Q4WEH3 · LP11B_ASPFU

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).

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 1 copper ion per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.8 μMH2O2

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site22Cu+ (UniProtKB | ChEBI); catalytic
Binding site82Cu+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionmetal ion binding
Molecular Functionmonooxygenase activity
Biological Processcellulose catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    AA11 family lytic polysaccharide monooxygenase B
  • EC number
  • Short names
    LPMO11B

Gene names

    • Name
      AA11B
    • ORF names
      AFUA_5G03010

Organism names

Accessions

  • Primary accession
    Q4WEH3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-21
ChainPRO_500424617222-418AA11 family lytic polysaccharide monooxygenase B
Disulfide bond50↔165
Disulfide bond87↔113
Glycosylation120N-linked (GlcNAc...) asparagine
Glycosylation134N-linked (GlcNAc...) asparagine
Disulfide bond206↔240

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region226-345Disordered
Compositional bias245-297Polar residues
Compositional bias309-345Polar residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    418
  • Mass (Da)
    42,802
  • Last updated
    2005-07-05 v1
  • Checksum
    58213D755A30F6A1
MMFSKSGLVAVAMLGASAVEAHMKMRQPTPYSDSSLNNSPLAADGSDFPCKLRDNAFVPPSQETIAQIGEVMPLTFTGSATHGGGSCQVSLTTDLKPSKDSKWMVIKSIEGGCPANVDGNMSGGADVPDPFEFNYTIPAGIEPGKYTLAWTWFNRIGNREMYMNCAPITVTAGSSKRDAAPVAEKVEVEKRSANFPAMFVANINGCTTKEGVDIRFPDPGDVVEYDGNPSNLQPAGEAACSGTPAWTVSGGSGSPSTPSTSSSTPAGTSAGVSVSVGATVGATPTAEPESSSSEPAESEGAPGVFAPTSATVFPSTPTASAAPTSSSSGAGSESDSSSSSNGALTGPCSTEGLWNCIDGSSFQRCANGQWTTAQQMAAGTECTVGQNAQFTISATAVKPRMINAMRHRKRAHGGHRHA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias245-297Polar residues
Compositional bias309-345Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHF01000011
EMBL· GenBank· DDBJ
EAL86004.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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