P07984 · GUNA_CELFI

  • Protein
    Endoglucanase A
  • Gene
    cenA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: 1 Endoglucanases which cut internal beta-1,4-glucosidic bonds; 2 Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; 3 Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

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.

144950100150200250300350400
TypeIDPosition(s)Description
Active site247
Active site283Proton donor
Active site423Nucleophile

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
Molecular Functioncellulase activity
Molecular Functionpolysaccharide binding
Biological Processcellulose catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • CBM2Carbohydrate-Binding Module Family 2
    • GH6Glycoside Hydrolase Family 6

Names & Taxonomy

Protein names

  • Recommended name
    Endoglucanase A
  • EC number
  • Alternative names
    • Cellulase A
    • Endo-1,4-beta-glucanase A

Gene names

    • Name
      cenA

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Cellulomonadaceae > Cellulomonas

Accessions

  • Primary accession
    P07984

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-31Tat-type signal
ChainPRO_000000790332-449Endoglucanase A
Disulfide bond35↔134
Disulfide bond248↔291
Disulfide bond390↔426

Post-translational modification

The linker region (also termed 'hinge') may be a potential site for proteolysis.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Keywords

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain32-137CBM2
Compositional bias127-141Polar residues
Region127-170Disordered
Region139-168Linker ('hinge') (Pro-Thr box)
Compositional bias142-167Pro residues
Region438-449Catalytic

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    449
  • Mass (Da)
    46,731
  • Last updated
    1988-08-01 v1
  • Checksum
    67FF887814B3348D
MSTRRTAAALLAAAAVAVGGLTALTTTAAQAAPGCRVDYAVTNQWPGGFGANVTITNLGDPVSSWKLDWTYTAGQRIQQLWNGTASTNGGQVSVTSLPWNGSIPTGGTASFGFNGSWAGSNPTPASFSLNGTTCTGTVPTTSPTPTPTPTTPTPTPTPTPTPTPTVTPQPTSGFYVDPTTQGYRAWQAASGTDKALLEKIALTPQAYWVGNWADASHAQAEVADYTGRAVAAGKTPMLVVYAIPGRDCGSHSGGGVSESEYARWVDTVAQGIKGNPIVILEPDALAQLGDCSGQGDRVGFLKYAAKSLTLKGARVYIDAGHAKWLSVDTPVNRLNQVGFEYAVGFALNTSNYQTTADSKAYGQQISQRLGGKKFVIDTSRNGNGSNGEWCNPRGRALGERPVAVNDGSGLDALLWVKLPGESDGACNGGPAAGQWWQEIALEMARNARW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias127-141Polar residues
Compositional bias142-167Pro residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M15823
EMBL· GenBank· DDBJ
AAA23084.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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