A0A2T4RRM7 · A0A2T4RRM7_MAMSC
- 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
- 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 | 12 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 12 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 12 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 13 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 14 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 16 | ADP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 82 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 82 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 83 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 83 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 134 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 134 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 243 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 243 | sn-glycerol 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 244 | glycerol (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 265 | ADP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 265 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 308 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 308 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 312 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 409 | ADP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 409 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 413 | 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-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
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Mammaliicoccus
Accessions
- Primary accessionA0A2T4RRM7
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 229 | 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 | 4-250 | Carbohydrate kinase FGGY N-terminal | ||||
Sequence: YILSIDQGTTSSRAILFDKEGTIKFVSQREFKQYFPKGGWVEHDANEIWTSVLAVISSVLNENNISPKQIEGIGITNQRETAVVWDKNTGRPVYHAIVWQSRQTQDICTELKSKDLEPIFKEKTGLLLDPYFSGTKVKWILDNVEGAREKAENGDLLFGTIDTWLIWKFTGDVHVTDYSNASRTLMYNIYDLKWDEELLEYLDVPASMLPEVKPSSEVYGYTQEHHFFGEKIAIAGVAGDQQAALFG | ||||||
Domain | 260-448 | Carbohydrate kinase FGGY C-terminal | ||||
Sequence: KNTYGTGGFMLMNTGEKAVKSESGLLTTLAYGLDGKVNYALEGSIFVSGSAIQWLRDGLRMIKSAPASEDYANRVKSTEGVYVVPAFVGLGTPYWDADARGAIFGLTRGTEKEHFIRATLESLCYQTRDVLEAMEKDSGINVETLRVDGGAVKNNFLMQFQADIVNTPVERPEVNETTALGAAYLAGLA |
Sequence similarities
Belongs to the FGGY kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length497
- Mass (Da)55,745
- Last updated2018-07-18 v1
- Checksum86F570346A8DB72C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP022046 EMBL· GenBank· DDBJ | ASE34306.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAAMFH010000001 EMBL· GenBank· DDBJ | NGX74551.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP065960 EMBL· GenBank· DDBJ | QQC96409.1 EMBL· GenBank· DDBJ | Genomic DNA |