node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CC_1169 | rutA | CC_1169 | CC_2798 | Conserved hypothetical protein; Identified by Glimmer2; putative. | Conserved hypothetical protein; 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 (By similarity). | 0.913 |
CC_1169 | rutB | CC_1169 | CC_2795 | Conserved hypothetical protein; Identified by Glimmer2; putative. | Isochorismatase family protein; 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 (By similarity); Belongs to the isochorismatase family. RutB subfamily. | 0.980 |
CC_1169 | rutC | CC_1169 | CC_2796 | Conserved hypothetical protein; Identified by Glimmer2; putative. | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.650 |
CC_1169 | rutD | CC_1169 | CC_2797 | Conserved hypothetical protein; Identified by Glimmer2; putative. | Hydrolase, alpha/beta hydrolase fold family; 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. | 0.739 |
CC_2794 | rutA | CC_2794 | CC_2798 | Transcriptional regulator, TetR family; Identified by match to protein family HMM. | Conserved hypothetical protein; 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 (By similarity). | 0.507 |
CC_2794 | rutB | CC_2794 | CC_2795 | Transcriptional regulator, TetR family; Identified by match to protein family HMM. | Isochorismatase family protein; 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 (By similarity); Belongs to the isochorismatase family. RutB subfamily. | 0.663 |
CC_2794 | rutC | CC_2794 | CC_2796 | Transcriptional regulator, TetR family; Identified by match to protein family HMM. | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.553 |
CC_2794 | rutD | CC_2794 | CC_2797 | Transcriptional regulator, TetR family; Identified by match to protein family HMM. | Hydrolase, alpha/beta hydrolase fold family; 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. | 0.507 |
CC_3105 | CC_3635 | CC_3105 | CC_3635 | Threonine dehydratase; Identified by match to protein family HMM. | 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. | 0.920 |
CC_3105 | rutC | CC_3105 | CC_2796 | Threonine dehydratase; Identified by match to protein family HMM. | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.509 |
CC_3635 | CC_3105 | CC_3635 | CC_3105 | 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. | Threonine dehydratase; Identified by match to protein family HMM. | 0.920 |
CC_3635 | rutC | CC_3635 | CC_2796 | 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. | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.481 |
fusA | rutC | CC_3200 | CC_2796 | 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 [...] | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.536 |
nnrE | rutB | CC_1965 | CC_2795 | YjeF family protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epim [...] | Isochorismatase family protein; 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 (By similarity); Belongs to the isochorismatase family. RutB subfamily. | 0.478 |
nnrE | rutC | CC_1965 | CC_2796 | YjeF family protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epim [...] | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.462 |
rph | rutC | CC_0152 | CC_2796 | Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.510 |
rutA | CC_1169 | CC_2798 | CC_1169 | Conserved hypothetical protein; 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 (By similarity). | Conserved hypothetical protein; Identified by Glimmer2; putative. | 0.913 |
rutA | CC_2794 | CC_2798 | CC_2794 | Conserved hypothetical protein; 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 (By similarity). | Transcriptional regulator, TetR family; Identified by match to protein family HMM. | 0.507 |
rutA | rutB | CC_2798 | CC_2795 | Conserved hypothetical protein; 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 (By similarity). | Isochorismatase family protein; 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 (By similarity); Belongs to the isochorismatase family. RutB subfamily. | 0.985 |
rutA | rutC | CC_2798 | CC_2796 | Conserved hypothetical protein; 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 (By similarity). | Conserved hypothetical protein; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.836 |