| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| argA | glnA | azo2830 | azo0738 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | Glutamine synthetase I (GS) plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Similar to pir|G83005 (70%) and to pir|AJECQ (66%). Pfam (PF00120): Glutamine synthetase, catalytic domain Pfam (PF03951): Glutamine synthetase, beta-Grasp domain; High confidence in function and specificity. | 0.510 |
| argA | glnE | azo2830 | azo1293 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | 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 [...] | 0.542 |
| argA | gltB | azo2830 | azo3642 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.725 |
| argA | hrpA | azo2830 | azo0716 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | ATP-dependent helicase hrpA. Not yet known. InterPro: DEAD/DEAH box helicase; High confidence in function and specificity. | 0.480 |
| argA | nadE | azo2830 | azo1360 | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | NAD(+) synthase (glutamine-hydrolyzing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.452 |
| azo1292 | azo1294 | azo1292 | azo1294 | Adenylate cyclase; Conserved hypothetical protein,40% identity to TrEMBL;Q88AR4 Has PF01928|CYTH domain(IPR008172);These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Has PF05235:CHAD domain(IPR007899);The CHAD domain is an alpha-helical domain functionally associated with the CYTH domains. It has conserved histidines that may chelate metals. | Conserved hypothetical protein. Homology to cv2096 of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains predicted no signal peptide 1 TMHs. | 0.416 |
| azo1292 | azo1295 | azo1292 | azo1295 | Adenylate cyclase; Conserved hypothetical protein,40% identity to TrEMBL;Q88AR4 Has PF01928|CYTH domain(IPR008172);These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Has PF05235:CHAD domain(IPR007899);The CHAD domain is an alpha-helical domain functionally associated with the CYTH domains. It has conserved histidines that may chelate metals. | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | 0.407 |
| azo1292 | glnE | azo1292 | azo1293 | Adenylate cyclase; Conserved hypothetical protein,40% identity to TrEMBL;Q88AR4 Has PF01928|CYTH domain(IPR008172);These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Has PF05235:CHAD domain(IPR007899);The CHAD domain is an alpha-helical domain functionally associated with the CYTH domains. It has conserved histidines that may chelate metals. | 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 [...] | 0.701 |
| azo1294 | azo1292 | azo1294 | azo1292 | Conserved hypothetical protein. Homology to cv2096 of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains predicted no signal peptide 1 TMHs. | Adenylate cyclase; Conserved hypothetical protein,40% identity to TrEMBL;Q88AR4 Has PF01928|CYTH domain(IPR008172);These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Has PF05235:CHAD domain(IPR007899);The CHAD domain is an alpha-helical domain functionally associated with the CYTH domains. It has conserved histidines that may chelate metals. | 0.416 |
| azo1294 | azo1295 | azo1294 | azo1295 | Conserved hypothetical protein. Homology to cv2096 of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains predicted no signal peptide 1 TMHs. | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | 0.865 |
| azo1294 | glnE | azo1294 | azo1293 | Conserved hypothetical protein. Homology to cv2096 of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains predicted no signal peptide 1 TMHs. | 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 [...] | 0.580 |
| azo1294 | tldD | azo1294 | azo1296 | Conserved hypothetical protein. Homology to cv2096 of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains predicted no signal peptide 1 TMHs. | Probable TldD protein. Homology to tldD of E. coli of 59% (sprot|TLDD_ECOLI). Suppresses the inhibitory activity of the carbon storage regulator (csrA). Pfam: putative modulator of DNA gyrase no signal peptide no TMHs; Function unclear. | 0.745 |
| azo1295 | azo1292 | azo1295 | azo1292 | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | Adenylate cyclase; Conserved hypothetical protein,40% identity to TrEMBL;Q88AR4 Has PF01928|CYTH domain(IPR008172);These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Has PF05235:CHAD domain(IPR007899);The CHAD domain is an alpha-helical domain functionally associated with the CYTH domains. It has conserved histidines that may chelate metals. | 0.407 |
| azo1295 | azo1294 | azo1295 | azo1294 | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | Conserved hypothetical protein. Homology to cv2096 of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains predicted no signal peptide 1 TMHs. | 0.865 |
| azo1295 | glnA | azo1295 | azo0738 | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | Glutamine synthetase I (GS) plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Similar to pir|G83005 (70%) and to pir|AJECQ (66%). Pfam (PF00120): Glutamine synthetase, catalytic domain Pfam (PF03951): Glutamine synthetase, beta-Grasp domain; High confidence in function and specificity. | 0.495 |
| azo1295 | glnE | azo1295 | azo1293 | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | 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 [...] | 0.611 |
| azo1295 | gltB | azo1295 | azo3642 | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.930 |
| azo1295 | nadE | azo1295 | azo1360 | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | NAD(+) synthase (glutamine-hydrolyzing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.531 |
| azo1295 | tldD | azo1295 | azo1296 | Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein. | Probable TldD protein. Homology to tldD of E. coli of 59% (sprot|TLDD_ECOLI). Suppresses the inhibitory activity of the carbon storage regulator (csrA). Pfam: putative modulator of DNA gyrase no signal peptide no TMHs; Function unclear. | 0.702 |
| glnA | argA | azo0738 | azo2830 | Glutamine synthetase I (GS) plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Similar to pir|G83005 (70%) and to pir|AJECQ (66%). Pfam (PF00120): Glutamine synthetase, catalytic domain Pfam (PF03951): Glutamine synthetase, beta-Grasp domain; High confidence in function and specificity. | Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear. | 0.510 |