node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Hoch_3933 | Hoch_3935 | Hoch_3933 | Hoch_3935 | Hypothetical protein; KEGG: GH10507 gene product from transcript GH10507- RA. | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. | 0.551 |
Hoch_3933 | nth-2 | Hoch_3933 | Hoch_3934 | Hypothetical protein; KEGG: GH10507 gene product from transcript GH10507- RA. | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.551 |
Hoch_3935 | Hoch_3933 | Hoch_3935 | Hoch_3933 | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. | Hypothetical protein; KEGG: GH10507 gene product from transcript GH10507- RA. | 0.551 |
Hoch_3935 | nth-2 | Hoch_3935 | Hoch_3934 | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.785 |
Hoch_3935 | rutB | Hoch_3935 | Hoch_3936 | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase 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. | 0.491 |
Hoch_3935 | rutC | Hoch_3935 | Hoch_3937 | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.471 |
nth-2 | Hoch_3933 | Hoch_3934 | Hoch_3933 | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | Hypothetical protein; KEGG: GH10507 gene product from transcript GH10507- RA. | 0.551 |
nth-2 | Hoch_3935 | Hoch_3934 | Hoch_3935 | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. | 0.785 |
nth-2 | rutB | Hoch_3934 | Hoch_3936 | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 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. | 0.482 |
nth-2 | rutC | Hoch_3934 | Hoch_3937 | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.500 |
rutB | Hoch_3935 | Hoch_3936 | Hoch_3935 | 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. | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. | 0.491 |
rutB | nth-2 | Hoch_3936 | Hoch_3934 | 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. | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.482 |
rutB | rutC | Hoch_3936 | Hoch_3937 | 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. | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 0.989 |
rutC | Hoch_3935 | Hoch_3937 | Hoch_3935 | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | PFAM: NUDIX hydrolase; KEGG: scl:sce1719 ADP-ribose pyrophosphatase; Belongs to the Nudix hydrolase family. | 0.471 |
rutC | nth-2 | Hoch_3937 | Hoch_3934 | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.500 |
rutC | rutB | Hoch_3937 | Hoch_3936 | Pyrimidine utilization protein C; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation. | 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. | 0.989 |