node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Cseg_1789 | Cseg_1790 | Cseg_1789 | Cseg_1790 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | 0.988 |
Cseg_1789 | rutA | Cseg_1789 | Cseg_2081 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | 0.913 |
Cseg_1789 | rutB | Cseg_1789 | Cseg_2078 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.975 |
Cseg_1789 | rutC | Cseg_1789 | Cseg_2079 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.473 |
Cseg_1789 | rutD | Cseg_1789 | Cseg_2080 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | Pyrimidine utilization protein D; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family. | 0.613 |
Cseg_1790 | Cseg_1789 | Cseg_1790 | Cseg_1789 | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | 0.988 |
Cseg_1790 | Cseg_1893 | Cseg_1790 | Cseg_1893 | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | 0.638 |
Cseg_1790 | rutA | Cseg_1790 | Cseg_2081 | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | 0.944 |
Cseg_1790 | rutB | Cseg_1790 | Cseg_2078 | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.923 |
Cseg_1790 | rutC | Cseg_1790 | Cseg_2079 | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.918 |
Cseg_1790 | rutD | Cseg_1790 | Cseg_2080 | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | Pyrimidine utilization protein D; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family. | 0.925 |
Cseg_1893 | Cseg_1790 | Cseg_1893 | Cseg_1790 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | PFAM: isochorismatase hydrolase; KEGG: cak:Caul_1793 isochorismatase hydrolase. | 0.638 |
Cseg_1893 | rutB | Cseg_1893 | Cseg_2078 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.764 |
Cseg_1893 | rutC | Cseg_1893 | Cseg_2079 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.473 |
Cseg_1893 | rutD | Cseg_1893 | Cseg_2080 | PFAM: Luciferase-like, subgroup; KEGG: ccs:CCNA_01227 nitrilotriacetate monooxygenase. | Pyrimidine utilization protein D; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family. | 0.613 |
Cseg_2077 | rutA | Cseg_2077 | Cseg_2081 | PFAM: Tetracycline transcriptional regulator YcdC domain protein; regulatory protein TetR; KEGG: ccs:CCNA_02884 transcriptional regulator, TetR family. | Pyrimidine utilization protein A; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. | 0.682 |
Cseg_2077 | rutB | Cseg_2077 | Cseg_2078 | PFAM: Tetracycline transcriptional regulator YcdC domain protein; regulatory protein TetR; KEGG: ccs:CCNA_02884 transcriptional regulator, TetR family. | Pyrimidine utilization protein B; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily. | 0.713 |
Cseg_2077 | rutC | Cseg_2077 | Cseg_2079 | PFAM: Tetracycline transcriptional regulator YcdC domain protein; regulatory protein TetR; KEGG: ccs:CCNA_02884 transcriptional regulator, TetR family. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.648 |
Cseg_2077 | rutD | Cseg_2077 | Cseg_2080 | PFAM: Tetracycline transcriptional regulator YcdC domain protein; regulatory protein TetR; KEGG: ccs:CCNA_02884 transcriptional regulator, TetR family. | Pyrimidine utilization protein D; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family. | 0.709 |
Cseg_4124 | fusA | Cseg_4124 | Cseg_0755 | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...] | 0.439 |