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glnD | Uridylyltransferase; 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. (890 aa) | ||||
glnK | 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); Belongs to the P(II) protein family. (112 aa) | ||||
amtB | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. (428 aa) | ||||
glnB | 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; Belongs to the P(II) protein family. (112 aa) | ||||
glnL | Sensory histidine kinase in two-component regulatory system with GlnG; 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. (349 aa) |
node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
amtB | glnB | b0451 | b2553 | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | 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; Belongs to the P(II) protein family. | 0.999 |
amtB | glnD | b0451 | b0167 | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | Uridylyltransferase; 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. | 0.945 |
amtB | glnK | b0451 | b0450 | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | 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); Belongs to the P(II) protein family. | 0.999 |
amtB | glnL | b0451 | b3869 | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | 0.985 |
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; Belongs to the P(II) protein family. | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | 0.999 |
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; Belongs to the P(II) protein family. | Uridylyltransferase; 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. | 0.999 |
glnB | glnK | b2553 | b0450 | 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; Belongs to the P(II) protein family. | 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); Belongs to the P(II) protein family. | 0.965 |
glnB | glnL | b2553 | b3869 | 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; Belongs to the P(II) protein family. | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | 0.999 |
glnD | amtB | b0167 | b0451 | Uridylyltransferase; 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. | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | 0.945 |
glnD | glnB | b0167 | b2553 | Uridylyltransferase; 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. | 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; Belongs to the P(II) protein family. | 0.999 |
glnD | glnK | b0167 | b0450 | Uridylyltransferase; 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. | 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); Belongs to the P(II) protein family. | 0.993 |
glnD | glnL | b0167 | b3869 | Uridylyltransferase; 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. | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | 0.973 |
glnK | amtB | b0450 | b0451 | 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); Belongs to the P(II) protein family. | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | 0.999 |
glnK | glnB | b0450 | b2553 | 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); Belongs to the P(II) protein family. | 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; Belongs to the P(II) protein family. | 0.965 |
glnK | glnD | b0450 | b0167 | 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); Belongs to the P(II) protein family. | Uridylyltransferase; 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. | 0.993 |
glnK | glnL | b0450 | b3869 | 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); Belongs to the P(II) protein family. | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | 0.997 |
glnL | amtB | b3869 | b0451 | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. | 0.985 |
glnL | glnB | b3869 | b2553 | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | 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; Belongs to the P(II) protein family. | 0.999 |
glnL | glnD | b3869 | b0167 | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | Uridylyltransferase; 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. | 0.973 |
glnL | glnK | b3869 | b0450 | Sensory histidine kinase in two-component regulatory system with GlnG; 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. | 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); Belongs to the P(II) protein family. | 0.997 |