| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMP22764.1 | AMP25326.1 | VC42_08445 | VC42_24790 | Exopolyphosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.619 |
| AMP25326.1 | AMP22764.1 | VC42_24790 | VC42_08445 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Exopolyphosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.619 |
| AMP25326.1 | AMP25783.1 | VC42_24790 | VC42_01295 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 2OG-Fe(II) oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron/ascorbate-dependent oxidoreductase family. | 0.669 |
| AMP25326.1 | aspS | VC42_24790 | VC42_24950 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.820 |
| AMP25326.1 | nadE | VC42_24790 | VC42_05795 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.664 |
| AMP25326.1 | pdxS | VC42_24790 | VC42_24765 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | 0.753 |
| AMP25326.1 | pdxT | VC42_24790 | VC42_24775 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glutamine amidotransferase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | 0.753 |
| AMP25326.1 | rplS | VC42_24790 | VC42_22865 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | 0.727 |
| AMP25326.1 | rpsA | VC42_24790 | VC42_26360 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 30S ribosomal protein S1; In Escherichia coli this protein is involved in binding to the leader sequence of mRNAs and is itself bound to the 30S subunit; autoregulates expression via a C-terminal domain; in most gram negative organisms this protein is composed of 6 repeats of the S1 domain while in gram positive there are 4 repeats; the S1 nucleic acid-binding domain is found associated with other proteins; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.616 |
| AMP25326.1 | ruvA | VC42_24790 | VC42_24820 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | 0.754 |
| AMP25326.1 | tyrS | VC42_24790 | VC42_00095 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. | 0.813 |
| AMP25783.1 | AMP25326.1 | VC42_01295 | VC42_24790 | 2OG-Fe(II) oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron/ascorbate-dependent oxidoreductase family. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.669 |
| aspS | AMP25326.1 | VC42_24950 | VC42_24790 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.820 |
| aspS | ruvA | VC42_24950 | VC42_24820 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | ATP-dependent DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | 0.661 |
| aspS | tyrS | VC42_24950 | VC42_00095 | aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. | 0.854 |
| nadE | AMP25326.1 | VC42_05795 | VC42_24790 | NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.664 |
| pdxS | AMP25326.1 | VC42_24765 | VC42_24790 | Pyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.753 |
| pdxS | pdxT | VC42_24765 | VC42_24775 | Pyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | Glutamine amidotransferase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | 0.999 |
| pdxT | AMP25326.1 | VC42_24775 | VC42_24790 | Glutamine amidotransferase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.753 |
| pdxT | pdxS | VC42_24775 | VC42_24765 | Glutamine amidotransferase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | Pyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. | 0.999 |