node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OLU06421.1 | aceK | BVK87_20280 | BVK87_01895 | SCP2 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional isocitrate dehydrogenase kinase/phosphatase; 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. | 0.407 |
OLU09927.1 | aceA | BVK87_02355 | BVK87_15925 | Isocitrate dehydrogenase (NADP(+)); Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.414 |
OLU09927.1 | aceK | BVK87_02355 | BVK87_01895 | Isocitrate dehydrogenase (NADP(+)); Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional isocitrate dehydrogenase kinase/phosphatase; 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. | 0.947 |
OLU09927.1 | glcB | BVK87_02355 | BVK87_27835 | Isocitrate dehydrogenase (NADP(+)); Derived by automated computational analysis using gene prediction method: Protein Homology. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.613 |
OLU10207.1 | OLU10208.1 | BVK87_01885 | BVK87_01890 | methylcrotonoyl-CoA carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family. | 0.588 |
OLU10207.1 | OLU10210.1 | BVK87_01885 | BVK87_01900 | methylcrotonoyl-CoA carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | isovaleryl-CoA dehydrogenase; Catalyzes the formation of 3-methylbut-2-enoyl CoA from 3-methylbutanoyl CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.983 |
OLU10207.1 | aceK | BVK87_01885 | BVK87_01895 | methylcrotonoyl-CoA carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional isocitrate dehydrogenase kinase/phosphatase; 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. | 0.405 |
OLU10208.1 | OLU10207.1 | BVK87_01890 | BVK87_01885 | acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family. | methylcrotonoyl-CoA carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.588 |
OLU10208.1 | OLU10210.1 | BVK87_01890 | BVK87_01900 | acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family. | isovaleryl-CoA dehydrogenase; Catalyzes the formation of 3-methylbut-2-enoyl CoA from 3-methylbutanoyl CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.767 |
OLU10208.1 | aceK | BVK87_01890 | BVK87_01895 | acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family. | Bifunctional isocitrate dehydrogenase kinase/phosphatase; 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. | 0.728 |
OLU10210.1 | OLU10207.1 | BVK87_01900 | BVK87_01885 | isovaleryl-CoA dehydrogenase; Catalyzes the formation of 3-methylbut-2-enoyl CoA from 3-methylbutanoyl CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. | methylcrotonoyl-CoA carboxylase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.983 |
OLU10210.1 | OLU10208.1 | BVK87_01900 | BVK87_01890 | isovaleryl-CoA dehydrogenase; Catalyzes the formation of 3-methylbut-2-enoyl CoA from 3-methylbutanoyl CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. | acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family. | 0.767 |
OLU10210.1 | OLU10211.1 | BVK87_01900 | BVK87_01905 | isovaleryl-CoA dehydrogenase; Catalyzes the formation of 3-methylbut-2-enoyl CoA from 3-methylbutanoyl CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Amidohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.456 |
OLU10210.1 | aceK | BVK87_01900 | BVK87_01895 | isovaleryl-CoA dehydrogenase; Catalyzes the formation of 3-methylbut-2-enoyl CoA from 3-methylbutanoyl CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional isocitrate dehydrogenase kinase/phosphatase; 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. | 0.781 |
OLU10211.1 | OLU10210.1 | BVK87_01905 | BVK87_01900 | Amidohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | isovaleryl-CoA dehydrogenase; Catalyzes the formation of 3-methylbut-2-enoyl CoA from 3-methylbutanoyl CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.456 |
OLU10211.1 | aceK | BVK87_01905 | BVK87_01895 | Amidohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional isocitrate dehydrogenase kinase/phosphatase; 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. | 0.442 |
OLU10347.1 | aceA | BVK87_00655 | BVK87_15925 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.678 |
OLU10347.1 | aceK | BVK87_00655 | BVK87_01895 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional isocitrate dehydrogenase kinase/phosphatase; 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. | 0.461 |
OLU10347.1 | glcB | BVK87_00655 | BVK87_27835 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Malate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. | 0.417 |
aceA | OLU09927.1 | BVK87_15925 | BVK87_02355 | Isocitrate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate dehydrogenase (NADP(+)); Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.414 |