O34450 · NAGA_BACSU
- ProteinN-acetylglucosamine-6-phosphate deacetylase
- GenenagA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids396 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides (PubMed:14557261).
Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate (PubMed:14557261).
Essential for growth on N-acetylglucosamine (PubMed:23667565).
Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate (PubMed:14557261).
Essential for growth on N-acetylglucosamine (PubMed:23667565).
Catalytic activity
- N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
Cofactor
Note: Binds 2 divalent metal cations per subunit.
Pathway
Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 63 | Fe cation 1 (UniProtKB | ChEBI) | |||
Binding site | 65 | Fe cation 1 (UniProtKB | ChEBI) | |||
Binding site | 136 | Fe cation 1 (UniProtKB | ChEBI) | |||
Binding site | 136 | Fe cation 2 (UniProtKB | ChEBI) | |||
Binding site | 147-148 | substrate | |||
Binding site | 202 | Fe cation 2 (UniProtKB | ChEBI) | |||
Binding site | 223 | Fe cation 2 (UniProtKB | ChEBI) | |||
Binding site | 226-227 | substrate | |||
Binding site | 234 | substrate | |||
Binding site | 255-258 | substrate | |||
Active site | 281 | Proton donor | |||
Binding site | 281 | Fe cation 1 (UniProtKB | ChEBI) | |||
Binding site | 314-316 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | iron ion binding | |
Molecular Function | N-acetylgalactosamine-6-phosphate deacetylase activity | |
Molecular Function | N-acetylglucosamine-6-phosphate deacetylase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | N-acetylglucosamine catabolic process | |
Biological Process | N-acetylneuraminate catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylglucosamine-6-phosphate deacetylase
- EC number
- Short namesGlcNAc 6-P deacetylase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionO34450
Proteomes
Phenotypes & Variants
Disruption phenotype
Deletion of the gene prevents growth on N-acetylglucosamine, but has no effect on growth on glucosamine.
Chemistry
Expression
Induction
Expression is repressed by the HTH-type transcriptional regulator NagR.
Interaction
Structure
Sequence
- Sequence statusComplete
- Length396
- Mass (Da)42,622
- Last updated1998-01-01 v1
- MD5 Checksum880D188D1C1128168EF426196FABBE52
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF017113 EMBL· GenBank· DDBJ | AAC67285.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB15506.1 EMBL· GenBank· DDBJ | Genomic DNA |