A0A0J9BC22 · A0A0J9BC22_9GAMM
- ProteinGlycerol kinase
- GeneglpK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids503 (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
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 | 16 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 16 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 16 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 17 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 18 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 20 | ADP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 86 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 86 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 87 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 87 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 138 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 138 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 237 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: G | ||||||
Binding site | 239 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: R | ||||||
Binding site | 248 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 249 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 270 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 270 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 313 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 313 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 317 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 414 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 414 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 418 | ADP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 481 | 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 | |
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 > Pseudomonadota > Gammaproteobacteria > Enterobacterales
Accessions
- Primary accessionA0A0J9BC22
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.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-255 | Carbohydrate kinase FGGY N-terminal | ||||
Sequence: YIVALDQGTTSSRAVILDHDANIVAVSQREFEQIYPKTGWVEHDPMDIWATQSSTLVEVLAHADISSDEVAAIGITNQRETTIVWDKETGKPIYNAIVWQDPRTADYCSGLKDQGYEDYIRDTTGLVINPYFSGTKVKWILDHVEGSRERAKRGELLFGTVDTWLVWKMTQGRVHITDYTNASRTMLFNIHTLEWDQKMLDLLDIPREILPEVKASSEVYGQTNIGGKGGTRIPIAGIAGDQQAALYG | ||||||
Domain | 265-453 | Carbohydrate kinase FGGY C-terminal | ||||
Sequence: KNTYGTGCFMLMNTGKEAITSKNGLLTTIACGPRGEVNYALEGAVFIGGASIQWLRDELKLFNDADDSEYFANKVKDSNGVYMVPAFTGLGAPYWDPYARGAIFGLTRGANANHIIRATLESIAFQTRDVLEAMQHDANTRLQTLRVDGGAVANNFLMQFQADILGAHVERPEVKEVTALGAAYLAGLA |
Sequence similarities
Belongs to the FGGY kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length503
- Mass (Da)55,973
- Last updated2015-10-14 v1
- Checksum46F0B5EF610CF32F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JMSP01000321 EMBL· GenBank· DDBJ | KMV70714.1 EMBL· GenBank· DDBJ | Genomic DNA |