W7CTH4 · W7CTH4_9LIST
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids497 (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) | ||||
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 | |
---|---|---|
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 > Bacillales > Listeriaceae > Brochothrix
Accessions
- Primary accessionW7CTH4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
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
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-252 | Carbohydrate kinase FGGY N-terminal | ||||
Sequence: YILAIDQGTTSTRAMLLNKQGKILGTEQREFTQHFPESGWVEHDANEIWSSVLATMSGVLVKTGVNAQEIAGIGITNQRETAVVWDKATSKPIYHAIVWQSRQTVDICTDLKAKGYEKMVTDKTGLLLDPYFAGTKVRWILDHVDGAQERAEKGELAFGTIDTWLIWKLSGGKVHVTDYSNASRTLMYNIYDLKWDEELLEMLNVPAAMLPEVHDSSHVYGHTVGYHFFGLETPIAGVAGDQQAALFG | ||||||
Domain | 262-450 | Carbohydrate kinase FGGY C-terminal | ||||
Sequence: KNTYGTGGFLLMNTGDKAIKSQNGLLTTLAWGINGKVSYALEGSIFVAGSALQWLRDGLRMVKTAPETEEYATRVDSTEGVYVVPAFVGLGAPYWDAEARGAVFGLTRGTTKEHFIRATLESLAYQTRDVIDSMEKDSGIKLETLRVDGGASANNFLMQFQSDLLQVPVERPENKETTVLGAAFLAGLA |
Sequence similarities
Belongs to the FGGY kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length497
- Mass (Da)55,026
- Last updated2014-04-16 v1
- Checksum58AA196867A6C97D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AODH01000022 EMBL· GenBank· DDBJ | EUJ39995.1 EMBL· GenBank· DDBJ | Genomic DNA |