C5E834 · C5E834_BIFLI
- ProteinPhosphoglucosamine mutase
- GeneglmM
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids461 (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 | 107 | Phosphoserine intermediate | |||
Binding site | 107 | Mg2+ (UniProtKB | ChEBI); via phosphate group | |||
Binding site | 254 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 256 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 258 | Mg2+ (UniProtKB | ChEBI) | |||
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 > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium
Accessions
- Primary accessionC5E834
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 107 | Phosphoserine | |||
Post-translational modification
Activated by phosphorylation.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-137 | Alpha-D-phosphohexomutase alpha/beta/alpha | |||
Domain | 164-267 | Alpha-D-phosphohexomutase alpha/beta/alpha | |||
Domain | 271-381 | Alpha-D-phosphohexomutase alpha/beta/alpha | |||
Domain | 387-453 | Alpha-D-phosphohexomutase C-terminal | |||
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length461
- Mass (Da)48,660
- Last updated2009-07-28 v1
- Checksum0EAEE3C7A4F91139
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS990238 EMBL· GenBank· DDBJ | EEQ54232.1 EMBL· GenBank· DDBJ | Genomic DNA |