A0A1E9B9I4 · A0A1E9B9I4_9STRE
- ProteinPhosphoglucosamine mutase
- GeneglmM
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids449 (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 | 101 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 101 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 240 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 242 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionA0A1E9B9I4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 101 | 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 | 3-135 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: KYFGTDGVRGEANVELTPELAFKLGRFGGYVLSQHTTEAPKVFVGRDTRISGQMLEAALIAGLLSVGIHVYKLGVLATPAVAYLVKTEGASAGVMISASHNPALDNGIKFFGGDGFKLDDDKEAEIEALLDAS | ||||||
Domain | 172-253 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: EGMKVALDTANGAAATSARQIFADLGAQLTVIGETPDGLNINLNVGSTHPEALQELVKESGSAIGLAFDGDSDRLIAVDENG | ||||||
Domain | 257-365 | Alpha-D-phosphohexomutase alpha/beta/alpha | ||||
Sequence: DGDKIMYIIGKYLSEKGQLAQNTIVTTVMSNLGFHKALDREGINKAVTAVGDRYVVEEMRKSGYNLGGEQSGHVILMDYNTTGDGQLSAVQLTKIMQETGKSLSQLAAE | ||||||
Domain | 373-441 | Alpha-D-phosphohexomutase C-terminal | ||||
Sequence: LVNIRVENSMKEKAMEVPAIKAIIEKMEEEMAGNGRILVRPSGTEPLLRVMAEAPTTEEVDYYVDTIAQ |
Sequence similarities
Belongs to the phosphohexose mutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)47,879
- Last updated2017-02-15 v1
- Checksum135AC4AB576AA1EF