A0A1C7WEC9 · A0A1C7WEC9_9GAMM
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids502 (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
Activity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system.
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 | 15 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 15 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 16 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 17 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 19 | ADP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 85 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 85 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 86 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 86 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 137 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 137 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 236 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: G | ||||||
Binding site | 238 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: R | ||||||
Binding site | 247 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 247 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 269 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 269 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 312 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 312 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 316 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 413 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 413 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 417 | ADP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 480 | Zn2+ (UniProtKB | ChEBI); ligand shared with EIIA-Glc | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glycerol kinase activity | |
Molecular Function | metal ion binding | |
Biological Process | glycerol catabolic 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia
Accessions
- Primary accessionA0A1C7WEC9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-254 | Carbohydrate kinase FGGY N-terminal | ||||
Sequence: YIVALDQGTTSSRAVVLDHDANIVAVSQREFTQIYPKAGWVEHDPMEIWSSQSSTLVEVLAKADISSDQIAGIGITNQRETTIVWEKETGKPIYNAIVWQCRRTADICEKLKRDGLEEYIRHNTGLVVDPYFSGTKVKWILDHVEGARERAKRGELLFGTVDTWLVWKMTQGRVHVTDYTNASRTMMFNIHELDWDDRMLEALDIPRAMLPKVRPSSEVYGQTNIGGKGGTRIPIAGIAGDQQAALYG | ||||||
Domain | 264-452 | Carbohydrate kinase FGGY C-terminal | ||||
Sequence: KNTYGTGCFLLMNTGKEAVRSNHGLLTTIACGPRGEVNYALEGAVFIGGASIQWLRDELKLISDAADSEYFATKVKDSNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNSNHIIRATLESIAYQTRDVLDAMQADANTRLQSLRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLA |
Sequence similarities
Belongs to the FGGY kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length502
- Mass (Da)55,728
- Last updated2016-11-30 v1
- ChecksumF8CD29D0644B632A