node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFO90319.1 | glnE | PGA1_c05890 | PGA1_c20010 | Thioesterase domain-containing protein. | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | 0.556 |
AFO91376.1 | glnD | PGA1_c16740 | PGA1_c26750 | Diguanylate cyclase domain-containing transport protein. | Uridylyltransferase GlnD; 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 assimilation and metabolism. | 0.517 |
AFO91376.1 | glnE | PGA1_c16740 | PGA1_c20010 | Diguanylate cyclase domain-containing transport protein. | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | 0.512 |
AFO91376.1 | gltB | PGA1_c16740 | PGA1_c36100 | Diguanylate cyclase domain-containing transport protein. | Glutamate synthase [NADPH] large chain. | 0.913 |
AFO91376.1 | nadE | PGA1_c16740 | PGA1_c26450 | Diguanylate cyclase domain-containing transport protein. | Glutamine-dependent NAD(+) synthetase NadE; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.711 |
AFO91688.1 | AFO91690.1 | PGA1_c19980 | PGA1_c20000 | Hypothetical protein. | Hypothetical protein. | 0.525 |
AFO91688.1 | glnE | PGA1_c19980 | PGA1_c20010 | Hypothetical protein. | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | 0.506 |
AFO91688.1 | rlmI | PGA1_c19980 | PGA1_c19990 | Hypothetical protein. | Ribosomal RNA large subunit methyltransferase I. | 0.823 |
AFO91690.1 | AFO91688.1 | PGA1_c20000 | PGA1_c19980 | Hypothetical protein. | Hypothetical protein. | 0.525 |
AFO91690.1 | glnE | PGA1_c20000 | PGA1_c20010 | Hypothetical protein. | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | 0.864 |
AFO91690.1 | rlmI | PGA1_c20000 | PGA1_c19990 | Hypothetical protein. | Ribosomal RNA large subunit methyltransferase I. | 0.538 |
bcp | glnE | PGA1_c17440 | PGA1_c20010 | Putative peroxiredoxin Bcp. | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | 0.650 |
glnA | glnE | PGA1_c18720 | PGA1_c20010 | Glutamine synthetase GlnA. | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | 0.567 |
glnA | gltB | PGA1_c18720 | PGA1_c36100 | Glutamine synthetase GlnA. | Glutamate synthase [NADPH] large chain. | 0.976 |
glnA | nadE | PGA1_c18720 | PGA1_c26450 | Glutamine synthetase GlnA. | Glutamine-dependent NAD(+) synthetase NadE; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.471 |
glnD | AFO91376.1 | PGA1_c26750 | PGA1_c16740 | Uridylyltransferase GlnD; 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 assimilation and metabolism. | Diguanylate cyclase domain-containing transport protein. | 0.517 |
glnD | glnE | PGA1_c26750 | PGA1_c20010 | Uridylyltransferase GlnD; 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 assimilation and metabolism. | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | 0.825 |
glnD | gltB | PGA1_c26750 | PGA1_c36100 | Uridylyltransferase GlnD; 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 assimilation and metabolism. | Glutamate synthase [NADPH] large chain. | 0.814 |
glnD | nadE | PGA1_c26750 | PGA1_c26450 | Uridylyltransferase GlnD; 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 assimilation and metabolism. | Glutamine-dependent NAD(+) synthetase NadE; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.434 |
glnE | AFO90319.1 | PGA1_c20010 | PGA1_c05890 | Glutamate-ammonia-ligase adenylyltransferase GlnE; 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 GlnE binds the signal t [...] | Thioesterase domain-containing protein. | 0.556 |