MULTISPECIES: diacylglycerol kinase [Enterobacteriaceae]
diacylglycerol kinase( domain architecture ID 10198050)
diacylglycerol kinase catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DAGK_IM | cd14264 | Integral membrane diacylglycerol kinase; This mostly bacterial family of homo-trimeric ... |
9-117 | 2.61e-50 | |||
Integral membrane diacylglycerol kinase; This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid. Escherichia coli DAGK participates in the membrane-derived oligosaccharide cycle (MDO cycle) by recycling lipids to restore phosphatidylglycerols that were used up in the biosynthesis of MDOs. DAGK also recycles diacylglycerols that are produced during the biosynthesis of lipopolysaccharides (LPS) back to phospholipids. DAGK is not the main source of phosphatidic acid in de-novo biosynthesis of glycerophospholipids. Escherichia coli DAGK has low activity as an undecaprenol kinase. : Pssm-ID: 260133 Cd Length: 109 Bit Score: 154.90 E-value: 2.61e-50
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Name | Accession | Description | Interval | E-value | |||
DAGK_IM | cd14264 | Integral membrane diacylglycerol kinase; This mostly bacterial family of homo-trimeric ... |
9-117 | 2.61e-50 | |||
Integral membrane diacylglycerol kinase; This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid. Escherichia coli DAGK participates in the membrane-derived oligosaccharide cycle (MDO cycle) by recycling lipids to restore phosphatidylglycerols that were used up in the biosynthesis of MDOs. DAGK also recycles diacylglycerols that are produced during the biosynthesis of lipopolysaccharides (LPS) back to phospholipids. DAGK is not the main source of phosphatidic acid in de-novo biosynthesis of glycerophospholipids. Escherichia coli DAGK has low activity as an undecaprenol kinase. Pssm-ID: 260133 Cd Length: 109 Bit Score: 154.90 E-value: 2.61e-50
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DgkA | COG0818 | Diacylglycerol kinase [Lipid transport and metabolism]; |
3-122 | 5.77e-45 | |||
Diacylglycerol kinase [Lipid transport and metabolism]; Pssm-ID: 440580 Cd Length: 120 Bit Score: 141.77 E-value: 5.77e-45
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DAGK_prokar | pfam01219 | Prokaryotic diacylglycerol kinase; |
16-117 | 1.33e-37 | |||
Prokaryotic diacylglycerol kinase; Pssm-ID: 460117 Cd Length: 102 Bit Score: 122.86 E-value: 1.33e-37
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Name | Accession | Description | Interval | E-value | |||
DAGK_IM | cd14264 | Integral membrane diacylglycerol kinase; This mostly bacterial family of homo-trimeric ... |
9-117 | 2.61e-50 | |||
Integral membrane diacylglycerol kinase; This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid. Escherichia coli DAGK participates in the membrane-derived oligosaccharide cycle (MDO cycle) by recycling lipids to restore phosphatidylglycerols that were used up in the biosynthesis of MDOs. DAGK also recycles diacylglycerols that are produced during the biosynthesis of lipopolysaccharides (LPS) back to phospholipids. DAGK is not the main source of phosphatidic acid in de-novo biosynthesis of glycerophospholipids. Escherichia coli DAGK has low activity as an undecaprenol kinase. Pssm-ID: 260133 Cd Length: 109 Bit Score: 154.90 E-value: 2.61e-50
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DgkA | COG0818 | Diacylglycerol kinase [Lipid transport and metabolism]; |
3-122 | 5.77e-45 | |||
Diacylglycerol kinase [Lipid transport and metabolism]; Pssm-ID: 440580 Cd Length: 120 Bit Score: 141.77 E-value: 5.77e-45
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DAGK_prokar | pfam01219 | Prokaryotic diacylglycerol kinase; |
16-117 | 1.33e-37 | |||
Prokaryotic diacylglycerol kinase; Pssm-ID: 460117 Cd Length: 102 Bit Score: 122.86 E-value: 1.33e-37
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DAGK_IM_like | cd14263 | Integral membrane diacylglycerol kinase and similar enzymes; This mostly bacterial family of ... |
12-117 | 1.22e-27 | |||
Integral membrane diacylglycerol kinase and similar enzymes; This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of substrates such as diacylglycerol to phosphatidic acid or of undecaprenol to undecaprenyl phosphate. They are not related other cytosolic or membrane-associated kinases, including the eukaryotic diacylglycerol kinases. Pssm-ID: 260132 Cd Length: 106 Bit Score: 97.52 E-value: 1.22e-27
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UDPK_IM_like | cd14265 | Integral membrane undecaprenol kinase and similar enzymes; This mostly bacterial family of ... |
12-117 | 9.39e-23 | |||
Integral membrane undecaprenol kinase and similar enzymes; This mostly bacterial family of homo-trimeric integral membrane enzymes, the products of the dgkA gene, catalyzes the ATP-dependent phosphorylation of undecaprenol to undecaprenyl phosphate. C55-isoprenyl (undecaprenyl) pyroposphate acts as a scaffold for the assembly of peptidoglycan components; undecaprenol kinase (UDPK) is involved in recycling undecaprenyl units for re-use in the peptidoglycan biosynthesis. UDPK does not participate in the de-novo biosynthesis of undecaprenyl phosphate. Gram-positive bacteria have a large pool of free undecaprenol, in contrast to gram-negative bacteria. UDPK may also play a role in a stress-induced pathway that affects the function of ribosomes. In Streptococcus mutans, UDPK has been shown to be required for biofilm formation, such as in the case of smooth surface dental caries. Members of the UDPK family have low activity as diacylglycerol kinases (DAGK), and many of them are annotated as DAGKs. Pssm-ID: 260134 Cd Length: 106 Bit Score: 85.13 E-value: 9.39e-23
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UDPK_IM_PAP2_like | cd14266 | Integral membrane undecaprenol kinase domain co-occurring with type 2 phosphatidic acid ... |
12-111 | 1.39e-10 | |||
Integral membrane undecaprenol kinase domain co-occurring with type 2 phosphatidic acid phosphatase-like domains; This bacterial family of homo-trimeric integral membrane enzyme domains catalyzes the ATP-dependent phosphorylation of of undecaprenol to undecaprenyl phosphate. They sit N-terminally to phosphatase domains that are members of the type 2 phosphatidic acid phosphatase superfamily, and the function of members of this domain architecture was determined to be undecaprenyl pyrophosphate phosphatases. The bi-functional enzymes might generate undecaprenyl phosphate via two mechanisms - the phosphorylation of undecaprenol or the cleavage of the terminal phosphate group of undecaprenyl pyrophosphate. Pssm-ID: 260135 Cd Length: 106 Bit Score: 54.10 E-value: 1.39e-10
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Blast search parameters | ||||
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