A0A384JXL6 · LP9F_BOTFB

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

  • [(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 site19Cu2+ (UniProtKB | ChEBI)
Binding site108Cu2+ (UniProtKB | ChEBI)
Binding site185O2 (UniProtKB | ChEBI)
Binding site194O2 (UniProtKB | ChEBI)
Binding site196Cu2+ (UniProtKB | ChEBI)

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
    AA9 family lytic polysaccharide monooxygenase F
  • EC number
  • Short names
    AA9F
  • Alternative names
    • Endo-1,4-beta-glucanase AA9F
      (Endoglucanase AA9F
      )
    • Glycosyl hydrolase 61 family protein AA9F

Gene names

    • Name
      AA9F
    • ORF names
      BCIN_11g05360

Organism names

Accessions

  • Primary accession
    A0A384JXL6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-18
ChainPRO_501686372319-250AA9 family lytic polysaccharide monooxygenase F
Glycosylation24N-linked (GlcNAc...) asparagine
Disulfide bond70↔199
Glycosylation85N-linked (GlcNAc...) asparagine
Glycosylation146N-linked (GlcNAc...) asparagine
Disulfide bond169↔250

Keywords

Expression

Induction

Expression is increased 8-fold in cellulose-inducible conditions (in Avicel- and wheat bran-containing complex medium).

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
    250
  • Mass (Da)
    26,371
  • Last updated
    2018-11-07 v1
  • Checksum
    1474C1E7B5E3C3A2
MHLKTFSNLLVFVATVAAHGYVDNVTVNGILYTGYQPNSDPYYATPPPRIIRPVQGNGPITDLTLIDLQCGGYTEGGIVGSQPANLTAGPVAAGSTVSLRWTLWPDSHSGPVITYMAKCPAAGCSTYVPGTAAVWFKIQATGRIGNTTVWGDTPLKTAGNSYSYTIPSCLSAGSYIVRHEILALHAAWTYPGVQFYPSCHQIQVTGSGTSTGPSSKVAIPGVYKATDPGIVYDMYAVQPYTIPGPAVFTC

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP009815
EMBL· GenBank· DDBJ
ATZ55262.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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