Q82DL7 · GLMM_STRAW
- ProteinPhosphoglucosamine mutase
- GeneglmM
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids452 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Catalytic activity
- alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 104 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 104 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 246 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 250 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoglucosamine mutase activity | |
Molecular Function | phosphomannomutase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoglucosamine mutase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionQ82DL7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000147982 | 1-452 | Phosphoglucosamine mutase | |||
Sequence: MGRLFGTDGVRGVANADLTAELALGLSVAAAHVLAEAGTFEGHRPVAVVGRDPRASGEFLEAAVVAGLASAGVDVLLVGVLPTPAVAHLTGALGADLGVMLSASHNAMPDNGIKFFARGGHKLADDLEDRIEAVYEEHRTGAPWDRPTGAGVGRVTSYGEGADQYVAHLMSVLPNRLDGIKVVLDEAHGAAARVSPDAFTRAGAEIITIGAEPDGLNINDGCGSTHLAKLRAAVVEHGADLGIAHDGDADRCLAVDHTGAEVDGDQILAVLALAMRERSALRSDTVVATVMSNLGFKLAMEREGLSFVQTAVGDRYVLEEMKEHGYALGGEQSGHVIILDHATTGDGTLTGLLLAARVAQTGRTLQDLASVMERLPQVLVNVPDVDRARVKTSAELATAVAEAERELGATGRVLLRPSGTEPLVRVMVEAADIEQARSVAGRLADAVKSALG | ||||||
Modified residue | 104 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Activated by phosphorylation.
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length452
- Mass (Da)46,747
- Last updated2003-06-01 v1
- Checksum288F20A4F2708C25
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000030 EMBL· GenBank· DDBJ | BAC72671.1 EMBL· GenBank· DDBJ | Genomic DNA |