A0A1V8YM39 · A0A1V8YM39_9ENTE
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids498 (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 | 14 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 14 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 14 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 16 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 18 | ADP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 84 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 84 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 85 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 85 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 136 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 136 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 246 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 247 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 268 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 268 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 311 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 311 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 315 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 412 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 412 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 416 | ADP (UniProtKB | ChEBI) | ||||
Sequence: N |
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 > Lactobacillales > Enterococcaceae > Enterococcus
Accessions
- Primary accessionA0A1V8YM39
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 232 | 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
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-253 | Carbohydrate kinase FGGY N-terminal | ||||
Sequence: YIMAIDQGTTSSRAIIFDKKGRHIGSSQKEFTQYFPRESWVEHDANEIWNSVQSVIAGAFIESGIKPNQIAGIGITNQRETTVIWEKDTGRPIYHAVVWQSRQSAEIADGLKKEGYQDFFHKKTGLVIDAYFSATKIRWILDHVEGAQERAEKGELLFGTIDSWLVWKLTDGQAHVTDYSNASRTMLFNIHDLDWDQEILDLLNIPRSMLPKPTSNSEIYGYTQGYHFYGSEVPISGMAGDQQAALFG | ||||||
Domain | 263-451 | Carbohydrate kinase FGGY C-terminal | ||||
Sequence: KNTYGTGSFIVMNTGEEPQLSKNNLLTTIGYGINGKVYYALEGSIFVAGSSIQWLRDGLQMLQKASDSEEAAKRSTSEDEVYVVPAFVGLGAPYWDQAARGSMFGLTRGTTKEDIIKATLQSIAYQVRDIIDTMQEDTGIKIPVLKVDGGAANNEYLMQFQTDILNIPIQKAENLETTALGAAFLAGLA |
Sequence similarities
Belongs to the FGGY kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length498
- Mass (Da)55,650
- Last updated2017-06-07 v1
- Checksum0AAE7E8C29FB41B1
Keywords
- Technical term