| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ahpC | ung | bbp_171 | bbp_172 | Peroxiredoxin 2; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.466 |
| dnaN | dut | bbp_011 | bbp_507 | Putative DNA polymerase III beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiat [...] | Deoxyuridine 5'-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. | 0.830 |
| dnaN | pheT | bbp_011 | bbp_124 | Putative DNA polymerase III beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiat [...] | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.469 |
| dnaN | polA | bbp_011 | bbp_382 | Putative DNA polymerase III beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiat [...] | Putative 5'-3' exonuclease; 5'-3' exonuclease acting preferentially on double-stranded DNA. | 0.999 |
| dnaN | thrA | bbp_011 | bbp_183 | Putative DNA polymerase III beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiat [...] | Aspartokinase; COG0527; COG0460; bifunctional aspartokinase/homoserine dehydrogenase (AK-HD); In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.559 |
| dnaN | ung | bbp_011 | bbp_172 | Putative DNA polymerase III beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiat [...] | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.741 |
| dut | dnaN | bbp_507 | bbp_011 | Deoxyuridine 5'-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. | Putative DNA polymerase III beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiat [...] | 0.830 |
| dut | polA | bbp_507 | bbp_382 | Deoxyuridine 5'-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. | Putative 5'-3' exonuclease; 5'-3' exonuclease acting preferentially on double-stranded DNA. | 0.626 |
| dut | ung | bbp_507 | bbp_172 | Deoxyuridine 5'-triphosphate nucleotidohydrolase; This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.469 |
| nfo | nth | bbp_128 | bbp_114 | Putative endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 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 |
| nfo | polA | bbp_128 | bbp_382 | Putative endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | Putative 5'-3' exonuclease; 5'-3' exonuclease acting preferentially on double-stranded DNA. | 0.593 |
| nfo | ung | bbp_128 | bbp_172 | Putative endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.520 |
| nth | nfo | bbp_114 | bbp_128 | 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. | Putative endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | 0.785 |
| nth | polA | bbp_114 | bbp_382 | 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. | Putative 5'-3' exonuclease; 5'-3' exonuclease acting preferentially on double-stranded DNA. | 0.812 |
| nth | ung | bbp_114 | bbp_172 | 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. | uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | 0.724 |
| pheT | dnaN | bbp_124 | bbp_011 | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | Putative DNA polymerase III beta chain; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiat [...] | 0.469 |
| pheT | polA | bbp_124 | bbp_382 | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | Putative 5'-3' exonuclease; 5'-3' exonuclease acting preferentially on double-stranded DNA. | 0.887 |
| pheT | thrA | bbp_124 | bbp_183 | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | Aspartokinase; COG0527; COG0460; bifunctional aspartokinase/homoserine dehydrogenase (AK-HD); In the C-terminal section; belongs to the homoserine dehydrogenase family. | 0.715 |
| pheT | trpD | bbp_124 | bbp_260 | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.409 |
| pheT | trpG | bbp_124 | bbp_525 | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | Anthranilate synthase component II; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concent [...] | 0.409 |