A0A0E2HAF4 · A0A0E2HAF4_9FIRM
- ProteinPhosphoglucosamine mutase
- GeneglmM
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids450 (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 | 102 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 102 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 242 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | 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 > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Enterocloster
Accessions
- Primary accessionA0A0E2HAF4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 102 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Activated by phosphorylation.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-136 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: KYFGTDGFRGEANVDLTVEHAYKVGRFLGWCYGQKMPDERCRVVIGKDTRRSSYMFEYSLVAGLTASGADVYLLHVTTTPSVSYVVRTEGFNCGIMISASHNPFYDNGIKVINERGEKLEESVILEIEKYLDGE | ||||||
Domain | 171-255 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: RSFKNMKVALDCSNGSASAIAKNVFDALGAETHVMNNEPNGLNINTNCGSTHIEHLQKFVVDEKCDIGFAYDGDADRCIAVDKNG | ||||||
Domain | 259-367 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: DGDSIMYICGKYMKEQGSLFNNTVVTTIMSNFGLYKAFDREGIAYVKTAVGDKYVYENMAATGHCLGGEQSGHIIFSKHATTGDGILTSLKVMEVVLEKKQPLDKLASE | ||||||
Domain | 375-440 | Alpha-D-phosphohexomutase C-terminal | ||||
Sequence: LKNVRVKDKKTAQDDETVQAEVARVTRSLGSDGRILLRQSGTEPVVRVMVEAPDIQTCETYVDQVI |
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length450
- Mass (Da)49,647
- Last updated2015-05-27 v1
- ChecksumF34434108AD79225
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGYR01000029 EMBL· GenBank· DDBJ | ENZ13719.1 EMBL· GenBank· DDBJ | Genomic DNA |