Q81EK9 · PGDA1_BACCR
- ProteinPeptidoglycan-N-acetylglucosamine deacetylase BC_1960
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids275 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
Cofactor
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).
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 mM | GlcNAc2 | |||||
2.46 mM | GlcNAc3 | |||||
1.18 mM | GlcNAc4 | |||||
0.37 mM | GlcNAc5 | |||||
0.3 mM | GlcNAc6 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
24.3 μmol/min/mg | with GlcNAc2 as substrate | ||||
30.6 μmol/min/mg | with GlcNAc3 as substrate | ||||
47.3 μmol/min/mg | with GlcNAc4 as substrate | ||||
15.5 μmol/min/mg | with GlcNAc5 as substrate | ||||
13.4 μmol/min/mg | with 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.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | |
Molecular Function | metal ion binding | |
Biological Process | carbohydrate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidoglycan-N-acetylglucosamine deacetylase BC_1960
- EC number
- Short namesPeptidoglycan GlcNAc deacetylase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Accessions
- Primary accessionQ81EK9
Proteomes
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000447692 | 1-275 | Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 | |||
Sequence: MYYFYSPEMFAPYQWGLERDVSYAYMPYNSFYYGDYINSLPYAYIPQNYEVQMKADDRGSWTPFSWVEKYAYAFSGPYNKAEVALTFDDGPDLEFTPKILDKLKQHNVKATFFLLGENAEKFPNIVKRIANEGHVIGNHTYSHPNLAKVNEDEYRNQIIKTEEILNRLAGYAPKFIRPPYGEILENQLKWATEQNFMIVQWSVDTVDWKGVSADTITNNVLGNSFPGSVILQHSTPGGHLQGSVDALDKIIPQLKTKGARFVTLPSMFQTSKERK | ||||||
Modified residue | 179 | 2-hydroxyproline; partial | ||||
Sequence: P |
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
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 81-262 | NodB homology | ||||
Sequence: AEVALTFDDGPDLEFTPKILDKLKQHNVKATFFLLGENAEKFPNIVKRIANEGHVIGNHTYSHPNLAKVNEDEYRNQIIKTEEILNRLAGYAPKFIRPPYGEILENQLKWATEQNFMIVQWSVDTVDWKGVSADTITNNVLGNSFPGSVILQHSTPGGHLQGSVDALDKIIPQLKTKGARFV |
Sequence similarities
Belongs to the polysaccharide deacetylase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length275
- Mass (Da)31,652
- Last updated2003-06-01 v1
- Checksum915046AEE0AC6EBF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016877 EMBL· GenBank· DDBJ | AAP08931.1 EMBL· GenBank· DDBJ | Genomic DNA |