| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APC12382.1 | APC12383.1 | RB151_027140 | RB151_027150 | N-acetylglutamate synthase. | YfcL protein. | 0.559 |
| APC12382.1 | epmC | RB151_027140 | RB151_027160 | N-acetylglutamate synthase. | Elongation factor P hydroxylase. | 0.501 |
| APC12382.1 | yfcA | RB151_027140 | RB151_027170 | N-acetylglutamate synthase. | Hypothetical protein. | 0.477 |
| APC12383.1 | APC12382.1 | RB151_027150 | RB151_027140 | YfcL protein. | N-acetylglutamate synthase. | 0.559 |
| APC12383.1 | aroC | RB151_027150 | RB151_027180 | YfcL protein. | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 0.479 |
| APC12383.1 | epmC | RB151_027150 | RB151_027160 | YfcL protein. | Elongation factor P hydroxylase. | 0.734 |
| APC12383.1 | yfcA | RB151_027150 | RB151_027170 | YfcL protein. | Hypothetical protein. | 0.697 |
| aroC | APC12383.1 | RB151_027180 | RB151_027150 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | YfcL protein. | 0.479 |
| aroC | epmC | RB151_027180 | RB151_027160 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Elongation factor P hydroxylase. | 0.518 |
| aroC | prmB | RB151_027180 | RB151_027190 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | 50S ribosomal protein L3 glutamine methyltransferase; Specifically methylates the 50S ribosomal protein L3 on a specific glutamine residue; Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily. | 0.654 |
| aroC | yfcA | RB151_027180 | RB151_027170 | Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. | Hypothetical protein. | 0.546 |
| efp | epmA | RB151_038600 | RB151_038440 | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | Elongation factor P--(R)-beta-lysine ligase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | 0.914 |
| efp | epmB | RB151_038600 | RB151_038610 | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | L-lysine 2,3-aminomutase. | 0.864 |
| efp | epmC | RB151_038600 | RB151_027160 | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | Elongation factor P hydroxylase. | 0.561 |
| epmA | efp | RB151_038440 | RB151_038600 | Elongation factor P--(R)-beta-lysine ligase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | 0.914 |
| epmA | epmB | RB151_038440 | RB151_038610 | Elongation factor P--(R)-beta-lysine ligase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | L-lysine 2,3-aminomutase. | 0.841 |
| epmA | epmC | RB151_038440 | RB151_027160 | Elongation factor P--(R)-beta-lysine ligase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | Elongation factor P hydroxylase. | 0.481 |
| epmB | efp | RB151_038610 | RB151_038600 | L-lysine 2,3-aminomutase. | Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family. | 0.864 |
| epmB | epmA | RB151_038610 | RB151_038440 | L-lysine 2,3-aminomutase. | Elongation factor P--(R)-beta-lysine ligase; With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P; Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily. | 0.841 |
| epmB | epmC | RB151_038610 | RB151_027160 | L-lysine 2,3-aminomutase. | Elongation factor P hydroxylase. | 0.559 |