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A0A5N6UNY1 · LP9E_ASPTM

  • Protein
    AA9 family lytic polysaccharide monooxygenase E
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

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 C1 or 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 site22Cu2+ (UniProtKB | ChEBI); catalytic
Binding site107Cu2+ (UniProtKB | ChEBI); catalytic
Binding site185O2 (UniProtKB | ChEBI)
Binding site194O2 (UniProtKB | ChEBI)
Binding site196Cu2+ (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
    AA9 family lytic polysaccharide monooxygenase E
  • EC number
  • Short names
    AtAA9E
  • Alternative names
    • Cellulase AA9E
    • Endo-beta-1,4-glucanase AA9E
      (Endoglucanase AA9E
      )
    • Glycosyl hydrolase 61 family protein AA9E

Gene names

    • ORF names
      BDV40DRAFT_218852

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 117626
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    A0A5N6UNY1

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

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

Type
IDPosition(s)Description
Signal1-21
ChainPRO_502506852022-250AA9 family lytic polysaccharide monooxygenase E
Disulfide bond77↔199
Disulfide bond118↔122
Glycosylation159N-linked (GlcNAc...) asparagine

Keywords

Expression

Induction

Expression is up-regulated on steam-exploded bagasse as carbon source compared to glucose.

Family & Domains

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    250
  • Mass (Da)
    26,134
  • Last updated
    2020-04-22 v1
  • MD5 Checksum
    17B66E876E46A78439D3CB22B4FA7414
MAMSKIMSLTGLLASASLVAGHGYVSGVVVDGQYYGGYLVDKYAYSDNPPETIGWSTTATDLGFVDGTGYQSPDIICHKDGKPGALSAEVAAGGEIELQWTEWPESHHGPVLNYLAPCGGDCSAVDKTSLEFFKIEAKGLIDGSSPPGHWATDDLISNNNSWTVTIPASVQEGNYVLRHEIIGLHSAGQKDGAQNYPQCINIKVTGGGAATPAGTAGEALYKDTDPGILFDIYSDLSGGYPIPGPEVFSA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ML738660
EMBL· GenBank· DDBJ
KAE8160256.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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