Q02YH8 · Q02YH8_LACLS
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids505 (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 | 21 | ADP (UniProtKB | ChEBI) | |||
Binding site | 21 | ATP (UniProtKB | ChEBI) | |||
Binding site | 21 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 22 | ATP (UniProtKB | ChEBI) | |||
Binding site | 23 | ATP (UniProtKB | ChEBI) | |||
Binding site | 25 | ADP (UniProtKB | ChEBI) | |||
Binding site | 91 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 91 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 92 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 92 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 143 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 143 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 253 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 253 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 254 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 275 | ADP (UniProtKB | ChEBI) | |||
Binding site | 275 | ATP (UniProtKB | ChEBI) | |||
Binding site | 318 | ADP (UniProtKB | ChEBI) | |||
Binding site | 318 | ATP (UniProtKB | ChEBI) | |||
Binding site | 322 | ATP (UniProtKB | ChEBI) | |||
Binding site | 419 | ADP (UniProtKB | ChEBI) | |||
Binding site | 419 | ATP (UniProtKB | ChEBI) | |||
Binding site | 423 | 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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Lactococcus > Lactococcus cremoris subsp. cremoris
Accessions
- Primary accessionQ02YH8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 239 | Phosphohistidine; by HPr | |||
Post-translational modification
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation, which leads to the activation of the enzyme.
Keywords
- PTM
Interaction
Subunit
Homotetramer and homodimer (in equilibrium).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 13-260 | Carbohydrate kinase FGGY N-terminal | |||
Domain | 270-458 | Carbohydrate kinase FGGY C-terminal | |||
Sequence similarities
Belongs to the FGGY kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length505
- Mass (Da)55,678
- Last updated2006-11-14 v1
- Checksum70F4DFC79F5314A2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000425 EMBL· GenBank· DDBJ | ABJ72994.1 EMBL· GenBank· DDBJ | Genomic DNA |