| Comment type | Description |
|---|
| Biophysicochemical Properties | Kinetic parameters: KM=0.3 mM for CTP {ECO:0000269|PubMed:18458076}; KM=0.4 mM for dCTP {ECO:0000269|PubMed:18458076}; Vmax=0.018 nM/min/mg enzyme {ECO:0000269|PubMed:18458076}; pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:18458076}; Temperature dependence: Maximum activity at 30 degrees Celsius. Labile above 40 degrees Celsius. {ECO:0000269|PubMed:18458076}; |
| Biophysicochemical Properties | Kinetic parameters: KM=0.3 mM for CTP ; KM=0.4 mM for dCTP ; Vmax=0.018 nM/min/mg enzyme ; pH dependence: Optimum pH is 7.0-7.5. ; Temperature dependence: Maximum activity at 30 degrees Celsius. Labile above 40 degrees Celsius. ; |
| Catalytic Activity | CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2- diacyl-sn-glycerol 3-phosphate. {ECO:0000269|PubMed:18458075, ECO:0000269|PubMed:18458076}. |
| Cofactor | Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:18458076}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18458076}; |
| Cofactor | Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence= ; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence= ; |
| Enzyme Regulation | Inhibited by N-ethylmaleimide, dCTP, and sphingoid bases including sphinganine, sphingosine and phytosphingosine. DAG pyrophosphate, cardiolipin, CDP-DAG, and lyso-PA inhibited activity by 23-66%. Also inhibited by Ca(2+) concentrations of more than 1 mM, by addition of EDTA or EGTA at 5 mM, and by 5 mM Mn(2+) and Zn(2+). Stimulated by major membrane phospholipids including phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidylglycerol, and phosphatidate. Also stimulated to a maximum by addition of TritonX-100 at a concentration of 1 mM, followed by an apparent inhibition of activity at concentrations above 1 mM |
| Enzyme Regulation | Inhibited by N-ethylmaleimide, dCTP, and sphingoid bases including sphinganine, sphingosine and phytosphingosine. DAG pyrophosphate, cardiolipin, CDP-DAG, and lyso-PA inhibited activity by 23-66%. Also inhibited by Ca(2+) concentrations of more than 1 mM, by addition of EDTA or EGTA at 5 mM, and by 5 mM Mn(2+) and Zn(2+). Stimulated by major membrane phospholipids including phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidylglycerol, and phosphatidate. Also stimulated to a maximum by addition of TritonX-100 at a concentration of 1 mM, followed by an apparent inhibition of activity at concentrations above 1 mM. {ECO:0000269|PubMed:18458076}. |
| Function | Involved in pre-tRNA splicing (By similarity). CTP- dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PAH1/SMP2. Involved in the resistance to nickel chloride and nalidixic acid. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus. {ECO:0000250, ECO:0000269|PubMed:10407277, ECO:0000269|PubMed:11481671, ECO:0000269|PubMed:18458075}. |
| Miscellaneous | Present with 784 molecules/cell in log phase SD medium |
| Miscellaneous | Present with 784 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Miscellaneous | Rescues the lethality of dephosphorylated PAH1/SMP2. Overexpression causes the appearance of phosphatidate- enriched membranes around the nucleus, leading to expansion of the nuclear membrane without proliferation of the cortical endoplasmic reticulum membrane. Deletion restores normal nuclear structure in PAH1/SMP2 deleted cells and returns the level of INO1 mRNA to normal. Deletion does not affect the abnormal levels of phosphatidylinositol and major neutral lipid triacylglycerol seen in the PAH1/SMP2 deletion mutant. |
| Similarity | Belongs to the DGK1 family |
| Similarity | Belongs to the DGK1 family. {ECO:0000305}. |
| Subcellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. |