Q9NJP9 · GLPK_TRYBB
- ProteinGlycerol kinase, glycosomal
- GeneGK
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids512 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the phosphorylation of glycerol using ATP (PubMed:10759857, PubMed:11154065).
Under anoxic conditions, when glycerol 3-phosphate accumulates in the glycosome, it catalyzes the reverse reaction, maintaining the ATP balance (PubMed:10759857, PubMed:11154065).
Key enzyme for the survival of bloodstream forms under anoxic conditions (PubMed:11154065).
Under anoxic conditions, when glycerol 3-phosphate accumulates in the glycosome, it catalyzes the reverse reaction, maintaining the ATP balance (PubMed:10759857, PubMed:11154065).
Key enzyme for the survival of bloodstream forms under anoxic conditions (PubMed:11154065).
Catalytic activity
- ATP + glycerol = ADP + H+ + sn-glycerol 3-phosphateThis reaction proceeds in the forward and the backward directions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.24 mM | ATP | |||||
0.246 mM | ATP | |||||
0.56 mM | ADP | |||||
3.29 mM | ADP | |||||
0.44 mM | glycerol | |||||
0.169 mM | glycerol | |||||
3.83 mM | sn-glycerol 3-phosphate | |||||
12.56 mM | sn-glycerol 3-phosphate |
pH Dependence
Optimum pH is 8.0 (PubMed:10759857).
Optimum pH is 8.5 for glycerol phosphorylation and 7.0 for ATP formation (PubMed:11154065).
Optimum pH is 8.5 for glycerol phosphorylation and 7.0 for ATP formation (PubMed:11154065).
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 | 11 | substrate | ||||
Sequence: T | ||||||
Binding site | 15 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 84 | substrate | ||||
Sequence: R | ||||||
Binding site | 139 | substrate | ||||
Sequence: Y | ||||||
Binding site | 254 | substrate | ||||
Sequence: D | ||||||
Binding site | 276 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 321 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 422-426 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLSKN |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | glycosome | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | glycerol kinase activity | |
Biological Process | glycerol catabolic process | |
Biological Process | glycerol-3-phosphate biosynthetic process | |
Biological Process | glycerol-3-phosphate metabolic process | |
Biological Process | glycolytic process | |
Biological Process | triglyceride metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol kinase, glycosomal
- EC number
- Short namesGK; Glycerokinase
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Trypanosoma
Accessions
- Primary accessionQ9NJP9
- Secondary accessions
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 3 | |||||
Sequence: Y → I | ||||||
Mutagenesis | 141 | Increased affinity for glycerol and glycerol 3-phosphate. | ||||
Sequence: A → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059541 | 1-512 | Glycerol kinase, glycosomal | |||
Sequence: MKYVGSIDQGTTSTRFIIFDERQRPVSVHQVPHTQHTPHPGWLEHDPMEIFRSACKCMSVAIAKLRQKDASFRKIEAIGITNQRETTVAWDRVTKEPLCYAPVWNDLRTYDITKKVTAELGGGDSMFASKITGLPVSTYFAAFKMRWMLENVPAVADACRRGTLCFGTIDTWLMYKLSGGKAFVTDVTNASRTFLMDLRTRKWSPELCEKLKIPMETLPEIRSNSELFGYVETDECGVAAALNERTPIMGSIGDQQSALFGNMCFEKGEAKNTYGTGCFLLMNVGEEARFSKHGLLSTVGFQVGRDGPCYYALEGAIACAGATVEWMRRNMNLFSHITECEKLARSVPGTQGIVFVPAFSGLLAPYWDPSARGTIVGMTLKTTRAHVIRAALQAIALQLNDVVGSMKRDAGLNLSSLRVDGGLSKNGLLMEIQASLLGVDILVPSMHETTALGAALCAGLAAGVWTSLEEVKAVSRRENSWKTVSPSGSAMEREAMIAEWREALKRTKWAKL |
Structure
Sequence
- Sequence statusComplete
- Length512
- Mass (Da)56,366
- Last updated2000-10-01 v1
- ChecksumA4A642AA0C572DB0
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 508-509 | in Ref. 2; CAC67800 | ||||
Sequence: KW → SG |