Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gadA | glnA | Z4930 | Z5406 | Glutamate decarboxylase isozyme; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria (By similarity). | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | 0.916 |
| gadA | glnE | Z4930 | Z4406 | Glutamate decarboxylase isozyme; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria (By similarity). | Adenylylating enzyme for glutamine synthetase; 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 trans [...] | 0.704 |
| gadA | gltB | Z4930 | Z4576 | Glutamate decarboxylase isozyme; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria (By similarity). | Glutamate synthase, large subunit; Residues 1 to 1517 of 1517 are 99.53 pct identical to residues 1 to 1517 of 1517 from Escherichia coli K-12 Strain MG1655: B3212. | 0.952 |
| gadA | xasA | Z4930 | Z2216 | Glutamate decarboxylase isozyme; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria (By similarity). | Acid sensitivity protein, putative transporter; Involved in glutamate-dependent acid resistance. Imports glutamate inside the cell while simultaneously exporting to the periplasm the GABA produced by GadA and GadB. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria (By similarity); Belongs to the amino acid-polyamine-organocation (APC) superfami [...] | 0.999 |
| glnA | gadA | Z5406 | Z4930 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | Glutamate decarboxylase isozyme; Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria (By similarity). | 0.916 |
| glnA | glnB | Z5406 | Z3829 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase 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 (By similarity). | 0.887 |
| glnA | glnD | Z5406 | Z0177 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | Protein PII; 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. | 0.854 |
| glnA | glnE | Z5406 | Z4406 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | Adenylylating enzyme for glutamine synthetase; 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 trans [...] | 0.854 |
| glnA | glnK | Z5406 | Z0562 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | Nitrogen regulatory protein P-II 2; 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. | 0.886 |
| glnA | gltB | Z5406 | Z4576 | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | Glutamate synthase, large subunit; Residues 1 to 1517 of 1517 are 99.53 pct identical to residues 1 to 1517 of 1517 from Escherichia coli K-12 Strain MG1655: B3212. | 0.990 |
| glnB | glnA | Z3829 | Z5406 | 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 (By similarity). | Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | 0.887 |
| glnB | glnD | Z3829 | Z0177 | 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 (By similarity). | Protein PII; 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. | 0.997 |
| glnB | glnE | Z3829 | Z4406 | 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 (By similarity). | Adenylylating enzyme for glutamine synthetase; 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 trans [...] | 0.734 |
| glnB | glnK | Z3829 | Z0562 | 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 (By similarity). | Nitrogen regulatory protein P-II 2; 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. | 0.825 |
| glnB | gltB | Z3829 | Z4576 | 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 (By similarity). | Glutamate synthase, large subunit; Residues 1 to 1517 of 1517 are 99.53 pct identical to residues 1 to 1517 of 1517 from Escherichia coli K-12 Strain MG1655: B3212. | 0.815 |
| glnD | glnA | Z0177 | Z5406 | Protein PII; 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 synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family. | 0.854 |
| glnD | glnB | Z0177 | Z3829 | Protein PII; 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. | 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 (By similarity). | 0.997 |
| glnD | glnE | Z0177 | Z4406 | Protein PII; 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. | Adenylylating enzyme for glutamine synthetase; 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 trans [...] | 0.930 |
| glnD | glnK | Z0177 | Z0562 | Protein PII; 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. | Nitrogen regulatory protein P-II 2; 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. | 0.980 |
| glnD | gltB | Z0177 | Z4576 | Protein PII; 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, large subunit; Residues 1 to 1517 of 1517 are 99.53 pct identical to residues 1 to 1517 of 1517 from Escherichia coli K-12 Strain MG1655: B3212. | 0.891 |
page 1 of 3