A0A024SH20 · GUN2_HYPJR

Function

function

Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates new chain ends for exocellobiohydrolases (CBHs). The CBH release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units.

Catalytic activity

  • Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
    EC:3.2.1.4 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

141850100150200250300350400
TypeIDPosition(s)Description
Active site239Proton donor/acceptor
Active site350Nucleophile

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
Molecular Functioncellulase activity
Molecular Functioncellulose binding
Biological Processcellulose catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Endoglucanase EG-II
  • EC number
  • Short names
    EGII
  • Alternative names
    • Cellulase
    • Endo-1,4-beta-glucanase

Gene names

    • Name
      egl2
    • ORF names
      M419DRAFT_72489

Organism names

Accessions

  • Primary accession
    A0A024SH20

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-21
Modified residue22Pyrrolidone carboxylic acid
ChainPRO_500153723122-418Endoglucanase EG-II
Disulfide bond107↔113
Glycosylation124N-linked (GlcNAc) asparagine
Disulfide bond183↔190
Disulfide bond323↔359
Disulfide bond364↔414

Keywords

PTM databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain22-57CBM1
Region58-91Linker
Region63-91Disordered
Region92-418Catalytic

Domain

The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.

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)
    44,155
  • Last updated
    2014-07-09 v1
  • Checksum
    D0F9B9284E062FED
MNKSVAPLLLAASILYGGAAAQQTVWGQCGGIGWSGPTNCAPGSACSTLNPYYAQCIPGATTITTSTRPPSGPTTTTRATSTSSSTPPTSSGVRFAGVNIAGFDFGCTTDGTCVTSKVYPPLKNFTGSNNYPDGIGQMQHFVNDDGMTIFRLPVGWQYLVNNNLGGNLDSTSISKYDQLVQGCLSLGAYCIVDIHNYARWNGGIIGQGGPTNAQFTSLWSQLASKYASQSRVWFGIMNEPHDVNINTWAATVQEVVTAIRNAGATSQFISLPGNDWQSAGAFISDGSAAALSQVTNPDGSTTNLIFDVHKYLDSDNSGTHAECTTNNIDGAFSPLATWLRQNNRQAILTETGGGNVQSCIQDMCQQIQYLNQNSDVYLGYVGWGAGSFDSTYVLTETPTGSGNSWTDTSLVSSCLARK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI911141
EMBL· GenBank· DDBJ
ETS04885.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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