node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
aceA | aceB | ECIAI39_4401 | ECIAI39_4400 | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | 0.999 |
aceA | aceK | ECIAI39_4401 | ECIAI39_4404 | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | 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. | 0.981 |
aceA | glcB | ECIAI39_4401 | ECIAI39_3463 | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | 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. | 0.995 |
aceA | icd-2 | ECIAI39_4401 | ECIAI39_1995 | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | 0.831 |
aceB | aceA | ECIAI39_4400 | ECIAI39_4401 | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | 0.999 |
aceB | aceK | ECIAI39_4400 | ECIAI39_4404 | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | 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. | 0.921 |
aceB | glcB | ECIAI39_4400 | ECIAI39_3463 | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | 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. | 0.960 |
aceB | icd-2 | ECIAI39_4400 | ECIAI39_1995 | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | 0.745 |
aceK | aceA | ECIAI39_4404 | ECIAI39_4401 | 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. | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | 0.981 |
aceK | aceB | ECIAI39_4404 | ECIAI39_4400 | 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. | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | 0.921 |
aceK | glcB | ECIAI39_4404 | ECIAI39_3463 | 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. | 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. | 0.536 |
aceK | icd-2 | ECIAI39_4404 | ECIAI39_1995 | 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. | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | 0.976 |
glcB | aceA | ECIAI39_3463 | ECIAI39_4401 | 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. | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | 0.995 |
glcB | aceB | ECIAI39_3463 | ECIAI39_4400 | 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. | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | 0.960 |
glcB | aceK | ECIAI39_3463 | ECIAI39_4404 | 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. | 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. | 0.536 |
glcB | icd-2 | ECIAI39_3463 | ECIAI39_1995 | 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. | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | 0.503 |
icd-2 | aceA | ECIAI39_1995 | ECIAI39_4401 | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | Isocitrate lyase; Function experimentally demonstrated in the studied species; enzyme. | 0.831 |
icd-2 | aceB | ECIAI39_1995 | ECIAI39_4400 | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | Malate synthase A; Function experimentally demonstrated in the studied species; enzyme; Belongs to the malate synthase family. | 0.745 |
icd-2 | aceK | ECIAI39_1995 | ECIAI39_4404 | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | 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. | 0.976 |
icd-2 | glcB | ECIAI39_1995 | ECIAI39_3463 | Isocitrate dehydrogenase, specific for NADP+; Function experimentally demonstrated in the studied species; extrachromosomal origin. | 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. | 0.503 |