Q7WUL3 · NAG3_CELFI

  • Protein
    Beta-N-acetylglucosaminidase/beta-glucosidase
  • Gene
    nag3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

Catalyzes the cleavage of beta-N-acetyl-D-glucosaminides and beta-D-glucosides. Might be involved in the degradation of glucuronic acid-containing glycosaminoglycans such as hyaluronic acid.

Miscellaneous

Catalyzes hydrolysis by a double-displacement mechanism via a covalent glycosyl-enzyme intermediate, involving the participation of a catalytic nucleophilic group in the enzyme active site.

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)
  • Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
    EC:3.2.1.21 (UniProtKB | ENZYME | Rhea)

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.7 mM4'-nitrophenyl beta-N-acetyl-D-glucosaminide
The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar.

pH Dependence

Optimum pH is 7.3 with 4'-nitrophenyl beta-D-glucopyranoside as substrate. Precipitates below pH 6 and stable from pH 6.8 to 8.4.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site283Nucleophile

GO annotations

AspectTerm
Molecular Functionbeta-glucosidase activity
Molecular Functionbeta-N-acetylhexosaminidase activity
Molecular FunctionN-acetyl-beta-D-galactosaminidase activity
Molecular Functionscopolin beta-glucosidase activity
Biological Processpeptidoglycan turnover
Biological Processpolysaccharide catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • GH3Glycoside Hydrolase Family 3

Names & Taxonomy

Protein names

  • Recommended name
    Beta-N-acetylglucosaminidase/beta-glucosidase
  • EC number
  • Alternative names
    • 3-beta-N-acetyl-D-glucosaminidase/beta-D-glucosidase
    • Nag3

Gene names

    • Name
      nag3
    • Synonyms
      nag3A

Organism names

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

Accessions

  • Primary accession
    Q7WUL3

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002524541-564Beta-N-acetylglucosaminidase/beta-glucosidase

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    564
  • Mass (Da)
    59,993
  • Last updated
    2003-10-01 v1
  • Checksum
    9B1428A4561F71D3
MIDLTAAPFSLDDDGIAWVRTTLAEMGEDEKLGQLFCLITYTSDPEYLGYLTRGLHVGGVMLRTMTAADAAATVTTLQSTATVPLLISANLEGGASQTVQEATHVGSNMALAATGSTDHVRRAATVIGREARALGINWAFTPVVDIDLNFRNPITNTRTFGADAATVAAMGAEYVEAIQAQGLAASAKHFPGDGVDERDQHLLASVNTMSVEEWDDSFGVVYRAAIAAGVKTVMVGHIMLPAYSRALRPGVADRDILPGVVAEELLNDLLRDRLGFNGLVVSDSTTMAGLASVLPRSQAVPRVIAAGCDMFLFTKNLDEDFGYMRAGIRDGVITPERLDEAVTRILALKASLGLHRGTNLPAQGAAGVLADPDHSATAREVAASSITLVKEEPGVLPITRERYPRVLVYDLQNGGSPIGQGARAGAVEQFVDALVEAGHDVTRFEPGGGWEGMAAPTTDVTERHDLVLYLANLSTRSNQTVVRIEWAEPMGANVPAYVHSVPTVFVSFENPYHLFDVPRVRTLINTYGSSPVVLETLLAALQGKAPFAGSSPVDAFCGQWDTHL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF478460
EMBL· GenBank· DDBJ
AAQ05801.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp