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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo1480 | glnD | azo1480 | azo1911 | Probable Nitrogen regulatory protein P-II 1. Could be involved in the regulation of nitrogen fixation.Belongs to the P(II) protein family.55% similarity with Methanothermobacter thermautotrophicus,TrEMBL:O26758 Pfam:PF00543, InterPro:IPR002332,IPR002187 No Signal peptide present. No TMH reported. | Putative protein-PII 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 fixation and metabolism. | 0.697 |
| azo1480 | gltB | azo1480 | azo3642 | Probable Nitrogen regulatory protein P-II 1. Could be involved in the regulation of nitrogen fixation.Belongs to the P(II) protein family.55% similarity with Methanothermobacter thermautotrophicus,TrEMBL:O26758 Pfam:PF00543, InterPro:IPR002332,IPR002187 No Signal peptide present. No TMH reported. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.603 |
| azo1480 | ntrB | azo1480 | azo0736 | Probable Nitrogen regulatory protein P-II 1. Could be involved in the regulation of nitrogen fixation.Belongs to the P(II) protein family.55% similarity with Methanothermobacter thermautotrophicus,TrEMBL:O26758 Pfam:PF00543, InterPro:IPR002332,IPR002187 No Signal peptide present. No TMH reported. | Nitrogen regulation protein NR(II),; High confidence in function and specificity. | 0.759 |
| cobB | glnD | azo3550 | azo1911 | Cobyrinic acid AC-diamide synthase. Responsible for the amidation of carboxylic groups at position A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP is hydrogenolyzed for each amidation (By similarity). cbiA: cobyrinic acid ac-diamide synthase; High confidence in function and specificity. | Putative protein-PII 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 fixation and metabolism. | 0.509 |
| glnB | glnD | azo1361 | azo1911 | PII-like signal transmitter proteins are involved in the regulation of ammonium assimilation and nitrogen fixation. The PII-like proteins differed from each other in details of N-sensing. They were covalently modified by uridylylation upon nitrogen limitation. Similar to trembl|Q9EZQ2 (100%) and to trembl|Q8XWX5 (82%). Pfam: Nitrogen regulatory protein P-II; High confidence in function and specificity. | Putative protein-PII 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 fixation and metabolism. | 0.986 |
| glnB | gltB | azo1361 | azo3642 | PII-like signal transmitter proteins are involved in the regulation of ammonium assimilation and nitrogen fixation. The PII-like proteins differed from each other in details of N-sensing. They were covalently modified by uridylylation upon nitrogen limitation. Similar to trembl|Q9EZQ2 (100%) and to trembl|Q8XWX5 (82%). Pfam: Nitrogen regulatory protein P-II; High confidence in function and specificity. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.603 |
| glnB | ntrB | azo1361 | azo0736 | PII-like signal transmitter proteins are involved in the regulation of ammonium assimilation and nitrogen fixation. The PII-like proteins differed from each other in details of N-sensing. They were covalently modified by uridylylation upon nitrogen limitation. Similar to trembl|Q9EZQ2 (100%) and to trembl|Q8XWX5 (82%). Pfam: Nitrogen regulatory protein P-II; High confidence in function and specificity. | Nitrogen regulation protein NR(II),; High confidence in function and specificity. | 0.988 |
| glnD | azo1480 | azo1911 | azo1480 | Putative protein-PII 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 fixation and metabolism. | Probable Nitrogen regulatory protein P-II 1. Could be involved in the regulation of nitrogen fixation.Belongs to the P(II) protein family.55% similarity with Methanothermobacter thermautotrophicus,TrEMBL:O26758 Pfam:PF00543, InterPro:IPR002332,IPR002187 No Signal peptide present. No TMH reported. | 0.697 |
| glnD | cobB | azo1911 | azo3550 | Putative protein-PII 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 fixation and metabolism. | Cobyrinic acid AC-diamide synthase. Responsible for the amidation of carboxylic groups at position A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP is hydrogenolyzed for each amidation (By similarity). cbiA: cobyrinic acid ac-diamide synthase; High confidence in function and specificity. | 0.509 |
| glnD | glnB | azo1911 | azo1361 | Putative protein-PII 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 fixation and metabolism. | PII-like signal transmitter proteins are involved in the regulation of ammonium assimilation and nitrogen fixation. The PII-like proteins differed from each other in details of N-sensing. They were covalently modified by uridylylation upon nitrogen limitation. Similar to trembl|Q9EZQ2 (100%) and to trembl|Q8XWX5 (82%). Pfam: Nitrogen regulatory protein P-II; High confidence in function and specificity. | 0.986 |
| glnD | glnE | azo1911 | azo1293 | Putative protein-PII 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 fixation and metabolism. | Probable [glutamate-ammonia-ligase] adenylyltransferase; 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 si [...] | 0.805 |
| glnD | glnK | azo1911 | azo3739 | Putative protein-PII 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 fixation and metabolism. | PII-like signal transmitter proteins are involved in the regulation of ammonium assimilation and nitrogen fixation. The PII-like proteins differed from each other in details of N-sensing. They were covalently modified by uridylylation upon nitrogen limitation. Similar to trembl|Q9EZQ3 (100%) and to trembl|Q7NQY3 (87%). Pfam: Nitrogen regulatory protein P-II; High confidence in function and specificity. | 0.882 |
| glnD | glnY | azo1911 | azo3014 | Putative protein-PII 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 fixation and metabolism. | PII-like signal transmitter proteins are involved in the regulation of ammonium assimilation and nitrogen fixation. The PII-like proteins differed from each other in details of N-sensing. They were covalently modified by uridylylation upon nitrogen limitation. Similar to trembl|Q9EZQ4 (100%) and to trembl|Q9RBK0 (78%). Pfam: Nitrogen regulatory protein P-II; High confidence in function and specificity. | 0.874 |
| glnD | gltB | azo1911 | azo3642 | Putative protein-PII 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 fixation and metabolism. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.676 |
| glnD | map | azo1911 | azo1910 | Putative protein-PII 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 fixation and metabolism. | Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.815 |
| glnD | ntrB | azo1911 | azo0736 | Putative protein-PII 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 fixation and metabolism. | Nitrogen regulation protein NR(II),; High confidence in function and specificity. | 0.603 |
| glnD | oma | azo1911 | azo1901 | Putative protein-PII 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 fixation and metabolism. | Outer membrane protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. | 0.635 |
| glnE | glnD | azo1293 | azo1911 | Probable [glutamate-ammonia-ligase] adenylyltransferase; 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 si [...] | Putative protein-PII 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 fixation and metabolism. | 0.805 |
| glnE | gltB | azo1293 | azo3642 | Probable [glutamate-ammonia-ligase] adenylyltransferase; 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 si [...] | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.623 |
| glnK | glnD | azo3739 | azo1911 | PII-like signal transmitter proteins are involved in the regulation of ammonium assimilation and nitrogen fixation. The PII-like proteins differed from each other in details of N-sensing. They were covalently modified by uridylylation upon nitrogen limitation. Similar to trembl|Q9EZQ3 (100%) and to trembl|Q7NQY3 (87%). Pfam: Nitrogen regulatory protein P-II; High confidence in function and specificity. | Putative protein-PII 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 fixation and metabolism. | 0.882 |
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