A0AAN4BKE4 · A0AAN4BKE4_LACRH
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids510 (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 | 13 | ADP (UniProtKB | ChEBI) | |||
Binding site | 13 | ATP (UniProtKB | ChEBI) | |||
Binding site | 13 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 14 | ATP (UniProtKB | ChEBI) | |||
Binding site | 15 | ATP (UniProtKB | ChEBI) | |||
Binding site | 17 | ADP (UniProtKB | ChEBI) | |||
Binding site | 83 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 83 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 84 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 84 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 135 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 135 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 245 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 245 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 246 | glycerol (UniProtKB | ChEBI) | |||
Binding site | 267 | ADP (UniProtKB | ChEBI) | |||
Binding site | 267 | ATP (UniProtKB | ChEBI) | |||
Binding site | 310 | ADP (UniProtKB | ChEBI) | |||
Binding site | 310 | ATP (UniProtKB | ChEBI) | |||
Binding site | 314 | ATP (UniProtKB | ChEBI) | |||
Binding site | 411 | ADP (UniProtKB | ChEBI) | |||
Binding site | 411 | ATP (UniProtKB | ChEBI) | |||
Binding site | 415 | ADP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | kinase activity | |
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 > Lactobacillaceae > Lacticaseibacillus
Accessions
- Primary accessionA0AAN4BKE4
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 231 | 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 | 5-252 | Carbohydrate kinase FGGY N-terminal | |||
Domain | 262-450 | Carbohydrate kinase FGGY C-terminal | |||
Sequence similarities
Belongs to the FGGY kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length510
- Mass (Da)55,982
- Last updated2024-10-02 v1
- Checksum23090CD9B377A35C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AMQW01000005 EMBL· GenBank· DDBJ | EKS52176.1 EMBL· GenBank· DDBJ | Genomic DNA |