S7QP81 · LP9D_GLOTA

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 (PubMed:27590806).
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 (By similarity).

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 site24Cu2+ (UniProtKB | ChEBI); catalytic
Binding site179O2 (UniProtKB | ChEBI)
Binding site190Cu2+ (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 D
  • EC number
  • Short names
    LPMO9D
  • Alternative names
    • Cellulase LPMO9D
    • Endo-beta-1,4-glucanase LPMO9D
      (Endoglucanase LPMO9D
      )
    • Glycosyl hydrolase 61 family protein LPMO9D

Gene names

    • Name
      LPMO9D
    • ORF names
      GLOTRDRAFT_69702

Organism names

Accessions

  • Primary accession
    S7QP81

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-23
ChainPRO_500455650924-344AA9 family lytic polysaccharide monooxygenase D
Disulfide bond70↔193
Glycosylation201N-linked (GlcNAc...) asparagine
Glycosylation207N-linked (GlcNAc...) asparagine
Glycosylation317N-linked (GlcNAc...) asparagine

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region240-321Disordered
Compositional bias243-321Polar 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
    344
  • Mass (Da)
    35,383
  • Last updated
    2013-10-16 v1
  • Checksum
    F58DD6C0EBC57730
MKTATSYAAFLLSALAALPHASAHGFVSKVVVNGQSYAGNTPGGDTSPSPIRQISTISPVKGAANKDMFCGYDAQVASQVAAADPGSKVTFTWSGGGGQNWPHNTGPLMTYMGACEGTTCDKYTATDAKWFKIDEVGREANGGDWVQQEIMNGGTYTVTLPSNIAPGDYLIRHEIIALHLGMTEGGAEFYPSCTQVRITGNGSGTPNQTVSFPGAYSDTDPGIWDKNVYDPSAPYTFPGPPLSNLVSGDSGTVDGQGGSTSSATLSGGAAPTGTASGSTPAGTSQPSSTTGTGNAGANPSSGKCSLKSRAAPTTSGNLSANYPRHFSRVMKRLLNDFQTTVHQW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias243-321Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KB469296
EMBL· GenBank· DDBJ
EPQ61333.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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