node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
amtB | glnA | b0451 | b3870 | Ammonium transporter, amt family; Involved in the uptake of ammonia | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | 0.960 |
amtB | glnB | b0451 | b2553 | Ammonium transporter, amt family; Involved in the uptake of ammonia | Regulatory protein p-ii for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme | 0.998 |
amtB | glnD | b0451 | b0167 | Ammonium transporter, amt family; Involved in the uptake of ammonia | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, 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 | 0.966 |
amtB | glnE | b0451 | b3053 | Ammonium transporter, amt family; Involved in the uptake of ammonia | [glutamine synthetase] adenylyltransferase / [glutamine synthetase]-adenylyl-l-tyrosine phosphorylase; 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 inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' 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 re [...] | 0.912 |
amtB | glnG | b0451 | b3868 | Ammonium transporter, amt family; Involved in the uptake of ammonia | Two-component system, ntrc family, nitrogen regulation response regulator glng; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabol [...] | 0.914 |
amtB | glnK | b0451 | b0450 | Ammonium transporter, amt family; Involved in the uptake of ammonia | Nitrogen assimilation regulatory protein for glnl, glne, and amtb; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity) | 0.999 |
amtB | glnL | b0451 | b3869 | Ammonium transporter, amt family; Involved in the uptake of ammonia | Two-component system, ntrc family, nitrogen regulation sensor histidine kinase glnl; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC | 0.979 |
amtB | gltB | b0451 | b3212 | Ammonium transporter, amt family; Involved in the uptake of ammonia | Glutamate synthase (nadph) large chain; Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate | 0.926 |
glnA | amtB | b3870 | b0451 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | Ammonium transporter, amt family; Involved in the uptake of ammonia | 0.960 |
glnA | glnB | b3870 | b2553 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | Regulatory protein p-ii for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme | 0.943 |
glnA | glnD | b3870 | b0167 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, 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 | 0.961 |
glnA | glnE | b3870 | b3053 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | [glutamine synthetase] adenylyltransferase / [glutamine synthetase]-adenylyl-l-tyrosine phosphorylase; 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 inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' 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 re [...] | 0.963 |
glnA | glnG | b3870 | b3868 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | Two-component system, ntrc family, nitrogen regulation response regulator glng; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabol [...] | 0.961 |
glnA | glnK | b3870 | b0450 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | Nitrogen assimilation regulatory protein for glnl, glne, and amtb; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity) | 0.948 |
glnA | glnL | b3870 | b3869 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | Two-component system, ntrc family, nitrogen regulation sensor histidine kinase glnl; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC | 0.994 |
glnA | gltB | b3870 | b3212 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | Glutamate synthase (nadph) large chain; Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate | 0.996 |
glnB | amtB | b2553 | b0451 | Regulatory protein p-ii for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme | Ammonium transporter, amt family; Involved in the uptake of ammonia | 0.998 |
glnB | glnA | b2553 | b3870 | Regulatory protein p-ii for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia | 0.943 |
glnB | glnD | b2553 | b0167 | Regulatory protein p-ii for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme | Pii uridylyltransferase/uridylyl removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, 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 | 0.998 |
glnB | glnE | b2553 | b3053 | Regulatory protein p-ii for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme | [glutamine synthetase] adenylyltransferase / [glutamine synthetase]-adenylyl-l-tyrosine phosphorylase; 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 inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' 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 re [...] | 0.994 |