASTTSTSGPRPSARGFRRSTGERPPTGVPTPRKS | ||||||
Compositional bias | 309-343 | Polar residues | ||||
Sequence: ATPAPSSSGSSPSSSSPGSSSTASTTSTSGPRPSA |
Sequence similarities
Belongs to the polysaccharide monooxygenase AA14 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)45,554
- Last updated2018-03-28 v1
- Checksum1EF80BA39CF6713A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 309-343 | Polar residues | ||||
Sequence: ATPAPSSSGSSPSSSSPGSSSTASTTSTSGPRPSA |
Mass Spectrometry
Keywords
- Technical term