| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMQ43188.1 | AMQ43642.1 | AMS64_12855 | AMS64_15435 | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.682 |
| AMQ43188.1 | aceA | AMS64_12855 | AMS64_15440 | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.518 |
| AMQ43188.1 | aceK | AMS64_12855 | AMS64_16835 | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.934 |
| AMQ43642.1 | AMQ43188.1 | AMS64_15435 | AMS64_12855 | Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology. | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.682 |
| AMQ43642.1 | aceA | AMS64_15435 | AMS64_15440 | Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| AMQ43642.1 | aceK | AMS64_15435 | AMS64_16835 | Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.624 |
| aceA | AMQ43188.1 | AMS64_15440 | AMS64_12855 | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.518 |
| aceA | AMQ43642.1 | AMS64_15440 | AMS64_15435 | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| aceA | aceK | AMS64_15440 | AMS64_16835 | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.943 |
| aceK | AMQ43188.1 | AMS64_16835 | AMS64_12855 | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.934 |
| aceK | AMQ43642.1 | AMS64_16835 | AMS64_15435 | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Malate synthase; Catalyzes the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.624 |
| aceK | aceA | AMS64_16835 | AMS64_15440 | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.943 |
| aceK | trmJ-2 | AMS64_16835 | AMS64_16830 | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | RNA methyltransferase; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. | 0.489 |
| trmJ-2 | aceK | AMS64_16830 | AMS64_16835 | RNA methyltransferase; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. | Isocitrate dehydrogenase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.489 |
