A0A9Q9DNK0 · A0A9Q9DNK0_CURCL

  • Protein
    AA9 family lytic polysaccharide monooxygenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and/or C4 oxidation products. 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.

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 )

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Cellular Componentmembrane
Molecular Functioncellulase activity
Molecular Functioncellulose binding
Biological Processcellulose catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    AA9 family lytic polysaccharide monooxygenase
  • EC number
  • Alternative names
    • Endo-beta-1,4-glucanase
    • Glycosyl hydrolase 61 family protein

Gene names

    • ORF names
      yc1106_00454

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Yc1106
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Pleosporineae > Pleosporaceae > Curvularia

Accessions

  • Primary accession
    A0A9Q9DNK0

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Multi-pass membrane protein
Secreted

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-18
ChainPRO_504048184519-712AA9 family lytic polysaccharide monooxygenase

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region234-347Disordered
Compositional bias244-296Polar residues
Domain346-382CBM1
Region441-463Disordered
Compositional bias444-463Polar residues

Domain

Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM).

Sequence similarities

Belongs to the peroxisomal membrane protein PXMP2/4 family.
Belongs to the polysaccharide monooxygenase AA9 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    712
  • Mass (Da)
    75,433
  • Last updated
    2023-09-13 v1
  • MD5 Checksum
    CE11763DF21CFE361B73AA6D282715AC
MKTFISALALAGMANAHATIWGISVNDKDQGFGNSQGGYIDAPPNNSPVTDVTSKAMECNVANIKATKSVNVNPGDEIAVQWYHNGPTAGDQIIDGSHKGPISVYMSKAGASMSWTKIAEDGYDGKTWAVEKLRNGAYNGKKGQHTFKVPSVAKGDYVFRPEIIALHEGNRVGGAQFYMECIHVTVGGSGTTALPAGVAIPGYVTANTPGVLFDIYNSFSSYPVPGPKVWNGAGGAATPASSPVASPPAASSPAASSPAANPPTTGSPSTGSPAAGSPVAGSPSAGSPTTGSPAAGSPAVESPAASSPAGDDSAECPEGSDDTEEPAEPAAEPANPPTTPSPSGGATAQKYYQCGGQGYTGPTNCVSGTKCVKQNDYYFQCLTVLSGIVLVMRSVPTSSPKSPEPPPSSAWVRVGLRRIPNAPSRNTGNTSNLERARLRLHPSNASRRYNSTTPEGGQTSAATARTIPGPSWLWLDPIVEPFRAYGRVQQRRPYMTQLVSSLIIYFIGDCVAQSITQPEPSVQQEKTNEADQVDEKGWVQQWSDDRDWSRTMRALAIGGLSAIPSYRWFLWLSNSFNYRSKTLSLSIKVFINQAFFTPLFNSYFFGMQTLLSGGTFPEIIERIKNTVPTSWWNSCKIWPAVTAFSFSYVPIQYRSIFGGVVAIGWQTYLNLLNQQAAAEEELERAAGHVAPANVMTVHTNAHHGQVMEKCAA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias244-296Polar residues
Compositional bias444-463Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP089274
EMBL· GenBank· DDBJ
USP73180.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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