A0A8C2PIQ2 · A0A8C2PIQ2_CAPHI

  • Protein
    Beta-hexosaminidase
  • Gene
    HEXA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A.

Catalytic activity

  • N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + H2O = alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-sulfogalactosamine
    This reaction proceeds in the forward direction.
  • N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H2O = a beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-acetyl-beta-D-galactosamine
    This reaction proceeds in the forward direction.
  • Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
    EC:3.2.1.52 (UniProtKB | ENZYME | Rhea)
  • a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GM3 (d18:1(4E)) + N-acetyl-beta-D-galactosamine
    This reaction proceeds in the forward direction.
  • a ganglioside GM2 + H2O = a ganglioside GM3 + N-acetyl-beta-D-galactosamine
    This reaction proceeds in the forward direction.
  • beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + N-acetyl-D-galactosamine
    This reaction proceeds in the forward direction.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site323Proton donor

GO annotations

AspectTerm
Cellular Componentlysosome
Cellular Componentmembrane
Molecular Functionbeta-N-acetylhexosaminidase 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

    • Name
      HEXA

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Capra

Accessions

  • Primary accession
    A0A8C2PIQ2

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-22
ChainPRO_503469832723-546Beta-hexosaminidase
Disulfide bond58↔104
Disulfide bond277↔328
Disulfide bond522↔539

Keywords

Interaction

Subunit

There are 3 beta-hexosaminidase isozymes: isozyme A (hexosaminidase A) is a heterodimer composed of one subunit alpha and one subunit beta (chain A and B); isozyme B (hexosaminidase B) is a homodimer of two beta subunits (two chains A and B); isozyme S (hexosaminidase S) is a homodimer of two alpha subunits. The composition of the dimer (isozyme A versus isozyme S) has a significant effect on the substrate specificity of the alpha subunit active site.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-145Beta-hexosaminidase eukaryotic type N-terminal
Domain167-504Glycoside hydrolase family 20 catalytic

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    546
  • Mass (Da)
    62,026
  • Last updated
    2022-01-19 v1
  • Checksum
    3DC223081C11B8D3
MAGSTLRFSLLLAAAFAGRATALWPWPQYIQTSELRYTIFPHSFQFQYHLSSAAQVGCSVLDEAFQRYRDLLFGSAAFRFPHPIEKRHTSEKNSLVVLVVTPGCDQFPSLGSVENYTLTINDEQCLLLSETVWGALRGLETFSQLIWRSPEGTFYVNKTDIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKFNVFHWHLVDDSSFPYESFTFPDLTKKGSYNPATHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGVPGLLTPCYSGSHPSGTFGPVNPALNNTYEFMSTFFLEISTVFPDFYLHLGGDEVDFTCWKSNPDIQAFMKKKGFGDDFKKLESFYIQTLLDIVSAYGKGYVVWQEVFDNKVKVRPDTIIQVWREEIPVKYVKEMALVTSAGFRALLSAPWYLNHITYGPDWKEIYLVEPLAFEGSPEQKALVIGGEACMWGEYVDSTNLVPRLCPLGVSHGDCWASLVAQWPRAGAVAERLWSNKMVSNLDFAFKRLAHFRCELLRRGVQAQPLSVGYCDMEFEQT

Genome annotation databases

Similar Proteins

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