| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CAZ98683.1 | CAZ98684.1 | ZOBELLIA_4548 | ZOBELLIA_4549 | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | Conserved protein containing a C-terminal OmpA-like domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space and/or in the outer membrane; Family membership. | 0.583 |
| CAZ98683.1 | CAZ98685.1 | ZOBELLIA_4548 | ZOBELLIA_4550 | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.492 |
| CAZ98683.1 | cpsA2 | ZOBELLIA_4548 | ZOBELLIA_4547 | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | 0.648 |
| CAZ98683.1 | parE | ZOBELLIA_4548 | ZOBELLIA_4546 | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | DNA topoisomerase IV, subunit B; DNA topoisomerase IV is essential for chromosome segregation. In an ATP-dependent manner, It acts to relax positive supercoils in DNA and performs the decatenation events required during the replication of a circular DNA molecule; DNA topoisomerase IV is composed of two subunits parC and parE; Belongs to the type-II topoisomerase family, type-IIA subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.420 |
| CAZ98684.1 | CAZ98683.1 | ZOBELLIA_4549 | ZOBELLIA_4548 | Conserved protein containing a C-terminal OmpA-like domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space and/or in the outer membrane; Family membership. | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | 0.583 |
| CAZ98684.1 | CAZ98685.1 | ZOBELLIA_4549 | ZOBELLIA_4550 | Conserved protein containing a C-terminal OmpA-like domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space and/or in the outer membrane; Family membership. | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.724 |
| CAZ98684.1 | cpsA2 | ZOBELLIA_4549 | ZOBELLIA_4547 | Conserved protein containing a C-terminal OmpA-like domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space and/or in the outer membrane; Family membership. | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | 0.472 |
| CAZ98685.1 | CAZ98683.1 | ZOBELLIA_4550 | ZOBELLIA_4548 | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | 0.492 |
| CAZ98685.1 | CAZ98684.1 | ZOBELLIA_4550 | ZOBELLIA_4549 | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Conserved protein containing a C-terminal OmpA-like domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space and/or in the outer membrane; Family membership. | 0.724 |
| CAZ98685.1 | cpsA2 | ZOBELLIA_4550 | ZOBELLIA_4547 | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | 0.411 |
| cpsA2 | CAZ98683.1 | ZOBELLIA_4547 | ZOBELLIA_4548 | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | 0.648 |
| cpsA2 | CAZ98684.1 | ZOBELLIA_4547 | ZOBELLIA_4549 | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | Conserved protein containing a C-terminal OmpA-like domain. OmpA-like domains are thought to be responsible for non-covalent interactions with peptidoglycan; Signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space and/or in the outer membrane; Family membership. | 0.472 |
| cpsA2 | CAZ98685.1 | ZOBELLIA_4547 | ZOBELLIA_4550 | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | Conserved hypothetical membrane protein; Contains a N-terminal transmembrane helix; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.411 |
| cpsA2 | dapD | ZOBELLIA_4547 | ZOBELLIA_2904 | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | 2,3,4,5-Tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; DapD is involved in L-Lysine and diaminopimelate biosynthesis. It catalyzes the reaction: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the transferase hexapeptide repeat family. | 0.545 |
| cpsA2 | parC | ZOBELLIA_4547 | ZOBELLIA_4545 | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | DNA topoisomerase IV is essential for chromosome segregation. In an ATP-dependent manner, it acts to relax positive supercoils in DNA and performs the decatenation events required during the replication of a circular DNA molecule; DNA topoisomerase IV is composed of two subunits parC and parE; Belongs to the type-II topoisomerase family, type-IIA subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.427 |
| cpsA2 | parE | ZOBELLIA_4547 | ZOBELLIA_4546 | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | DNA topoisomerase IV, subunit B; DNA topoisomerase IV is essential for chromosome segregation. In an ATP-dependent manner, It acts to relax positive supercoils in DNA and performs the decatenation events required during the replication of a circular DNA molecule; DNA topoisomerase IV is composed of two subunits parC and parE; Belongs to the type-II topoisomerase family, type-IIA subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.444 |
| dapD | cpsA2 | ZOBELLIA_2904 | ZOBELLIA_4547 | 2,3,4,5-Tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; DapD is involved in L-Lysine and diaminopimelate biosynthesis. It catalyzes the reaction: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the transferase hexapeptide repeat family. | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | 0.545 |
| parC | cpsA2 | ZOBELLIA_4545 | ZOBELLIA_4547 | DNA topoisomerase IV is essential for chromosome segregation. In an ATP-dependent manner, it acts to relax positive supercoils in DNA and performs the decatenation events required during the replication of a circular DNA molecule; DNA topoisomerase IV is composed of two subunits parC and parE; Belongs to the type-II topoisomerase family, type-IIA subfamily; Localized in the cytoplasm; High confidence in function and specificity. | Carboxypeptidase, family M20; Carboxypeptidase catalyzes the hydrolysis of C-terminal amino acid residues from oligopeptides or polypeptides. This enzyme can release basic, acidic, aromatic, and, to a lesser extent, aliphatic amino acids. Belongs to the family M20 of the metallopeptidase. CpsA binds two co-catalytic zinc ions, which are coordinated by five conserved residues (His/Asp, Asp, Glu, Glu/Asp, His). The zinc ions stabilize the tetrahedral intermediate and activate the catalytic water molecule. Features a signal peptide cleaved between the residues 20 and 21. Localized in the [...] | 0.427 |
| parC | parE | ZOBELLIA_4545 | ZOBELLIA_4546 | DNA topoisomerase IV is essential for chromosome segregation. In an ATP-dependent manner, it acts to relax positive supercoils in DNA and performs the decatenation events required during the replication of a circular DNA molecule; DNA topoisomerase IV is composed of two subunits parC and parE; Belongs to the type-II topoisomerase family, type-IIA subfamily; Localized in the cytoplasm; High confidence in function and specificity. | DNA topoisomerase IV, subunit B; DNA topoisomerase IV is essential for chromosome segregation. In an ATP-dependent manner, It acts to relax positive supercoils in DNA and performs the decatenation events required during the replication of a circular DNA molecule; DNA topoisomerase IV is composed of two subunits parC and parE; Belongs to the type-II topoisomerase family, type-IIA subfamily; Localized in the cytoplasm; High confidence in function and specificity. | 0.996 |
| parE | CAZ98683.1 | ZOBELLIA_4546 | ZOBELLIA_4548 | DNA topoisomerase IV, subunit B; DNA topoisomerase IV is essential for chromosome segregation. In an ATP-dependent manner, It acts to relax positive supercoils in DNA and performs the decatenation events required during the replication of a circular DNA molecule; DNA topoisomerase IV is composed of two subunits parC and parE; Belongs to the type-II topoisomerase family, type-IIA subfamily; Localized in the cytoplasm; High confidence in function and specificity. | FMN / Fe-S cluster binding protein; Conserved protein Localized in the cytoplasmic membrane; Conserved hypothetical protein; Belongs to the glutamate synthase family. | 0.420 |