Q81EK9 · PGDA1_BACCR

Function

function

Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan (PubMed:15961396, PubMed:29983281).
Also acts on soluble chitin substrates and N-acetylchitooligomers. Acts on cell wall peptidoglycan from the Gram-positive bacteria B.cereus and B.subtilis and the Gram-negative bacterium H.pylori. Not active on acetylated xylan (PubMed:15961396).

Catalytic activity

  • peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate.
    EC:3.5.1.104 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Activity regulation

Deacetylase activity is stimulated by hydroxylation on Pro-179 (PubMed:28333455).
Inhibited by CuCl2 and ZnCl2 (PubMed:15961396).
Inhibited by the hydroxamate N-hydroxy-4-(naphthalene-1-yl)benzamide (NHNB) (PubMed:29983281).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
4.1 mMGlcNAc2
2.46 mMGlcNAc3
1.18 mMGlcNAc4
0.37 mMGlcNAc5
0.3 mMGlcNAc6
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
24.3 μmol/min/mgwith GlcNAc2 as substrate
30.6 μmol/min/mgwith GlcNAc3 as substrate
47.3 μmol/min/mgwith GlcNAc4 as substrate
15.5 μmol/min/mgwith GlcNAc5 as substrate
13.4 μmol/min/mgwith GlcNAc6 as substrate

pH Dependence

Optimum pH is 6.0.

Temperature Dependence

Optimum temperature is 50 degrees Celsius.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site88Proton acceptor
Binding site89Zn2+ (UniProtKB | ChEBI)
Binding site139Zn2+ (UniProtKB | ChEBI)
Binding site143Zn2+ (UniProtKB | ChEBI)
Active site233Proton donor

GO annotations

AspectTerm
Molecular Functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Molecular Functionmetal ion binding
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidoglycan-N-acetylglucosamine deacetylase BC_1960
  • EC number
  • Short names
    Peptidoglycan GlcNAc deacetylase

Gene names

    • Ordered locus names
      BC_1960

Organism names

Accessions

  • Primary accession
    Q81EK9

Proteomes

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004476921-275Peptidoglycan-N-acetylglucosamine deacetylase BC_1960
Modified residue1792-hydroxyproline; partial

Post-translational modification

Hydroxylated on Pro-179. Hydroxylation alters the active site and enhances significantly deacetylase activity, probably by creating a more favorable environment for transition-state stabilization. It might be autocatalytic.

Keywords

Interaction

Protein-protein interaction databases

Chemistry

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain81-262NodB homology

Sequence similarities

Belongs to the polysaccharide deacetylase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    275
  • Mass (Da)
    31,652
  • Last updated
    2003-06-01 v1
  • Checksum
    915046AEE0AC6EBF
MYYFYSPEMFAPYQWGLERDVSYAYMPYNSFYYGDYINSLPYAYIPQNYEVQMKADDRGSWTPFSWVEKYAYAFSGPYNKAEVALTFDDGPDLEFTPKILDKLKQHNVKATFFLLGENAEKFPNIVKRIANEGHVIGNHTYSHPNLAKVNEDEYRNQIIKTEEILNRLAGYAPKFIRPPYGEILENQLKWATEQNFMIVQWSVDTVDWKGVSADTITNNVLGNSFPGSVILQHSTPGGHLQGSVDALDKIIPQLKTKGARFVTLPSMFQTSKERK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016877
EMBL· GenBank· DDBJ
AAP08931.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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