| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AHF02992.1 | AHF02994.1 | MARPU_03215 | MARPU_03225 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ribonuclease; Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions. | 0.592 |
| AHF02992.1 | AHF02995.1 | MARPU_03215 | MARPU_03230 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Isocitrate lyase; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.440 |
| AHF02992.1 | aceK | MARPU_03215 | MARPU_03220 | Thioredoxin; 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. | 0.699 |
| AHF02994.1 | AHF02992.1 | MARPU_03225 | MARPU_03215 | Ribonuclease; Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.592 |
| AHF02994.1 | AHF02995.1 | MARPU_03225 | MARPU_03230 | Ribonuclease; Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions. | Isocitrate lyase; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.786 |
| AHF02994.1 | aceK | MARPU_03225 | MARPU_03220 | Ribonuclease; Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions. | 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. | 0.822 |
| AHF02995.1 | AHF02992.1 | MARPU_03230 | MARPU_03215 | Isocitrate lyase; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.440 |
| AHF02995.1 | AHF02994.1 | MARPU_03230 | MARPU_03225 | Isocitrate lyase; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ribonuclease; Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions. | 0.786 |
| AHF02995.1 | aceK | MARPU_03230 | MARPU_03220 | Isocitrate lyase; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; 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. | 0.945 |
| AHF02995.1 | glcB | MARPU_03230 | MARPU_12235 | Isocitrate lyase; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; Derived by automated computational analysis using gene prediction method: Protein Homology. | Malate synthase; 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. | 0.994 |
| AHF04417.1 | aceK | MARPU_11610 | MARPU_03220 | 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. | 0.921 |
| AHF04417.1 | glcB | MARPU_11610 | MARPU_12235 | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | Malate synthase; 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. | 0.626 |
| aceK | AHF02992.1 | MARPU_03220 | MARPU_03215 | 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. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.699 |
| aceK | AHF02994.1 | MARPU_03220 | MARPU_03225 | 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. | Ribonuclease; Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2- oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions. | 0.822 |
| aceK | AHF02995.1 | MARPU_03220 | MARPU_03230 | 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; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.945 |
| aceK | AHF04417.1 | MARPU_03220 | MARPU_11610 | 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. | 0.921 |
| aceK | glcB | MARPU_03220 | MARPU_12235 | 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; 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. | 0.470 |
| glcB | AHF02995.1 | MARPU_12235 | MARPU_03230 | Malate synthase; 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; Catalyzes the reversible formation of glyoxylate and succinate from isocitrate; glyoxylate bypass pathway; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| glcB | AHF04417.1 | MARPU_12235 | MARPU_11610 | Malate synthase; 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. | Converts isocitrate to alpha ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.626 |
| glcB | aceK | MARPU_12235 | MARPU_03220 | Malate synthase; 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; 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. | 0.470 |
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