node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OFA32507.1 | glnE | BAE46_05710 | BAE46_05705 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | 0.584 |
glnA | glnD | BAE46_04350 | BAE46_05930 | Type I glutamate--ammonia ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.471 |
glnA | glnE | BAE46_04350 | BAE46_05705 | Type I glutamate--ammonia ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | 0.792 |
glnA | gltB | BAE46_04350 | BAE46_11030 | Type I glutamate--ammonia ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.987 |
glnD | glnA | BAE46_05930 | BAE46_04350 | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | Type I glutamate--ammonia ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.471 |
glnD | glnE | BAE46_05930 | BAE46_05705 | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | 0.776 |
glnD | gltB | BAE46_05930 | BAE46_11030 | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.592 |
glnE | OFA32507.1 | BAE46_05705 | BAE46_05710 | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.584 |
glnE | glnA | BAE46_05705 | BAE46_04350 | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | Type I glutamate--ammonia ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.792 |
glnE | glnD | BAE46_05705 | BAE46_05930 | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.776 |
glnE | gltB | BAE46_05705 | BAE46_11030 | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.528 |
glnE | hrpA | BAE46_05705 | BAE46_00255 | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | ATP-dependent RNA helicase HrpA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.628 |
glnE | tyrA | BAE46_05705 | BAE46_09905 | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | Bifunctional chorismate mutase/prephenate dehydrogenase; Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.421 |
gltB | glnA | BAE46_11030 | BAE46_04350 | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Type I glutamate--ammonia ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.987 |
gltB | glnD | BAE46_11030 | BAE46_05930 | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | protein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.592 |
gltB | glnE | BAE46_11030 | BAE46_05705 | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | 0.528 |
gltB | tyrA | BAE46_11030 | BAE46_09905 | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional chorismate mutase/prephenate dehydrogenase; Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.438 |
hrpA | glnE | BAE46_00255 | BAE46_05705 | ATP-dependent RNA helicase HrpA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | 0.628 |
tyrA | glnE | BAE46_09905 | BAE46_05705 | Bifunctional chorismate mutase/prephenate dehydrogenase; Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of [...] | 0.421 |
tyrA | gltB | BAE46_09905 | BAE46_11030 | Bifunctional chorismate mutase/prephenate dehydrogenase; Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.438 |