Q03DS8 · GLPK_PEDPA
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids504 (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
- ATP + glycerol = ADP + H+ + sn-glycerol 3-phosphate
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) | ||||
Sequence: T | ||||||
Binding site | 13 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 13 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 14 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 17 | ADP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 83 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 83 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 84 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 84 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 135 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 135 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 245 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 245 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 267 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 267 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 310 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 310 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 314 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 411 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 411 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 415 | ADP (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | glycerol kinase activity | |
Biological Process | glycerol catabolic process | |
Biological Process | glycerol metabolic process | |
Biological Process | glycerol-3-phosphate metabolic process |
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 > Pediococcus
Accessions
- Primary accessionQ03DS8
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000020755 | 1-504 | Glycerol kinase | |||
Sequence: MADKYILAIDEGTTSTRTIIFDHAGNKMADAQREFPQYFPKPGWVEHNANEIWNAVLSTIANAFIESGIKPNQISGIGITNQRETTVIWDKKTGLPIYNAVVWQSRQTAEIAEQLVKDGYGDMIHQKTGLVTDAYFSATKIRWILDHVDGAQARAERGELLFGTIDTWLMWKLTDGDVHVTDYSNASRTMLYNIHKLEWDKEILALLNIPASMLPEVKPNSTIYGKTKDYHFYGSEVPISGMAGDQQAALFGQLAFEPGMVKNTYGTGAFTVMNTGEKPQLSDNNLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGMKLFKKASESEAAAVASQNDNEVYVVPAFTGLGAPYWDPNARGSVFGITRGTTREDFIKATLQSLAYQSRDVIDTMKKDSGIDIPSIRVDGGASNNDYLMQFQSDILGIEIDRASDLETTALGAAFLAGLAVGFWKDLEDLKKEYKPGKVFKPKMSTDEREDLYTGWQEAVAATRQFKHRPRQSK | ||||||
Modified residue | 231 | Phosphohistidine; by HPr | ||||
Sequence: H |
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
Structure
Sequence
- Sequence statusComplete
- Length504
- Mass (Da)55,949
- Last updated2006-11-14 v1
- Checksum5C8B8024DA2F4931
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000422 EMBL· GenBank· DDBJ | ABJ68644.1 EMBL· GenBank· DDBJ | Genomic DNA |