W4KMP1 · LP9B_HETIT

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).

Catalytic activity

  • [(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-beta-D-glucosyl-[(1->4)-beta-D-glucosyl]n-1 + [(1->4)-beta-D-glucosyl]m + acceptor + H2O.
    EC:1.14.99.56 (UniProtKB | ENZYME | Rhea)

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

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.

TypeIDPosition(s)Description
Binding site20Cu2+ (UniProtKB | ChEBI); catalytic
Binding site39(1,4-beta-D-glucosyl)n (UniProtKB | ChEBI)
Binding site99Cu2+ (UniProtKB | ChEBI); catalytic
Binding site178O2 (UniProtKB | ChEBI)
Binding site184O2 (UniProtKB | ChEBI)
Binding site186Cu2+ (UniProtKB | ChEBI); catalytic
Binding site224(1,4-beta-D-glucosyl)n (UniProtKB | ChEBI)
Binding site226(1,4-beta-D-glucosyl)n (UniProtKB | ChEBI)
Binding site229(1,4-beta-D-glucosyl)n (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionhydrolase activity, acting on glycosyl bonds
Molecular Functionmetal ion binding
Biological Processcellulose catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    AA9 family lytic polysaccharide monooxygenase B
  • EC number
  • Short names
    LPMO9B
  • Alternative names
    • Cellulase LPMO9B
    • Endo-beta-1,4-glucanase LPMO9B
      (Endoglucanase LPMO9B
      )
    • Glycosyl hydrolase 61 family protein LPMO9B

Gene names

    • Name
      LPMO9B
    • ORF names
      HETIRDRAFT_166613

Organism names

  • Taxonomic identifier
  • Strain
    • TC 32-1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Russulales > Bondarzewiaceae > Heterobasidion > Heterobasidion annosum species complex

Accessions

  • Primary accession
    W4KMP1

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-19
ChainPRO_500484453120-244AA9 family lytic polysaccharide monooxygenase B
Disulfide bond68↔189
Disulfide bond111↔115
Glycosylation152N-linked (GlcNAc...) asparagine
Glycosylation233N-linked (GlcNAc...) asparagine

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

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
    244
  • Mass (Da)
    25,744
  • Last updated
    2014-03-19 v1
  • Checksum
    0B9FD48C83A7538A
MFLVPLLAALSLSAPKVAAHGGVLAYSLAGTWYNGFVPYNTPTGQSTIQREWDTYNPITDPTDASISCNINGASLGSAQKSATVAAGSSVTAYWNQWPHTIGPVMVYMANCGGDCTTATTSSLEWFKINQVGLVSGTLTSGTWGMGQLVANNNSWTTSIPSSLAAGNYILRHELLAIHTSNQPQFYPECAQLIVTGGEGATPPASYLVKLPGAYSMSDPGVNIDIYSHETETNYTIPGPAVWQG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI925454
EMBL· GenBank· DDBJ
ETW87087.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp