A0A2I6QB00 · LP14B_TRAC3

Function

function

Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves xylan with both C1 and C4 regioselectivity and that specifically targets the protective shield made by heteroxylans that cover cellulose microfibrils in wood (PubMed:29377002, PubMed:32793303).
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:29377002).
Cleavage occurs only when xylans are bound to cellulose and not when they are in solution (PubMed:29377002).
Increases the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers via synergistic relationship with xylan-active enzymes, xylobiohydrolases and cellobiohydrolases (PubMed:29377002, PubMed:32793303).

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 1 copper ion per subunit.

Biotechnology

The unique enzyme activity of AA14 family LPMOs involved in the degradation of woody biomass in nature offers an innovative solution for improving enzyme cocktails for biorefinery applications.

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionmetal ion binding
Molecular Functionmonooxygenase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    AA14 family lytic polysaccharide monooxygenase B
  • EC number
  • Short names
    LPMO AA14B

Gene names

    • Name
      AA14B
    • ORF names
      PYCCODRAFT_1372210

Organism names

Accessions

  • Primary accession
    A0A2I6QB00
  • Secondary accessions
    • A0A1Y2IFD5

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-18
ChainPRO_501431900619-418AA14 family lytic polysaccharide monooxygenase B
Glycosylation31N-linked (GlcNAc...) asparagine
Disulfide bond85↔108
Glycosylation94N-linked (GlcNAc...) asparagine
Disulfide bond127↔154
Glycosylation151N-linked (GlcNAc...) asparagine
Disulfide bond171↔176
Disulfide bond178↔200
Glycosylation201N-linked (GlcNAc...) asparagine
Disulfide bond220↔236
Glycosylation235N-linked (GlcNAc...) asparagine

Keywords

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region307-364Disordered
Compositional bias309-343Polar 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)
    45,554
  • Last updated
    2018-03-28 v1
  • Checksum
    1EF80BA39CF6713A
MIPVFLAAVAAFLPLTSGHIAFWHNSMYGFNVTEQTFPYDNRPVVPLQYMTFQEWWFHNHLDYPPHPGDFFDFPAGKAATAELACNKGATTWFNSSEGGNIQNGNDPCPGSPPSEYHTTGIDDVKGCAMAIAYESDVRKIKPEDFTVFSVNQTCVWYRFTDFQVPERMPPCPPGGCHCAWFWIHSPDSGGEQIYMNGFQCNITGSTSHVPLAKPKVARRCGADPDHGKPDAVPGNCTYGAKQPLYWLQKEGNNEFDDYIAPPFYNDLYNFKDGAQNDIFVDSYPDGIPDPSPEQTIVPTPVNAAAVAAATPAPSSSGSSPSSSSPGSSSTASTTSTSGPRPSARGFRRSTGERPPTGVPTPRKSWTQTRKLRYVCLDRARIVLCCKGLALMVHRLALQRGRHQEPSAQGASLAFLAAG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias309-343Polar residues

Mass Spectrometry

Molecular mass is 46,450 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KY769370
EMBL· GenBank· DDBJ
AUM86167.1
EMBL· GenBank· DDBJ
mRNA
KZ084123
EMBL· GenBank· DDBJ
OSC99905.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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