A0A7U5GXA0 · A0A7U5GXA0_9BACL
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids502 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Catalytic activity
- glycerol + ATP = sn-glycerol 3-phosphate + ADP + H+
Activity regulation
Activated by phosphorylation and inhibited by fructose 1,6-bisphosphate (FBP).
Pathway
Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 17 | ADP (UniProtKB | ChEBI) | |||
Binding site | 17 | ATP (UniProtKB | ChEBI) | |||
Binding site | 17 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 18 | ATP (UniProtKB | ChEBI) | |||
Binding site | 88 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 88 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 138 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 138 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 248 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 248 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 249 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 270 | ADP (UniProtKB | ChEBI) | |||
Binding site | 270 | ATP (UniProtKB | ChEBI) | |||
Binding site | 313 | ADP (UniProtKB | ChEBI) | |||
Binding site | 313 | ATP (UniProtKB | ChEBI) | |||
Binding site | 317 | ATP (UniProtKB | ChEBI) | |||
Binding site | 414 | ADP (UniProtKB | ChEBI) | |||
Binding site | 414 | ATP (UniProtKB | ChEBI) | |||
Binding site | 418 | ADP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glycerol kinase activity | |
Biological Process | glycerol catabolic process | |
Biological Process | glycerol-3-phosphate metabolic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Planococcaceae > Sporosarcina
Accessions
- Primary accessionA0A7U5GXA0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homotetramer and homodimer (in equilibrium).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 11-255 | Carbohydrate kinase FGGY N-terminal | |||
Domain | 267-453 | Carbohydrate kinase FGGY C-terminal | |||
Sequence similarities
Belongs to the FGGY kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length502
- Mass (Da)55,130
- Last updated2021-06-02 v1
- Checksum3CCFF5A62AE2DEF7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP015349 EMBL· GenBank· DDBJ | ARK25166.1 EMBL· GenBank· DDBJ | Genomic DNA |