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A0A068WA89 · A0A068WA89_ECHGR

Function

Catalytic activity

  • Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
    EC:3.2.1.52 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

151750100150200250300350400450500
TypeIDPosition(s)Description
Active site314Proton donor

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 Componentlysosome
Cellular Componentmembrane
Molecular Functionbeta-N-acetylhexosaminidase activity
Molecular FunctionN-acetyl-beta-D-galactosaminidase activity
Biological Processcarbohydrate metabolic process
Biological Processganglioside catabolic process
Biological Processglycosaminoglycan metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Beta-hexosaminidase
  • EC number

Gene names

    • ORF names
      EgrG_000901900

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Spiralia > Lophotrochozoa > Platyhelminthes > Cestoda > Eucestoda > Cyclophyllidea > Taeniidae > Echinococcus > Echinococcus granulosus group

Accessions

  • Primary accession
    A0A068WA89

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-21
ChainPRO_503371100022-517Beta-hexosaminidase
Disulfide bond51↔93
Disulfide bond268↔319
Disulfide bond496↔514

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain22-154Beta-hexosaminidase bacterial type N-terminal
Domain158-478Glycoside hydrolase family 20 catalytic

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    517
  • Mass (Da)
    59,034
  • Last updated
    2014-10-01 v1
  • MD5 Checksum
    70EFF26B66D19E6A76C6942A7FB15F67
MSQVCTSLYLLLLLLLSPSLSLIPQPVSFGISPQYYRLPFEVDVQHNAPYCFTLHASIKRLLESFNLRHLIRDLPTSFAGNITHLLINISSECNELLGVLYPKEGSKEDYQVIISGGVIWINASEVWGAMHGLTSVAQLVMSTSKYLPNVRISDMPRWPFRSFLIDTSRHFLPLQYILQFLKAMATVKMNVLHWHIVDDQSFPYESYTFPKLSDKGAYSQIHATYTQQDVRIIIEYARSLGIRVMPEIDTPGHTRSWGYGYPTLLTPCFSRRGPTGRYGPLNPIKNTTYDFVGQLIAEIAKTFPDSALHLGGDEVDFSCWESNPEIRDFMQKMGFNSSYTKLEDYYFANLFKKIKEVTKKPIKVYMWQEIFDDGVEINDSTTVHVWKDGAWPKEMDMVTRAGKEVIFSACWYLSSIRFGEDWIDRYQCDPASFTNNTKQLALIKGGGAAMWGEYVDHTNLISRSWPRGAAVAERLWSPAQVHDVNDMRIRLISYRCFLLAMGLNGEPIAGPDYCDFA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LK028576
EMBL· GenBank· DDBJ
CDS16591.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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